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pET28a(+)
2024-11-10 16:52:00 +00:00
HEADER HYDROLASE 12-MAR-12 4E46
TITLE STRUCTURE OF RHODOCOCCUS RHODOCHROUS HALOALKANE DEHALOGENASE DHAA IN
TITLE 2 COMPLEX WITH 2-PROPANOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 STRAIN: NCIB 13064;
SOURCE 5 GENE: DHAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAQN
KEYWDS CATALYTIC PENTAD, ALPHA/BETA HYDROLASE FOLD, HALIDE BINDING,
KEYWDS 2 HYDROLYTIC DEHALOGENATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.STSIAPANAVA,R.CHALOUPKOVA,J.DAMBORSKY,I.KUTA SMATANOVA
REVDAT 4 13-SEP-23 4E46 1 REMARK SEQADV
REVDAT 3 15-NOV-17 4E46 1 REMARK
REVDAT 2 14-JAN-15 4E46 1 JRNL
REVDAT 1 13-MAR-13 4E46 0
JRNL AUTH V.STEPANKOVA,M.KHABIRI,J.BREZOVSKY,A.PAVELKA,J.SYKORA,
JRNL AUTH 2 M.AMARO,B.MINOFAR,Z.PROKOP,M.HOF,R.ETTRICH,R.CHALOUPKOVA,
JRNL AUTH 3 J.DAMBORSKY
JRNL TITL EXPANSION OF ACCESS TUNNELS AND ACTIVE-SITE CAVITIES
JRNL TITL 2 INFLUENCE ACTIVITY OF HALOALKANE DEHALOGENASES IN ORGANIC
JRNL TITL 3 COSOLVENTS.
JRNL REF CHEMBIOCHEM V. 14 890 2013
JRNL REFN ISSN 1439-4227
JRNL PMID 23564727
JRNL DOI 10.1002/CBIC.201200733
REMARK 2
REMARK 2 RESOLUTION. 1.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.113
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.113
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 69524
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.106
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 62755
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2359
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 542
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2902.4
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2134.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 49
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 24815
REMARK 3 NUMBER OF RESTRAINTS : 30840
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.027
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.027
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.083
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.076
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.027
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.033
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE SOLUTION AND REFINEMENT WERE
REMARK 3 PERFORMED USING FREE R FOR CROSS-VALIDATION THROUGHOUT: FREE R =
REMARK 3 0.150 FROM A RANDOM TEST SET COMPRISING 5% OF REFLECTIONS (3476
REMARK 3 TOTAL). FINAL REFINEMENT WAS PERFORMED USING ALL REFLECTIONS.
REMARK 4
REMARK 4 4E46 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111),
REMARK 200 HORIZONTALLY FOCUSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65492
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.260
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.11300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3FBW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 24% PEG4000,
REMARK 280 11% 2-PROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 296 C HIS A 296 O 0.214
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 86 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 133 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 GLU A 183 CB - CG - CD ANGL. DEV. = 19.9 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TYR A 225 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
REMARK 500 TYR A 225 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 42 48.00 -104.46
REMARK 500 THR A 43 -159.73 -101.86
REMARK 500 GLU A 98 -94.94 -110.13
REMARK 500 ASP A 106 -125.36 53.02
REMARK 500 ARG A 153 47.14 -87.48
REMARK 500 ASP A 156 -72.68 -104.21
REMARK 500 VAL A 245 -78.59 -133.30
REMARK 500 LEU A 271 -97.74 -117.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FBW RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA MUTANT C176Y
REMARK 900 RELATED ID: 3FWH RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA MUTANT C176Y,I135F
REMARK 900 RELATED ID: 3G9X RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA MUTANT I135F
REMARK 900 RELATED ID: 1BN6 RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA
REMARK 900 RELATED ID: 1CQW RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA WITH IODIDE ION
DBREF 4E46 A 1 293 UNP P0A3G2 DHAA_RHORH 1 293
SEQADV 4E46 HIS A 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 4E46 HIS A 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 4E46 HIS A 296 UNP P0A3G2 EXPRESSION TAG
SEQRES 1 A 296 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 296 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 296 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 296 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 296 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 296 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 296 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 296 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 296 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 296 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 296 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 296 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP
SEQRES 13 A 296 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 296 GLU GLY ALA LEU PRO LYS CYS VAL VAL ARG PRO LEU THR
SEQRES 15 A 296 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 296 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 296 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 296 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 296 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 296 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 296 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 296 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 296 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS
HET IPA A1001 4
HET ACT A1002 4
HET ACT A1003 4
HET CL A1004 1
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETSYN IPA 2-PROPANOL
FORMUL 2 IPA C3 H8 O
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 CL CL 1-
FORMUL 6 HOH *542(H2 O)
HELIX 1 1 SER A 44 ARG A 49 5 6
HELIX 2 2 ILE A 51 ALA A 56 1 6
HELIX 3 3 PHE A 80 LEU A 95 1 16
HELIX 4 4 ASP A 106 ASN A 119 1 14
HELIX 5 5 THR A 137 TRP A 141 5 5
HELIX 6 6 PRO A 142 PHE A 144 5 3
HELIX 7 7 ALA A 145 ARG A 153 1 9
HELIX 8 8 ASP A 156 ILE A 163 1 8
HELIX 9 9 ASN A 166 GLY A 171 1 6
HELIX 10 10 GLY A 171 CYS A 176 1 6
HELIX 11 11 THR A 182 GLU A 191 1 10
HELIX 12 12 PRO A 192 LEU A 194 5 3
HELIX 13 13 LYS A 195 ASP A 198 5 4
HELIX 14 14 ARG A 199 LEU A 209 1 11
HELIX 15 15 PRO A 215 SER A 232 1 18
HELIX 16 16 PRO A 248 LEU A 259 1 12
HELIX 17 17 TYR A 273 ASN A 278 1 6
HELIX 18 18 ASN A 278 LEU A 290 1 13
HELIX 19 19 PRO A 291 HIS A 294 5 4
SHEET 1 A 8 HIS A 13 VAL A 17 0
SHEET 2 A 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 A 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 A 8 VAL A 35 LEU A 38 1 N VAL A 35 O ILE A 62
SHEET 5 A 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 A 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 A 8 LYS A 236 PRO A 243 1 O LEU A 237 N CYS A 128
SHEET 8 A 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
CISPEP 1 ASN A 41 PRO A 42 0 -5.95
CISPEP 2 GLU A 214 PRO A 215 0 -8.46
CISPEP 3 GLU A 214 PRO A 215 0 -1.72
CISPEP 4 THR A 242 PRO A 243 0 4.39
SITE 1 AC1 5 ASN A 41 ASP A 106 HIS A 272 TYR A 273
SITE 2 AC1 5 CL A1004
SITE 1 AC2 7 THR A 33 HIS A 59 LYS A 124 LEU A 290
SITE 2 AC2 7 HIS A 294 HOH A2052 HOH A2165
SITE 1 AC3 7 PRO A 12 GLN A 231 PRO A 233 HOH A2095
SITE 2 AC3 7 HOH A2126 HOH A2202 HOH A2206
SITE 1 AC4 4 ASN A 41 TRP A 107 PRO A 206 IPA A1001
CRYST1 42.646 44.480 46.334 115.39 98.05 109.40 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023449 0.008258 0.008735 0.00000
SCALE2 0.000000 0.023835 0.014092 0.00000
SCALE3 0.000000 0.000000 0.025322 0.00000
ATOM 1 N ILE A 4 14.139 14.628 -4.648 1.00 14.98 N
ANISOU 1 N ILE A 4 922 1615 3156 -16 163 196 N
ATOM 2 CA ILE A 4 12.885 13.839 -4.674 1.00 10.31 C
ANISOU 2 CA ILE A 4 1009 1187 1722 77 84 34 C
ATOM 3 C ILE A 4 11.710 14.806 -4.734 1.00 7.68 C
ANISOU 3 C ILE A 4 800 919 1198 -192 306 38 C
ATOM 4 O ILE A 4 11.567 15.722 -3.931 1.00 8.59 O
ANISOU 4 O ILE A 4 1112 1119 1033 -166 256 -80 O
ATOM 5 CB ILE A 4 12.796 12.905 -3.468 1.00 9.55 C
ANISOU 5 CB ILE A 4 717 1254 1656 145 -59 -67 C
ATOM 6 CG1 ILE A 4 13.836 11.791 -3.524 1.00 9.75 C
ANISOU 6 CG1 ILE A 4 1016 915 1773 80 107 -81 C
ATOM 7 CG2 ILE A 4 11.399 12.301 -3.375 1.00 9.86 C
ANISOU 7 CG2 ILE A 4 890 1468 1388 -118 18 -84 C
ATOM 8 CD1 ILE A 4 14.024 10.929 -2.326 1.00 11.66 C
ANISOU 8 CD1 ILE A 4 1264 1094 2073 -9 -269 147 C
ATOM 9 N GLY A 5 10.864 14.590 -5.738 1.00 8.01 N
ANISOU 9 N GLY A 5 805 817 1420 -70 210 -270 N
ATOM 10 CA GLY A 5 9.820 15.590 -5.981 1.00 8.14 C
ANISOU 10 CA GLY A 5 1030 1021 1040 73 257 9 C
ATOM 11 C GLY A 5 8.723 15.605 -4.921 1.00 6.47 C
ANISOU 11 C GLY A 5 758 544 1158 -107 161 -83 C
ATOM 12 O GLY A 5 8.342 14.571 -4.381 1.00 7.66 O
ANISOU 12 O GLY A 5 1120 645 1147 -217 72 45 O
ATOM 13 N THR A 6 8.204 16.785 -4.607 1.00 7.39 N
ANISOU 13 N THR A 6 1043 645 1120 1 357 10 N
ATOM 14 CA THR A 6 7.158 16.944 -3.621 1.00 6.17 C
ANISOU 14 CA THR A 6 855 512 975 -66 260 116 C
ATOM 15 C THR A 6 5.803 17.210 -4.237 1.00 7.14 C
ANISOU 15 C THR A 6 962 466 1286 -46 159 97 C
ATOM 16 O THR A 6 4.796 17.187 -3.502 1.00 8.29 O
ANISOU 16 O THR A 6 873 663 1613 96 281 44 O
ATOM 17 CB THR A 6 7.520 18.084 -2.641 1.00 7.53 C
ANISOU 17 CB THR A 6 1036 616 1207 200 170 -130 C
ATOM 18 OG1 THR A 6 7.555 19.314 -3.346 1.00 8.87 O
ANISOU 18 OG1 THR A 6 1198 609 1565 -129 41 13 O
ATOM 19 CG2 THR A 6 8.902 17.850 -2.025 1.00 7.52 C
ANISOU 19 CG2 THR A 6 949 561 1348 32 203 -277 C
ATOM 20 N GLY A 7 5.754 17.551 -5.503 1.00 7.40 N
ANISOU 20 N GLY A 7 810 592 1408 3 13 131 N
ATOM 21 CA GLY A 7 4.484 17.869 -6.120 1.00 8.89 C
ANISOU 21 CA GLY A 7 979 613 1785 -113 -282 132 C
ATOM 22 C GLY A 7 3.709 16.628 -6.524 1.00 7.74 C
ANISOU 22 C GLY A 7 828 618 1494 -133 73 43 C
ATOM 23 O GLY A 7 4.170 15.489 -6.555 1.00 7.66 O
ANISOU 23 O GLY A 7 943 668 1301 25 -37 125 O
ATOM 24 N PHE A 8 2.446 16.855 -6.886 1.00 7.01 N
ANISOU 24 N PHE A 8 844 441 1378 -68 10 68 N
ATOM 25 CA PHE A 8 1.514 15.827 -7.320 1.00 6.52 C
ANISOU 25 CA PHE A 8 697 565 1213 42 35 66 C
ATOM 26 C PHE A 8 0.847 16.299 -8.612 1.00 6.22 C
ANISOU 26 C PHE A 8 610 571 1182 -53 137 107 C
ATOM 27 O PHE A 8 -0.299 16.750 -8.585 1.00 7.20 O
ANISOU 27 O PHE A 8 642 798 1296 104 32 225 O
ATOM 28 CB PHE A 8 0.470 15.554 -6.216 1.00 6.63 C
ANISOU 28 CB PHE A 8 830 621 1067 -16 43 46 C
ATOM 29 CG PHE A 8 -0.303 14.279 -6.465 1.00 6.19 C
ANISOU 29 CG PHE A 8 770 538 1045 62 113 -29 C
ATOM 30 CD1 PHE A 8 0.304 13.040 -6.298 1.00 6.00 C
ANISOU 30 CD1 PHE A 8 917 587 773 64 11 162 C
ATOM 31 CD2 PHE A 8 -1.639 14.310 -6.882 1.00 6.98 C
ANISOU 31 CD2 PHE A 8 754 714 1186 92 122 -156 C
ATOM 32 CE1 PHE A 8 -0.427 11.867 -6.527 1.00 6.34 C
ANISOU 32 CE1 PHE A 8 972 556 880 52 266 67 C
ATOM 33 CE2 PHE A 8 -2.335 13.164 -7.093 1.00 7.12 C
ANISOU 33 CE2 PHE A 8 850 866 990 -50 -44 47 C
ATOM 34 CZ PHE A 8 -1.745 11.934 -6.941 1.00 7.13 C
ANISOU 34 CZ PHE A 8 1134 715 859 -65 -63 -7 C
ATOM 35 N PRO A 9 1.580 16.195 -9.722 1.00 6.62 N
ANISOU 35 N PRO A 9 737 546 1232 12 177 148 N
ATOM 36 CA PRO A 9 1.094 16.754 -10.990 1.00 7.85 C
ANISOU 36 CA PRO A 9 974 757 1252 -7 138 244 C
ATOM 37 C PRO A 9 0.255 15.744 -11.751 1.00 8.35 C
ANISOU 37 C PRO A 9 1422 735 1017 -176 138 291 C
ATOM 38 O PRO A 9 0.579 15.377 -12.892 1.00 12.04 O
ANISOU 38 O PRO A 9 2075 1427 1071 -258 312 102 O
ATOM 39 CB PRO A 9 2.412 17.074 -11.726 1.00 9.89 C
ANISOU 39 CB PRO A 9 1217 1193 1346 -155 221 327 C
ATOM 40 CG PRO A 9 3.275 15.911 -11.309 1.00 10.26 C
ANISOU 40 CG PRO A 9 1120 1327 1452 183 360 -157 C
ATOM 41 CD PRO A 9 2.951 15.694 -9.839 1.00 8.13 C
ANISOU 41 CD PRO A 9 745 805 1538 71 294 195 C
ATOM 42 N PHE A 10 -0.817 15.293 -11.114 1.00 6.77 N
ANISOU 42 N PHE A 10 998 515 1062 95 27 124 N
ATOM 43 CA PHE A 10 -1.734 14.333 -11.689 1.00 6.98 C
ANISOU 43 CA PHE A 10 932 610 1111 149 5 90 C
ATOM 44 C PHE A 10 -3.160 14.848 -11.605 1.00 7.00 C
ANISOU 44 C PHE A 10 955 575 1130 94 28 -10 C
ATOM 45 O PHE A 10 -3.636 15.168 -10.517 1.00 8.31 O
ANISOU 45 O PHE A 10 1108 829 1220 230 84 -183 O
ATOM 46 CB PHE A 10 -1.657 12.952 -11.032 1.00 6.79 C
ANISOU 46 CB PHE A 10 933 532 1115 25 -5 28 C
ATOM 47 CG PHE A 10 -0.241 12.414 -11.106 1.00 6.41 C
ANISOU 47 CG PHE A 10 994 532 908 102 88 153 C
ATOM 48 CD1 PHE A 10 0.236 11.828 -12.251 1.00 7.43 C
ANISOU 48 CD1 PHE A 10 1150 903 769 158 38 121 C
ATOM 49 CD2 PHE A 10 0.634 12.515 -10.029 1.00 7.07 C
ANISOU 49 CD2 PHE A 10 1058 834 794 161 85 88 C
ATOM 50 CE1 PHE A 10 1.522 11.351 -12.415 1.00 8.28 C
ANISOU 50 CE1 PHE A 10 1339 593 1215 280 158 -106 C
ATOM 51 CE2 PHE A 10 1.903 12.015 -10.161 1.00 8.24 C
ANISOU 51 CE2 PHE A 10 1270 659 1202 424 -178 43 C
ATOM 52 CZ PHE A 10 2.361 11.436 -11.325 1.00 8.55 C
ANISOU 52 CZ PHE A 10 1153 626 1470 384 40 -43 C
ATOM 53 N ASP A 11 -3.853 14.871 -12.731 1.00 6.79 N
ANISOU 53 N ASP A 11 789 701 1088 43 116 -11 N
ATOM 54 CA ASP A 11 -5.242 15.309 -12.744 1.00 6.93 C
ANISOU 54 CA ASP A 11 824 539 1269 169 182 -28 C
ATOM 55 C ASP A 11 -6.118 14.332 -11.982 1.00 6.80 C
ANISOU 55 C ASP A 11 869 623 1091 50 194 -153 C
ATOM 56 O ASP A 11 -5.921 13.120 -12.050 1.00 7.32 O
ANISOU 56 O ASP A 11 919 562 1299 40 277 -137 O
ATOM 57 CB ASP A 11 -5.784 15.419 -14.159 1.00 8.33 C
ANISOU 57 CB ASP A 11 1058 798 1308 235 19 105 C
ATOM 58 CG ASP A 11 -5.107 16.434 -15.047 1.00 10.19 C
ANISOU 58 CG ASP A 11 1464 1039 1369 102 22 235 C
ATOM 59 OD1 ASP A 11 -4.519 17.359 -14.496 1.00 10.67 O
ANISOU 59 OD1 ASP A 11 1554 1092 1410 -72 56 354 O
ATOM 60 OD2 ASP A 11 -5.190 16.292 -16.300 1.00 15.18 O
ANISOU 60 OD2 ASP A 11 2691 1751 1326 -341 17 253 O
ATOM 61 N PRO A 12 -7.095 14.826 -11.266 1.00 6.00 N
ANISOU 61 N PRO A 12 873 469 937 210 87 52 N
ATOM 62 CA PRO A 12 -7.999 13.927 -10.529 1.00 6.40 C
ANISOU 62 CA PRO A 12 824 533 1075 146 188 -49 C
ATOM 63 C PRO A 12 -8.988 13.209 -11.429 1.00 7.13 C
ANISOU 63 C PRO A 12 906 530 1273 182 -4 -26 C
ATOM 64 O PRO A 12 -9.580 13.808 -12.356 1.00 10.95 O
ANISOU 64 O PRO A 12 1512 687 1963 107 -654 242 O
ATOM 65 CB PRO A 12 -8.704 14.855 -9.550 1.00 8.29 C
ANISOU 65 CB PRO A 12 1090 839 1222 119 318 -232 C
ATOM 66 CG PRO A 12 -8.710 16.200 -10.234 1.00 9.52 C
ANISOU 66 CG PRO A 12 1449 684 1484 350 423 -280 C
ATOM 67 CD PRO A 12 -7.421 16.248 -11.004 1.00 7.45 C
ANISOU 67 CD PRO A 12 1083 496 1252 198 60 -77 C
ATOM 68 N HIS A 13 -9.179 11.930 -11.166 1.00 5.75 N
ANISOU 68 N HIS A 13 675 652 858 15 181 80 N
ATOM 69 CA HIS A 13 -10.270 11.139 -11.747 1.00 5.88 C
ANISOU 69 CA HIS A 13 603 671 960 111 44 82 C
ATOM 70 C HIS A 13 -11.098 10.579 -10.595 1.00 5.67 C
ANISOU 70 C HIS A 13 608 507 1040 74 65 -67 C
ATOM 71 O HIS A 13 -10.558 10.251 -9.565 1.00 6.40 O
ANISOU 71 O HIS A 13 728 768 936 111 131 24 O
ATOM 72 CB HIS A 13 -9.755 10.017 -12.664 1.00 6.96 C
ANISOU 72 CB HIS A 13 1137 660 847 98 101 74 C
ATOM 73 CG HIS A 13 -8.870 10.557 -13.739 1.00 7.41 C
ANISOU 73 CG HIS A 13 1081 782 952 17 186 -40 C
ATOM 74 ND1 HIS A 13 -7.512 10.798 -13.722 1.00 9.60 N
ANISOU 74 ND1 HIS A 13 1153 1171 1322 14 246 30 N
ATOM 75 CD2 HIS A 13 -9.317 10.935 -14.971 1.00 11.82 C
ANISOU 75 CD2 HIS A 13 1250 2410 831 -73 287 308 C
ATOM 76 CE1 HIS A 13 -7.159 11.320 -14.903 1.00 8.97 C
ANISOU 76 CE1 HIS A 13 1227 887 1295 27 441 -2 C
ATOM 77 NE2 HIS A 13 -8.230 11.378 -15.642 1.00 15.91 N
ANISOU 77 NE2 HIS A 13 1653 3089 1305 -438 308 658 N
ATOM 78 N TYR A 14 -12.387 10.435 -10.832 1.00 7.58 N
ANISOU 78 N TYR A 14 594 1018 1268 31 117 178 N
ATOM 79 CA ATYR A 14 -13.275 9.881 -9.818 0.60 7.78 C
ANISOU 79 CA ATYR A 14 809 858 1291 -104 242 3 C
ATOM 80 CA BTYR A 14 -13.331 9.922 -9.884 0.40 6.46 C
ANISOU 80 CA BTYR A 14 605 598 1253 194 178 91 C
ATOM 81 C TYR A 14 -14.226 8.860 -10.468 1.00 6.95 C
ANISOU 81 C TYR A 14 563 1018 1058 35 226 10 C
ATOM 82 O TYR A 14 -14.660 8.969 -11.610 1.00 9.17 O
ANISOU 82 O TYR A 14 840 1332 1312 35 -145 275 O
ATOM 83 CB ATYR A 14 -14.023 11.004 -9.079 0.60 10.03 C
ANISOU 83 CB ATYR A 14 781 1499 1530 -44 150 -511 C
ATOM 84 CB BTYR A 14 -14.307 11.040 -9.459 0.40 7.67 C
ANISOU 84 CB BTYR A 14 354 1096 1466 468 -250 -103 C
ATOM 85 CG ATYR A 14 -13.255 11.996 -8.229 0.60 7.37 C
ANISOU 85 CG ATYR A 14 585 796 1419 310 -224 -46 C
ATOM 86 CG BTYR A 14 -13.535 12.233 -8.957 0.40 6.62 C
ANISOU 86 CG BTYR A 14 285 871 1360 662 -28 -202 C
ATOM 87 CD1ATYR A 14 -12.971 11.779 -6.888 0.60 9.67 C
ANISOU 87 CD1ATYR A 14 1493 760 1421 341 -277 -37 C
ATOM 88 CD1BTYR A 14 -12.916 12.150 -7.723 0.40 6.55 C
ANISOU 88 CD1BTYR A 14 340 736 1414 657 -110 -281 C
ATOM 89 CD2ATYR A 14 -12.824 13.210 -8.751 0.60 8.00 C
ANISOU 89 CD2ATYR A 14 927 712 1400 511 38 -101 C
ATOM 90 CD2BTYR A 14 -13.426 13.392 -9.705 0.40 8.91 C
ANISOU 90 CD2BTYR A 14 1030 671 1685 837 -362 -207 C
ATOM 91 CE1ATYR A 14 -12.272 12.708 -6.128 0.60 8.77 C
ANISOU 91 CE1ATYR A 14 1046 1118 1168 327 -117 -58 C
ATOM 92 CE1BTYR A 14 -12.197 13.221 -7.235 0.40 9.92 C
ANISOU 92 CE1BTYR A 14 1045 1093 1633 188 -227 -272 C
ATOM 93 CE2ATYR A 14 -12.128 14.147 -8.022 0.60 8.66 C
ANISOU 93 CE2ATYR A 14 1036 775 1481 102 327 -39 C
ATOM 94 CE2BTYR A 14 -12.716 14.465 -9.219 0.40 11.04 C
ANISOU 94 CE2BTYR A 14 1487 894 1813 390 -193 -204 C
ATOM 95 CZ ATYR A 14 -11.857 13.900 -6.697 0.60 8.84 C
ANISOU 95 CZ ATYR A 14 866 919 1573 363 45 -263 C
ATOM 96 CZ BTYR A 14 -12.106 14.368 -7.988 0.40 9.15 C
ANISOU 96 CZ BTYR A 14 946 1114 1419 37 300 -366 C
ATOM 97 OH ATYR A 14 -11.160 14.824 -5.954 0.60 12.62 O
ANISOU 97 OH ATYR A 14 1415 1334 2045 113 -106 -522 O
ATOM 98 OH BTYR A 14 -11.406 15.450 -7.519 0.40 11.27 O
ANISOU 98 OH BTYR A 14 1066 1036 2179 178 133 -621 O
ATOM 99 N VAL A 15 -14.533 7.859 -9.646 1.00 7.32 N
ANISOU 99 N VAL A 15 763 863 1156 -71 198 1 N
ATOM 100 CA VAL A 15 -15.546 6.903 -10.042 1.00 6.96 C
ANISOU 100 CA VAL A 15 713 945 984 31 59 45 C
ATOM 101 C VAL A 15 -16.400 6.661 -8.795 1.00 6.94 C
ANISOU 101 C VAL A 15 819 785 1034 -182 73 42 C
ATOM 102 O VAL A 15 -15.912 6.544 -7.665 1.00 7.95 O
ANISOU 102 O VAL A 15 849 1247 925 -218 78 -180 O
ATOM 103 CB VAL A 15 -14.891 5.639 -10.621 1.00 8.87 C
ANISOU 103 CB VAL A 15 1107 929 1334 69 92 -97 C
ATOM 104 CG1 VAL A 15 -14.024 4.923 -9.580 1.00 9.51 C
ANISOU 104 CG1 VAL A 15 886 1072 1654 267 129 -59 C
ATOM 105 CG2 VAL A 15 -15.952 4.720 -11.154 1.00 13.60 C
ANISOU 105 CG2 VAL A 15 1280 1327 2561 210 -414 -692 C
ATOM 106 N GLU A 16 -17.692 6.536 -9.010 1.00 7.77 N
ANISOU 106 N GLU A 16 767 1175 1011 218 87 186 N
ATOM 107 CA AGLU A 16 -18.706 6.238 -8.018 0.50 7.94 C
ANISOU 107 CA AGLU A 16 736 1039 1242 71 138 169 C
ATOM 108 CA BGLU A 16 -18.565 6.229 -7.892 0.50 7.53 C
ANISOU 108 CA BGLU A 16 688 1083 1090 -8 10 189 C
ATOM 109 C GLU A 16 -18.828 4.725 -7.799 1.00 7.03 C
ANISOU 109 C GLU A 16 666 981 1022 262 214 -25 C
ATOM 110 O GLU A 16 -19.283 4.035 -8.716 1.00 9.83 O
ANISOU 110 O GLU A 16 1269 1381 1084 -427 -3 45 O
ATOM 111 CB AGLU A 16 -20.079 6.787 -8.446 0.50 9.76 C
ANISOU 111 CB AGLU A 16 909 1116 1682 499 226 -18 C
ATOM 112 CB BGLU A 16 -19.873 7.018 -8.008 0.50 9.56 C
ANISOU 112 CB BGLU A 16 1125 1066 1441 400 466 228 C
ATOM 113 CG AGLU A 16 -20.212 8.287 -8.558 0.50 10.26 C
ANISOU 113 CG AGLU A 16 1468 1078 1350 305 67 220 C
ATOM 114 CG BGLU A 16 -20.638 6.964 -6.706 0.50 12.99 C
ANISOU 114 CG BGLU A 16 1317 1632 1986 -402 1024 -16 C
ATOM 115 CD AGLU A 16 -20.055 9.119 -7.307 0.50 13.11 C
ANISOU 115 CD AGLU A 16 1537 1533 1913 -342 928 -440 C
ATOM 116 CD BGLU A 16 -21.701 8.006 -6.515 0.50 14.18 C
ANISOU 116 CD BGLU A 16 1051 2114 2224 -358 1062 -418 C
ATOM 117 OE1AGLU A 16 -20.336 8.601 -6.208 0.50 11.26 O
ANISOU 117 OE1AGLU A 16 715 2028 1533 98 467 -400 O
ATOM 118 OE1BGLU A 16 -22.779 7.563 -6.083 0.50 25.13 O
ANISOU 118 OE1BGLU A 16 1366 4597 3586 -1090 1953 -1250 O
ATOM 119 OE2AGLU A 16 -19.677 10.308 -7.454 0.50 17.05 O
ANISOU 119 OE2AGLU A 16 1780 1564 3136 -524 1435 -753 O
ATOM 120 OE2BGLU A 16 -21.499 9.226 -6.730 0.50 19.97 O
ANISOU 120 OE2BGLU A 16 2017 1832 3740 -55 -346 -434 O
ATOM 121 N VAL A 17 -18.486 4.252 -6.609 1.00 5.94 N
ANISOU 121 N VAL A 17 483 861 914 150 278 -95 N
ATOM 122 CA AVAL A 17 -18.445 2.852 -6.250 0.50 8.49 C
ANISOU 122 CA AVAL A 17 1064 975 1187 255 383 77 C
ATOM 123 CA BVAL A 17 -18.698 2.822 -6.373 0.50 7.85 C
ANISOU 123 CA BVAL A 17 871 997 1116 58 120 73 C
ATOM 124 C VAL A 17 -19.200 2.678 -4.942 1.00 7.73 C
ANISOU 124 C VAL A 17 986 816 1135 4 274 -16 C
ATOM 125 O VAL A 17 -18.805 3.335 -3.991 1.00 7.43 O
ANISOU 125 O VAL A 17 534 995 1292 -29 388 -261 O
ATOM 126 CB AVAL A 17 -16.925 2.561 -6.243 0.50 10.40 C
ANISOU 126 CB AVAL A 17 1210 1399 1343 815 377 -77 C
ATOM 127 CB BVAL A 17 -17.464 1.919 -6.549 0.50 6.72 C
ANISOU 127 CB BVAL A 17 848 476 1231 -183 346 40 C
ATOM 128 CG1AVAL A 17 -16.530 1.487 -5.277 0.50 11.15 C
ANISOU 128 CG1AVAL A 17 1273 1124 1841 135 -164 93 C
ATOM 129 CG1BVAL A 17 -17.112 1.819 -8.017 0.50 8.42 C
ANISOU 129 CG1BVAL A 17 674 1509 1016 19 -242 -389 C
ATOM 130 CG2AVAL A 17 -16.492 2.235 -7.676 0.50 13.10 C
ANISOU 130 CG2AVAL A 17 1562 2040 1375 1756 -36 -500 C
ATOM 131 CG2BVAL A 17 -16.358 2.531 -5.690 0.50 5.29 C
ANISOU 131 CG2BVAL A 17 962 794 252 178 130 434 C
ATOM 132 N LEU A 18 -20.227 1.825 -4.859 1.00 7.43 N
ANISOU 132 N LEU A 18 745 1013 1066 54 114 -100 N
ATOM 133 CA LEU A 18 -20.824 1.547 -3.540 1.00 7.79 C
ANISOU 133 CA LEU A 18 644 1169 1148 8 231 -60 C
ATOM 134 C LEU A 18 -21.218 2.822 -2.804 1.00 7.56 C
ANISOU 134 C LEU A 18 607 1096 1168 -191 267 -112 C
ATOM 135 O LEU A 18 -20.960 2.978 -1.617 1.00 8.80 O
ANISOU 135 O LEU A 18 743 1510 1093 -200 372 -144 O
ATOM 136 CB LEU A 18 -19.898 0.647 -2.722 1.00 6.95 C
ANISOU 136 CB LEU A 18 386 1331 925 -112 219 -97 C
ATOM 137 CG LEU A 18 -19.388 -0.631 -3.405 1.00 7.70 C
ANISOU 137 CG LEU A 18 613 1191 1121 -42 228 -85 C
ATOM 138 CD1 LEU A 18 -18.432 -1.389 -2.474 1.00 9.16 C
ANISOU 138 CD1 LEU A 18 943 1219 1319 5 -9 -116 C
ATOM 139 CD2 LEU A 18 -20.496 -1.544 -3.833 1.00 12.64 C
ANISOU 139 CD2 LEU A 18 1285 1222 2294 -150 -596 -179 C
ATOM 140 N GLY A 19 -21.836 3.734 -3.576 1.00 7.87 N
ANISOU 140 N GLY A 19 342 1251 1396 94 233 -269 N
ATOM 141 CA GLY A 19 -22.348 4.964 -3.048 1.00 8.09 C
ANISOU 141 CA GLY A 19 416 1418 1238 137 222 -424 C
ATOM 142 C GLY A 19 -21.390 6.097 -2.791 1.00 7.65 C
ANISOU 142 C GLY A 19 466 1199 1239 219 91 -266 C
ATOM 143 O GLY A 19 -21.776 7.146 -2.259 1.00 9.50 O
ANISOU 143 O GLY A 19 808 1220 1581 289 204 -340 O
ATOM 144 N GLU A 20 -20.113 5.901 -3.103 1.00 7.33 N
ANISOU 144 N GLU A 20 518 973 1295 1 164 -193 N
ATOM 145 CA GLU A 20 -19.049 6.777 -2.673 1.00 6.73 C
ANISOU 145 CA GLU A 20 580 897 1080 16 71 -37 C
ATOM 146 C GLU A 20 -18.066 6.980 -3.816 1.00 6.70 C
ANISOU 146 C GLU A 20 375 1053 1119 98 64 -121 C
ATOM 147 O GLU A 20 -17.815 6.116 -4.623 1.00 9.46 O
ANISOU 147 O GLU A 20 907 1094 1592 -31 487 -233 O
ATOM 148 CB GLU A 20 -18.307 6.186 -1.459 1.00 8.75 C
ANISOU 148 CB GLU A 20 671 1367 1288 217 28 147 C
ATOM 149 CG GLU A 20 -19.242 5.800 -0.306 1.00 9.47 C
ANISOU 149 CG GLU A 20 1247 1382 970 -176 4 9 C
ATOM 150 CD GLU A 20 -19.873 6.943 0.430 1.00 10.56 C
ANISOU 150 CD GLU A 20 1151 1633 1227 -228 150 -194 C
ATOM 151 OE1 GLU A 20 -19.262 8.043 0.490 1.00 12.14 O
ANISOU 151 OE1 GLU A 20 1126 1620 1867 -225 326 -449 O
ATOM 152 OE2 GLU A 20 -20.977 6.782 0.995 1.00 12.01 O
ANISOU 152 OE2 GLU A 20 1067 1733 1764 -214 191 -194 O
ATOM 153 N ARG A 21 -17.476 8.143 -3.846 1.00 7.67 N
ANISOU 153 N ARG A 21 707 1198 1007 -119 78 16 N
ATOM 154 CA ARG A 21 -16.504 8.465 -4.876 1.00 9.00 C
ANISOU 154 CA ARG A 21 975 1218 1227 -213 292 -124 C
ATOM 155 C ARG A 21 -15.112 8.026 -4.478 1.00 8.52 C
ANISOU 155 C ARG A 21 876 1410 949 -306 412 -121 C
ATOM 156 O ARG A 21 -14.677 8.328 -3.345 1.00 10.86 O
ANISOU 156 O ARG A 21 840 2135 1152 -67 350 -512 O
ATOM 157 CB AARG A 21 -16.405 9.981 -5.008 0.45 12.62 C
ANISOU 157 CB AARG A 21 1988 1268 1539 -259 280 340 C
ATOM 158 CB BARG A 21 -16.527 9.967 -5.180 0.20 11.77 C
ANISOU 158 CB BARG A 21 1628 1302 1542 -224 416 185 C
ATOM 159 CB CARG A 21 -16.568 9.967 -5.173 0.35 11.74 C
ANISOU 159 CB CARG A 21 1562 1274 1624 -228 451 140 C
ATOM 160 CG AARG A 21 -17.419 10.714 -5.846 0.45 11.84 C
ANISOU 160 CG AARG A 21 1520 1432 1545 123 640 78 C
ATOM 161 CG BARG A 21 -17.921 10.561 -5.284 0.20 11.83 C
ANISOU 161 CG BARG A 21 1735 1046 1714 -169 439 330 C
ATOM 162 CG CARG A 21 -16.060 10.423 -6.529 0.35 8.29 C
ANISOU 162 CG CARG A 21 239 1256 1655 182 369 139 C
ATOM 163 CD AARG A 21 -16.766 11.970 -6.416 0.45 12.82 C
ANISOU 163 CD AARG A 21 1932 1269 1669 -178 -394 269 C
ATOM 164 CD BARG A 21 -17.857 12.018 -5.723 0.20 13.30 C
ANISOU 164 CD BARG A 21 2214 1123 1717 -290 272 436 C
ATOM 165 CD CARG A 21 -16.076 11.940 -6.631 0.35 11.80 C
ANISOU 165 CD CARG A 21 1573 1281 1628 62 126 313 C
ATOM 166 NE AARG A 21 -15.945 12.689 -5.442 0.45 14.69 N
ANISOU 166 NE AARG A 21 2739 856 1986 387 -1136 179 N
ATOM 167 NE BARG A 21 -17.508 12.916 -4.633 0.20 18.94 N
ANISOU 167 NE BARG A 21 3142 1474 2579 -783 927 -355 N
ATOM 168 NE CARG A 21 -16.673 12.405 -7.881 0.35 18.59 N
ANISOU 168 NE CARG A 21 3253 1662 2147 -469 -698 773 N
ATOM 169 CZ AARG A 21 -15.463 13.910 -5.610 0.45 8.93 C
ANISOU 169 CZ AARG A 21 566 872 1957 764 -268 -249 C
ATOM 170 CZ BARG A 21 -18.172 13.054 -3.492 0.20 13.17 C
ANISOU 170 CZ BARG A 21 2855 -125 2276 834 495 312 C
ATOM 171 CZ CARG A 21 -16.623 13.670 -8.287 0.35 17.92 C
ANISOU 171 CZ CARG A 21 3315 1775 1718 -1071 -482 867 C
ATOM 172 NH1AARG A 21 -15.708 14.551 -6.726 0.45 7.59 N
ANISOU 172 NH1AARG A 21 692 627 1565 318 365 -365 N
ATOM 173 NH1BARG A 21 -19.263 12.327 -3.266 0.20 8.03 N
ANISOU 173 NH1BARG A 21 1313 1030 708 1366 -83 -308 N
ATOM 174 NH1CARG A 21 -16.000 14.572 -7.537 0.35 23.19 N
ANISOU 174 NH1CARG A 21 4597 1633 2582 -66 -1373 -20 N
ATOM 175 NH2AARG A 21 -14.731 14.500 -4.677 0.45 13.35 N
ANISOU 175 NH2AARG A 21 1438 1179 2457 923 -732 -720 N
ATOM 176 NH2BARG A 21 -17.727 13.919 -2.590 0.20 12.75 N
ANISOU 176 NH2BARG A 21 2042 520 2283 724 326 242 N
ATOM 177 NH2CARG A 21 -17.189 14.025 -9.433 0.35 15.89 N
ANISOU 177 NH2CARG A 21 1612 1573 2853 -363 -984 852 N
ATOM 178 N MET A 22 -14.421 7.354 -5.376 1.00 8.22 N
ANISOU 178 N MET A 22 837 1262 1024 -179 260 -111 N
ATOM 179 CA MET A 22 -12.999 7.091 -5.177 1.00 7.59 C
ANISOU 179 CA MET A 22 792 1153 940 -260 206 -106 C
ATOM 180 C MET A 22 -12.231 7.930 -6.192 1.00 6.96 C
ANISOU 180 C MET A 22 672 993 981 -38 36 110 C
ATOM 181 O MET A 22 -12.549 7.992 -7.377 1.00 8.47 O
ANISOU 181 O MET A 22 1043 1324 850 -280 157 -176 O
ATOM 182 CB MET A 22 -12.704 5.597 -5.362 1.00 7.37 C
ANISOU 182 CB MET A 22 661 1108 1031 -326 70 46 C
ATOM 183 CG MET A 22 -13.264 4.787 -4.190 1.00 9.32 C
ANISOU 183 CG MET A 22 1264 1165 1111 -341 457 -39 C
ATOM 184 SD MET A 22 -12.995 3.002 -4.334 1.00 10.25 S
ANISOU 184 SD MET A 22 1432 1108 1356 -418 233 -23 S
ATOM 185 CE MET A 22 -11.246 2.938 -4.059 1.00 11.38 C
ANISOU 185 CE MET A 22 1581 1240 1504 -185 -315 77 C
ATOM 186 N HIS A 23 -11.185 8.577 -5.667 1.00 5.66 N
ANISOU 186 N HIS A 23 632 637 881 56 202 4 N
ATOM 187 CA HIS A 23 -10.242 9.285 -6.519 1.00 5.54 C
ANISOU 187 CA HIS A 23 693 691 721 64 274 -66 C
ATOM 188 C HIS A 23 -9.126 8.371 -7.001 1.00 5.59 C
ANISOU 188 C HIS A 23 725 710 689 178 157 7 C
ATOM 189 O HIS A 23 -8.702 7.454 -6.274 1.00 6.42 O
ANISOU 189 O HIS A 23 734 843 862 69 164 211 O
ATOM 190 CB HIS A 23 -9.605 10.435 -5.745 1.00 5.49 C
ANISOU 190 CB HIS A 23 614 745 726 81 224 -29 C
ATOM 191 CG HIS A 23 -8.452 11.057 -6.419 1.00 5.71 C
ANISOU 191 CG HIS A 23 712 710 746 16 111 -6 C
ATOM 192 ND1 HIS A 23 -7.143 10.781 -6.043 1.00 6.54 N
ANISOU 192 ND1 HIS A 23 591 913 981 -19 190 9 N
ATOM 193 CD2 HIS A 23 -8.389 11.942 -7.437 1.00 5.83 C
ANISOU 193 CD2 HIS A 23 781 760 674 -97 207 -44 C
ATOM 194 CE1 HIS A 23 -6.361 11.493 -6.838 1.00 7.22 C
ANISOU 194 CE1 HIS A 23 782 1104 856 33 267 96 C
ATOM 195 NE2 HIS A 23 -7.084 12.229 -7.727 1.00 7.16 N
ANISOU 195 NE2 HIS A 23 714 1152 854 -84 139 50 N
ATOM 196 N TYR A 24 -8.636 8.617 -8.210 1.00 5.05 N
ANISOU 196 N TYR A 24 553 579 787 162 201 67 N
ATOM 197 CA TYR A 24 -7.528 7.862 -8.748 1.00 4.83 C
ANISOU 197 CA TYR A 24 354 632 848 145 72 -15 C
ATOM 198 C TYR A 24 -6.724 8.681 -9.765 1.00 5.18 C
ANISOU 198 C TYR A 24 611 609 748 218 202 -32 C
ATOM 199 O TYR A 24 -7.298 9.496 -10.463 1.00 5.64 O
ANISOU 199 O TYR A 24 680 686 777 211 69 -16 O
ATOM 200 CB TYR A 24 -7.972 6.532 -9.343 1.00 5.57 C
ANISOU 200 CB TYR A 24 706 689 721 70 148 -55 C
ATOM 201 CG TYR A 24 -8.929 6.608 -10.521 1.00 5.06 C
ANISOU 201 CG TYR A 24 574 587 762 -94 146 41 C
ATOM 202 CD1 TYR A 24 -10.261 6.925 -10.329 1.00 5.25 C
ANISOU 202 CD1 TYR A 24 681 480 833 92 168 28 C
ATOM 203 CD2 TYR A 24 -8.470 6.352 -11.803 1.00 4.82 C
ANISOU 203 CD2 TYR A 24 647 442 743 132 124 135 C
ATOM 204 CE1 TYR A 24 -11.096 6.991 -11.406 1.00 6.47 C
ANISOU 204 CE1 TYR A 24 713 788 958 101 73 52 C
ATOM 205 CE2 TYR A 24 -9.302 6.399 -12.891 1.00 5.24 C
ANISOU 205 CE2 TYR A 24 839 495 658 134 96 111 C
ATOM 206 CZ TYR A 24 -10.631 6.723 -12.680 1.00 7.08 C
ANISOU 206 CZ TYR A 24 868 920 902 357 -76 -14 C
ATOM 207 OH TYR A 24 -11.508 6.796 -13.721 1.00 8.88 O
ANISOU 207 OH TYR A 24 860 1445 1070 130 -140 -82 O
ATOM 208 N VAL A 25 -5.440 8.398 -9.807 1.00 4.58 N
ANISOU 208 N VAL A 25 542 530 669 17 89 121 N
ATOM 209 CA VAL A 25 -4.569 8.772 -10.910 1.00 4.27 C
ANISOU 209 CA VAL A 25 620 415 586 188 183 68 C
ATOM 210 C VAL A 25 -4.835 7.855 -12.083 1.00 4.63 C
ANISOU 210 C VAL A 25 648 426 687 249 75 64 C
ATOM 211 O VAL A 25 -4.981 6.639 -11.873 1.00 5.05 O
ANISOU 211 O VAL A 25 734 429 754 109 83 69 O
ATOM 212 CB VAL A 25 -3.087 8.652 -10.484 1.00 5.78 C
ANISOU 212 CB VAL A 25 563 651 982 94 192 -125 C
ATOM 213 CG1 VAL A 25 -2.174 8.967 -11.652 1.00 5.86 C
ANISOU 213 CG1 VAL A 25 561 722 942 183 122 32 C
ATOM 214 CG2 VAL A 25 -2.823 9.564 -9.296 1.00 6.72 C
ANISOU 214 CG2 VAL A 25 931 711 911 -4 34 -33 C
ATOM 215 N ASP A 26 -4.860 8.409 -13.284 1.00 5.01 N
ANISOU 215 N ASP A 26 687 570 647 243 88 81 N
ATOM 216 CA ASP A 26 -4.985 7.583 -14.501 1.00 5.74 C
ANISOU 216 CA ASP A 26 672 849 662 212 17 26 C
ATOM 217 C ASP A 26 -4.234 8.277 -15.609 1.00 5.62 C
ANISOU 217 C ASP A 26 919 560 655 195 100 -70 C
ATOM 218 O ASP A 26 -4.741 9.274 -16.140 1.00 6.72 O
ANISOU 218 O ASP A 26 946 598 1010 237 165 46 O
ATOM 219 CB ASP A 26 -6.427 7.384 -14.873 1.00 6.67 C
ANISOU 219 CB ASP A 26 693 1171 672 311 -1 -131 C
ATOM 220 CG ASP A 26 -6.652 6.342 -15.937 1.00 6.06 C
ANISOU 220 CG ASP A 26 890 636 776 116 51 48 C
ATOM 221 OD1 ASP A 26 -5.682 5.823 -16.512 1.00 7.04 O
ANISOU 221 OD1 ASP A 26 1016 819 841 265 127 -66 O
ATOM 222 OD2 ASP A 26 -7.827 6.029 -16.196 1.00 9.75 O
ANISOU 222 OD2 ASP A 26 922 1220 1562 254 -169 -450 O
ATOM 223 N VAL A 27 -3.038 7.792 -15.928 1.00 5.79 N
ANISOU 223 N VAL A 27 821 617 762 121 98 79 N
ATOM 224 CA VAL A 27 -2.203 8.368 -16.959 1.00 5.98 C
ANISOU 224 CA VAL A 27 830 658 784 159 129 83 C
ATOM 225 C VAL A 27 -1.683 7.252 -17.855 1.00 6.40 C
ANISOU 225 C VAL A 27 1017 577 838 24 192 35 C
ATOM 226 O VAL A 27 -1.730 6.086 -17.486 1.00 7.06 O
ANISOU 226 O VAL A 27 1137 629 917 97 290 95 O
ATOM 227 CB VAL A 27 -1.027 9.168 -16.399 1.00 5.85 C
ANISOU 227 CB VAL A 27 811 652 761 120 242 -33 C
ATOM 228 CG1 VAL A 27 -1.539 10.408 -15.677 1.00 6.91 C
ANISOU 228 CG1 VAL A 27 966 795 863 247 181 -75 C
ATOM 229 CG2 VAL A 27 -0.171 8.311 -15.495 1.00 6.90 C
ANISOU 229 CG2 VAL A 27 671 836 1115 149 131 -40 C
ATOM 230 N GLY A 28 -1.218 7.604 -19.033 1.00 6.89 N
ANISOU 230 N GLY A 28 1247 544 828 181 267 134 N
ATOM 231 CA GLY A 28 -0.608 6.650 -19.945 1.00 7.15 C
ANISOU 231 CA GLY A 28 1098 572 1045 -87 338 -54 C
ATOM 232 C GLY A 28 -1.556 6.078 -20.965 1.00 7.76 C
ANISOU 232 C GLY A 28 1140 821 986 -266 392 1 C
ATOM 233 O GLY A 28 -2.779 6.339 -20.931 1.00 9.16 O
ANISOU 233 O GLY A 28 1245 878 1356 79 58 -129 O
ATOM 234 N PRO A 29 -1.020 5.292 -21.882 1.00 7.87 N
ANISOU 234 N PRO A 29 1407 743 839 93 66 68 N
ATOM 235 CA PRO A 29 -1.817 4.762 -22.985 1.00 9.74 C
ANISOU 235 CA PRO A 29 1909 744 1048 -188 -63 -11 C
ATOM 236 C PRO A 29 -2.906 3.795 -22.525 1.00 8.80 C
ANISOU 236 C PRO A 29 1535 638 1171 86 76 -81 C
ATOM 237 O PRO A 29 -2.730 3.100 -21.557 1.00 10.30 O
ANISOU 237 O PRO A 29 1768 1057 1088 -187 178 22 O
ATOM 238 CB PRO A 29 -0.771 3.989 -23.795 1.00 10.10 C
ANISOU 238 CB PRO A 29 2106 927 804 -391 349 83 C
ATOM 239 CG PRO A 29 0.289 3.654 -22.829 1.00 9.94 C
ANISOU 239 CG PRO A 29 1866 1062 850 -61 473 -317 C
ATOM 240 CD PRO A 29 0.384 4.876 -21.942 1.00 8.42 C
ANISOU 240 CD PRO A 29 1449 716 1034 -32 396 -126 C
ATOM 241 N ARG A 30 -4.003 3.758 -23.294 1.00 11.63 N
ANISOU 241 N ARG A 30 1487 1171 1761 262 -107 -120 N
ATOM 242 CA BARG A 30 -5.111 2.893 -22.896 0.40 13.19 C
ANISOU 242 CA BARG A 30 1537 1313 2163 80 -270 -101 C
ATOM 243 CA CARG A 30 -5.202 2.989 -23.076 0.30 13.75 C
ANISOU 243 CA CARG A 30 1540 1410 2275 96 -296 -176 C
ATOM 244 CA DARG A 30 -5.177 2.959 -22.992 0.30 13.56 C
ANISOU 244 CA DARG A 30 1528 1359 2266 100 -267 -137 C
ATOM 245 C ARG A 30 -5.242 1.586 -23.661 1.00 13.97 C
ANISOU 245 C ARG A 30 1631 1494 2181 -2 -471 -213 C
ATOM 246 O ARG A 30 -6.201 0.841 -23.397 1.00 16.06 O
ANISOU 246 O ARG A 30 1827 1719 2555 -314 -641 -64 O
ATOM 247 CB BARG A 30 -6.454 3.616 -23.075 0.40 17.45 C
ANISOU 247 CB BARG A 30 1421 2304 2904 299 -381 -921 C
ATOM 248 CB CARG A 30 -6.365 3.747 -23.770 0.30 17.95 C
ANISOU 248 CB CARG A 30 1663 2190 2967 693 -654 -831 C
ATOM 249 CB DARG A 30 -6.455 3.700 -23.436 0.30 16.39 C
ANISOU 249 CB DARG A 30 1562 1820 2844 228 -575 -457 C
ATOM 250 CG BARG A 30 -6.547 4.903 -22.275 0.40 14.99 C
ANISOU 250 CG BARG A 30 1243 2032 2420 210 31 -559 C
ATOM 251 CG CARG A 30 -7.369 4.308 -22.774 0.30 18.57 C
ANISOU 251 CG CARG A 30 1684 2531 2842 523 -659 -1040 C
ATOM 252 CG DARG A 30 -6.337 5.207 -23.580 0.30 14.94 C
ANISOU 252 CG DARG A 30 1396 1713 2568 577 -661 -603 C
ATOM 253 CD BARG A 30 -6.934 4.552 -20.843 0.40 14.86 C
ANISOU 253 CD BARG A 30 2016 1407 2224 260 -644 -102 C
ATOM 254 CD CARG A 30 -6.886 5.606 -22.175 0.30 16.89 C
ANISOU 254 CD CARG A 30 1622 2172 2624 796 -955 -698 C
ATOM 255 CD DARG A 30 -7.104 5.944 -22.498 0.30 17.32 C
ANISOU 255 CD DARG A 30 1422 2485 2672 649 -668 -897 C
ATOM 256 NE BARG A 30 -7.241 5.734 -20.061 0.40 12.02 N
ANISOU 256 NE BARG A 30 1373 1410 1783 -193 -257 42 N
ATOM 257 NE CARG A 30 -5.719 5.482 -21.297 0.30 11.89 N
ANISOU 257 NE CARG A 30 1386 1122 2011 421 -542 197 N
ATOM 258 NE DARG A 30 -6.923 5.387 -21.152 0.30 20.35 N
ANISOU 258 NE DARG A 30 2607 2583 2542 -162 -559 -853 N
ATOM 259 CZ BARG A 30 -8.489 6.164 -19.901 0.40 15.22 C
ANISOU 259 CZ BARG A 30 1553 1948 2282 246 -801 -485 C
ATOM 260 CZ CARG A 30 -5.821 5.773 -19.998 0.30 11.41 C
ANISOU 260 CZ CARG A 30 1710 648 1976 94 -404 352 C
ATOM 261 CZ DARG A 30 -7.183 6.104 -20.061 0.30 17.88 C
ANISOU 261 CZ DARG A 30 2056 2094 2643 32 -647 -742 C
ATOM 262 NH1BARG A 30 -9.520 5.518 -20.451 0.40 10.66 N
ANISOU 262 NH1BARG A 30 1400 1619 1031 109 -721 582 N
ATOM 263 NH1CARG A 30 -6.996 6.164 -19.524 0.30 13.43 N
ANISOU 263 NH1CARG A 30 1646 1773 1683 589 -1020 -449 N
ATOM 264 NH1DARG A 30 -7.022 5.606 -18.848 0.30 14.66 N
ANISOU 264 NH1DARG A 30 1686 1290 2593 151 -195 -861 N
ATOM 265 NH2BARG A 30 -8.619 7.258 -19.167 0.40 12.46 N
ANISOU 265 NH2BARG A 30 2258 1333 1143 384 -548 358 N
ATOM 266 NH2CARG A 30 -4.776 5.672 -19.192 0.30 14.41 N
ANISOU 266 NH2CARG A 30 555 3251 1668 -952 262 -424 N
ATOM 267 NH2DARG A 30 -7.618 7.350 -20.198 0.30 21.08 N
ANISOU 267 NH2DARG A 30 3101 2162 2748 175 -1215 -511 N
ATOM 268 N ASP A 31 -4.288 1.300 -24.518 1.00 12.63 N
ANISOU 268 N ASP A 31 1991 1276 1530 359 -595 149 N
ATOM 269 CA ASP A 31 -4.507 0.086 -25.313 1.00 13.67 C
ANISOU 269 CA ASP A 31 2397 1310 1487 260 -617 130 C
ATOM 270 C ASP A 31 -3.723 -1.124 -24.876 1.00 13.09 C
ANISOU 270 C ASP A 31 2209 1259 1506 271 -553 -62 C
ATOM 271 O ASP A 31 -3.548 -2.068 -25.661 1.00 20.85 O
ANISOU 271 O ASP A 31 4475 1788 1658 1186 -1035 -384 O
ATOM 272 CB ASP A 31 -4.198 0.525 -26.755 1.00 14.12 C
ANISOU 272 CB ASP A 31 2240 1480 1645 620 -124 128 C
ATOM 273 CG ASP A 31 -2.758 0.998 -26.892 1.00 17.80 C
ANISOU 273 CG ASP A 31 2446 1930 2389 316 118 -133 C
ATOM 274 OD1 ASP A 31 -2.127 1.427 -25.886 1.00 21.77 O
ANISOU 274 OD1 ASP A 31 3016 2703 2551 -1020 247 -97 O
ATOM 275 OD2 ASP A 31 -2.267 0.885 -28.041 1.00 26.59 O
ANISOU 275 OD2 ASP A 31 2899 5149 2056 -714 152 576 O
ATOM 276 N GLY A 32 -3.245 -1.188 -23.652 1.00 9.37 N
ANISOU 276 N GLY A 32 1433 965 1161 177 77 147 N
ATOM 277 CA GLY A 32 -2.411 -2.267 -23.196 1.00 9.34 C
ANISOU 277 CA GLY A 32 1673 995 883 200 104 48 C
ATOM 278 C GLY A 32 -2.835 -2.789 -21.848 1.00 7.89 C
ANISOU 278 C GLY A 32 1275 839 883 363 207 -52 C
ATOM 279 O GLY A 32 -3.991 -2.722 -21.452 1.00 8.40 O
ANISOU 279 O GLY A 32 1034 1166 991 154 -81 -11 O
ATOM 280 N THR A 33 -1.874 -3.339 -21.111 1.00 7.10 N
ANISOU 280 N THR A 33 929 981 787 17 146 -52 N
ATOM 281 CA THR A 33 -2.118 -3.876 -19.780 1.00 6.57 C
ANISOU 281 CA THR A 33 908 774 814 100 210 -83 C
ATOM 282 C THR A 33 -1.761 -2.790 -18.791 1.00 5.71 C
ANISOU 282 C THR A 33 761 592 818 105 169 18 C
ATOM 283 O THR A 33 -0.617 -2.300 -18.759 1.00 7.54 O
ANISOU 283 O THR A 33 816 1007 1042 -28 250 -145 O
ATOM 284 CB THR A 33 -1.268 -5.125 -19.524 1.00 7.94 C
ANISOU 284 CB THR A 33 1260 599 1156 99 208 -50 C
ATOM 285 OG1 THR A 33 -1.661 -6.122 -20.463 1.00 10.85 O
ANISOU 285 OG1 THR A 33 1985 874 1262 373 127 -344 O
ATOM 286 CG2 THR A 33 -1.504 -5.668 -18.128 1.00 7.91 C
ANISOU 286 CG2 THR A 33 998 907 1100 309 134 18 C
ATOM 287 N PRO A 34 -2.706 -2.367 -17.961 1.00 5.46 N
ANISOU 287 N PRO A 34 706 668 700 -31 131 -12 N
ATOM 288 CA PRO A 34 -2.422 -1.322 -17.003 1.00 5.46 C
ANISOU 288 CA PRO A 34 816 573 685 70 83 29 C
ATOM 289 C PRO A 34 -1.647 -1.803 -15.772 1.00 4.95 C
ANISOU 289 C PRO A 34 732 513 634 43 164 16 C
ATOM 290 O PRO A 34 -1.678 -2.994 -15.438 1.00 5.38 O
ANISOU 290 O PRO A 34 840 397 807 31 101 -17 O
ATOM 291 CB PRO A 34 -3.822 -0.858 -16.575 1.00 7.21 C
ANISOU 291 CB PRO A 34 984 1026 729 379 64 0 C
ATOM 292 CG PRO A 34 -4.693 -2.055 -16.733 1.00 9.84 C
ANISOU 292 CG PRO A 34 775 1486 1477 132 364 -211 C
ATOM 293 CD PRO A 34 -4.127 -2.827 -17.899 1.00 6.95 C
ANISOU 293 CD PRO A 34 736 1025 879 -120 67 47 C
ATOM 294 N VAL A 35 -0.987 -0.850 -15.148 1.00 4.59 N
ANISOU 294 N VAL A 35 785 317 643 162 94 51 N
ATOM 295 CA VAL A 35 -0.251 -1.056 -13.927 1.00 4.56 C
ANISOU 295 CA VAL A 35 732 496 505 125 183 81 C
ATOM 296 C VAL A 35 -1.049 -0.368 -12.814 1.00 4.75 C
ANISOU 296 C VAL A 35 684 430 689 -32 220 -81 C
ATOM 297 O VAL A 35 -1.269 0.851 -12.862 1.00 5.53 O
ANISOU 297 O VAL A 35 852 481 767 155 167 35 O
ATOM 298 CB VAL A 35 1.183 -0.536 -14.046 1.00 4.44 C
ANISOU 298 CB VAL A 35 657 300 730 276 156 -28 C
ATOM 299 CG1 VAL A 35 1.963 -0.837 -12.782 1.00 5.61 C
ANISOU 299 CG1 VAL A 35 816 602 713 130 31 -33 C
ATOM 300 CG2 VAL A 35 1.891 -1.126 -15.263 1.00 5.83 C
ANISOU 300 CG2 VAL A 35 797 661 757 112 230 -229 C
ATOM 301 N LEU A 36 -1.466 -1.179 -11.841 1.00 4.28 N
ANISOU 301 N LEU A 36 615 444 569 110 194 -45 N
ATOM 302 CA LEU A 36 -2.333 -0.740 -10.748 1.00 4.18 C
ANISOU 302 CA LEU A 36 526 483 579 133 136 -69 C
ATOM 303 C LEU A 36 -1.500 -0.619 -9.494 1.00 3.94 C
ANISOU 303 C LEU A 36 497 470 529 58 171 23 C
ATOM 304 O LEU A 36 -0.968 -1.627 -9.013 1.00 4.84 O
ANISOU 304 O LEU A 36 511 551 775 197 106 -51 O
ATOM 305 CB LEU A 36 -3.456 -1.760 -10.573 1.00 4.61 C
ANISOU 305 CB LEU A 36 661 435 655 16 140 -160 C
ATOM 306 CG LEU A 36 -4.455 -1.487 -9.457 1.00 4.58 C
ANISOU 306 CG LEU A 36 486 613 641 82 64 41 C
ATOM 307 CD1 LEU A 36 -5.241 -0.199 -9.683 1.00 6.59 C
ANISOU 307 CD1 LEU A 36 808 411 1285 88 169 -237 C
ATOM 308 CD2 LEU A 36 -5.426 -2.655 -9.284 1.00 5.82 C
ANISOU 308 CD2 LEU A 36 711 512 988 7 300 -114 C
ATOM 309 N PHE A 37 -1.404 0.579 -8.962 1.00 4.08 N
ANISOU 309 N PHE A 37 432 536 582 208 117 -125 N
ATOM 310 CA PHE A 37 -0.565 0.922 -7.817 1.00 4.19 C
ANISOU 310 CA PHE A 37 541 410 640 164 83 -7 C
ATOM 311 C PHE A 37 -1.427 1.027 -6.570 1.00 4.09 C
ANISOU 311 C PHE A 37 553 391 611 57 150 -54 C
ATOM 312 O PHE A 37 -2.369 1.837 -6.572 1.00 4.98 O
ANISOU 312 O PHE A 37 835 436 623 200 231 27 O
ATOM 313 CB PHE A 37 0.143 2.273 -8.012 1.00 4.41 C
ANISOU 313 CB PHE A 37 569 454 651 103 160 -98 C
ATOM 314 CG PHE A 37 1.141 2.303 -9.149 1.00 4.69 C
ANISOU 314 CG PHE A 37 679 446 655 5 261 -140 C
ATOM 315 CD1 PHE A 37 0.723 2.414 -10.463 1.00 4.29 C
ANISOU 315 CD1 PHE A 37 441 449 740 144 171 -22 C
ATOM 316 CD2 PHE A 37 2.501 2.209 -8.883 1.00 5.02 C
ANISOU 316 CD2 PHE A 37 614 648 647 -19 204 -104 C
ATOM 317 CE1 PHE A 37 1.628 2.448 -11.508 1.00 5.52 C
ANISOU 317 CE1 PHE A 37 805 679 615 143 241 -46 C
ATOM 318 CE2 PHE A 37 3.399 2.259 -9.957 1.00 5.55 C
ANISOU 318 CE2 PHE A 37 598 671 841 -18 291 -101 C
ATOM 319 CZ PHE A 37 2.983 2.387 -11.245 1.00 5.21 C
ANISOU 319 CZ PHE A 37 650 606 723 -39 440 -213 C
ATOM 320 N LEU A 38 -1.120 0.254 -5.529 1.00 4.09 N
ANISOU 320 N LEU A 38 385 580 589 207 135 -98 N
ATOM 321 CA LEU A 38 -1.960 0.208 -4.323 1.00 4.04 C
ANISOU 321 CA LEU A 38 542 407 586 183 199 -77 C
ATOM 322 C LEU A 38 -1.159 0.592 -3.093 1.00 3.84 C
ANISOU 322 C LEU A 38 502 412 544 56 192 71 C
ATOM 323 O LEU A 38 -0.237 -0.108 -2.691 1.00 4.86 O
ANISOU 323 O LEU A 38 503 647 695 194 157 -73 O
ATOM 324 CB LEU A 38 -2.587 -1.180 -4.156 1.00 4.62 C
ANISOU 324 CB LEU A 38 695 395 664 159 149 -185 C
ATOM 325 CG LEU A 38 -3.403 -1.725 -5.319 1.00 5.21 C
ANISOU 325 CG LEU A 38 693 620 666 4 49 10 C
ATOM 326 CD1 LEU A 38 -3.893 -3.134 -4.998 1.00 5.17 C
ANISOU 326 CD1 LEU A 38 508 520 937 42 244 -132 C
ATOM 327 CD2 LEU A 38 -4.564 -0.782 -5.628 1.00 5.43 C
ANISOU 327 CD2 LEU A 38 664 603 795 -21 114 78 C
ATOM 328 N HIS A 39 -1.499 1.759 -2.532 1.00 4.72 N
ANISOU 328 N HIS A 39 645 545 604 74 249 -121 N
ATOM 329 CA HIS A 39 -0.888 2.268 -1.307 1.00 4.87 C
ANISOU 329 CA HIS A 39 732 591 529 114 241 -62 C
ATOM 330 C HIS A 39 -1.471 1.581 -0.071 1.00 4.69 C
ANISOU 330 C HIS A 39 772 428 582 -25 174 -3 C
ATOM 331 O HIS A 39 -2.469 0.852 -0.157 1.00 5.34 O
ANISOU 331 O HIS A 39 748 499 781 -19 117 -112 O
ATOM 332 CB HIS A 39 -1.093 3.778 -1.191 1.00 4.44 C
ANISOU 332 CB HIS A 39 526 488 673 -73 242 72 C
ATOM 333 CG HIS A 39 -2.468 4.199 -0.851 1.00 4.32 C
ANISOU 333 CG HIS A 39 557 434 649 -23 175 10 C
ATOM 334 ND1 HIS A 39 -2.934 4.210 0.474 1.00 4.10 N
ANISOU 334 ND1 HIS A 39 536 310 711 119 215 -52 N
ATOM 335 CD2 HIS A 39 -3.528 4.554 -1.616 1.00 4.32 C
ANISOU 335 CD2 HIS A 39 464 438 740 -81 213 -69 C
ATOM 336 CE1 HIS A 39 -4.226 4.595 0.435 1.00 4.25 C
ANISOU 336 CE1 HIS A 39 536 382 696 20 99 -7 C
ATOM 337 NE2 HIS A 39 -4.627 4.824 -0.819 1.00 4.59 N
ANISOU 337 NE2 HIS A 39 605 524 614 142 177 13 N
ATOM 338 N GLY A 40 -0.856 1.861 1.088 1.00 4.63 N
ANISOU 338 N GLY A 40 651 555 553 14 300 -104 N
ATOM 339 CA GLY A 40 -1.315 1.375 2.365 1.00 4.53 C
ANISOU 339 CA GLY A 40 744 484 492 123 109 3 C
ATOM 340 C GLY A 40 -1.499 2.457 3.392 1.00 3.65 C
ANISOU 340 C GLY A 40 457 424 507 129 158 1 C
ATOM 341 O GLY A 40 -1.986 3.555 3.082 1.00 5.06 O
ANISOU 341 O GLY A 40 762 516 646 249 29 63 O
ATOM 342 N ASN A 41 -1.205 2.157 4.644 1.00 4.03 N
ANISOU 342 N ASN A 41 561 475 494 73 161 12 N
ATOM 343 CA ASN A 41 -1.516 3.056 5.764 1.00 4.04 C
ANISOU 343 CA ASN A 41 638 440 457 123 74 72 C
ATOM 344 C ASN A 41 -0.318 3.895 6.125 1.00 3.73 C
ANISOU 344 C ASN A 41 543 485 390 157 183 -19 C
ATOM 345 O ASN A 41 0.778 3.301 6.288 1.00 5.45 O
ANISOU 345 O ASN A 41 536 597 938 173 260 -70 O
ATOM 346 CB ASN A 41 -1.944 2.205 6.968 1.00 4.42 C
ANISOU 346 CB ASN A 41 720 509 448 97 56 133 C
ATOM 347 CG ASN A 41 -2.583 3.033 8.055 1.00 5.30 C
ANISOU 347 CG ASN A 41 872 475 666 24 316 176 C
ATOM 348 OD1 ASN A 41 -3.213 4.031 7.773 1.00 5.73 O
ANISOU 348 OD1 ASN A 41 938 557 684 120 237 84 O
ATOM 349 ND2 ASN A 41 -2.419 2.590 9.292 1.00 5.26 N
ANISOU 349 ND2 ASN A 41 796 632 569 176 138 -5 N
ATOM 350 N PRO A 42 -0.427 5.180 6.365 1.00 4.24 N
ANISOU 350 N PRO A 42 477 496 638 118 211 -119 N
ATOM 351 CA PRO A 42 -1.570 6.094 6.246 1.00 3.52 C
ANISOU 351 CA PRO A 42 355 450 531 73 363 -64 C
ATOM 352 C PRO A 42 -1.436 6.982 5.002 1.00 4.16 C
ANISOU 352 C PRO A 42 656 359 567 65 400 -109 C
ATOM 353 O PRO A 42 -1.561 8.196 5.070 1.00 5.07 O
ANISOU 353 O PRO A 42 866 406 654 98 265 -30 O
ATOM 354 CB PRO A 42 -1.376 6.938 7.486 1.00 4.62 C
ANISOU 354 CB PRO A 42 681 476 597 -2 413 -117 C
ATOM 355 CG PRO A 42 0.095 7.179 7.495 1.00 4.43 C
ANISOU 355 CG PRO A 42 642 500 542 14 263 -149 C
ATOM 356 CD PRO A 42 0.708 5.923 6.956 1.00 4.47 C
ANISOU 356 CD PRO A 42 582 490 627 136 46 -41 C
ATOM 357 N THR A 43 -1.130 6.364 3.880 1.00 3.83 N
ANISOU 357 N THR A 43 704 264 486 14 320 -24 N
ATOM 358 CA THR A 43 -0.727 7.086 2.687 1.00 4.05 C
ANISOU 358 CA THR A 43 596 422 522 -25 298 -82 C
ATOM 359 C THR A 43 -1.844 7.201 1.669 1.00 4.95 C
ANISOU 359 C THR A 43 734 510 639 43 186 93 C
ATOM 360 O THR A 43 -3.027 7.115 2.025 1.00 4.93 O
ANISOU 360 O THR A 43 641 525 709 84 250 7 O
ATOM 361 CB THR A 43 0.579 6.444 2.137 1.00 4.47 C
ANISOU 361 CB THR A 43 601 588 508 1 311 -85 C
ATOM 362 OG1 THR A 43 0.227 5.129 1.692 1.00 4.97 O
ANISOU 362 OG1 THR A 43 675 425 789 101 178 -122 O
ATOM 363 CG2 THR A 43 1.660 6.445 3.148 1.00 5.53 C
ANISOU 363 CG2 THR A 43 705 766 629 104 96 -71 C
ATOM 364 N SER A 44 -1.540 7.456 0.408 1.00 4.77 N
ANISOU 364 N SER A 44 564 659 589 -96 172 21 N
ATOM 365 CA SER A 44 -2.462 7.668 -0.666 1.00 4.56 C
ANISOU 365 CA SER A 44 520 616 596 68 136 -52 C
ATOM 366 C SER A 44 -1.679 7.480 -1.960 1.00 4.03 C
ANISOU 366 C SER A 44 317 601 613 15 158 -128 C
ATOM 367 O SER A 44 -0.487 7.145 -1.921 1.00 4.65 O
ANISOU 367 O SER A 44 387 572 807 71 109 -2 O
ATOM 368 CB SER A 44 -3.084 9.055 -0.638 1.00 5.67 C
ANISOU 368 CB SER A 44 653 601 902 172 200 -245 C
ATOM 369 OG SER A 44 -2.118 10.024 -0.978 1.00 8.09 O
ANISOU 369 OG SER A 44 1425 673 975 31 667 160 O
ATOM 370 N SER A 45 -2.302 7.745 -3.100 1.00 4.22 N
ANISOU 370 N SER A 45 370 617 615 162 121 -94 N
ATOM 371 CA SER A 45 -1.616 7.795 -4.368 1.00 4.39 C
ANISOU 371 CA SER A 45 595 403 670 149 215 -110 C
ATOM 372 C SER A 45 -0.428 8.767 -4.364 1.00 3.77 C
ANISOU 372 C SER A 45 489 347 597 215 71 -65 C
ATOM 373 O SER A 45 0.479 8.567 -5.179 1.00 4.68 O
ANISOU 373 O SER A 45 680 547 551 130 249 -88 O
ATOM 374 CB SER A 45 -2.594 8.131 -5.499 1.00 4.60 C
ANISOU 374 CB SER A 45 527 660 561 31 227 -123 C
ATOM 375 OG SER A 45 -3.230 9.385 -5.281 1.00 5.48 O
ANISOU 375 OG SER A 45 709 536 838 120 84 134 O
ATOM 376 N TYR A 46 -0.385 9.722 -3.451 1.00 3.82 N
ANISOU 376 N TYR A 46 470 432 551 103 217 -80 N
ATOM 377 CA TYR A 46 0.780 10.593 -3.302 1.00 4.06 C
ANISOU 377 CA TYR A 46 519 421 602 35 142 -21 C
ATOM 378 C TYR A 46 2.069 9.793 -3.146 1.00 4.61 C
ANISOU 378 C TYR A 46 495 524 733 63 145 -39 C
ATOM 379 O TYR A 46 3.142 10.208 -3.604 1.00 4.61 O
ANISOU 379 O TYR A 46 535 407 809 -8 179 -103 O
ATOM 380 CB TYR A 46 0.541 11.559 -2.123 1.00 4.86 C
ANISOU 380 CB TYR A 46 658 496 692 16 275 -100 C
ATOM 381 CG TYR A 46 1.609 12.615 -1.945 1.00 4.84 C
ANISOU 381 CG TYR A 46 632 446 760 61 176 -165 C
ATOM 382 CD1 TYR A 46 1.645 13.715 -2.777 1.00 4.77 C
ANISOU 382 CD1 TYR A 46 564 440 809 54 168 -168 C
ATOM 383 CD2 TYR A 46 2.591 12.481 -0.973 1.00 5.43 C
ANISOU 383 CD2 TYR A 46 683 627 752 167 159 -229 C
ATOM 384 CE1 TYR A 46 2.641 14.675 -2.642 1.00 5.14 C
ANISOU 384 CE1 TYR A 46 591 577 784 -30 211 -37 C
ATOM 385 CE2 TYR A 46 3.562 13.442 -0.840 1.00 5.92 C
ANISOU 385 CE2 TYR A 46 606 755 890 111 61 -83 C
ATOM 386 CZ TYR A 46 3.595 14.540 -1.654 1.00 5.22 C
ANISOU 386 CZ TYR A 46 521 586 875 154 165 -249 C
ATOM 387 OH TYR A 46 4.590 15.494 -1.491 1.00 6.55 O
ANISOU 387 OH TYR A 46 664 662 1163 -10 139 -289 O
ATOM 388 N LEU A 47 1.991 8.631 -2.494 1.00 4.36 N
ANISOU 388 N LEU A 47 439 490 727 62 187 3 N
ATOM 389 CA LEU A 47 3.166 7.806 -2.271 1.00 4.44 C
ANISOU 389 CA LEU A 47 501 445 741 87 242 -139 C
ATOM 390 C LEU A 47 3.829 7.339 -3.535 1.00 4.28 C
ANISOU 390 C LEU A 47 445 538 642 24 163 -87 C
ATOM 391 O LEU A 47 5.014 7.040 -3.544 1.00 4.70 O
ANISOU 391 O LEU A 47 468 504 815 44 178 -25 O
ATOM 392 CB LEU A 47 2.752 6.596 -1.402 1.00 4.64 C
ANISOU 392 CB LEU A 47 569 465 730 273 405 -82 C
ATOM 393 CG LEU A 47 3.852 5.612 -0.990 1.00 5.28 C
ANISOU 393 CG LEU A 47 503 572 931 280 411 -60 C
ATOM 394 CD1 LEU A 47 4.897 6.276 -0.137 1.00 8.48 C
ANISOU 394 CD1 LEU A 47 1179 1216 827 243 -129 24 C
ATOM 395 CD2 LEU A 47 3.212 4.457 -0.261 1.00 8.76 C
ANISOU 395 CD2 LEU A 47 1204 709 1414 382 553 287 C
ATOM 396 N TRP A 48 3.083 7.246 -4.621 1.00 4.52 N
ANISOU 396 N TRP A 48 456 599 661 -5 186 -52 N
ATOM 397 CA TRP A 48 3.561 6.761 -5.903 1.00 4.35 C
ANISOU 397 CA TRP A 48 633 336 684 78 217 -112 C
ATOM 398 C TRP A 48 3.967 7.878 -6.860 1.00 4.07 C
ANISOU 398 C TRP A 48 390 519 639 -6 167 -102 C
ATOM 399 O TRP A 48 4.362 7.594 -7.987 1.00 4.64 O
ANISOU 399 O TRP A 48 534 557 673 99 260 -94 O
ATOM 400 CB TRP A 48 2.452 5.917 -6.549 1.00 4.20 C
ANISOU 400 CB TRP A 48 618 397 579 57 102 18 C
ATOM 401 CG TRP A 48 2.020 4.725 -5.749 1.00 3.47 C
ANISOU 401 CG TRP A 48 494 375 449 73 168 -67 C
ATOM 402 CD1 TRP A 48 0.785 4.528 -5.209 1.00 4.36 C
ANISOU 402 CD1 TRP A 48 496 278 882 19 190 -124 C
ATOM 403 CD2 TRP A 48 2.786 3.565 -5.395 1.00 3.99 C
ANISOU 403 CD2 TRP A 48 534 420 564 67 215 -8 C
ATOM 404 NE1 TRP A 48 0.722 3.341 -4.525 1.00 4.38 N
ANISOU 404 NE1 TRP A 48 490 490 686 -23 218 12 N
ATOM 405 CE2 TRP A 48 1.940 2.726 -4.635 1.00 4.09 C
ANISOU 405 CE2 TRP A 48 598 463 494 0 100 32 C
ATOM 406 CE3 TRP A 48 4.094 3.149 -5.631 1.00 4.62 C
ANISOU 406 CE3 TRP A 48 611 357 786 144 314 -198 C
ATOM 407 CZ2 TRP A 48 2.360 1.529 -4.139 1.00 4.78 C
ANISOU 407 CZ2 TRP A 48 780 443 593 58 136 70 C
ATOM 408 CZ3 TRP A 48 4.529 1.936 -5.128 1.00 4.84 C
ANISOU 408 CZ3 TRP A 48 612 463 765 97 57 -38 C
ATOM 409 CH2 TRP A 48 3.666 1.131 -4.387 1.00 5.25 C
ANISOU 409 CH2 TRP A 48 711 625 658 88 103 11 C
ATOM 410 N ARG A 49 3.900 9.138 -6.409 1.00 4.36 N
ANISOU 410 N ARG A 49 667 439 551 -56 138 -31 N
ATOM 411 CA ARG A 49 4.041 10.281 -7.288 1.00 4.28 C
ANISOU 411 CA ARG A 49 494 533 601 70 168 55 C
ATOM 412 C ARG A 49 5.367 10.297 -8.046 1.00 5.28 C
ANISOU 412 C ARG A 49 585 804 618 36 200 130 C
ATOM 413 O ARG A 49 5.392 10.796 -9.182 1.00 5.45 O
ANISOU 413 O ARG A 49 790 656 623 14 280 108 O
ATOM 414 CB ARG A 49 3.897 11.571 -6.470 1.00 5.19 C
ANISOU 414 CB ARG A 49 786 386 799 73 56 27 C
ATOM 415 CG ARG A 49 5.098 11.838 -5.568 1.00 4.85 C
ANISOU 415 CG ARG A 49 675 538 628 89 113 80 C
ATOM 416 CD ARG A 49 4.743 12.901 -4.491 1.00 5.30 C
ANISOU 416 CD ARG A 49 711 532 769 10 98 38 C
ATOM 417 NE ARG A 49 5.896 13.148 -3.648 1.00 5.03 N
ANISOU 417 NE ARG A 49 663 481 767 -96 119 -41 N
ATOM 418 CZ ARG A 49 6.312 12.346 -2.665 1.00 4.50 C
ANISOU 418 CZ ARG A 49 483 621 606 -114 237 -16 C
ATOM 419 NH1 ARG A 49 5.621 11.230 -2.364 1.00 4.61 N
ANISOU 419 NH1 ARG A 49 426 502 825 -31 289 -55 N
ATOM 420 NH2 ARG A 49 7.412 12.632 -1.956 1.00 5.50 N
ANISOU 420 NH2 ARG A 49 484 683 920 63 58 -184 N
ATOM 421 N ASN A 50 6.459 9.799 -7.478 1.00 4.47 N
ANISOU 421 N ASN A 50 556 560 582 82 231 -7 N
ATOM 422 CA ASN A 50 7.773 9.844 -8.100 1.00 4.41 C
ANISOU 422 CA ASN A 50 603 464 610 14 221 69 C
ATOM 423 C ASN A 50 8.145 8.536 -8.786 1.00 4.91 C
ANISOU 423 C ASN A 50 524 677 663 104 176 -97 C
ATOM 424 O ASN A 50 9.189 8.384 -9.414 1.00 6.36 O
ANISOU 424 O ASN A 50 732 743 942 129 358 -123 O
ATOM 425 CB ASN A 50 8.847 10.263 -7.081 1.00 4.93 C
ANISOU 425 CB ASN A 50 512 664 697 79 279 -80 C
ATOM 426 CG ASN A 50 8.598 11.645 -6.571 1.00 5.19 C
ANISOU 426 CG ASN A 50 650 534 789 -177 169 4 C
ATOM 427 OD1 ASN A 50 8.280 12.548 -7.357 1.00 6.52 O
ANISOU 427 OD1 ASN A 50 915 659 904 -96 126 75 O
ATOM 428 ND2 ASN A 50 8.703 11.820 -5.278 1.00 5.43 N
ANISOU 428 ND2 ASN A 50 635 622 806 18 259 -118 N
ATOM 429 N ILE A 51 7.267 7.522 -8.678 1.00 4.69 N
ANISOU 429 N ILE A 51 792 521 470 83 154 -34 N
ATOM 430 CA ILE A 51 7.434 6.221 -9.303 1.00 4.95 C
ANISOU 430 CA ILE A 51 626 583 671 121 17 -19 C
ATOM 431 C ILE A 51 6.668 6.178 -10.613 1.00 4.23 C
ANISOU 431 C ILE A 51 528 465 614 57 131 -44 C
ATOM 432 O ILE A 51 7.191 5.712 -11.632 1.00 5.19 O
ANISOU 432 O ILE A 51 776 598 596 107 255 13 O
ATOM 433 CB ILE A 51 7.054 5.132 -8.289 1.00 4.62 C
ANISOU 433 CB ILE A 51 690 425 641 313 231 -48 C
ATOM 434 CG1 ILE A 51 8.110 5.102 -7.150 1.00 5.86 C
ANISOU 434 CG1 ILE A 51 1089 451 684 91 43 13 C
ATOM 435 CG2 ILE A 51 6.937 3.759 -8.911 1.00 4.66 C
ANISOU 435 CG2 ILE A 51 557 610 605 91 318 -125 C
ATOM 436 CD1 ILE A 51 7.647 4.342 -5.926 1.00 6.48 C
ANISOU 436 CD1 ILE A 51 911 769 783 60 79 128 C
ATOM 437 N ILE A 52 5.416 6.644 -10.591 1.00 4.51 N
ANISOU 437 N ILE A 52 558 571 585 157 127 54 N
ATOM 438 CA ILE A 52 4.591 6.655 -11.808 1.00 4.51 C
ANISOU 438 CA ILE A 52 568 531 616 81 123 50 C
ATOM 439 C ILE A 52 5.302 7.258 -13.001 1.00 4.70 C
ANISOU 439 C ILE A 52 763 487 534 160 107 39 C
ATOM 440 O ILE A 52 5.139 6.719 -14.102 1.00 5.31 O
ANISOU 440 O ILE A 52 770 648 599 217 155 -107 O
ATOM 441 CB ILE A 52 3.242 7.315 -11.483 1.00 4.99 C
ANISOU 441 CB ILE A 52 555 552 791 99 76 -82 C
ATOM 442 CG1 ILE A 52 2.370 6.386 -10.613 1.00 6.14 C
ANISOU 442 CG1 ILE A 52 815 712 804 -94 325 -273 C
ATOM 443 CG2 ILE A 52 2.547 7.741 -12.776 1.00 6.19 C
ANISOU 443 CG2 ILE A 52 798 818 736 372 51 -216 C
ATOM 444 CD1 ILE A 52 1.149 7.013 -10.012 1.00 7.03 C
ANISOU 444 CD1 ILE A 52 696 1301 674 231 174 91 C
ATOM 445 N PRO A 53 6.025 8.372 -12.883 1.00 4.95 N
ANISOU 445 N PRO A 53 750 570 562 62 110 63 N
ATOM 446 CA PRO A 53 6.640 8.959 -14.101 1.00 5.20 C
ANISOU 446 CA PRO A 53 840 522 616 200 161 101 C
ATOM 447 C PRO A 53 7.574 8.033 -14.826 1.00 5.15 C
ANISOU 447 C PRO A 53 723 617 618 182 164 106 C
ATOM 448 O PRO A 53 7.803 8.242 -16.056 1.00 5.68 O
ANISOU 448 O PRO A 53 1004 569 586 65 196 104 O
ATOM 449 CB PRO A 53 7.360 10.179 -13.581 1.00 6.79 C
ANISOU 449 CB PRO A 53 1261 584 734 -38 308 61 C
ATOM 450 CG PRO A 53 6.516 10.567 -12.366 1.00 6.88 C
ANISOU 450 CG PRO A 53 1240 498 877 122 290 16 C
ATOM 451 CD PRO A 53 6.204 9.255 -11.715 1.00 6.16 C
ANISOU 451 CD PRO A 53 1059 641 642 -90 184 -2 C
ATOM 452 N HIS A 54 8.151 7.040 -14.147 1.00 4.99 N
ANISOU 452 N HIS A 54 720 550 628 192 23 46 N
ATOM 453 CA HIS A 54 9.004 6.091 -14.854 1.00 5.00 C
ANISOU 453 CA HIS A 54 822 458 618 95 119 116 C
ATOM 454 C HIS A 54 8.240 5.083 -15.692 1.00 4.09 C
ANISOU 454 C HIS A 54 734 333 487 130 92 195 C
ATOM 455 O HIS A 54 8.763 4.518 -16.674 1.00 5.84 O
ANISOU 455 O HIS A 54 964 495 758 122 318 2 O
ATOM 456 CB HIS A 54 9.840 5.317 -13.812 1.00 5.57 C
ANISOU 456 CB HIS A 54 668 774 674 258 24 64 C
ATOM 457 CG HIS A 54 10.868 6.138 -13.115 1.00 5.74 C
ANISOU 457 CG HIS A 54 738 676 768 194 123 65 C
ATOM 458 ND1 HIS A 54 12.176 6.170 -13.582 1.00 8.22 N
ANISOU 458 ND1 HIS A 54 771 1345 1005 -85 187 -1 N
ATOM 459 CD2 HIS A 54 10.768 6.954 -12.037 1.00 6.57 C
ANISOU 459 CD2 HIS A 54 1073 439 984 -19 178 -3 C
ATOM 460 CE1 HIS A 54 12.853 6.994 -12.792 1.00 8.43 C
ANISOU 460 CE1 HIS A 54 975 1274 954 -158 59 95 C
ATOM 461 NE2 HIS A 54 12.045 7.463 -11.860 1.00 8.00 N
ANISOU 461 NE2 HIS A 54 1181 897 963 -195 54 65 N
ATOM 462 N VAL A 55 7.007 4.791 -15.298 1.00 4.77 N
ANISOU 462 N VAL A 55 766 570 476 77 121 77 N
ATOM 463 CA VAL A 55 6.172 3.746 -15.879 1.00 5.20 C
ANISOU 463 CA VAL A 55 701 661 612 69 67 -73 C
ATOM 464 C VAL A 55 5.204 4.251 -16.929 1.00 5.09 C
ANISOU 464 C VAL A 55 570 546 819 46 110 -34 C
ATOM 465 O VAL A 55 4.995 3.630 -17.976 1.00 5.71 O
ANISOU 465 O VAL A 55 876 654 641 111 85 -64 O
ATOM 466 CB VAL A 55 5.426 3.020 -14.744 1.00 4.94 C
ANISOU 466 CB VAL A 55 547 462 867 247 287 -53 C
ATOM 467 CG1 VAL A 55 4.493 1.952 -15.296 1.00 6.45 C
ANISOU 467 CG1 VAL A 55 814 632 1003 61 263 -3 C
ATOM 468 CG2 VAL A 55 6.423 2.426 -13.771 1.00 5.91 C
ANISOU 468 CG2 VAL A 55 871 508 868 196 240 114 C
ATOM 469 N ALA A 56 4.632 5.427 -16.690 1.00 5.40 N
ANISOU 469 N ALA A 56 915 534 602 103 -22 -90 N
ATOM 470 CA ALA A 56 3.693 6.087 -17.596 1.00 5.30 C
ANISOU 470 CA ALA A 56 739 535 740 16 133 71 C
ATOM 471 C ALA A 56 4.163 6.169 -19.051 1.00 5.52 C
ANISOU 471 C ALA A 56 841 594 663 135 79 -40 C
ATOM 472 O ALA A 56 3.280 6.079 -19.919 1.00 6.32 O
ANISOU 472 O ALA A 56 851 707 844 310 -12 -137 O
ATOM 473 CB ALA A 56 3.335 7.458 -17.047 1.00 6.37 C
ANISOU 473 CB ALA A 56 914 759 748 306 42 -101 C
ATOM 474 N PRO A 57 5.406 6.363 -19.366 1.00 5.49 N
ANISOU 474 N PRO A 57 786 657 644 73 173 40 N
ATOM 475 CA PRO A 57 5.818 6.408 -20.783 1.00 6.40 C
ANISOU 475 CA PRO A 57 1070 731 631 31 118 160 C
ATOM 476 C PRO A 57 5.401 5.185 -21.565 1.00 6.17 C
ANISOU 476 C PRO A 57 1037 755 554 14 216 109 C
ATOM 477 O PRO A 57 5.123 5.290 -22.747 1.00 7.11 O
ANISOU 477 O PRO A 57 1387 719 596 163 111 94 O
ATOM 478 CB PRO A 57 7.354 6.566 -20.717 1.00 6.74 C
ANISOU 478 CB PRO A 57 1058 888 614 -102 319 176 C
ATOM 479 CG PRO A 57 7.544 7.369 -19.457 1.00 6.75 C
ANISOU 479 CG PRO A 57 842 935 787 -63 276 83 C
ATOM 480 CD PRO A 57 6.563 6.711 -18.511 1.00 5.82 C
ANISOU 480 CD PRO A 57 894 722 595 50 135 130 C
ATOM 481 N SER A 58 5.381 4.012 -20.946 1.00 5.71 N
ANISOU 481 N SER A 58 880 751 538 -9 21 99 N
ATOM 482 CA SER A 58 5.145 2.765 -21.626 1.00 5.98 C
ANISOU 482 CA SER A 58 839 803 629 -28 130 -12 C
ATOM 483 C SER A 58 3.800 2.135 -21.273 1.00 5.91 C
ANISOU 483 C SER A 58 957 700 589 -25 178 48 C
ATOM 484 O SER A 58 3.299 1.334 -22.080 1.00 6.53 O
ANISOU 484 O SER A 58 865 771 843 -93 215 -144 O
ATOM 485 CB SER A 58 6.244 1.733 -21.364 1.00 7.24 C
ANISOU 485 CB SER A 58 1028 944 780 121 107 -1 C
ATOM 486 OG SER A 58 6.322 1.433 -19.970 1.00 6.24 O
ANISOU 486 OG SER A 58 991 638 741 208 239 -40 O
ATOM 487 N HIS A 59 3.251 2.453 -20.117 1.00 5.32 N
ANISOU 487 N HIS A 59 777 546 701 118 202 57 N
ATOM 488 CA HIS A 59 2.074 1.741 -19.598 1.00 5.03 C
ANISOU 488 CA HIS A 59 742 498 673 35 163 -1 C
ATOM 489 C HIS A 59 1.118 2.680 -18.902 1.00 5.68 C
ANISOU 489 C HIS A 59 800 744 613 204 73 -29 C
ATOM 490 O HIS A 59 1.526 3.628 -18.237 1.00 6.19 O
ANISOU 490 O HIS A 59 860 682 808 36 219 -71 O
ATOM 491 CB HIS A 59 2.474 0.654 -18.566 1.00 5.39 C
ANISOU 491 CB HIS A 59 764 581 704 62 192 8 C
ATOM 492 CG HIS A 59 3.141 -0.536 -19.202 1.00 5.70 C
ANISOU 492 CG HIS A 59 879 686 601 161 96 -20 C
ATOM 493 ND1 HIS A 59 4.453 -0.458 -19.656 1.00 6.32 N
ANISOU 493 ND1 HIS A 59 934 634 832 250 213 -167 N
ATOM 494 CD2 HIS A 59 2.680 -1.759 -19.477 1.00 6.30 C
ANISOU 494 CD2 HIS A 59 1018 577 797 233 -3 35 C
ATOM 495 CE1 HIS A 59 4.728 -1.640 -20.192 1.00 6.77 C
ANISOU 495 CE1 HIS A 59 1108 476 990 138 188 -143 C
ATOM 496 NE2 HIS A 59 3.684 -2.462 -20.104 1.00 6.53 N
ANISOU 496 NE2 HIS A 59 775 627 1078 213 -43 -45 N
ATOM 497 N ARG A 60 -0.156 2.328 -18.991 1.00 5.41 N
ANISOU 497 N ARG A 60 798 627 629 263 48 -202 N
ATOM 498 CA ARG A 60 -1.139 3.025 -18.166 1.00 4.90 C
ANISOU 498 CA ARG A 60 811 441 610 139 144 -47 C
ATOM 499 C ARG A 60 -0.801 2.807 -16.691 1.00 4.59 C
ANISOU 499 C ARG A 60 719 412 612 56 122 6 C
ATOM 500 O ARG A 60 -0.476 1.688 -16.308 1.00 5.94 O
ANISOU 500 O ARG A 60 939 508 809 236 68 62 O
ATOM 501 CB ARG A 60 -2.516 2.480 -18.458 1.00 5.48 C
ANISOU 501 CB ARG A 60 797 563 723 84 47 -7 C
ATOM 502 CG ARG A 60 -3.676 3.224 -17.827 1.00 6.42 C
ANISOU 502 CG ARG A 60 821 902 717 227 35 28 C
ATOM 503 CD ARG A 60 -4.991 2.647 -18.353 1.00 7.11 C
ANISOU 503 CD ARG A 60 778 695 1228 307 -13 -103 C
ATOM 504 NE ARG A 60 -6.137 3.304 -17.753 1.00 6.83 N
ANISOU 504 NE ARG A 60 845 725 1024 106 135 -226 N
ATOM 505 CZ ARG A 60 -7.382 2.800 -17.844 1.00 8.51 C
ANISOU 505 CZ ARG A 60 832 987 1416 31 219 -372 C
ATOM 506 NH1 ARG A 60 -7.593 1.652 -18.487 1.00 8.83 N
ANISOU 506 NH1 ARG A 60 1118 1015 1223 -68 53 -383 N
ATOM 507 NH2 ARG A 60 -8.378 3.450 -17.276 1.00 9.67 N
ANISOU 507 NH2 ARG A 60 877 1236 1561 147 247 -447 N
ATOM 508 N CYS A 61 -0.933 3.857 -15.915 1.00 5.68 N
ANISOU 508 N CYS A 61 1029 488 640 119 21 -4 N
ATOM 509 CA CYS A 61 -0.753 3.830 -14.471 1.00 5.12 C
ANISOU 509 CA CYS A 61 858 499 588 72 246 -9 C
ATOM 510 C CYS A 61 -2.059 4.239 -13.823 1.00 5.27 C
ANISOU 510 C CYS A 61 679 495 829 138 155 16 C
ATOM 511 O CYS A 61 -2.552 5.349 -14.096 1.00 6.17 O
ANISOU 511 O CYS A 61 811 606 929 110 239 158 O
ATOM 512 CB CYS A 61 0.348 4.798 -14.045 1.00 5.53 C
ANISOU 512 CB CYS A 61 684 732 687 76 154 -7 C
ATOM 513 SG CYS A 61 1.965 4.383 -14.711 1.00 6.26 S
ANISOU 513 SG CYS A 61 798 760 821 71 261 -50 S
ATOM 514 N ILE A 62 -2.615 3.364 -13.005 1.00 4.59 N
ANISOU 514 N ILE A 62 621 460 662 247 169 -32 N
ATOM 515 CA ILE A 62 -3.836 3.603 -12.258 1.00 4.27 C
ANISOU 515 CA ILE A 62 646 334 644 171 155 -67 C
ATOM 516 C ILE A 62 -3.485 3.536 -10.777 1.00 4.36 C
ANISOU 516 C ILE A 62 452 548 657 238 134 -18 C
ATOM 517 O ILE A 62 -2.982 2.522 -10.328 1.00 4.83 O
ANISOU 517 O ILE A 62 478 635 724 200 53 38 O
ATOM 518 CB ILE A 62 -4.939 2.614 -12.614 1.00 4.81 C
ANISOU 518 CB ILE A 62 792 385 651 32 242 -64 C
ATOM 519 CG1 ILE A 62 -5.187 2.569 -14.116 1.00 7.88 C
ANISOU 519 CG1 ILE A 62 896 1399 697 -338 177 -106 C
ATOM 520 CG2 ILE A 62 -6.212 2.920 -11.815 1.00 7.12 C
ANISOU 520 CG2 ILE A 62 719 1093 893 -12 299 -136 C
ATOM 521 CD1 ILE A 62 -6.145 1.481 -14.553 1.00 7.67 C
ANISOU 521 CD1 ILE A 62 944 1176 794 -218 204 -283 C
ATOM 522 N ALA A 63 -3.734 4.607 -10.013 1.00 4.29 N
ANISOU 522 N ALA A 63 519 563 550 113 127 -33 N
ATOM 523 CA ALA A 63 -3.369 4.624 -8.600 1.00 4.61 C
ANISOU 523 CA ALA A 63 570 493 688 142 78 -61 C
ATOM 524 C ALA A 63 -4.568 5.166 -7.813 1.00 4.68 C
ANISOU 524 C ALA A 63 654 477 647 82 205 -106 C
ATOM 525 O ALA A 63 -4.702 6.374 -7.678 1.00 5.08 O
ANISOU 525 O ALA A 63 814 433 682 106 156 -33 O
ATOM 526 CB ALA A 63 -2.101 5.445 -8.362 1.00 4.54 C
ANISOU 526 CB ALA A 63 612 650 464 82 194 -166 C
ATOM 527 N PRO A 64 -5.439 4.287 -7.311 1.00 4.61 N
ANISOU 527 N PRO A 64 655 355 740 169 237 -46 N
ATOM 528 CA PRO A 64 -6.547 4.755 -6.503 1.00 4.75 C
ANISOU 528 CA PRO A 64 670 558 576 211 151 9 C
ATOM 529 C PRO A 64 -6.114 5.163 -5.105 1.00 4.38 C
ANISOU 529 C PRO A 64 467 492 704 113 55 -133 C
ATOM 530 O PRO A 64 -5.175 4.642 -4.512 1.00 5.45 O
ANISOU 530 O PRO A 64 661 785 624 246 96 -54 O
ATOM 531 CB PRO A 64 -7.454 3.511 -6.415 1.00 4.84 C
ANISOU 531 CB PRO A 64 578 720 541 29 98 -180 C
ATOM 532 CG PRO A 64 -6.491 2.360 -6.521 1.00 5.08 C
ANISOU 532 CG PRO A 64 476 556 899 -78 70 -13 C
ATOM 533 CD PRO A 64 -5.443 2.821 -7.499 1.00 5.15 C
ANISOU 533 CD PRO A 64 816 462 679 69 258 -115 C
ATOM 534 N ASP A 65 -6.901 6.056 -4.524 1.00 4.75 N
ANISOU 534 N ASP A 65 787 403 615 132 197 -6 N
ATOM 535 CA ASP A 65 -6.919 6.315 -3.108 1.00 4.38 C
ANISOU 535 CA ASP A 65 516 521 628 169 145 -57 C
ATOM 536 C ASP A 65 -7.951 5.399 -2.478 1.00 4.58 C
ANISOU 536 C ASP A 65 539 612 589 65 107 -119 C
ATOM 537 O ASP A 65 -9.117 5.408 -2.861 1.00 5.09 O
ANISOU 537 O ASP A 65 445 628 861 157 145 -107 O
ATOM 538 CB ASP A 65 -7.245 7.774 -2.859 1.00 4.78 C
ANISOU 538 CB ASP A 65 534 553 728 77 174 -177 C
ATOM 539 CG ASP A 65 -6.163 8.739 -3.316 1.00 4.78 C
ANISOU 539 CG ASP A 65 658 518 639 101 185 10 C
ATOM 540 OD1 ASP A 65 -5.028 8.316 -3.504 1.00 5.29 O
ANISOU 540 OD1 ASP A 65 537 668 805 77 141 14 O
ATOM 541 OD2 ASP A 65 -6.510 9.939 -3.459 1.00 5.90 O
ANISOU 541 OD2 ASP A 65 760 534 950 143 208 15 O
ATOM 542 N LEU A 66 -7.514 4.592 -1.528 1.00 4.22 N
ANISOU 542 N LEU A 66 357 611 635 23 193 -73 N
ATOM 543 CA LEU A 66 -8.438 3.669 -0.867 1.00 4.26 C
ANISOU 543 CA LEU A 66 381 511 726 60 224 -88 C
ATOM 544 C LEU A 66 -9.568 4.476 -0.252 1.00 4.38 C
ANISOU 544 C LEU A 66 375 579 710 47 181 -175 C
ATOM 545 O LEU A 66 -9.432 5.639 0.105 1.00 4.73 O
ANISOU 545 O LEU A 66 538 574 685 68 206 -150 O
ATOM 546 CB LEU A 66 -7.689 2.882 0.176 1.00 5.07 C
ANISOU 546 CB LEU A 66 622 603 700 74 230 -12 C
ATOM 547 CG LEU A 66 -6.558 1.954 -0.290 1.00 5.46 C
ANISOU 547 CG LEU A 66 610 413 1052 126 189 62 C
ATOM 548 CD1 LEU A 66 -5.970 1.229 0.908 1.00 5.85 C
ANISOU 548 CD1 LEU A 66 533 725 963 75 223 16 C
ATOM 549 CD2 LEU A 66 -7.048 0.979 -1.314 1.00 5.93 C
ANISOU 549 CD2 LEU A 66 774 467 1014 175 184 17 C
ATOM 550 N ILE A 67 -10.731 3.822 -0.101 1.00 4.57 N
ANISOU 550 N ILE A 67 376 562 799 76 194 -213 N
ATOM 551 CA ILE A 67 -11.860 4.471 0.509 1.00 4.70 C
ANISOU 551 CA ILE A 67 391 631 765 111 200 -117 C
ATOM 552 C ILE A 67 -11.481 5.012 1.877 1.00 4.82 C
ANISOU 552 C ILE A 67 286 760 785 65 234 -181 C
ATOM 553 O ILE A 67 -10.734 4.402 2.648 1.00 5.22 O
ANISOU 553 O ILE A 67 431 764 788 -59 149 7 O
ATOM 554 CB ILE A 67 -13.084 3.529 0.564 1.00 5.43 C
ANISOU 554 CB ILE A 67 371 636 1056 54 155 -112 C
ATOM 555 CG1 ILE A 67 -14.396 4.265 0.830 1.00 5.59 C
ANISOU 555 CG1 ILE A 67 442 498 1184 24 290 -164 C
ATOM 556 CG2 ILE A 67 -12.937 2.380 1.555 1.00 5.79 C
ANISOU 556 CG2 ILE A 67 436 637 1125 41 138 -107 C
ATOM 557 CD1 ILE A 67 -14.813 5.263 -0.226 1.00 6.94 C
ANISOU 557 CD1 ILE A 67 535 911 1193 236 -68 -215 C
ATOM 558 N GLY A 68 -11.956 6.218 2.195 1.00 5.15 N
ANISOU 558 N GLY A 68 445 774 738 73 135 -165 N
ATOM 559 CA GLY A 68 -11.622 6.922 3.406 1.00 5.45 C
ANISOU 559 CA GLY A 68 566 852 651 -19 178 -155 C
ATOM 560 C GLY A 68 -10.262 7.552 3.443 1.00 4.79 C
ANISOU 560 C GLY A 68 491 636 693 120 231 -155 C
ATOM 561 O GLY A 68 -9.860 8.073 4.495 1.00 6.47 O
ANISOU 561 O GLY A 68 654 1043 760 -30 186 -266 O
ATOM 562 N MET A 69 -9.508 7.483 2.357 1.00 4.70 N
ANISOU 562 N MET A 69 480 553 754 135 244 -215 N
ATOM 563 CA MET A 69 -8.135 7.971 2.314 1.00 4.46 C
ANISOU 563 CA MET A 69 483 519 691 85 191 -42 C
ATOM 564 C MET A 69 -7.902 8.880 1.123 1.00 4.03 C
ANISOU 564 C MET A 69 406 402 722 182 97 -102 C
ATOM 565 O MET A 69 -8.682 8.893 0.172 1.00 4.96 O
ANISOU 565 O MET A 69 551 573 760 47 38 -63 O
ATOM 566 CB AMET A 69 -7.198 6.762 2.304 0.65 4.99 C
ANISOU 566 CB AMET A 69 480 634 782 174 -19 86 C
ATOM 567 CB BMET A 69 -7.219 6.757 2.188 0.35 4.94 C
ANISOU 567 CB BMET A 69 387 313 1175 -65 324 83 C
ATOM 568 CG AMET A 69 -7.422 5.909 3.529 0.65 3.79 C
ANISOU 568 CG AMET A 69 251 373 818 18 110 -61 C
ATOM 569 CG BMET A 69 -7.616 5.591 3.075 0.35 8.04 C
ANISOU 569 CG BMET A 69 1483 475 1098 -261 222 206 C
ATOM 570 SD AMET A 69 -6.287 4.511 3.622 0.65 3.20 S
ANISOU 570 SD AMET A 69 361 283 570 101 188 -87 S
ATOM 571 SD BMET A 69 -6.804 5.697 4.679 0.35 12.27 S
ANISOU 571 SD BMET A 69 1729 1575 1358 -437 -81 458 S
ATOM 572 CE AMET A 69 -4.882 5.369 4.386 0.65 2.52 C
ANISOU 572 CE AMET A 69 228 325 404 61 254 124 C
ATOM 573 CE BMET A 69 -5.080 5.493 4.221 0.35 16.47 C
ANISOU 573 CE BMET A 69 1896 3283 1080 406 -196 -205 C
ATOM 574 N GLY A 70 -6.818 9.637 1.160 1.00 4.42 N
ANISOU 574 N GLY A 70 539 445 694 -30 100 -94 N
ATOM 575 CA GLY A 70 -6.506 10.483 -0.011 1.00 5.12 C
ANISOU 575 CA GLY A 70 699 670 574 23 54 -56 C
ATOM 576 C GLY A 70 -7.648 11.430 -0.301 1.00 5.03 C
ANISOU 576 C GLY A 70 472 597 843 -85 16 -75 C
ATOM 577 O GLY A 70 -8.214 12.050 0.600 1.00 5.82 O
ANISOU 577 O GLY A 70 696 671 844 -26 197 -18 O
ATOM 578 N LYS A 71 -7.939 11.548 -1.598 1.00 4.48 N
ANISOU 578 N LYS A 71 514 403 785 52 147 -42 N
ATOM 579 CA LYS A 71 -9.038 12.386 -2.072 1.00 5.24 C
ANISOU 579 CA LYS A 71 683 506 801 164 48 -68 C
ATOM 580 C LYS A 71 -10.337 11.613 -2.230 1.00 4.76 C
ANISOU 580 C LYS A 71 664 585 561 165 11 21 C
ATOM 581 O LYS A 71 -11.298 12.158 -2.733 1.00 6.56 O
ANISOU 581 O LYS A 71 663 796 1033 238 -5 -20 O
ATOM 582 CB LYS A 71 -8.614 13.035 -3.405 1.00 6.79 C
ANISOU 582 CB LYS A 71 1062 531 985 -117 -71 118 C
ATOM 583 CG LYS A 71 -7.326 13.851 -3.320 1.00 9.96 C
ANISOU 583 CG LYS A 71 1301 1221 1261 -527 -144 191 C
ATOM 584 CD LYS A 71 -7.041 14.523 -4.674 1.00 11.20 C
ANISOU 584 CD LYS A 71 1431 1363 1460 -718 -407 469 C
ATOM 585 CE LYS A 71 -5.641 15.083 -4.726 1.00 11.55 C
ANISOU 585 CE LYS A 71 1267 1463 1658 -468 152 103 C
ATOM 586 NZ LYS A 71 -5.343 15.791 -6.015 1.00 11.59 N
ANISOU 586 NZ LYS A 71 1397 1415 1593 -35 481 11 N
ATOM 587 N SER A 72 -10.363 10.344 -1.825 1.00 5.09 N
ANISOU 587 N SER A 72 557 558 819 85 47 -110 N
ATOM 588 CA SER A 72 -11.610 9.581 -1.874 1.00 5.59 C
ANISOU 588 CA SER A 72 559 656 909 93 86 -86 C
ATOM 589 C SER A 72 -12.564 10.051 -0.784 1.00 5.86 C
ANISOU 589 C SER A 72 581 580 1064 184 149 -100 C
ATOM 590 O SER A 72 -12.203 10.700 0.202 1.00 6.23 O
ANISOU 590 O SER A 72 604 884 879 109 71 -98 O
ATOM 591 CB SER A 72 -11.314 8.098 -1.799 1.00 5.43 C
ANISOU 591 CB SER A 72 574 597 890 54 146 -157 C
ATOM 592 OG SER A 72 -10.617 7.688 -2.949 1.00 6.00 O
ANISOU 592 OG SER A 72 586 858 837 97 174 -215 O
ATOM 593 N ASP A 73 -13.836 9.704 -0.973 1.00 6.19 N
ANISOU 593 N ASP A 73 572 799 981 124 108 -233 N
ATOM 594 CA ASP A 73 -14.854 10.051 -0.016 1.00 6.32 C
ANISOU 594 CA ASP A 73 579 969 854 7 108 -269 C
ATOM 595 C ASP A 73 -14.659 9.277 1.267 1.00 7.11 C
ANISOU 595 C ASP A 73 728 936 1038 228 201 -199 C
ATOM 596 O ASP A 73 -13.886 8.336 1.362 1.00 7.05 O
ANISOU 596 O ASP A 73 658 824 1195 62 283 -106 O
ATOM 597 CB ASP A 73 -16.273 9.776 -0.559 1.00 8.20 C
ANISOU 597 CB ASP A 73 515 1143 1456 42 13 -135 C
ATOM 598 CG ASP A 73 -16.752 10.785 -1.571 1.00 9.59 C
ANISOU 598 CG ASP A 73 784 1113 1746 468 -198 -300 C
ATOM 599 OD1 ASP A 73 -16.135 11.835 -1.739 1.00 11.76 O
ANISOU 599 OD1 ASP A 73 1363 1099 2007 395 -244 -27 O
ATOM 600 OD2 ASP A 73 -17.806 10.511 -2.213 1.00 12.34 O
ANISOU 600 OD2 ASP A 73 1073 1768 1847 527 -473 -467 O
ATOM 601 N LYS A 74 -15.355 9.706 2.295 1.00 6.99 N
ANISOU 601 N LYS A 74 824 844 989 319 303 99 N
ATOM 602 CA LYS A 74 -15.219 9.306 3.659 1.00 9.06 C
ANISOU 602 CA LYS A 74 1190 1225 1028 -127 116 208 C
ATOM 603 C LYS A 74 -16.559 8.814 4.251 1.00 8.24 C
ANISOU 603 C LYS A 74 1164 1114 855 22 271 9 C
ATOM 604 O LYS A 74 -17.121 9.437 5.162 1.00 10.91 O
ANISOU 604 O LYS A 74 1620 1126 1400 228 551 -98 O
ATOM 605 CB LYS A 74 -14.758 10.455 4.535 1.00 14.46 C
ANISOU 605 CB LYS A 74 2343 2069 1082 -1062 201 -1 C
ATOM 606 CG LYS A 74 -13.461 11.058 4.056 1.00 11.21 C
ANISOU 606 CG LYS A 74 1367 1573 1321 -265 -350 233 C
ATOM 607 CD LYS A 74 -13.087 12.218 4.983 1.00 10.97 C
ANISOU 607 CD LYS A 74 1080 1511 1578 -129 -80 74 C
ATOM 608 CE LYS A 74 -11.794 12.887 4.570 1.00 10.39 C
ANISOU 608 CE LYS A 74 713 1497 1736 82 -190 -107 C
ATOM 609 NZ LYS A 74 -10.679 11.896 4.573 1.00 10.23 N
ANISOU 609 NZ LYS A 74 1270 1242 1375 309 42 23 N
ATOM 610 N PRO A 75 -17.046 7.705 3.774 1.00 7.99 N
ANISOU 610 N PRO A 75 573 1011 1451 282 212 -80 N
ATOM 611 CA PRO A 75 -18.214 7.100 4.432 1.00 8.32 C
ANISOU 611 CA PRO A 75 406 1177 1579 357 197 86 C
ATOM 612 C PRO A 75 -17.809 6.806 5.862 1.00 8.18 C
ANISOU 612 C PRO A 75 690 928 1489 317 247 -77 C
ATOM 613 O PRO A 75 -16.636 6.591 6.257 1.00 8.88 O
ANISOU 613 O PRO A 75 720 1347 1308 350 207 14 O
ATOM 614 CB PRO A 75 -18.475 5.844 3.595 1.00 9.49 C
ANISOU 614 CB PRO A 75 699 1547 1360 -115 100 152 C
ATOM 615 CG PRO A 75 -17.166 5.560 2.965 1.00 8.44 C
ANISOU 615 CG PRO A 75 935 1078 1194 15 175 -89 C
ATOM 616 CD PRO A 75 -16.565 6.896 2.637 1.00 8.17 C
ANISOU 616 CD PRO A 75 658 1062 1386 47 226 -157 C
ATOM 617 N ASP A 76 -18.793 6.770 6.742 1.00 9.65 N
ANISOU 617 N ASP A 76 714 1402 1552 301 314 -38 N
ATOM 618 CA ASP A 76 -18.543 6.474 8.157 1.00 9.03 C
ANISOU 618 CA ASP A 76 768 1122 1539 273 266 -72 C
ATOM 619 C ASP A 76 -18.549 4.973 8.330 1.00 9.51 C
ANISOU 619 C ASP A 76 1128 1079 1405 127 680 -256 C
ATOM 620 O ASP A 76 -19.540 4.394 8.758 1.00 15.03 O
ANISOU 620 O ASP A 76 1580 1356 2776 97 1292 41 O
ATOM 621 CB ASP A 76 -19.632 7.111 9.027 1.00 12.72 C
ANISOU 621 CB ASP A 76 1614 1365 1855 477 667 -343 C
ATOM 622 CG ASP A 76 -19.311 7.017 10.484 1.00 14.47 C
ANISOU 622 CG ASP A 76 1737 1910 1849 595 596 -481 C
ATOM 623 OD1 ASP A 76 -18.222 6.559 10.883 1.00 20.15 O
ANISOU 623 OD1 ASP A 76 2330 3105 2223 1291 74 -920 O
ATOM 624 OD2 ASP A 76 -20.159 7.445 11.289 1.00 18.40 O
ANISOU 624 OD2 ASP A 76 2152 2735 2105 689 1115 -282 O
ATOM 625 N LEU A 77 -17.475 4.311 7.942 1.00 10.04 N
ANISOU 625 N LEU A 77 894 1044 1878 241 382 -56 N
ATOM 626 CA LEU A 77 -17.331 2.870 7.993 1.00 8.91 C
ANISOU 626 CA LEU A 77 850 1001 1535 14 245 -136 C
ATOM 627 C LEU A 77 -16.503 2.513 9.222 1.00 6.87 C
ANISOU 627 C LEU A 77 655 759 1195 142 545 -297 C
ATOM 628 O LEU A 77 -15.807 3.307 9.813 1.00 7.80 O
ANISOU 628 O LEU A 77 917 735 1312 1 271 4 O
ATOM 629 CB LEU A 77 -16.637 2.327 6.750 1.00 7.90 C
ANISOU 629 CB LEU A 77 992 778 1233 -97 117 -32 C
ATOM 630 CG LEU A 77 -17.221 2.739 5.382 1.00 9.19 C
ANISOU 630 CG LEU A 77 1088 936 1467 -62 -27 150 C
ATOM 631 CD1 LEU A 77 -16.395 2.085 4.275 1.00 9.55 C
ANISOU 631 CD1 LEU A 77 1580 935 1113 -53 -283 -53 C
ATOM 632 CD2 LEU A 77 -18.703 2.396 5.269 1.00 12.89 C
ANISOU 632 CD2 LEU A 77 1173 1200 2525 -174 -468 67 C
ATOM 633 N ASP A 78 -16.514 1.215 9.552 1.00 7.99 N
ANISOU 633 N ASP A 78 635 739 1663 125 408 -212 N
ATOM 634 CA ASP A 78 -15.518 0.685 10.472 1.00 7.96 C
ANISOU 634 CA ASP A 78 890 902 1234 106 428 -146 C
ATOM 635 C ASP A 78 -14.138 0.598 9.808 1.00 6.14 C
ANISOU 635 C ASP A 78 760 587 986 168 227 -62 C
ATOM 636 O ASP A 78 -13.117 0.601 10.478 1.00 7.53 O
ANISOU 636 O ASP A 78 914 1005 942 206 124 -112 O
ATOM 637 CB ASP A 78 -15.953 -0.714 10.955 1.00 9.23 C
ANISOU 637 CB ASP A 78 1013 1134 1361 -181 178 67 C
ATOM 638 CG ASP A 78 -17.168 -0.674 11.839 1.00 11.42 C
ANISOU 638 CG ASP A 78 1314 1126 1897 -252 563 -13 C
ATOM 639 OD1 ASP A 78 -17.364 0.251 12.636 1.00 22.31 O
ANISOU 639 OD1 ASP A 78 3272 2547 2659 -1678 2029 -1285 O
ATOM 640 OD2 ASP A 78 -17.967 -1.623 11.690 1.00 13.13 O
ANISOU 640 OD2 ASP A 78 1134 1503 2353 -397 409 -271 O
ATOM 641 N TYR A 79 -14.084 0.498 8.488 1.00 5.91 N
ANISOU 641 N TYR A 79 586 664 995 117 157 -66 N
ATOM 642 CA TYR A 79 -12.838 0.466 7.707 1.00 5.67 C
ANISOU 642 CA TYR A 79 604 642 908 39 162 -100 C
ATOM 643 C TYR A 79 -12.035 -0.787 8.050 1.00 5.44 C
ANISOU 643 C TYR A 79 583 595 889 22 273 -133 C
ATOM 644 O TYR A 79 -10.821 -0.774 8.056 1.00 6.40 O
ANISOU 644 O TYR A 79 636 810 986 101 284 -32 O
ATOM 645 CB TYR A 79 -12.031 1.734 7.872 1.00 5.87 C
ANISOU 645 CB TYR A 79 698 608 927 31 167 -100 C
ATOM 646 CG TYR A 79 -12.666 2.917 7.158 1.00 5.54 C
ANISOU 646 CG TYR A 79 540 738 826 47 150 -86 C
ATOM 647 CD1 TYR A 79 -12.540 3.026 5.785 1.00 5.81 C
ANISOU 647 CD1 TYR A 79 715 659 835 85 180 -161 C
ATOM 648 CD2 TYR A 79 -13.376 3.893 7.833 1.00 5.28 C
ANISOU 648 CD2 TYR A 79 587 666 751 41 149 -72 C
ATOM 649 CE1 TYR A 79 -13.093 4.066 5.087 1.00 5.89 C
ANISOU 649 CE1 TYR A 79 536 876 826 109 252 7 C
ATOM 650 CE2 TYR A 79 -13.937 4.945 7.136 1.00 5.46 C
ANISOU 650 CE2 TYR A 79 557 669 849 -41 98 -112 C
ATOM 651 CZ TYR A 79 -13.794 5.046 5.766 1.00 5.36 C
ANISOU 651 CZ TYR A 79 537 633 867 -9 225 59 C
ATOM 652 OH TYR A 79 -14.354 6.090 5.078 1.00 6.96 O
ANISOU 652 OH TYR A 79 820 655 1170 25 99 155 O
ATOM 653 N PHE A 80 -12.731 -1.896 8.284 1.00 6.65 N
ANISOU 653 N PHE A 80 794 561 1173 83 419 -43 N
ATOM 654 CA PHE A 80 -12.084 -3.192 8.278 1.00 5.65 C
ANISOU 654 CA PHE A 80 723 611 812 143 172 20 C
ATOM 655 C PHE A 80 -11.470 -3.462 6.906 1.00 5.93 C
ANISOU 655 C PHE A 80 791 658 803 121 100 -131 C
ATOM 656 O PHE A 80 -11.851 -2.888 5.886 1.00 5.76 O
ANISOU 656 O PHE A 80 692 660 838 129 232 25 O
ATOM 657 CB PHE A 80 -13.110 -4.275 8.591 1.00 7.05 C
ANISOU 657 CB PHE A 80 1006 513 1159 135 299 51 C
ATOM 658 CG PHE A 80 -13.530 -4.385 10.051 1.00 7.90 C
ANISOU 658 CG PHE A 80 1008 723 1268 -83 476 62 C
ATOM 659 CD1 PHE A 80 -12.744 -5.056 10.955 1.00 9.94 C
ANISOU 659 CD1 PHE A 80 1191 1510 1077 -111 404 205 C
ATOM 660 CD2 PHE A 80 -14.707 -3.849 10.488 1.00 13.16 C
ANISOU 660 CD2 PHE A 80 2028 1243 1730 764 974 51 C
ATOM 661 CE1 PHE A 80 -13.101 -5.191 12.267 1.00 10.47 C
ANISOU 661 CE1 PHE A 80 1570 1248 1161 -169 612 241 C
ATOM 662 CE2 PHE A 80 -15.094 -3.975 11.811 1.00 14.48 C
ANISOU 662 CE2 PHE A 80 2010 1771 1722 576 997 -190 C
ATOM 663 CZ PHE A 80 -14.288 -4.647 12.706 1.00 13.46 C
ANISOU 663 CZ PHE A 80 2074 1438 1603 69 976 47 C
ATOM 664 N PHE A 81 -10.512 -4.400 6.916 1.00 5.91 N
ANISOU 664 N PHE A 81 738 712 797 160 206 -6 N
ATOM 665 CA PHE A 81 -9.968 -4.868 5.644 1.00 5.83 C
ANISOU 665 CA PHE A 81 977 592 645 156 223 87 C
ATOM 666 C PHE A 81 -11.071 -5.259 4.662 1.00 6.81 C
ANISOU 666 C PHE A 81 951 858 779 -38 289 -72 C
ATOM 667 O PHE A 81 -11.022 -4.923 3.473 1.00 6.56 O
ANISOU 667 O PHE A 81 1007 794 692 241 211 -23 O
ATOM 668 CB PHE A 81 -9.037 -6.035 5.864 1.00 6.72 C
ANISOU 668 CB PHE A 81 1103 524 926 192 311 26 C
ATOM 669 CG PHE A 81 -8.404 -6.612 4.619 1.00 6.13 C
ANISOU 669 CG PHE A 81 917 516 895 224 170 51 C
ATOM 670 CD1 PHE A 81 -7.450 -5.879 3.949 1.00 6.24 C
ANISOU 670 CD1 PHE A 81 737 849 783 156 63 18 C
ATOM 671 CD2 PHE A 81 -8.749 -7.845 4.146 1.00 7.58 C
ANISOU 671 CD2 PHE A 81 1361 399 1121 300 387 -1 C
ATOM 672 CE1 PHE A 81 -6.840 -6.347 2.823 1.00 8.79 C
ANISOU 672 CE1 PHE A 81 998 1348 993 275 290 -83 C
ATOM 673 CE2 PHE A 81 -8.142 -8.341 3.006 1.00 8.71 C
ANISOU 673 CE2 PHE A 81 1365 875 1071 511 217 -187 C
ATOM 674 CZ PHE A 81 -7.173 -7.591 2.364 1.00 8.73 C
ANISOU 674 CZ PHE A 81 1295 1204 819 654 250 -118 C
ATOM 675 N ASP A 82 -12.091 -5.957 5.166 1.00 7.45 N
ANISOU 675 N ASP A 82 973 1010 845 15 346 39 N
ATOM 676 CA ASP A 82 -13.177 -6.368 4.282 1.00 7.93 C
ANISOU 676 CA ASP A 82 935 873 1206 -29 380 -224 C
ATOM 677 C ASP A 82 -13.857 -5.179 3.625 1.00 8.43 C
ANISOU 677 C ASP A 82 778 989 1439 -3 56 -292 C
ATOM 678 O ASP A 82 -14.343 -5.295 2.473 1.00 8.99 O
ANISOU 678 O ASP A 82 928 1221 1265 -41 184 -221 O
ATOM 679 CB AASP A 82 -14.214 -7.169 5.066 0.50 10.87 C
ANISOU 679 CB AASP A 82 1361 1169 1598 -340 751 -332 C
ATOM 680 CB BASP A 82 -14.136 -7.232 5.096 0.50 11.26 C
ANISOU 680 CB BASP A 82 1387 1425 1468 -465 427 -85 C
ATOM 681 CG AASP A 82 -15.281 -7.697 4.114 0.50 11.03 C
ANISOU 681 CG AASP A 82 1652 754 1786 -693 536 165 C
ATOM 682 CG BASP A 82 -13.720 -8.634 5.486 0.50 13.70 C
ANISOU 682 CG BASP A 82 1822 1316 2068 -619 454 114 C
ATOM 683 OD1AASP A 82 -14.936 -8.511 3.230 0.50 16.51 O
ANISOU 683 OD1AASP A 82 2228 1050 2996 -533 -44 -846 O
ATOM 684 OD1BASP A 82 -12.741 -9.232 4.972 0.50 16.50 O
ANISOU 684 OD1BASP A 82 2189 1981 2099 222 226 342 O
ATOM 685 OD2AASP A 82 -16.448 -7.281 4.278 0.50 19.63 O
ANISOU 685 OD2AASP A 82 1466 3025 2968 -550 465 -661 O
ATOM 686 OD2BASP A 82 -14.400 -9.229 6.363 0.50 18.85 O
ANISOU 686 OD2BASP A 82 3046 1564 2554 -801 981 270 O
ATOM 687 N ASP A 83 -13.968 -4.028 4.286 1.00 6.99 N
ANISOU 687 N ASP A 83 706 872 1078 3 152 -58 N
ATOM 688 CA ASP A 83 -14.511 -2.856 3.637 1.00 7.24 C
ANISOU 688 CA ASP A 83 706 950 1096 116 180 -171 C
ATOM 689 C ASP A 83 -13.640 -2.441 2.449 1.00 6.55 C
ANISOU 689 C ASP A 83 849 632 1008 340 146 -158 C
ATOM 690 O ASP A 83 -14.125 -2.130 1.354 1.00 7.99 O
ANISOU 690 O ASP A 83 1060 977 998 271 10 -175 O
ATOM 691 CB ASP A 83 -14.655 -1.684 4.621 1.00 8.09 C
ANISOU 691 CB ASP A 83 1051 1009 1012 358 72 -203 C
ATOM 692 CG ASP A 83 -15.692 -1.935 5.685 1.00 11.60 C
ANISOU 692 CG ASP A 83 885 1882 1639 152 411 -699 C
ATOM 693 OD1 ASP A 83 -16.757 -2.464 5.337 1.00 18.69 O
ANISOU 693 OD1 ASP A 83 906 4007 2189 -240 290 -1147 O
ATOM 694 OD2 ASP A 83 -15.451 -1.569 6.846 1.00 10.16 O
ANISOU 694 OD2 ASP A 83 1076 1451 1333 -74 522 -224 O
ATOM 695 N HIS A 84 -12.330 -2.418 2.694 1.00 5.85 N
ANISOU 695 N HIS A 84 730 356 1135 229 190 -119 N
ATOM 696 CA HIS A 84 -11.412 -2.050 1.608 1.00 6.64 C
ANISOU 696 CA HIS A 84 1018 529 977 -125 20 93 C
ATOM 697 C HIS A 84 -11.479 -3.031 0.438 1.00 6.06 C
ANISOU 697 C HIS A 84 755 700 848 69 23 93 C
ATOM 698 O HIS A 84 -11.374 -2.632 -0.711 1.00 6.55 O
ANISOU 698 O HIS A 84 807 784 898 -54 -3 157 O
ATOM 699 CB HIS A 84 -9.982 -1.927 2.141 1.00 6.29 C
ANISOU 699 CB HIS A 84 892 468 1031 -65 80 -29 C
ATOM 700 CG HIS A 84 -9.793 -0.707 2.967 1.00 5.41 C
ANISOU 700 CG HIS A 84 736 553 768 161 259 -121 C
ATOM 701 ND1 HIS A 84 -9.777 0.550 2.378 1.00 5.06 N
ANISOU 701 ND1 HIS A 84 618 574 730 67 253 -80 N
ATOM 702 CD2 HIS A 84 -9.670 -0.572 4.307 1.00 5.30 C
ANISOU 702 CD2 HIS A 84 560 561 893 227 56 -32 C
ATOM 703 CE1 HIS A 84 -9.618 1.409 3.368 1.00 4.76 C
ANISOU 703 CE1 HIS A 84 533 565 709 118 256 -106 C
ATOM 704 NE2 HIS A 84 -9.545 0.775 4.567 1.00 5.25 N
ANISOU 704 NE2 HIS A 84 693 522 780 67 127 -96 N
ATOM 705 N VAL A 85 -11.640 -4.320 0.738 1.00 5.97 N
ANISOU 705 N VAL A 85 955 638 674 16 184 20 N
ATOM 706 CA VAL A 85 -11.761 -5.323 -0.299 1.00 6.39 C
ANISOU 706 CA VAL A 85 906 820 700 -169 313 -21 C
ATOM 707 C VAL A 85 -12.962 -5.031 -1.169 1.00 5.99 C
ANISOU 707 C VAL A 85 895 517 866 -273 259 -42 C
ATOM 708 O VAL A 85 -12.873 -5.070 -2.397 1.00 7.11 O
ANISOU 708 O VAL A 85 1167 743 791 -148 102 -73 O
ATOM 709 CB VAL A 85 -11.851 -6.739 0.296 1.00 6.98 C
ANISOU 709 CB VAL A 85 1032 714 907 73 343 -129 C
ATOM 710 CG1 VAL A 85 -12.202 -7.764 -0.780 1.00 8.51 C
ANISOU 710 CG1 VAL A 85 1177 889 1170 -148 151 -263 C
ATOM 711 CG2 VAL A 85 -10.557 -7.118 0.985 1.00 7.77 C
ANISOU 711 CG2 VAL A 85 1257 780 916 104 110 -226 C
ATOM 712 N ARG A 86 -14.109 -4.745 -0.585 1.00 7.26 N
ANISOU 712 N ARG A 86 926 772 1060 -171 272 -18 N
ATOM 713 CA ARG A 86 -15.346 -4.458 -1.295 1.00 7.91 C
ANISOU 713 CA ARG A 86 901 902 1201 -146 202 -293 C
ATOM 714 C ARG A 86 -15.169 -3.255 -2.204 1.00 6.83 C
ANISOU 714 C ARG A 86 532 798 1264 116 147 -280 C
ATOM 715 O ARG A 86 -15.528 -3.285 -3.395 1.00 7.88 O
ANISOU 715 O ARG A 86 687 934 1372 -59 7 -237 O
ATOM 716 CB ARG A 86 -16.505 -4.202 -0.335 1.00 10.21 C
ANISOU 716 CB ARG A 86 961 1335 1586 -225 439 -391 C
ATOM 717 CG ARG A 86 -17.155 -5.421 0.228 1.00 15.43 C
ANISOU 717 CG ARG A 86 1863 1828 2173 -713 991 -297 C
ATOM 718 CD ARG A 86 -18.555 -5.138 0.801 1.00 13.86 C
ANISOU 718 CD ARG A 86 1691 2202 1375 -524 696 269 C
ATOM 719 NE ARG A 86 -18.512 -4.065 1.745 1.00 14.43 N
ANISOU 719 NE ARG A 86 1296 2486 1701 -2 452 91 N
ATOM 720 CZ ARG A 86 -19.119 -2.924 1.845 1.00 13.71 C
ANISOU 720 CZ ARG A 86 1320 2635 1252 66 524 -20 C
ATOM 721 NH1 ARG A 86 -18.786 -2.190 2.880 1.00 15.80 N
ANISOU 721 NH1 ARG A 86 1916 2284 1802 -520 -141 74 N
ATOM 722 NH2 ARG A 86 -20.035 -2.539 0.944 1.00 13.07 N
ANISOU 722 NH2 ARG A 86 1964 1846 1157 -52 210 -111 N
ATOM 723 N TYR A 87 -14.617 -2.157 -1.656 1.00 6.83 N
ANISOU 723 N TYR A 87 626 780 1189 32 135 -167 N
ATOM 724 CA TYR A 87 -14.462 -0.951 -2.443 1.00 6.43 C
ANISOU 724 CA TYR A 87 500 939 1006 -49 102 -124 C
ATOM 725 C TYR A 87 -13.448 -1.154 -3.583 1.00 6.90 C
ANISOU 725 C TYR A 87 582 1079 960 107 54 -172 C
ATOM 726 O TYR A 87 -13.684 -0.709 -4.716 1.00 6.74 O
ANISOU 726 O TYR A 87 635 911 1014 11 6 -112 O
ATOM 727 CB TYR A 87 -14.073 0.293 -1.582 1.00 6.76 C
ANISOU 727 CB TYR A 87 584 865 1120 -41 60 -219 C
ATOM 728 CG TYR A 87 -15.386 0.814 -0.992 1.00 6.11 C
ANISOU 728 CG TYR A 87 472 735 1115 -31 -64 -160 C
ATOM 729 CD1 TYR A 87 -15.961 0.328 0.149 1.00 6.14 C
ANISOU 729 CD1 TYR A 87 444 898 993 166 -115 -47 C
ATOM 730 CD2 TYR A 87 -16.059 1.814 -1.649 1.00 7.22 C
ANISOU 730 CD2 TYR A 87 595 836 1310 -58 -67 81 C
ATOM 731 CE1 TYR A 87 -17.164 0.797 0.681 1.00 7.34 C
ANISOU 731 CE1 TYR A 87 683 962 1144 203 81 -25 C
ATOM 732 CE2 TYR A 87 -17.278 2.271 -1.124 1.00 7.47 C
ANISOU 732 CE2 TYR A 87 762 846 1229 220 -155 -22 C
ATOM 733 CZ TYR A 87 -17.826 1.805 0.018 1.00 7.35 C
ANISOU 733 CZ TYR A 87 667 795 1330 305 59 -154 C
ATOM 734 OH TYR A 87 -19.042 2.229 0.511 1.00 9.92 O
ANISOU 734 OH TYR A 87 789 1049 1931 295 258 51 O
ATOM 735 N LEU A 88 -12.304 -1.780 -3.302 1.00 5.76 N
ANISOU 735 N LEU A 88 584 693 910 76 130 -129 N
ATOM 736 CA LEU A 88 -11.317 -1.957 -4.372 1.00 5.92 C
ANISOU 736 CA LEU A 88 579 724 947 -25 107 -179 C
ATOM 737 C LEU A 88 -11.802 -2.925 -5.442 1.00 5.88 C
ANISOU 737 C LEU A 88 522 707 1004 58 174 -219 C
ATOM 738 O LEU A 88 -11.556 -2.695 -6.619 1.00 6.07 O
ANISOU 738 O LEU A 88 564 797 946 103 122 -144 O
ATOM 739 CB LEU A 88 -9.953 -2.366 -3.807 1.00 5.62 C
ANISOU 739 CB LEU A 88 574 463 1100 37 144 -66 C
ATOM 740 CG LEU A 88 -8.874 -2.495 -4.909 1.00 7.40 C
ANISOU 740 CG LEU A 88 600 1085 1126 129 137 102 C
ATOM 741 CD1 LEU A 88 -8.565 -1.144 -5.511 1.00 9.05 C
ANISOU 741 CD1 LEU A 88 802 1392 1244 -116 215 323 C
ATOM 742 CD2 LEU A 88 -7.646 -3.194 -4.309 1.00 7.82 C
ANISOU 742 CD2 LEU A 88 442 1301 1228 136 218 -62 C
ATOM 743 N ASP A 89 -12.481 -3.988 -5.015 1.00 6.42 N
ANISOU 743 N ASP A 89 668 699 1071 -18 227 -206 N
ATOM 744 CA ASP A 89 -13.016 -4.927 -6.013 1.00 6.25 C
ANISOU 744 CA ASP A 89 926 703 747 -29 206 -103 C
ATOM 745 C ASP A 89 -13.912 -4.175 -6.990 1.00 6.60 C
ANISOU 745 C ASP A 89 785 735 987 -15 201 -30 C
ATOM 746 O ASP A 89 -13.875 -4.344 -8.204 1.00 6.73 O
ANISOU 746 O ASP A 89 761 855 941 42 6 -24 O
ATOM 747 CB ASP A 89 -13.840 -6.041 -5.364 1.00 7.06 C
ANISOU 747 CB ASP A 89 856 760 1068 -117 111 41 C
ATOM 748 CG ASP A 89 -13.037 -7.211 -4.845 1.00 7.57 C
ANISOU 748 CG ASP A 89 844 642 1391 -93 -18 -70 C
ATOM 749 OD1 ASP A 89 -11.780 -7.241 -5.013 1.00 8.25 O
ANISOU 749 OD1 ASP A 89 864 928 1342 -48 61 33 O
ATOM 750 OD2 ASP A 89 -13.649 -8.114 -4.237 1.00 8.61 O
ANISOU 750 OD2 ASP A 89 971 685 1616 20 158 57 O
ATOM 751 N ALA A 90 -14.792 -3.326 -6.429 1.00 7.02 N
ANISOU 751 N ALA A 90 793 778 1098 -28 62 -141 N
ATOM 752 CA ALA A 90 -15.772 -2.569 -7.226 1.00 7.46 C
ANISOU 752 CA ALA A 90 823 784 1229 -32 -68 -110 C
ATOM 753 C ALA A 90 -15.075 -1.535 -8.081 1.00 7.38 C
ANISOU 753 C ALA A 90 996 788 1020 -14 -56 -182 C
ATOM 754 O ALA A 90 -15.459 -1.335 -9.238 1.00 8.33 O
ANISOU 754 O ALA A 90 922 1107 1134 160 -185 9 O
ATOM 755 CB ALA A 90 -16.836 -1.957 -6.311 1.00 7.72 C
ANISOU 755 CB ALA A 90 935 810 1189 65 -25 -155 C
ATOM 756 N PHE A 91 -14.043 -0.876 -7.544 1.00 5.92 N
ANISOU 756 N PHE A 91 706 614 929 132 57 -78 N
ATOM 757 CA PHE A 91 -13.224 0.073 -8.315 1.00 6.02 C
ANISOU 757 CA PHE A 91 723 805 760 158 -2 64 C
ATOM 758 C PHE A 91 -12.677 -0.593 -9.574 1.00 6.58 C
ANISOU 758 C PHE A 91 580 955 964 18 68 -130 C
ATOM 759 O PHE A 91 -12.746 -0.039 -10.690 1.00 6.69 O
ANISOU 759 O PHE A 91 759 930 854 82 161 -199 O
ATOM 760 CB PHE A 91 -12.112 0.604 -7.426 1.00 6.24 C
ANISOU 760 CB PHE A 91 697 749 923 102 50 -13 C
ATOM 761 CG PHE A 91 -11.125 1.484 -8.160 1.00 6.28 C
ANISOU 761 CG PHE A 91 875 516 995 58 163 -220 C
ATOM 762 CD1 PHE A 91 -11.375 2.837 -8.298 1.00 6.86 C
ANISOU 762 CD1 PHE A 91 838 595 1172 48 198 -104 C
ATOM 763 CD2 PHE A 91 -9.958 0.954 -8.690 1.00 6.99 C
ANISOU 763 CD2 PHE A 91 746 720 1189 36 162 -172 C
ATOM 764 CE1 PHE A 91 -10.494 3.644 -8.977 1.00 7.38 C
ANISOU 764 CE1 PHE A 91 885 719 1201 27 49 110 C
ATOM 765 CE2 PHE A 91 -9.097 1.746 -9.401 1.00 7.14 C
ANISOU 765 CE2 PHE A 91 691 897 1124 45 -9 62 C
ATOM 766 CZ PHE A 91 -9.359 3.069 -9.547 1.00 6.84 C
ANISOU 766 CZ PHE A 91 922 836 841 2 114 -3 C
ATOM 767 N ILE A 92 -12.055 -1.750 -9.387 1.00 6.42 N
ANISOU 767 N ILE A 92 532 978 927 -21 78 -109 N
ATOM 768 CA ILE A 92 -11.394 -2.447 -10.497 1.00 5.75 C
ANISOU 768 CA ILE A 92 710 692 784 -153 109 -74 C
ATOM 769 C ILE A 92 -12.423 -2.794 -11.561 1.00 7.06 C
ANISOU 769 C ILE A 92 642 1061 980 134 108 -281 C
ATOM 770 O ILE A 92 -12.174 -2.570 -12.747 1.00 8.15 O
ANISOU 770 O ILE A 92 1061 1199 837 23 -119 -209 O
ATOM 771 CB ILE A 92 -10.607 -3.643 -9.972 1.00 6.66 C
ANISOU 771 CB ILE A 92 766 828 936 -57 67 -133 C
ATOM 772 CG1 ILE A 92 -9.394 -3.228 -9.141 1.00 6.53 C
ANISOU 772 CG1 ILE A 92 754 714 1011 -74 54 -40 C
ATOM 773 CG2 ILE A 92 -10.172 -4.593 -11.096 1.00 7.44 C
ANISOU 773 CG2 ILE A 92 918 994 917 249 -118 -141 C
ATOM 774 CD1 ILE A 92 -8.752 -4.372 -8.391 1.00 7.67 C
ANISOU 774 CD1 ILE A 92 787 682 1444 46 -80 -94 C
ATOM 775 N GLU A 93 -13.589 -3.282 -11.165 1.00 7.91 N
ANISOU 775 N GLU A 93 625 1045 1334 -32 -93 -184 N
ATOM 776 CA GLU A 93 -14.602 -3.627 -12.168 1.00 8.80 C
ANISOU 776 CA GLU A 93 836 1166 1343 -34 -209 20 C
ATOM 777 C GLU A 93 -15.172 -2.365 -12.823 1.00 8.36 C
ANISOU 777 C GLU A 93 1063 1024 1088 -87 -64 19 C
ATOM 778 O GLU A 93 -15.465 -2.381 -14.009 1.00 9.47 O
ANISOU 778 O GLU A 93 1036 1385 1176 108 -173 -101 O
ATOM 779 CB GLU A 93 -15.710 -4.489 -11.561 1.00 10.36 C
ANISOU 779 CB GLU A 93 1235 908 1793 -435 -344 -24 C
ATOM 780 CG GLU A 93 -15.266 -5.859 -11.087 1.00 9.96 C
ANISOU 780 CG GLU A 93 1081 1079 1623 -142 -186 -21 C
ATOM 781 CD GLU A 93 -14.342 -6.588 -12.027 1.00 10.20 C
ANISOU 781 CD GLU A 93 1128 1312 1435 -211 -169 -64 C
ATOM 782 OE1 GLU A 93 -14.810 -6.830 -13.180 1.00 12.47 O
ANISOU 782 OE1 GLU A 93 1383 1576 1779 185 -560 -351 O
ATOM 783 OE2 GLU A 93 -13.192 -6.958 -11.676 1.00 9.91 O
ANISOU 783 OE2 GLU A 93 1195 1353 1218 -100 -173 -250 O
ATOM 784 N ALA A 94 -15.332 -1.281 -12.069 1.00 8.42 N
ANISOU 784 N ALA A 94 851 1179 1168 77 -277 -34 N
ATOM 785 CA ALA A 94 -15.872 -0.059 -12.624 1.00 8.55 C
ANISOU 785 CA ALA A 94 805 1205 1240 215 -260 -156 C
ATOM 786 C ALA A 94 -14.994 0.485 -13.728 1.00 9.23 C
ANISOU 786 C ALA A 94 1160 1176 1169 161 -237 -16 C
ATOM 787 O ALA A 94 -15.505 1.077 -14.675 1.00 11.54 O
ANISOU 787 O ALA A 94 1385 1586 1412 278 -264 211 O
ATOM 788 CB ALA A 94 -16.077 0.982 -11.545 1.00 11.53 C
ANISOU 788 CB ALA A 94 1224 1586 1569 455 -99 -475 C
ATOM 789 N LEU A 95 -13.687 0.289 -13.624 1.00 8.45 N
ANISOU 789 N LEU A 95 1128 850 1231 101 -105 -103 N
ATOM 790 CA LEU A 95 -12.802 0.743 -14.652 1.00 9.42 C
ANISOU 790 CA LEU A 95 1305 1039 1236 73 -71 24 C
ATOM 791 C LEU A 95 -12.675 -0.245 -15.813 1.00 9.10 C
ANISOU 791 C LEU A 95 737 1265 1454 126 75 -144 C
ATOM 792 O LEU A 95 -11.947 0.038 -16.784 1.00 10.89 O
ANISOU 792 O LEU A 95 1527 1443 1169 -76 21 -27 O
ATOM 793 CB LEU A 95 -11.413 1.059 -14.082 1.00 10.49 C
ANISOU 793 CB LEU A 95 1314 1379 1294 -99 -52 51 C
ATOM 794 CG LEU A 95 -11.165 2.474 -13.573 1.00 11.93 C
ANISOU 794 CG LEU A 95 1335 1581 1618 -181 -103 -180 C
ATOM 795 CD1 LEU A 95 -12.143 2.936 -12.526 1.00 19.47 C
ANISOU 795 CD1 LEU A 95 1639 2332 3427 -734 772 -1395 C
ATOM 796 CD2 LEU A 95 -9.735 2.581 -13.066 1.00 14.56 C
ANISOU 796 CD2 LEU A 95 1303 2286 1944 -453 -100 -216 C
ATOM 797 N GLY A 96 -13.313 -1.389 -15.742 1.00 9.15 N
ANISOU 797 N GLY A 96 1346 1110 1021 125 -133 -4 N
ATOM 798 CA GLY A 96 -13.304 -2.385 -16.793 1.00 11.23 C
ANISOU 798 CA GLY A 96 1441 1409 1417 274 -279 -310 C
ATOM 799 C GLY A 96 -11.960 -3.051 -16.937 1.00 10.85 C
ANISOU 799 C GLY A 96 1584 1032 1508 347 -369 -190 C
ATOM 800 O GLY A 96 -11.601 -3.507 -18.021 1.00 12.76 O
ANISOU 800 O GLY A 96 1630 1730 1487 317 -74 -174 O
ATOM 801 N LEU A 97 -11.161 -3.119 -15.865 1.00 9.60 N
ANISOU 801 N LEU A 97 1375 861 1414 223 -167 152 N
ATOM 802 CA LEU A 97 -9.854 -3.746 -15.974 1.00 10.61 C
ANISOU 802 CA LEU A 97 1428 1076 1525 333 -216 -113 C
ATOM 803 C LEU A 97 -10.057 -5.251 -16.139 1.00 9.71 C
ANISOU 803 C LEU A 97 1065 1062 1562 249 -166 -40 C
ATOM 804 O LEU A 97 -10.911 -5.895 -15.509 1.00 11.82 O
ANISOU 804 O LEU A 97 1478 1343 1670 125 163 -50 O
ATOM 805 CB LEU A 97 -9.014 -3.399 -14.744 1.00 10.46 C
ANISOU 805 CB LEU A 97 1156 1234 1584 -145 -157 48 C
ATOM 806 CG LEU A 97 -8.931 -1.939 -14.330 1.00 9.75 C
ANISOU 806 CG LEU A 97 890 1213 1599 -125 -45 66 C
ATOM 807 CD1 LEU A 97 -7.914 -1.774 -13.190 1.00 9.44 C
ANISOU 807 CD1 LEU A 97 887 1316 1385 -210 92 -17 C
ATOM 808 CD2 LEU A 97 -8.577 -1.093 -15.525 1.00 10.38 C
ANISOU 808 CD2 LEU A 97 1339 1207 1398 45 110 -42 C
ATOM 809 N GLU A 98 -9.224 -5.799 -17.006 1.00 9.23 N
ANISOU 809 N GLU A 98 932 927 1647 168 -129 -11 N
ATOM 810 CA GLU A 98 -9.184 -7.221 -17.271 1.00 9.31 C
ANISOU 810 CA GLU A 98 1055 933 1550 69 -134 -46 C
ATOM 811 C GLU A 98 -7.878 -7.743 -16.694 1.00 9.15 C
ANISOU 811 C GLU A 98 1078 888 1512 143 -178 -33 C
ATOM 812 O GLU A 98 -7.892 -8.022 -15.485 1.00 9.87 O
ANISOU 812 O GLU A 98 1046 1219 1482 -77 -168 -141 O
ATOM 813 CB GLU A 98 -9.351 -7.446 -18.765 1.00 13.46 C
ANISOU 813 CB GLU A 98 1515 1822 1779 231 -578 -459 C
ATOM 814 CG AGLU A 98 -10.778 -7.222 -19.238 0.50 14.78 C
ANISOU 814 CG AGLU A 98 1672 1490 2455 10 -939 51 C
ATOM 815 CG BGLU A 98 -10.672 -6.838 -19.239 0.50 14.25 C
ANISOU 815 CG BGLU A 98 1897 1204 2314 63 -901 248 C
ATOM 816 CD AGLU A 98 -10.904 -7.193 -20.744 0.50 19.74 C
ANISOU 816 CD AGLU A 98 2330 2669 2503 270 -1357 -514 C
ATOM 817 CD BGLU A 98 -10.927 -7.089 -20.707 0.50 16.79 C
ANISOU 817 CD BGLU A 98 2052 1946 2380 161 -1049 63 C
ATOM 818 OE1AGLU A 98 -9.930 -7.528 -21.451 0.50 28.34 O
ANISOU 818 OE1AGLU A 98 3162 4813 2792 -51 -783 -1764 O
ATOM 819 OE1BGLU A 98 -10.341 -6.373 -21.545 0.50 16.96 O
ANISOU 819 OE1BGLU A 98 2293 1896 2254 650 -379 -139 O
ATOM 820 OE2AGLU A 98 -12.008 -6.834 -21.213 0.50 28.37 O
ANISOU 820 OE2AGLU A 98 3865 3200 3716 1536 -2696 -1025 O
ATOM 821 OE2BGLU A 98 -11.724 -8.011 -20.987 0.50 34.24 O
ANISOU 821 OE2BGLU A 98 7116 2983 2911 -2446 -2000 334 O
ATOM 822 N GLU A 99 -6.807 -7.864 -17.463 1.00 9.10 N
ANISOU 822 N GLU A 99 1045 1183 1231 107 -374 146 N
ATOM 823 CA AGLU A 99 -5.498 -8.186 -16.911 0.60 9.30 C
ANISOU 823 CA AGLU A 99 1048 654 1831 231 -505 -183 C
ATOM 824 CA BGLU A 99 -5.474 -8.175 -16.984 0.40 9.01 C
ANISOU 824 CA BGLU A 99 1004 731 1690 119 -431 -77 C
ATOM 825 C GLU A 99 -4.785 -6.939 -16.416 1.00 7.14 C
ANISOU 825 C GLU A 99 930 773 1010 -1 10 -2 C
ATOM 826 O GLU A 99 -4.948 -5.840 -16.957 1.00 8.46 O
ANISOU 826 O GLU A 99 1035 826 1354 -141 -291 146 O
ATOM 827 CB AGLU A 99 -4.583 -8.913 -17.922 0.60 13.30 C
ANISOU 827 CB AGLU A 99 1608 1149 2298 697 -640 -711 C
ATOM 828 CB BGLU A 99 -4.572 -8.749 -18.092 0.40 13.48 C
ANISOU 828 CB BGLU A 99 1538 1261 2323 652 -502 -848 C
ATOM 829 CG AGLU A 99 -5.173 -10.220 -18.449 0.60 13.15 C
ANISOU 829 CG AGLU A 99 2090 925 1981 301 126 -378 C
ATOM 830 CG BGLU A 99 -5.171 -9.844 -18.963 0.40 17.60 C
ANISOU 830 CG BGLU A 99 2143 2169 2376 -614 308 -1097 C
ATOM 831 CD AGLU A 99 -4.635 -10.662 -19.796 0.60 16.75 C
ANISOU 831 CD AGLU A 99 2284 1973 2109 229 86 -958 C
ATOM 832 CD BGLU A 99 -6.152 -9.329 -19.997 0.40 19.02 C
ANISOU 832 CD BGLU A 99 1814 4234 1176 -928 553 -1316 C
ATOM 833 OE1AGLU A 99 -4.790 -11.841 -20.169 0.60 29.50 O
ANISOU 833 OE1AGLU A 99 6164 1825 3220 557 1349 -1262 O
ATOM 834 OE1BGLU A 99 -6.957 -10.162 -20.483 0.40 33.95 O
ANISOU 834 OE1BGLU A 99 2958 5314 4626 1 -720 -4484 O
ATOM 835 OE2AGLU A 99 -4.069 -9.808 -20.508 0.60 28.62 O
ANISOU 835 OE2AGLU A 99 5280 3071 2523 -952 1640 -1332 O
ATOM 836 OE2BGLU A 99 -6.122 -8.109 -20.282 0.40 23.32 O
ANISOU 836 OE2BGLU A 99 1165 5520 2176 -1457 491 1578 O
ATOM 837 N VAL A 100 -3.993 -7.131 -15.350 1.00 6.48 N
ANISOU 837 N VAL A 100 778 622 1062 46 22 -13 N
ATOM 838 CA VAL A 100 -3.250 -6.030 -14.758 1.00 6.42 C
ANISOU 838 CA VAL A 100 816 636 989 187 65 -160 C
ATOM 839 C VAL A 100 -1.867 -6.476 -14.348 1.00 6.00 C
ANISOU 839 C VAL A 100 813 493 973 179 -23 -267 C
ATOM 840 O VAL A 100 -1.619 -7.676 -14.179 1.00 6.58 O
ANISOU 840 O VAL A 100 788 456 1257 33 33 -63 O
ATOM 841 CB VAL A 100 -3.983 -5.439 -13.521 1.00 7.09 C
ANISOU 841 CB VAL A 100 749 875 1068 171 162 -180 C
ATOM 842 CG1 VAL A 100 -5.355 -4.929 -13.885 1.00 8.84 C
ANISOU 842 CG1 VAL A 100 836 1284 1239 320 230 -148 C
ATOM 843 CG2 VAL A 100 -4.006 -6.482 -12.415 1.00 8.82 C
ANISOU 843 CG2 VAL A 100 907 1259 1185 177 287 24 C
ATOM 844 N VAL A 101 -0.981 -5.512 -14.146 1.00 5.17 N
ANISOU 844 N VAL A 101 838 378 747 199 1 -27 N
ATOM 845 CA VAL A 101 0.228 -5.672 -13.356 1.00 5.09 C
ANISOU 845 CA VAL A 101 742 560 631 136 120 -35 C
ATOM 846 C VAL A 101 -0.001 -4.944 -12.049 1.00 4.44 C
ANISOU 846 C VAL A 101 478 523 687 44 121 -36 C
ATOM 847 O VAL A 101 -0.487 -3.823 -12.063 1.00 6.05 O
ANISOU 847 O VAL A 101 1097 486 715 235 176 35 O
ATOM 848 CB VAL A 101 1.461 -5.143 -14.076 1.00 6.07 C
ANISOU 848 CB VAL A 101 769 867 672 176 231 -129 C
ATOM 849 CG1 VAL A 101 2.681 -5.207 -13.210 1.00 6.07 C
ANISOU 849 CG1 VAL A 101 710 817 779 200 230 -53 C
ATOM 850 CG2 VAL A 101 1.710 -5.967 -15.353 1.00 7.87 C
ANISOU 850 CG2 VAL A 101 799 1258 932 -44 369 -422 C
ATOM 851 N LEU A 102 0.335 -5.564 -10.915 1.00 4.27 N
ANISOU 851 N LEU A 102 594 369 660 81 88 -82 N
ATOM 852 CA LEU A 102 0.168 -4.940 -9.624 1.00 4.40 C
ANISOU 852 CA LEU A 102 566 399 707 162 39 -101 C
ATOM 853 C LEU A 102 1.473 -4.344 -9.094 1.00 4.19 C
ANISOU 853 C LEU A 102 513 566 512 195 -25 -24 C
ATOM 854 O LEU A 102 2.512 -5.020 -9.242 1.00 5.17 O
ANISOU 854 O LEU A 102 591 722 650 239 123 -102 O
ATOM 855 CB LEU A 102 -0.321 -6.004 -8.617 1.00 5.51 C
ANISOU 855 CB LEU A 102 894 549 651 -1 -58 7 C
ATOM 856 CG LEU A 102 -1.715 -6.566 -8.856 1.00 5.33 C
ANISOU 856 CG LEU A 102 765 626 633 45 216 -162 C
ATOM 857 CD1 LEU A 102 -2.017 -7.694 -7.889 1.00 6.95 C
ANISOU 857 CD1 LEU A 102 891 733 1017 7 281 45 C
ATOM 858 CD2 LEU A 102 -2.785 -5.498 -8.727 1.00 8.42 C
ANISOU 858 CD2 LEU A 102 862 738 1598 111 344 157 C
ATOM 859 N VAL A 103 1.427 -3.189 -8.463 1.00 4.66 N
ANISOU 859 N VAL A 103 535 545 689 131 71 -64 N
ATOM 860 CA VAL A 103 2.514 -2.570 -7.783 1.00 3.81 C
ANISOU 860 CA VAL A 103 375 404 667 272 105 -80 C
ATOM 861 C VAL A 103 1.999 -2.205 -6.396 1.00 4.30 C
ANISOU 861 C VAL A 103 442 481 712 51 123 -56 C
ATOM 862 O VAL A 103 1.112 -1.372 -6.283 1.00 4.33 O
ANISOU 862 O VAL A 103 557 471 618 198 228 -45 O
ATOM 863 CB VAL A 103 3.078 -1.330 -8.487 1.00 4.44 C
ANISOU 863 CB VAL A 103 475 505 705 175 90 -11 C
ATOM 864 CG1 VAL A 103 4.168 -0.698 -7.635 1.00 5.23 C
ANISOU 864 CG1 VAL A 103 531 704 753 7 99 20 C
ATOM 865 CG2 VAL A 103 3.559 -1.674 -9.879 1.00 4.76 C
ANISOU 865 CG2 VAL A 103 738 289 784 173 210 -43 C
ATOM 866 N ILE A 104 2.473 -2.912 -5.344 1.00 3.94 N
ANISOU 866 N ILE A 104 294 517 684 78 174 -42 N
ATOM 867 CA ILE A 104 1.776 -2.941 -4.080 1.00 4.38 C
ANISOU 867 CA ILE A 104 461 544 660 160 191 -167 C
ATOM 868 C ILE A 104 2.680 -2.801 -2.868 1.00 5.20 C
ANISOU 868 C ILE A 104 487 776 714 96 128 -146 C
ATOM 869 O ILE A 104 3.837 -3.214 -2.886 1.00 5.81 O
ANISOU 869 O ILE A 104 576 787 846 221 15 -118 O
ATOM 870 CB ILE A 104 0.917 -4.214 -3.986 1.00 4.00 C
ANISOU 870 CB ILE A 104 488 537 497 89 318 -104 C
ATOM 871 CG1 ILE A 104 1.703 -5.526 -3.978 1.00 5.35 C
ANISOU 871 CG1 ILE A 104 803 543 685 142 34 -8 C
ATOM 872 CG2 ILE A 104 -0.144 -4.240 -5.095 1.00 5.34 C
ANISOU 872 CG2 ILE A 104 737 487 805 45 37 1 C
ATOM 873 CD1 ILE A 104 0.903 -6.810 -4.077 1.00 6.08 C
ANISOU 873 CD1 ILE A 104 945 580 785 56 315 -240 C
ATOM 874 N HIS A 105 2.077 -2.229 -1.823 1.00 6.48 N
ANISOU 874 N HIS A 105 745 971 745 -35 145 -365 N
ATOM 875 CA HIS A 105 2.783 -1.897 -0.578 1.00 5.96 C
ANISOU 875 CA HIS A 105 745 721 798 140 9 -214 C
ATOM 876 C HIS A 105 1.907 -2.077 0.654 1.00 6.23 C
ANISOU 876 C HIS A 105 937 611 820 64 164 -128 C
ATOM 877 O HIS A 105 0.769 -1.614 0.602 1.00 7.08 O
ANISOU 877 O HIS A 105 761 1140 790 -6 -5 -83 O
ATOM 878 CB HIS A 105 3.235 -0.449 -0.637 1.00 6.71 C
ANISOU 878 CB HIS A 105 870 968 712 -245 38 -83 C
ATOM 879 CG HIS A 105 4.032 0.022 0.546 1.00 5.04 C
ANISOU 879 CG HIS A 105 604 587 723 29 74 -48 C
ATOM 880 ND1 HIS A 105 3.762 1.206 1.205 1.00 6.23 N
ANISOU 880 ND1 HIS A 105 693 786 890 242 143 -173 N
ATOM 881 CD2 HIS A 105 5.091 -0.536 1.180 1.00 5.93 C
ANISOU 881 CD2 HIS A 105 776 724 753 223 56 -206 C
ATOM 882 CE1 HIS A 105 4.651 1.347 2.186 1.00 5.32 C
ANISOU 882 CE1 HIS A 105 604 462 958 6 139 -114 C
ATOM 883 NE2 HIS A 105 5.469 0.299 2.201 1.00 5.23 N
ANISOU 883 NE2 HIS A 105 832 561 594 170 80 -86 N
ATOM 884 N ASP A 106 2.307 -2.633 1.792 1.00 7.28 N
ANISOU 884 N ASP A 106 861 911 993 203 189 5 N
ATOM 885 CA ASP A 106 1.563 -2.615 3.087 1.00 6.97 C
ANISOU 885 CA ASP A 106 555 1191 904 48 29 -132 C
ATOM 886 C ASP A 106 0.120 -3.125 2.933 1.00 6.14 C
ANISOU 886 C ASP A 106 603 690 1039 113 50 -35 C
ATOM 887 O ASP A 106 -0.076 -4.214 2.372 1.00 6.92 O
ANISOU 887 O ASP A 106 744 848 1039 56 190 -192 O
ATOM 888 CB ASP A 106 1.713 -1.200 3.687 1.00 6.88 C
ANISOU 888 CB ASP A 106 379 1214 1022 -2 125 -196 C
ATOM 889 CG ASP A 106 1.150 -1.088 5.079 1.00 7.81 C
ANISOU 889 CG ASP A 106 587 1376 1003 218 76 -204 C
ATOM 890 OD1 ASP A 106 1.748 -1.772 5.956 1.00 9.09 O
ANISOU 890 OD1 ASP A 106 1089 1251 1114 317 47 -27 O
ATOM 891 OD2 ASP A 106 0.101 -0.413 5.258 1.00 6.34 O
ANISOU 891 OD2 ASP A 106 687 633 1090 1 252 -237 O
ATOM 892 N TRP A 107 -0.877 -2.366 3.340 1.00 4.51 N
ANISOU 892 N TRP A 107 581 508 624 -20 180 79 N
ATOM 893 CA TRP A 107 -2.269 -2.832 3.127 1.00 4.48 C
ANISOU 893 CA TRP A 107 651 406 646 -77 311 -51 C
ATOM 894 C TRP A 107 -2.616 -2.876 1.661 1.00 3.79 C
ANISOU 894 C TRP A 107 553 208 680 72 159 -63 C
ATOM 895 O TRP A 107 -3.492 -3.640 1.290 1.00 5.35 O
ANISOU 895 O TRP A 107 715 513 804 -50 189 -32 O
ATOM 896 CB TRP A 107 -3.237 -1.972 3.954 1.00 5.03 C
ANISOU 896 CB TRP A 107 662 587 664 113 297 8 C
ATOM 897 CG TRP A 107 -3.149 -2.384 5.392 1.00 4.65 C
ANISOU 897 CG TRP A 107 636 508 623 24 257 -7 C
ATOM 898 CD1 TRP A 107 -2.598 -1.733 6.426 1.00 4.36 C
ANISOU 898 CD1 TRP A 107 628 315 712 86 413 -138 C
ATOM 899 CD2 TRP A 107 -3.674 -3.612 5.903 1.00 4.05 C
ANISOU 899 CD2 TRP A 107 586 276 676 185 230 -114 C
ATOM 900 NE1 TRP A 107 -2.734 -2.476 7.591 1.00 4.89 N
ANISOU 900 NE1 TRP A 107 655 614 590 78 198 -79 N
ATOM 901 CE2 TRP A 107 -3.395 -3.636 7.277 1.00 4.49 C
ANISOU 901 CE2 TRP A 107 457 613 637 20 345 8 C
ATOM 902 CE3 TRP A 107 -4.360 -4.703 5.338 1.00 6.16 C
ANISOU 902 CE3 TRP A 107 890 574 878 -224 276 -78 C
ATOM 903 CZ2 TRP A 107 -3.774 -4.706 8.085 1.00 5.08 C
ANISOU 903 CZ2 TRP A 107 706 507 720 165 315 -11 C
ATOM 904 CZ3 TRP A 107 -4.720 -5.755 6.151 1.00 6.24 C
ANISOU 904 CZ3 TRP A 107 929 510 934 -169 270 -84 C
ATOM 905 CH2 TRP A 107 -4.428 -5.749 7.504 1.00 6.16 C
ANISOU 905 CH2 TRP A 107 917 527 896 18 427 -39 C
ATOM 906 N GLY A 108 -1.960 -2.114 0.805 1.00 4.65 N
ANISOU 906 N GLY A 108 704 419 645 -19 320 -100 N
ATOM 907 CA GLY A 108 -2.153 -2.296 -0.611 1.00 5.09 C
ANISOU 907 CA GLY A 108 681 564 688 121 279 -105 C
ATOM 908 C GLY A 108 -1.697 -3.648 -1.133 1.00 4.44 C
ANISOU 908 C GLY A 108 630 487 569 -8 250 -16 C
ATOM 909 O GLY A 108 -2.254 -4.191 -2.084 1.00 5.15 O
ANISOU 909 O GLY A 108 693 602 664 -7 244 -121 O
ATOM 910 N SER A 109 -0.688 -4.184 -0.475 1.00 4.63 N
ANISOU 910 N SER A 109 641 450 669 77 221 -38 N
ATOM 911 CA SER A 109 -0.225 -5.533 -0.793 1.00 5.12 C
ANISOU 911 CA SER A 109 704 400 841 -27 87 -164 C
ATOM 912 C SER A 109 -1.183 -6.604 -0.304 1.00 4.77 C
ANISOU 912 C SER A 109 639 416 758 78 197 -51 C
ATOM 913 O SER A 109 -1.411 -7.585 -1.013 1.00 5.30 O
ANISOU 913 O SER A 109 738 433 844 -21 227 -26 O
ATOM 914 CB SER A 109 1.201 -5.837 -0.316 1.00 5.01 C
ANISOU 914 CB SER A 109 660 321 922 39 239 -145 C
ATOM 915 OG SER A 109 1.309 -6.007 1.074 1.00 6.46 O
ANISOU 915 OG SER A 109 815 702 939 157 -2 -149 O
ATOM 916 N ALA A 110 -1.778 -6.425 0.877 1.00 5.37 N
ANISOU 916 N ALA A 110 667 534 839 -28 145 -176 N
ATOM 917 CA ALA A 110 -2.804 -7.385 1.316 1.00 4.92 C
ANISOU 917 CA ALA A 110 677 376 815 29 168 -42 C
ATOM 918 C ALA A 110 -3.951 -7.353 0.331 1.00 4.87 C
ANISOU 918 C ALA A 110 548 436 866 104 223 -100 C
ATOM 919 O ALA A 110 -4.456 -8.389 -0.104 1.00 5.40 O
ANISOU 919 O ALA A 110 741 481 831 15 104 -51 O
ATOM 920 CB ALA A 110 -3.231 -7.077 2.732 1.00 5.78 C
ANISOU 920 CB ALA A 110 647 672 879 174 127 -41 C
ATOM 921 N LEU A 111 -4.397 -6.167 -0.072 1.00 4.95 N
ANISOU 921 N LEU A 111 604 467 809 10 114 -104 N
ATOM 922 CA LEU A 111 -5.453 -6.062 -1.073 1.00 4.99 C
ANISOU 922 CA LEU A 111 672 392 833 48 61 -91 C
ATOM 923 C LEU A 111 -5.037 -6.662 -2.397 1.00 4.83 C
ANISOU 923 C LEU A 111 695 361 779 33 99 15 C
ATOM 924 O LEU A 111 -5.804 -7.422 -3.018 1.00 5.41 O
ANISOU 924 O LEU A 111 666 450 942 -47 179 -183 O
ATOM 925 CB LEU A 111 -5.852 -4.589 -1.272 1.00 5.45 C
ANISOU 925 CB LEU A 111 613 521 936 126 117 -85 C
ATOM 926 CG LEU A 111 -6.625 -3.970 -0.107 1.00 6.11 C
ANISOU 926 CG LEU A 111 797 453 1073 -26 262 -239 C
ATOM 927 CD1 LEU A 111 -6.587 -2.455 -0.183 1.00 6.77 C
ANISOU 927 CD1 LEU A 111 677 462 1431 187 242 -19 C
ATOM 928 CD2 LEU A 111 -8.065 -4.479 -0.044 1.00 6.79 C
ANISOU 928 CD2 LEU A 111 726 672 1181 42 300 -181 C
ATOM 929 N GLY A 112 -3.852 -6.344 -2.870 1.00 5.02 N
ANISOU 929 N GLY A 112 552 610 744 90 24 -61 N
ATOM 930 CA GLY A 112 -3.403 -6.842 -4.158 1.00 5.37 C
ANISOU 930 CA GLY A 112 856 476 709 -12 179 66 C
ATOM 931 C GLY A 112 -3.199 -8.340 -4.187 1.00 4.85 C
ANISOU 931 C GLY A 112 629 474 741 -18 148 -41 C
ATOM 932 O GLY A 112 -3.621 -9.000 -5.129 1.00 6.00 O
ANISOU 932 O GLY A 112 847 613 819 46 72 -130 O
ATOM 933 N PHE A 113 -2.577 -8.899 -3.162 1.00 4.90 N
ANISOU 933 N PHE A 113 716 445 700 194 197 -173 N
ATOM 934 CA PHE A 113 -2.353 -10.340 -3.128 1.00 5.17 C
ANISOU 934 CA PHE A 113 652 494 816 186 187 -88 C
ATOM 935 C PHE A 113 -3.669 -11.081 -2.943 1.00 5.14 C
ANISOU 935 C PHE A 113 706 598 648 56 97 -108 C
ATOM 936 O PHE A 113 -3.859 -12.140 -3.541 1.00 5.92 O
ANISOU 936 O PHE A 113 919 543 787 83 95 -49 O
ATOM 937 CB PHE A 113 -1.418 -10.737 -2.002 1.00 5.01 C
ANISOU 937 CB PHE A 113 661 465 777 110 115 -100 C
ATOM 938 CG PHE A 113 0.054 -10.390 -2.187 1.00 5.23 C
ANISOU 938 CG PHE A 113 700 574 715 -13 117 147 C
ATOM 939 CD1 PHE A 113 0.710 -10.666 -3.368 1.00 5.49 C
ANISOU 939 CD1 PHE A 113 744 552 789 131 120 117 C
ATOM 940 CD2 PHE A 113 0.762 -9.819 -1.150 1.00 5.81 C
ANISOU 940 CD2 PHE A 113 737 442 1030 45 113 -137 C
ATOM 941 CE1 PHE A 113 2.079 -10.411 -3.476 1.00 6.49 C
ANISOU 941 CE1 PHE A 113 803 540 1124 77 363 -72 C
ATOM 942 CE2 PHE A 113 2.126 -9.562 -1.248 1.00 6.34 C
ANISOU 942 CE2 PHE A 113 729 547 1134 22 64 -45 C
ATOM 943 CZ PHE A 113 2.776 -9.840 -2.433 1.00 6.32 C
ANISOU 943 CZ PHE A 113 744 419 1238 70 192 48 C
ATOM 944 N HIS A 114 -4.576 -10.513 -2.163 1.00 5.40 N
ANISOU 944 N HIS A 114 583 644 823 102 170 -19 N
ATOM 945 CA HIS A 114 -5.886 -11.138 -1.986 1.00 5.78 C
ANISOU 945 CA HIS A 114 739 570 887 3 177 -140 C
ATOM 946 C HIS A 114 -6.668 -11.118 -3.293 1.00 5.13 C
ANISOU 946 C HIS A 114 599 460 892 -110 217 -54 C
ATOM 947 O HIS A 114 -7.326 -12.099 -3.666 1.00 6.49 O
ANISOU 947 O HIS A 114 829 534 1102 -166 62 -128 O
ATOM 948 CB HIS A 114 -6.655 -10.474 -0.872 1.00 5.88 C
ANISOU 948 CB HIS A 114 712 701 822 10 300 47 C
ATOM 949 CG HIS A 114 -7.968 -11.097 -0.534 1.00 5.96 C
ANISOU 949 CG HIS A 114 753 598 914 -20 215 80 C
ATOM 950 ND1 HIS A 114 -8.093 -12.432 -0.163 1.00 6.81 N
ANISOU 950 ND1 HIS A 114 927 636 1024 -115 244 31 N
ATOM 951 CD2 HIS A 114 -9.154 -10.471 -0.467 1.00 6.55 C
ANISOU 951 CD2 HIS A 114 670 751 1067 -86 316 56 C
ATOM 952 CE1 HIS A 114 -9.370 -12.636 0.087 1.00 7.84 C
ANISOU 952 CE1 HIS A 114 879 641 1460 -153 216 -20 C
ATOM 953 NE2 HIS A 114 -10.048 -11.503 -0.080 1.00 7.94 N
ANISOU 953 NE2 HIS A 114 812 767 1436 -147 267 93 N
ATOM 954 N TRP A 115 -6.571 -10.035 -4.042 1.00 5.44 N
ANISOU 954 N TRP A 115 659 502 907 -34 251 -81 N
ATOM 955 CA TRP A 115 -7.243 -9.951 -5.353 1.00 5.87 C
ANISOU 955 CA TRP A 115 711 600 921 23 199 -62 C
ATOM 956 C TRP A 115 -6.590 -10.933 -6.326 1.00 5.16 C
ANISOU 956 C TRP A 115 817 360 786 56 105 78 C
ATOM 957 O TRP A 115 -7.280 -11.606 -7.086 1.00 6.23 O
ANISOU 957 O TRP A 115 858 452 1058 74 5 -85 O
ATOM 958 CB TRP A 115 -7.224 -8.504 -5.869 1.00 5.88 C
ANISOU 958 CB TRP A 115 747 555 934 118 171 -110 C
ATOM 959 CG TRP A 115 -8.064 -8.277 -7.079 1.00 5.86 C
ANISOU 959 CG TRP A 115 805 480 942 36 138 -120 C
ATOM 960 CD1 TRP A 115 -9.390 -7.936 -7.053 1.00 6.56 C
ANISOU 960 CD1 TRP A 115 723 781 987 -51 131 -111 C
ATOM 961 CD2 TRP A 115 -7.669 -8.357 -8.445 1.00 6.68 C
ANISOU 961 CD2 TRP A 115 987 574 977 119 182 -149 C
ATOM 962 NE1 TRP A 115 -9.842 -7.800 -8.332 1.00 7.41 N
ANISOU 962 NE1 TRP A 115 924 778 1112 31 18 51 N
ATOM 963 CE2 TRP A 115 -8.814 -8.064 -9.202 1.00 6.54 C
ANISOU 963 CE2 TRP A 115 1179 319 987 111 48 -22 C
ATOM 964 CE3 TRP A 115 -6.493 -8.667 -9.134 1.00 7.57 C
ANISOU 964 CE3 TRP A 115 1004 796 1076 -152 403 -23 C
ATOM 965 CZ2 TRP A 115 -8.837 -8.051 -10.582 1.00 8.60 C
ANISOU 965 CZ2 TRP A 115 1269 956 1042 6 85 -60 C
ATOM 966 CZ3 TRP A 115 -6.534 -8.645 -10.523 1.00 8.20 C
ANISOU 966 CZ3 TRP A 115 1196 831 1087 -158 356 65 C
ATOM 967 CH2 TRP A 115 -7.672 -8.342 -11.237 1.00 8.63 C
ANISOU 967 CH2 TRP A 115 1383 688 1209 114 239 -27 C
ATOM 968 N ALA A 116 -5.255 -10.975 -6.316 1.00 5.84 N
ANISOU 968 N ALA A 116 788 706 724 29 179 -33 N
ATOM 969 CA ALA A 116 -4.551 -11.878 -7.240 1.00 5.98 C
ANISOU 969 CA ALA A 116 904 575 793 110 193 39 C
ATOM 970 C ALA A 116 -4.890 -13.337 -7.004 1.00 6.43 C
ANISOU 970 C ALA A 116 845 636 963 35 89 -24 C
ATOM 971 O ALA A 116 -5.122 -14.116 -7.934 1.00 6.96 O
ANISOU 971 O ALA A 116 969 615 1060 56 53 -123 O
ATOM 972 CB ALA A 116 -3.060 -11.655 -7.123 1.00 6.80 C
ANISOU 972 CB ALA A 116 889 528 1167 57 257 -140 C
ATOM 973 N LYS A 117 -4.934 -13.754 -5.724 1.00 5.80 N
ANISOU 973 N LYS A 117 835 387 983 38 63 -77 N
ATOM 974 CA LYS A 117 -5.299 -15.109 -5.393 1.00 6.47 C
ANISOU 974 CA LYS A 117 880 345 1234 81 205 -51 C
ATOM 975 C LYS A 117 -6.650 -15.485 -5.964 1.00 6.95 C
ANISOU 975 C LYS A 117 937 661 1042 -106 307 -179 C
ATOM 976 O LYS A 117 -6.883 -16.598 -6.451 1.00 8.50 O
ANISOU 976 O LYS A 117 1312 613 1307 -127 42 -166 O
ATOM 977 CB LYS A 117 -5.301 -15.269 -3.863 1.00 8.57 C
ANISOU 977 CB LYS A 117 1419 516 1321 -122 -143 103 C
ATOM 978 CG LYS A 117 -5.681 -16.706 -3.449 1.00 12.95 C
ANISOU 978 CG LYS A 117 2944 457 1520 -305 -676 338 C
ATOM 979 CD LYS A 117 -6.217 -16.823 -2.048 1.00 13.65 C
ANISOU 979 CD LYS A 117 2472 614 2099 -380 -16 411 C
ATOM 980 CE LYS A 117 -7.637 -16.322 -1.905 1.00 15.48 C
ANISOU 980 CE LYS A 117 2179 1631 2071 -244 -940 493 C
ATOM 981 NZ LYS A 117 -8.195 -16.483 -0.479 1.00 13.99 N
ANISOU 981 NZ LYS A 117 1926 1000 2388 -116 -446 62 N
ATOM 982 N ARG A 118 -7.595 -14.536 -5.885 1.00 7.19 N
ANISOU 982 N ARG A 118 843 558 1333 -144 138 -108 N
ATOM 983 CA ARG A 118 -8.947 -14.742 -6.354 1.00 7.54 C
ANISOU 983 CA ARG A 118 919 642 1305 -177 159 -31 C
ATOM 984 C ARG A 118 -9.080 -14.562 -7.855 1.00 8.00 C
ANISOU 984 C ARG A 118 1128 653 1257 -69 108 -167 C
ATOM 985 O ARG A 118 -10.074 -15.018 -8.425 1.00 11.71 O
ANISOU 985 O ARG A 118 1488 1527 1435 -591 11 -141 O
ATOM 986 CB ARG A 118 -9.884 -13.765 -5.626 1.00 8.29 C
ANISOU 986 CB ARG A 118 870 990 1289 -36 93 -109 C
ATOM 987 CG ARG A 118 -10.021 -14.075 -4.159 1.00 7.16 C
ANISOU 987 CG ARG A 118 702 647 1370 -76 212 8 C
ATOM 988 CD ARG A 118 -10.912 -13.099 -3.438 1.00 7.40 C
ANISOU 988 CD ARG A 118 748 640 1425 -124 233 -34 C
ATOM 989 NE ARG A 118 -10.370 -11.754 -3.471 1.00 7.50 N
ANISOU 989 NE ARG A 118 675 640 1534 -48 123 -130 N
ATOM 990 CZ ARG A 118 -11.045 -10.619 -3.693 1.00 7.95 C
ANISOU 990 CZ ARG A 118 690 596 1735 45 165 -294 C
ATOM 991 NH1 ARG A 118 -12.371 -10.615 -3.931 1.00 9.57 N
ANISOU 991 NH1 ARG A 118 665 945 2028 24 35 -255 N
ATOM 992 NH2 ARG A 118 -10.412 -9.437 -3.693 1.00 6.98 N
ANISOU 992 NH2 ARG A 118 899 658 1094 -108 271 8 N
ATOM 993 N ASN A 119 -8.142 -13.940 -8.536 1.00 7.73 N
ANISOU 993 N ASN A 119 1170 643 1123 -118 55 -188 N
ATOM 994 CA ASN A 119 -8.191 -13.610 -9.946 1.00 7.97 C
ANISOU 994 CA ASN A 119 992 840 1196 -112 -42 -85 C
ATOM 995 C ASN A 119 -6.845 -13.898 -10.633 1.00 7.54 C
ANISOU 995 C ASN A 119 1028 730 1109 -7 9 -133 C
ATOM 996 O ASN A 119 -6.328 -12.995 -11.272 1.00 8.01 O
ANISOU 996 O ASN A 119 1189 771 1084 -97 49 -99 O
ATOM 997 CB ASN A 119 -8.527 -12.131 -10.173 1.00 7.75 C
ANISOU 997 CB ASN A 119 944 931 1072 178 -181 -146 C
ATOM 998 CG ASN A 119 -9.901 -11.834 -9.599 1.00 8.45 C
ANISOU 998 CG ASN A 119 902 1010 1299 -46 -78 28 C
ATOM 999 OD1 ASN A 119 -10.890 -12.117 -10.249 1.00 14.00 O
ANISOU 999 OD1 ASN A 119 971 2022 2326 316 -488 -767 O
ATOM 1000 ND2 ASN A 119 -9.921 -11.242 -8.405 1.00 8.51 N
ANISOU 1000 ND2 ASN A 119 850 893 1490 -97 208 -127 N
ATOM 1001 N PRO A 120 -6.302 -15.094 -10.452 1.00 7.62 N
ANISOU 1001 N PRO A 120 1039 781 1075 -79 18 29 N
ATOM 1002 CA PRO A 120 -4.909 -15.283 -10.813 1.00 8.22 C
ANISOU 1002 CA PRO A 120 1100 768 1256 9 110 -29 C
ATOM 1003 C PRO A 120 -4.692 -15.158 -12.308 1.00 8.67 C
ANISOU 1003 C PRO A 120 1116 982 1197 113 87 -131 C
ATOM 1004 O PRO A 120 -3.601 -14.765 -12.706 1.00 9.57 O
ANISOU 1004 O PRO A 120 980 1607 1049 170 65 -289 O
ATOM 1005 CB PRO A 120 -4.604 -16.699 -10.305 1.00 9.08 C
ANISOU 1005 CB PRO A 120 1435 694 1319 125 175 -171 C
ATOM 1006 CG PRO A 120 -5.960 -17.381 -10.341 1.00 10.83 C
ANISOU 1006 CG PRO A 120 1551 783 1781 -6 502 -30 C
ATOM 1007 CD PRO A 120 -6.893 -16.305 -9.864 1.00 8.92 C
ANISOU 1007 CD PRO A 120 1360 784 1246 -70 259 -39 C
ATOM 1008 N GLU A 121 -5.696 -15.438 -13.110 1.00 9.02 N
ANISOU 1008 N GLU A 121 1258 826 1341 -147 61 -184 N
ATOM 1009 CA GLU A 121 -5.523 -15.336 -14.547 1.00 9.73 C
ANISOU 1009 CA GLU A 121 1478 924 1293 349 -148 -248 C
ATOM 1010 C GLU A 121 -5.420 -13.908 -15.050 1.00 8.91 C
ANISOU 1010 C GLU A 121 1128 1043 1214 -197 199 -240 C
ATOM 1011 O GLU A 121 -5.126 -13.636 -16.212 1.00 12.41 O
ANISOU 1011 O GLU A 121 1971 1515 1230 -290 339 -207 O
ATOM 1012 CB GLU A 121 -6.678 -16.054 -15.272 1.00 11.61 C
ANISOU 1012 CB GLU A 121 1877 1192 1343 -466 147 -339 C
ATOM 1013 CG GLU A 121 -8.016 -15.380 -15.358 1.00 21.83 C
ANISOU 1013 CG GLU A 121 1618 4461 2215 44 -327 -306 C
ATOM 1014 CD GLU A 121 -8.782 -15.133 -14.060 1.00 21.90 C
ANISOU 1014 CD GLU A 121 1778 3662 2879 381 233 -323 C
ATOM 1015 OE1 GLU A 121 -8.484 -15.642 -12.949 1.00 19.90 O
ANISOU 1015 OE1 GLU A 121 2515 2603 2442 -1207 272 -474 O
ATOM 1016 OE2 GLU A 121 -9.785 -14.393 -14.181 1.00 28.50 O
ANISOU 1016 OE2 GLU A 121 2921 2039 5870 692 606 -534 O
ATOM 1017 N ARG A 122 -5.729 -12.950 -14.177 1.00 7.58 N
ANISOU 1017 N ARG A 122 1012 825 1043 -78 -52 -85 N
ATOM 1018 CA ARG A 122 -5.729 -11.538 -14.534 1.00 8.28 C
ANISOU 1018 CA ARG A 122 918 899 1330 -80 -93 126 C
ATOM 1019 C ARG A 122 -4.499 -10.789 -14.026 1.00 9.37 C
ANISOU 1019 C ARG A 122 1076 774 1711 25 -387 -132 C
ATOM 1020 O ARG A 122 -4.446 -9.570 -14.153 1.00 11.14 O
ANISOU 1020 O ARG A 122 1260 813 2160 -72 -468 311 O
ATOM 1021 CB ARG A 122 -6.996 -10.901 -13.972 1.00 8.66 C
ANISOU 1021 CB ARG A 122 1045 842 1403 -84 -72 6 C
ATOM 1022 CG ARG A 122 -8.237 -11.353 -14.749 1.00 8.94 C
ANISOU 1022 CG ARG A 122 948 741 1707 -18 -86 -161 C
ATOM 1023 CD ARG A 122 -9.499 -11.003 -13.983 1.00 10.72 C
ANISOU 1023 CD ARG A 122 1000 1129 1942 41 -29 -254 C
ATOM 1024 NE ARG A 122 -9.817 -9.584 -14.045 1.00 9.18 N
ANISOU 1024 NE ARG A 122 902 1186 1399 144 52 -112 N
ATOM 1025 CZ ARG A 122 -10.796 -9.033 -13.343 1.00 8.72 C
ANISOU 1025 CZ ARG A 122 729 1326 1259 150 -95 -144 C
ATOM 1026 NH1 ARG A 122 -11.520 -9.766 -12.507 1.00 11.80 N
ANISOU 1026 NH1 ARG A 122 956 1824 1701 -20 160 -45 N
ATOM 1027 NH2 ARG A 122 -11.064 -7.746 -13.457 1.00 11.18 N
ANISOU 1027 NH2 ARG A 122 1307 1338 1602 408 -431 -275 N
ATOM 1028 N VAL A 123 -3.535 -11.518 -13.470 1.00 7.12 N
ANISOU 1028 N VAL A 123 889 678 1138 107 -20 -236 N
ATOM 1029 CA VAL A 123 -2.358 -10.827 -12.939 1.00 6.99 C
ANISOU 1029 CA VAL A 123 886 742 1028 22 -65 -89 C
ATOM 1030 C VAL A 123 -1.134 -11.264 -13.730 1.00 6.75 C
ANISOU 1030 C VAL A 123 883 676 1005 150 -144 -32 C
ATOM 1031 O VAL A 123 -0.730 -12.430 -13.679 1.00 8.54 O
ANISOU 1031 O VAL A 123 1337 688 1221 274 -38 -36 O
ATOM 1032 CB VAL A 123 -2.177 -11.106 -11.451 1.00 7.71 C
ANISOU 1032 CB VAL A 123 893 947 1089 65 -53 45 C
ATOM 1033 CG1 VAL A 123 -0.888 -10.461 -10.937 1.00 7.33 C
ANISOU 1033 CG1 VAL A 123 927 993 865 135 -36 -114 C
ATOM 1034 CG2 VAL A 123 -3.342 -10.598 -10.647 1.00 10.56 C
ANISOU 1034 CG2 VAL A 123 991 1830 1189 -41 88 -305 C
ATOM 1035 N LYS A 124 -0.551 -10.307 -14.450 1.00 6.77 N
ANISOU 1035 N LYS A 124 757 629 1185 224 -9 -140 N
ATOM 1036 CA LYS A 124 0.609 -10.601 -15.296 1.00 6.47 C
ANISOU 1036 CA LYS A 124 890 526 1040 173 33 -272 C
ATOM 1037 C LYS A 124 1.943 -10.442 -14.560 1.00 5.60 C
ANISOU 1037 C LYS A 124 781 755 590 6 257 -75 C
ATOM 1038 O LYS A 124 2.976 -10.917 -15.033 1.00 7.06 O
ANISOU 1038 O LYS A 124 868 917 898 50 271 -205 O
ATOM 1039 CB LYS A 124 0.603 -9.697 -16.511 1.00 9.06 C
ANISOU 1039 CB LYS A 124 1106 1197 1138 329 -40 72 C
ATOM 1040 CG LYS A 124 -0.455 -9.895 -17.600 1.00 14.39 C
ANISOU 1040 CG LYS A 124 1923 2139 1404 336 -581 -7 C
ATOM 1041 CD LYS A 124 0.131 -9.466 -18.978 1.00 20.78 C
ANISOU 1041 CD LYS A 124 2328 4350 1216 -72 -324 -381 C
ATOM 1042 CE LYS A 124 -0.950 -9.319 -20.028 1.00 20.16 C
ANISOU 1042 CE LYS A 124 2319 4237 1103 -570 -186 150 C
ATOM 1043 NZ LYS A 124 -0.426 -8.853 -21.331 1.00 15.69 N
ANISOU 1043 NZ LYS A 124 2305 2059 1599 311 230 296 N
ATOM 1044 N GLY A 125 1.950 -9.776 -13.419 1.00 5.44 N
ANISOU 1044 N GLY A 125 852 491 723 73 170 -97 N
ATOM 1045 CA GLY A 125 3.157 -9.594 -12.629 1.00 5.50 C
ANISOU 1045 CA GLY A 125 890 547 654 58 208 -115 C
ATOM 1046 C GLY A 125 2.821 -8.873 -11.342 1.00 4.63 C
ANISOU 1046 C GLY A 125 731 340 688 213 86 -55 C
ATOM 1047 O GLY A 125 1.824 -8.167 -11.292 1.00 4.76 O
ANISOU 1047 O GLY A 125 586 500 721 157 55 -63 O
ATOM 1048 N ILE A 126 3.650 -9.049 -10.319 1.00 4.48 N
ANISOU 1048 N ILE A 126 554 435 712 99 73 -126 N
ATOM 1049 CA ILE A 126 3.479 -8.345 -9.071 1.00 4.72 C
ANISOU 1049 CA ILE A 126 645 456 692 166 86 -113 C
ATOM 1050 C ILE A 126 4.806 -7.740 -8.647 1.00 4.82 C
ANISOU 1050 C ILE A 126 672 524 636 111 27 -67 C
ATOM 1051 O ILE A 126 5.780 -8.470 -8.404 1.00 5.37 O
ANISOU 1051 O ILE A 126 659 555 826 160 138 -138 O
ATOM 1052 CB ILE A 126 2.941 -9.244 -7.926 1.00 5.97 C
ANISOU 1052 CB ILE A 126 812 681 774 70 250 -133 C
ATOM 1053 CG1 ILE A 126 1.647 -9.937 -8.363 1.00 5.74 C
ANISOU 1053 CG1 ILE A 126 767 580 832 147 305 -122 C
ATOM 1054 CG2 ILE A 126 2.798 -8.402 -6.676 1.00 6.78 C
ANISOU 1054 CG2 ILE A 126 1348 403 826 30 390 -71 C
ATOM 1055 CD1 ILE A 126 1.063 -10.940 -7.364 1.00 7.08 C
ANISOU 1055 CD1 ILE A 126 1004 678 1010 -32 278 -115 C
ATOM 1056 N ALA A 127 4.861 -6.426 -8.575 1.00 4.57 N
ANISOU 1056 N ALA A 127 726 466 544 34 8 61 N
ATOM 1057 CA ALA A 127 5.940 -5.693 -7.946 1.00 4.62 C
ANISOU 1057 CA ALA A 127 583 584 589 60 106 16 C
ATOM 1058 C ALA A 127 5.489 -5.346 -6.520 1.00 4.59 C
ANISOU 1058 C ALA A 127 682 451 612 190 118 -144 C
ATOM 1059 O ALA A 127 4.393 -4.824 -6.342 1.00 5.58 O
ANISOU 1059 O ALA A 127 696 745 680 313 77 -54 O
ATOM 1060 CB ALA A 127 6.288 -4.439 -8.735 1.00 5.34 C
ANISOU 1060 CB ALA A 127 807 613 609 -16 -45 112 C
ATOM 1061 N CYS A 128 6.300 -5.720 -5.536 1.00 4.39 N
ANISOU 1061 N CYS A 128 582 497 590 193 130 -169 N
ATOM 1062 CA CYS A 128 5.895 -5.562 -4.146 1.00 5.03 C
ANISOU 1062 CA CYS A 128 554 768 591 96 161 -67 C
ATOM 1063 C CYS A 128 7.071 -5.076 -3.316 1.00 3.90 C
ANISOU 1063 C CYS A 128 495 472 514 202 175 -13 C
ATOM 1064 O CYS A 128 8.218 -5.164 -3.719 1.00 4.62 O
ANISOU 1064 O CYS A 128 530 575 651 110 210 -192 O
ATOM 1065 CB CYS A 128 5.276 -6.842 -3.594 1.00 5.49 C
ANISOU 1065 CB CYS A 128 574 824 688 50 193 -121 C
ATOM 1066 SG CYS A 128 6.352 -8.291 -3.695 1.00 7.47 S
ANISOU 1066 SG CYS A 128 864 749 1224 73 152 -18 S
ATOM 1067 N MET A 129 6.738 -4.562 -2.149 1.00 4.98 N
ANISOU 1067 N MET A 129 573 693 625 62 222 -167 N
ATOM 1068 CA MET A 129 7.725 -4.006 -1.253 1.00 4.85 C
ANISOU 1068 CA MET A 129 698 559 583 278 187 -236 C
ATOM 1069 C MET A 129 7.082 -3.906 0.119 1.00 4.61 C
ANISOU 1069 C MET A 129 650 476 625 225 137 -143 C
ATOM 1070 O MET A 129 5.938 -3.473 0.156 1.00 5.02 O
ANISOU 1070 O MET A 129 542 736 631 279 148 -61 O
ATOM 1071 CB MET A 129 8.201 -2.632 -1.779 1.00 6.55 C
ANISOU 1071 CB MET A 129 802 761 926 -9 362 -125 C
ATOM 1072 CG MET A 129 7.068 -1.596 -1.947 1.00 6.79 C
ANISOU 1072 CG MET A 129 1021 517 1042 64 537 -68 C
ATOM 1073 SD MET A 129 7.366 -0.439 -3.350 1.00 8.87 S
ANISOU 1073 SD MET A 129 1228 885 1258 57 360 153 S
ATOM 1074 CE MET A 129 6.926 -1.464 -4.715 1.00 9.85 C
ANISOU 1074 CE MET A 129 1076 1630 1036 275 164 -16 C
ATOM 1075 N GLU A 130 7.799 -4.272 1.171 1.00 4.32 N
ANISOU 1075 N GLU A 130 466 636 540 180 211 -30 N
ATOM 1076 CA GLU A 130 7.329 -4.011 2.545 1.00 4.82 C
ANISOU 1076 CA GLU A 130 526 703 604 75 252 -254 C
ATOM 1077 C GLU A 130 5.853 -4.428 2.698 1.00 4.47 C
ANISOU 1077 C GLU A 130 554 623 523 85 405 -225 C
ATOM 1078 O GLU A 130 4.971 -3.678 3.062 1.00 5.25 O
ANISOU 1078 O GLU A 130 552 547 894 14 389 -149 O
ATOM 1079 CB GLU A 130 7.593 -2.577 2.940 1.00 4.88 C
ANISOU 1079 CB GLU A 130 625 607 622 71 199 -30 C
ATOM 1080 CG GLU A 130 9.037 -2.378 3.406 1.00 4.88 C
ANISOU 1080 CG GLU A 130 651 624 581 53 155 -33 C
ATOM 1081 CD GLU A 130 9.279 -2.947 4.785 1.00 4.79 C
ANISOU 1081 CD GLU A 130 856 330 633 201 213 -44 C
ATOM 1082 OE1 GLU A 130 8.410 -2.709 5.682 1.00 4.93 O
ANISOU 1082 OE1 GLU A 130 766 566 542 256 223 59 O
ATOM 1083 OE2 GLU A 130 10.319 -3.633 4.997 1.00 5.32 O
ANISOU 1083 OE2 GLU A 130 750 580 690 194 242 69 O
ATOM 1084 N PHE A 131 5.632 -5.681 2.290 1.00 5.33 N
ANISOU 1084 N PHE A 131 427 644 955 101 277 -189 N
ATOM 1085 CA PHE A 131 4.291 -6.231 2.164 1.00 4.91 C
ANISOU 1085 CA PHE A 131 527 457 880 106 238 -34 C
ATOM 1086 C PHE A 131 3.897 -6.983 3.432 1.00 4.95 C
ANISOU 1086 C PHE A 131 683 325 874 66 128 -42 C
ATOM 1087 O PHE A 131 4.719 -7.335 4.291 1.00 6.59 O
ANISOU 1087 O PHE A 131 815 755 933 90 30 -18 O
ATOM 1088 CB PHE A 131 4.225 -7.102 0.917 1.00 5.42 C
ANISOU 1088 CB PHE A 131 526 714 819 181 67 -35 C
ATOM 1089 CG PHE A 131 4.998 -8.392 0.936 1.00 5.96 C
ANISOU 1089 CG PHE A 131 691 546 1027 159 231 -117 C
ATOM 1090 CD1 PHE A 131 4.536 -9.562 1.515 1.00 6.69 C
ANISOU 1090 CD1 PHE A 131 727 652 1162 35 40 -51 C
ATOM 1091 CD2 PHE A 131 6.251 -8.479 0.352 1.00 7.80 C
ANISOU 1091 CD2 PHE A 131 947 643 1373 239 545 -218 C
ATOM 1092 CE1 PHE A 131 5.221 -10.733 1.521 1.00 7.63 C
ANISOU 1092 CE1 PHE A 131 1026 570 1304 43 266 93 C
ATOM 1093 CE2 PHE A 131 6.965 -9.657 0.350 1.00 9.38 C
ANISOU 1093 CE2 PHE A 131 824 595 2143 150 645 -195 C
ATOM 1094 CZ PHE A 131 6.469 -10.798 0.943 1.00 9.77 C
ANISOU 1094 CZ PHE A 131 1019 688 2006 34 468 -89 C
ATOM 1095 N ILE A 132 2.599 -7.227 3.534 1.00 4.82 N
ANISOU 1095 N ILE A 132 714 482 637 47 164 112 N
ATOM 1096 CA ILE A 132 2.011 -7.899 4.683 1.00 4.96 C
ANISOU 1096 CA ILE A 132 838 613 433 198 254 -22 C
ATOM 1097 C ILE A 132 1.977 -9.410 4.481 1.00 5.83 C
ANISOU 1097 C ILE A 132 898 553 765 -12 187 99 C
ATOM 1098 O ILE A 132 1.411 -9.954 3.507 1.00 6.30 O
ANISOU 1098 O ILE A 132 1072 522 799 -49 193 36 O
ATOM 1099 CB ILE A 132 0.590 -7.369 4.990 1.00 5.93 C
ANISOU 1099 CB ILE A 132 748 689 814 78 262 -5 C
ATOM 1100 CG1 ILE A 132 0.668 -5.932 5.500 1.00 6.00 C
ANISOU 1100 CG1 ILE A 132 890 554 837 175 352 41 C
ATOM 1101 CG2 ILE A 132 -0.144 -8.285 5.967 1.00 7.33 C
ANISOU 1101 CG2 ILE A 132 850 608 1326 85 471 91 C
ATOM 1102 CD1 ILE A 132 -0.648 -5.228 5.613 1.00 6.74 C
ANISOU 1102 CD1 ILE A 132 811 774 975 169 314 -86 C
ATOM 1103 N ARG A 133 2.572 -10.103 5.418 1.00 6.12 N
ANISOU 1103 N ARG A 133 1079 531 716 6 239 111 N
ATOM 1104 CA ARG A 133 2.457 -11.535 5.572 1.00 6.38 C
ANISOU 1104 CA ARG A 133 1174 388 861 190 338 -50 C
ATOM 1105 C ARG A 133 2.187 -11.777 7.047 1.00 5.94 C
ANISOU 1105 C ARG A 133 911 498 848 69 -29 181 C
ATOM 1106 O ARG A 133 2.266 -10.863 7.869 1.00 6.32 O
ANISOU 1106 O ARG A 133 939 651 812 65 190 8 O
ATOM 1107 CB ARG A 133 3.678 -12.246 5.060 1.00 10.28 C
ANISOU 1107 CB ARG A 133 1197 839 1870 203 471 -335 C
ATOM 1108 CG ARG A 133 4.925 -11.949 5.780 1.00 8.32 C
ANISOU 1108 CG ARG A 133 1264 800 1096 225 424 40 C
ATOM 1109 CD ARG A 133 6.092 -12.722 5.130 1.00 12.54 C
ANISOU 1109 CD ARG A 133 1353 977 2435 614 -12 -529 C
ATOM 1110 NE ARG A 133 7.252 -12.456 5.953 1.00 14.94 N
ANISOU 1110 NE ARG A 133 1148 1877 2649 130 233 -891 N
ATOM 1111 CZ ARG A 133 8.429 -13.049 5.743 1.00 11.06 C
ANISOU 1111 CZ ARG A 133 1306 1370 1524 340 145 5 C
ATOM 1112 NH1 ARG A 133 9.415 -12.726 6.555 1.00 15.46 N
ANISOU 1112 NH1 ARG A 133 1635 1822 2418 396 -441 -113 N
ATOM 1113 NH2 ARG A 133 8.538 -13.907 4.735 1.00 14.19 N
ANISOU 1113 NH2 ARG A 133 1969 1857 1564 468 431 -232 N
ATOM 1114 N PRO A 134 1.867 -13.006 7.461 1.00 6.40 N
ANISOU 1114 N PRO A 134 999 595 838 -78 330 45 N
ATOM 1115 CA PRO A 134 1.590 -13.185 8.907 1.00 6.27 C
ANISOU 1115 CA PRO A 134 886 678 819 -51 323 32 C
ATOM 1116 C PRO A 134 2.844 -12.884 9.714 1.00 6.36 C
ANISOU 1116 C PRO A 134 880 597 942 127 262 -102 C
ATOM 1117 O PRO A 134 3.951 -13.237 9.277 1.00 7.33 O
ANISOU 1117 O PRO A 134 910 821 1053 245 310 -102 O
ATOM 1118 CB PRO A 134 1.228 -14.663 9.009 1.00 7.99 C
ANISOU 1118 CB PRO A 134 1227 741 1068 -201 320 163 C
ATOM 1119 CG PRO A 134 0.779 -15.040 7.609 1.00 7.95 C
ANISOU 1119 CG PRO A 134 1401 486 1133 -28 195 115 C
ATOM 1120 CD PRO A 134 1.731 -14.262 6.765 1.00 7.09 C
ANISOU 1120 CD PRO A 134 1134 666 895 -80 58 -6 C
ATOM 1121 N ILE A 135 2.672 -12.252 10.853 1.00 5.89 N
ANISOU 1121 N ILE A 135 910 621 708 99 351 67 N
ATOM 1122 CA ILE A 135 3.753 -12.007 11.819 1.00 5.98 C
ANISOU 1122 CA ILE A 135 951 653 669 235 413 -71 C
ATOM 1123 C ILE A 135 3.419 -12.908 13.000 1.00 6.69 C
ANISOU 1123 C ILE A 135 1142 761 639 339 374 18 C
ATOM 1124 O ILE A 135 2.597 -12.526 13.824 1.00 7.09 O
ANISOU 1124 O ILE A 135 1184 771 740 194 499 -4 O
ATOM 1125 CB ILE A 135 3.871 -10.531 12.170 1.00 6.84 C
ANISOU 1125 CB ILE A 135 855 712 1031 111 441 -146 C
ATOM 1126 CG1 ILE A 135 4.006 -9.616 10.952 1.00 8.08 C
ANISOU 1126 CG1 ILE A 135 1421 574 1074 267 156 -73 C
ATOM 1127 CG2 ILE A 135 5.049 -10.394 13.137 1.00 8.64 C
ANISOU 1127 CG2 ILE A 135 1537 561 1183 15 0 60 C
ATOM 1128 CD1 ILE A 135 2.696 -9.007 10.482 1.00 10.74 C
ANISOU 1128 CD1 ILE A 135 1313 1194 1575 -118 -188 172 C
ATOM 1129 N PRO A 136 3.900 -14.156 13.020 1.00 7.46 N
ANISOU 1129 N PRO A 136 1110 742 983 287 495 75 N
ATOM 1130 CA PRO A 136 3.217 -15.112 13.913 1.00 8.10 C
ANISOU 1130 CA PRO A 136 1367 765 946 26 374 22 C
ATOM 1131 C PRO A 136 3.334 -14.841 15.407 1.00 7.70 C
ANISOU 1131 C PRO A 136 1283 704 941 116 392 -32 C
ATOM 1132 O PRO A 136 2.435 -15.306 16.160 1.00 7.71 O
ANISOU 1132 O PRO A 136 1277 612 1041 216 430 72 O
ATOM 1133 CB PRO A 136 3.886 -16.429 13.543 1.00 11.18 C
ANISOU 1133 CB PRO A 136 2300 737 1211 103 700 -92 C
ATOM 1134 CG PRO A 136 4.308 -16.188 12.116 1.00 14.75 C
ANISOU 1134 CG PRO A 136 3353 905 1347 293 1072 -98 C
ATOM 1135 CD PRO A 136 4.860 -14.779 12.114 1.00 8.97 C
ANISOU 1135 CD PRO A 136 1602 896 911 549 525 81 C
ATOM 1136 N THR A 137 4.354 -14.174 15.871 1.00 7.25 N
ANISOU 1136 N THR A 137 1097 806 851 231 423 -16 N
ATOM 1137 CA THR A 137 4.510 -13.771 17.256 1.00 7.19 C
ANISOU 1137 CA THR A 137 1087 781 864 346 312 17 C
ATOM 1138 C THR A 137 5.014 -12.352 17.328 1.00 6.41 C
ANISOU 1138 C THR A 137 932 844 660 237 220 79 C
ATOM 1139 O THR A 137 5.569 -11.822 16.341 1.00 7.97 O
ANISOU 1139 O THR A 137 1027 1080 921 169 362 154 O
ATOM 1140 CB THR A 137 5.484 -14.674 18.024 1.00 8.84 C
ANISOU 1140 CB THR A 137 1259 956 1143 352 214 255 C
ATOM 1141 OG1 THR A 137 6.746 -14.572 17.364 1.00 11.34 O
ANISOU 1141 OG1 THR A 137 1005 1528 1776 331 141 214 O
ATOM 1142 CG2 THR A 137 5.083 -16.129 17.979 1.00 9.42 C
ANISOU 1142 CG2 THR A 137 1489 902 1189 366 119 112 C
ATOM 1143 N TRP A 138 4.858 -11.670 18.442 1.00 7.27 N
ANISOU 1143 N TRP A 138 1132 830 800 420 190 18 N
ATOM 1144 CA TRP A 138 5.339 -10.304 18.613 1.00 7.49 C
ANISOU 1144 CA TRP A 138 1063 882 899 416 89 -4 C
ATOM 1145 C TRP A 138 6.843 -10.205 18.501 1.00 9.16 C
ANISOU 1145 C TRP A 138 1054 1099 1326 362 177 103 C
ATOM 1146 O TRP A 138 7.364 -9.173 18.079 1.00 9.24 O
ANISOU 1146 O TRP A 138 1254 1146 1109 230 26 97 O
ATOM 1147 CB TRP A 138 4.825 -9.680 19.916 1.00 7.58 C
ANISOU 1147 CB TRP A 138 1187 932 759 245 111 -48 C
ATOM 1148 CG TRP A 138 3.436 -9.111 19.745 1.00 7.44 C
ANISOU 1148 CG TRP A 138 1220 850 755 296 139 -97 C
ATOM 1149 CD1 TRP A 138 2.253 -9.596 20.200 1.00 7.72 C
ANISOU 1149 CD1 TRP A 138 1269 665 998 369 356 -125 C
ATOM 1150 CD2 TRP A 138 3.129 -7.910 19.034 1.00 7.88 C
ANISOU 1150 CD2 TRP A 138 1198 921 876 214 121 7 C
ATOM 1151 NE1 TRP A 138 1.219 -8.782 19.822 1.00 8.98 N
ANISOU 1151 NE1 TRP A 138 1260 955 1196 324 380 97 N
ATOM 1152 CE2 TRP A 138 1.743 -7.729 19.107 1.00 7.47 C
ANISOU 1152 CE2 TRP A 138 1170 888 779 210 175 -16 C
ATOM 1153 CE3 TRP A 138 3.898 -6.969 18.355 1.00 7.14 C
ANISOU 1153 CE3 TRP A 138 981 775 955 297 99 -74 C
ATOM 1154 CZ2 TRP A 138 1.101 -6.652 18.528 1.00 7.56 C
ANISOU 1154 CZ2 TRP A 138 1171 683 1020 255 334 -160 C
ATOM 1155 CZ3 TRP A 138 3.253 -5.878 17.763 1.00 7.42 C
ANISOU 1155 CZ3 TRP A 138 940 697 1181 272 35 -74 C
ATOM 1156 CH2 TRP A 138 1.881 -5.742 17.857 1.00 7.78 C
ANISOU 1156 CH2 TRP A 138 937 773 1246 224 67 63 C
ATOM 1157 N ASP A 139 7.544 -11.286 18.834 1.00 8.87 N
ANISOU 1157 N ASP A 139 933 1217 1218 361 150 206 N
ATOM 1158 CA ASP A 139 8.988 -11.235 18.668 1.00 10.00 C
ANISOU 1158 CA ASP A 139 831 1558 1410 173 -52 196 C
ATOM 1159 C ASP A 139 9.375 -11.151 17.199 1.00 10.91 C
ANISOU 1159 C ASP A 139 916 1710 1518 144 237 -47 C
ATOM 1160 O ASP A 139 10.481 -10.719 16.889 1.00 13.58 O
ANISOU 1160 O ASP A 139 1087 2298 1774 -36 192 378 O
ATOM 1161 CB ASP A 139 9.667 -12.452 19.289 1.00 13.54 C
ANISOU 1161 CB ASP A 139 977 1892 2276 521 -42 460 C
ATOM 1162 CG ASP A 139 9.763 -12.385 20.811 1.00 28.85 C
ANISOU 1162 CG ASP A 139 5239 3208 2514 1335 -2209 222 C
ATOM 1163 OD1 ASP A 139 10.005 -13.462 21.416 1.00 36.99 O
ANISOU 1163 OD1 ASP A 139 7542 3742 2771 1644 -953 1024 O
ATOM 1164 OD2 ASP A 139 9.606 -11.308 21.458 1.00 28.20 O
ANISOU 1164 OD2 ASP A 139 5114 3384 2215 331 -452 159 O
ATOM 1165 N GLU A 140 8.497 -11.525 16.290 1.00 9.10 N
ANISOU 1165 N GLU A 140 1124 1035 1300 89 398 -80 N
ATOM 1166 CA GLU A 140 8.765 -11.408 14.864 1.00 10.03 C
ANISOU 1166 CA GLU A 140 1148 1319 1344 336 478 -72 C
ATOM 1167 C GLU A 140 8.402 -10.052 14.253 1.00 9.55 C
ANISOU 1167 C GLU A 140 1059 1415 1156 316 218 -58 C
ATOM 1168 O GLU A 140 8.628 -9.810 13.047 1.00 10.87 O
ANISOU 1168 O GLU A 140 1396 1645 1091 362 342 -72 O
ATOM 1169 CB GLU A 140 8.096 -12.570 14.113 1.00 9.88 C
ANISOU 1169 CB GLU A 140 1065 1396 1293 428 298 -91 C
ATOM 1170 CG GLU A 140 8.707 -13.902 14.562 1.00 15.16 C
ANISOU 1170 CG GLU A 140 1746 1350 2664 766 46 -221 C
ATOM 1171 CD GLU A 140 7.940 -15.102 14.058 1.00 16.54 C
ANISOU 1171 CD GLU A 140 2148 1450 2688 408 1059 -614 C
ATOM 1172 OE1 GLU A 140 6.979 -15.589 14.727 1.00 17.67 O
ANISOU 1172 OE1 GLU A 140 1807 2025 2880 491 1041 -500 O
ATOM 1173 OE2 GLU A 140 8.281 -15.531 12.935 1.00 28.88 O
ANISOU 1173 OE2 GLU A 140 3534 3455 3982 -818 2449 -2190 O
ATOM 1174 N TRP A 141 7.864 -9.170 15.088 1.00 8.91 N
ANISOU 1174 N TRP A 141 1227 1172 985 252 334 132 N
ATOM 1175 CA TRP A 141 7.647 -7.760 14.759 1.00 8.35 C
ANISOU 1175 CA TRP A 141 1026 1225 921 221 256 177 C
ATOM 1176 C TRP A 141 8.898 -6.959 15.104 1.00 8.61 C
ANISOU 1176 C TRP A 141 1051 1173 1049 227 190 108 C
ATOM 1177 O TRP A 141 9.504 -7.296 16.128 1.00 10.09 O
ANISOU 1177 O TRP A 141 1153 1535 1146 -7 100 311 O
ATOM 1178 CB TRP A 141 6.446 -7.205 15.494 1.00 8.21 C
ANISOU 1178 CB TRP A 141 1098 1102 920 97 347 96 C
ATOM 1179 CG TRP A 141 6.011 -5.821 15.084 1.00 7.81 C
ANISOU 1179 CG TRP A 141 801 1144 1022 124 165 23 C
ATOM 1180 CD1 TRP A 141 6.324 -4.650 15.724 1.00 8.93 C
ANISOU 1180 CD1 TRP A 141 893 1235 1264 224 -88 -143 C
ATOM 1181 CD2 TRP A 141 5.203 -5.454 13.942 1.00 7.84 C
ANISOU 1181 CD2 TRP A 141 956 1166 858 334 221 -200 C
ATOM 1182 NE1 TRP A 141 5.758 -3.591 15.070 1.00 9.23 N
ANISOU 1182 NE1 TRP A 141 960 1184 1364 357 -99 -273 N
ATOM 1183 CE2 TRP A 141 5.064 -4.053 13.972 1.00 8.54 C
ANISOU 1183 CE2 TRP A 141 763 1179 1302 317 -36 -183 C
ATOM 1184 CE3 TRP A 141 4.601 -6.212 12.939 1.00 7.33 C
ANISOU 1184 CE3 TRP A 141 673 1127 986 -14 172 100 C
ATOM 1185 CZ2 TRP A 141 4.325 -3.368 13.000 1.00 7.78 C
ANISOU 1185 CZ2 TRP A 141 700 1102 1154 171 167 -78 C
ATOM 1186 CZ3 TRP A 141 3.881 -5.529 11.992 1.00 7.49 C
ANISOU 1186 CZ3 TRP A 141 1067 1099 682 183 285 17 C
ATOM 1187 CH2 TRP A 141 3.763 -4.139 12.036 1.00 7.19 C
ANISOU 1187 CH2 TRP A 141 539 1157 1035 171 212 19 C
ATOM 1188 N PRO A 142 9.341 -5.983 14.335 1.00 7.92 N
ANISOU 1188 N PRO A 142 1030 784 1195 393 88 40 N
ATOM 1189 CA PRO A 142 10.589 -5.292 14.665 1.00 9.77 C
ANISOU 1189 CA PRO A 142 1391 1038 1283 11 3 35 C
ATOM 1190 C PRO A 142 10.547 -4.635 16.045 1.00 10.18 C
ANISOU 1190 C PRO A 142 1261 1276 1331 399 -84 -59 C
ATOM 1191 O PRO A 142 9.596 -3.943 16.444 1.00 10.55 O
ANISOU 1191 O PRO A 142 1051 1594 1365 322 55 4 O
ATOM 1192 CB PRO A 142 10.735 -4.225 13.590 1.00 12.39 C
ANISOU 1192 CB PRO A 142 1957 1306 1445 -197 217 167 C
ATOM 1193 CG PRO A 142 9.807 -4.615 12.533 1.00 13.08 C
ANISOU 1193 CG PRO A 142 2063 1465 1440 -29 -19 420 C
ATOM 1194 CD PRO A 142 8.730 -5.449 13.108 1.00 9.32 C
ANISOU 1194 CD PRO A 142 1432 1016 1095 434 49 96 C
ATOM 1195 N GLU A 143 11.582 -4.853 16.841 1.00 10.41 N
ANISOU 1195 N GLU A 143 894 1913 1149 222 169 45 N
ATOM 1196 CA AGLU A 143 11.664 -4.386 18.227 0.60 11.58 C
ANISOU 1196 CA AGLU A 143 1147 2135 1117 415 157 30 C
ATOM 1197 CA BGLU A 143 11.655 -4.387 18.220 0.40 11.61 C
ANISOU 1197 CA BGLU A 143 1166 2134 1111 446 114 56 C
ATOM 1198 C GLU A 143 11.355 -2.898 18.340 1.00 11.34 C
ANISOU 1198 C GLU A 143 910 2151 1249 329 -91 -171 C
ATOM 1199 O GLU A 143 10.608 -2.491 19.203 1.00 13.52 O
ANISOU 1199 O GLU A 143 1485 2420 1234 495 6 -367 O
ATOM 1200 CB AGLU A 143 13.064 -4.658 18.808 0.60 19.14 C
ANISOU 1200 CB AGLU A 143 2097 3212 1962 1320 -869 -426 C
ATOM 1201 CB BGLU A 143 13.049 -4.660 18.815 0.40 18.03 C
ANISOU 1201 CB BGLU A 143 2063 3189 1599 1190 -707 131 C
ATOM 1202 CG AGLU A 143 13.136 -4.783 20.313 0.60 26.10 C
ANISOU 1202 CG AGLU A 143 3368 4554 1996 1353 -1318 -657 C
ATOM 1203 CG BGLU A 143 13.228 -4.119 20.217 0.40 23.61 C
ANISOU 1203 CG BGLU A 143 2199 4503 2267 2361 -1152 -983 C
ATOM 1204 CD AGLU A 143 14.534 -5.029 20.848 0.60 32.81 C
ANISOU 1204 CD AGLU A 143 3730 6155 2583 1451 -2000 -927 C
ATOM 1205 CD BGLU A 143 13.988 -2.810 20.300 0.40 30.32 C
ANISOU 1205 CD BGLU A 143 3364 5773 2382 999 -1909 -1211 C
ATOM 1206 OE1AGLU A 143 15.404 -4.167 20.595 0.60 37.76 O
ANISOU 1206 OE1AGLU A 143 3315 6201 4832 1479 -1734 -1420 O
ATOM 1207 OE1BGLU A 143 14.295 -2.237 19.231 0.40 33.62 O
ANISOU 1207 OE1BGLU A 143 3027 5679 4069 1541 -2648 804 O
ATOM 1208 OE2AGLU A 143 14.799 -6.051 21.525 0.60 39.19 O
ANISOU 1208 OE2AGLU A 143 3886 6618 4385 2331 -2118 -359 O
ATOM 1209 OE2BGLU A 143 14.252 -2.351 21.431 0.40 70.50 O
ANISOU 1209 OE2BGLU A 143 9932 13284 3570 -4714 -1676 -3436 O
ATOM 1210 N PHE A 144 11.951 -2.087 17.459 1.00 12.73 N
ANISOU 1210 N PHE A 144 1032 2021 1786 186 -58 -23 N
ATOM 1211 CA PHE A 144 11.805 -0.631 17.628 1.00 13.82 C
ANISOU 1211 CA PHE A 144 1287 2086 1880 114 -165 -274 C
ATOM 1212 C PHE A 144 10.349 -0.183 17.556 1.00 13.08 C
ANISOU 1212 C PHE A 144 1203 1793 1974 79 9 -112 C
ATOM 1213 O PHE A 144 9.995 0.882 18.060 1.00 14.96 O
ANISOU 1213 O PHE A 144 1539 1889 2256 255 -409 -301 O
ATOM 1214 CB PHE A 144 12.639 0.165 16.601 1.00 12.94 C
ANISOU 1214 CB PHE A 144 869 1771 2279 54 -233 -282 C
ATOM 1215 CG PHE A 144 11.963 0.329 15.236 1.00 13.37 C
ANISOU 1215 CG PHE A 144 1356 1819 1903 333 89 -283 C
ATOM 1216 CD1 PHE A 144 11.949 -0.694 14.290 1.00 12.50 C
ANISOU 1216 CD1 PHE A 144 1161 1922 1666 247 472 -221 C
ATOM 1217 CD2 PHE A 144 11.356 1.524 14.920 1.00 13.63 C
ANISOU 1217 CD2 PHE A 144 1959 1578 1642 47 153 54 C
ATOM 1218 CE1 PHE A 144 11.326 -0.497 13.078 1.00 13.95 C
ANISOU 1218 CE1 PHE A 144 1294 2038 1968 709 124 -510 C
ATOM 1219 CE2 PHE A 144 10.708 1.747 13.714 1.00 19.99 C
ANISOU 1219 CE2 PHE A 144 3353 1777 2464 763 -1091 -631 C
ATOM 1220 CZ PHE A 144 10.720 0.719 12.782 1.00 16.23 C
ANISOU 1220 CZ PHE A 144 2070 1749 2348 488 -380 -552 C
ATOM 1221 N ALA A 145 9.499 -0.980 16.939 1.00 12.54 N
ANISOU 1221 N ALA A 145 1034 2162 1570 353 81 -466 N
ATOM 1222 CA ALA A 145 8.126 -0.590 16.654 1.00 10.65 C
ANISOU 1222 CA ALA A 145 1059 1495 1492 356 166 -439 C
ATOM 1223 C ALA A 145 7.129 -1.413 17.461 1.00 10.15 C
ANISOU 1223 C ALA A 145 982 1696 1179 382 -63 -244 C
ATOM 1224 O ALA A 145 5.931 -1.308 17.274 1.00 11.41 O
ANISOU 1224 O ALA A 145 875 1805 1653 443 14 -527 O
ATOM 1225 CB ALA A 145 7.839 -0.743 15.187 1.00 12.15 C
ANISOU 1225 CB ALA A 145 1161 1979 1479 -79 49 65 C
ATOM 1226 N ARG A 146 7.626 -2.279 18.330 1.00 12.39 N
ANISOU 1226 N ARG A 146 1341 2070 1296 340 -230 -112 N
ATOM 1227 CA ARG A 146 6.776 -3.220 19.025 1.00 11.68 C
ANISOU 1227 CA ARG A 146 1516 1332 1590 638 -129 -152 C
ATOM 1228 C ARG A 146 5.886 -2.559 20.054 1.00 10.43 C
ANISOU 1228 C ARG A 146 1310 1019 1633 346 -81 -113 C
ATOM 1229 O ARG A 146 4.663 -2.738 20.023 1.00 11.01 O
ANISOU 1229 O ARG A 146 1260 1289 1633 486 -355 -192 O
ATOM 1230 CB ARG A 146 7.715 -4.253 19.671 1.00 15.01 C
ANISOU 1230 CB ARG A 146 2018 1507 2177 987 -476 -292 C
ATOM 1231 CG ARG A 146 7.006 -5.429 20.249 1.00 22.49 C
ANISOU 1231 CG ARG A 146 3662 1660 3223 200 -1645 498 C
ATOM 1232 CD ARG A 146 7.997 -6.483 20.687 1.00 20.41 C
ANISOU 1232 CD ARG A 146 3045 1762 2948 303 -1202 218 C
ATOM 1233 NE ARG A 146 8.799 -7.046 19.592 1.00 20.10 N
ANISOU 1233 NE ARG A 146 3140 2291 2207 -102 -1222 417 N
ATOM 1234 CZ ARG A 146 10.088 -7.337 19.715 1.00 21.96 C
ANISOU 1234 CZ ARG A 146 3095 3552 1696 66 -1016 -14 C
ATOM 1235 NH1 ARG A 146 10.765 -7.132 20.853 1.00 24.08 N
ANISOU 1235 NH1 ARG A 146 2701 4832 1616 -1206 -769 264 N
ATOM 1236 NH2 ARG A 146 10.719 -7.848 18.676 1.00 21.67 N
ANISOU 1236 NH2 ARG A 146 3488 2857 1890 -976 -216 151 N
ATOM 1237 N GLU A 147 6.436 -1.797 21.004 1.00 10.34 N
ANISOU 1237 N GLU A 147 990 1564 1376 293 6 -157 N
ATOM 1238 CA AGLU A 147 5.489 -1.228 21.979 0.60 10.55 C
ANISOU 1238 CA AGLU A 147 1062 1311 1636 190 154 -208 C
ATOM 1239 CA BGLU A 147 5.607 -1.098 21.983 0.40 11.26 C
ANISOU 1239 CA BGLU A 147 1187 1680 1410 345 147 -161 C
ATOM 1240 C GLU A 147 4.573 -0.226 21.288 1.00 10.71 C
ANISOU 1240 C GLU A 147 1267 1366 1438 324 115 -361 C
ATOM 1241 O GLU A 147 3.403 -0.152 21.679 1.00 10.16 O
ANISOU 1241 O GLU A 147 1270 1405 1184 388 -1 -159 O
ATOM 1242 CB AGLU A 147 6.204 -0.663 23.199 0.60 16.69 C
ANISOU 1242 CB AGLU A 147 2139 2536 1665 880 -339 -703 C
ATOM 1243 CB BGLU A 147 6.473 -0.238 22.888 0.40 9.26 C
ANISOU 1243 CB BGLU A 147 886 1431 1199 385 414 -26 C
ATOM 1244 CG AGLU A 147 6.057 -1.600 24.404 0.60 30.41 C
ANISOU 1244 CG AGLU A 147 6594 2912 2046 156 -1388 -215 C
ATOM 1245 CG BGLU A 147 5.769 0.621 23.933 0.40 18.78 C
ANISOU 1245 CG BGLU A 147 1471 3347 2319 1383 -210 -1467 C
ATOM 1246 CD AGLU A 147 7.188 -1.586 25.393 0.60 34.42 C
ANISOU 1246 CD AGLU A 147 6937 3498 2643 645 -1877 254 C
ATOM 1247 CD BGLU A 147 6.828 1.401 24.707 0.40 27.37 C
ANISOU 1247 CD BGLU A 147 3087 3622 3691 1358 -1317 -2254 C
ATOM 1248 OE1AGLU A 147 8.025 -0.656 25.388 0.60 37.31 O
ANISOU 1248 OE1AGLU A 147 3758 6179 4239 371 226 -1121 O
ATOM 1249 OE1BGLU A 147 7.591 0.765 25.468 0.40 25.60 O
ANISOU 1249 OE1BGLU A 147 1378 4477 3870 793 -723 -1544 O
ATOM 1250 OE2AGLU A 147 7.264 -2.527 26.225 0.60 60.59 O
ANISOU 1250 OE2AGLU A 147 14405 5131 3485 1077 -3926 1313 O
ATOM 1251 OE2BGLU A 147 6.903 2.626 24.510 0.40 36.66 O
ANISOU 1251 OE2BGLU A 147 3545 3379 7005 1581 -2184 -2607 O
ATOM 1252 N THR A 148 4.992 0.481 20.251 1.00 9.57 N
ANISOU 1252 N THR A 148 848 1361 1426 173 -160 -370 N
ATOM 1253 CA THR A 148 4.118 1.390 19.534 1.00 10.65 C
ANISOU 1253 CA THR A 148 1173 1228 1645 200 -186 -374 C
ATOM 1254 C THR A 148 2.939 0.655 18.951 1.00 7.79 C
ANISOU 1254 C THR A 148 1014 908 1039 328 -110 -70 C
ATOM 1255 O THR A 148 1.809 1.094 19.107 1.00 7.49 O
ANISOU 1255 O THR A 148 1042 796 1007 275 74 -51 O
ATOM 1256 CB THR A 148 4.905 2.081 18.405 1.00 12.64 C
ANISOU 1256 CB THR A 148 1307 1229 2268 -34 -259 109 C
ATOM 1257 OG1 THR A 148 5.841 2.966 19.054 1.00 15.37 O
ANISOU 1257 OG1 THR A 148 1274 1793 2772 -194 -351 -76 O
ATOM 1258 CG2 THR A 148 3.982 2.879 17.498 1.00 14.40 C
ANISOU 1258 CG2 THR A 148 1862 1564 2047 316 -392 -44 C
ATOM 1259 N PHE A 149 3.158 -0.443 18.251 1.00 7.80 N
ANISOU 1259 N PHE A 149 890 753 1319 280 60 -37 N
ATOM 1260 CA PHE A 149 2.057 -1.129 17.594 1.00 7.31 C
ANISOU 1260 CA PHE A 149 946 837 995 245 49 5 C
ATOM 1261 C PHE A 149 1.209 -1.884 18.594 1.00 7.82 C
ANISOU 1261 C PHE A 149 1125 707 1137 158 41 21 C
ATOM 1262 O PHE A 149 -0.006 -2.029 18.389 1.00 7.05 O
ANISOU 1262 O PHE A 149 997 641 1041 272 72 30 O
ATOM 1263 CB PHE A 149 2.557 -2.014 16.457 1.00 7.47 C
ANISOU 1263 CB PHE A 149 955 637 1245 407 49 -18 C
ATOM 1264 CG PHE A 149 2.634 -1.197 15.162 1.00 7.68 C
ANISOU 1264 CG PHE A 149 982 912 1025 218 32 -131 C
ATOM 1265 CD1 PHE A 149 3.685 -0.326 14.968 1.00 8.98 C
ANISOU 1265 CD1 PHE A 149 973 1195 1242 137 -43 108 C
ATOM 1266 CD2 PHE A 149 1.687 -1.271 14.168 1.00 7.21 C
ANISOU 1266 CD2 PHE A 149 867 872 1002 246 134 -104 C
ATOM 1267 CE1 PHE A 149 3.799 0.466 13.846 1.00 8.33 C
ANISOU 1267 CE1 PHE A 149 1308 849 1008 60 152 -259 C
ATOM 1268 CE2 PHE A 149 1.780 -0.464 13.052 1.00 7.05 C
ANISOU 1268 CE2 PHE A 149 995 806 879 298 238 -186 C
ATOM 1269 CZ PHE A 149 2.836 0.403 12.876 1.00 8.41 C
ANISOU 1269 CZ PHE A 149 1294 806 1096 145 58 18 C
ATOM 1270 N GLN A 150 1.834 -2.324 19.706 1.00 7.51 N
ANISOU 1270 N GLN A 150 1080 733 1042 250 40 -54 N
ATOM 1271 CA GLN A 150 1.007 -2.928 20.758 1.00 7.89 C
ANISOU 1271 CA GLN A 150 1167 768 1064 194 67 -55 C
ATOM 1272 C GLN A 150 0.025 -1.897 21.326 1.00 7.44 C
ANISOU 1272 C GLN A 150 1136 918 771 144 16 -120 C
ATOM 1273 O GLN A 150 -1.130 -2.227 21.608 1.00 9.12 O
ANISOU 1273 O GLN A 150 1192 1065 1209 117 280 38 O
ATOM 1274 CB GLN A 150 1.835 -3.564 21.872 1.00 9.38 C
ANISOU 1274 CB GLN A 150 1561 874 1130 276 11 60 C
ATOM 1275 CG GLN A 150 2.542 -4.815 21.394 1.00 10.47 C
ANISOU 1275 CG GLN A 150 1854 772 1353 386 -2 269 C
ATOM 1276 CD GLN A 150 3.605 -5.330 22.347 1.00 16.33 C
ANISOU 1276 CD GLN A 150 2889 1170 2145 745 -736 562 C
ATOM 1277 OE1 GLN A 150 4.268 -4.606 23.093 1.00 21.65 O
ANISOU 1277 OE1 GLN A 150 3358 2070 2799 1750 -1473 -645 O
ATOM 1278 NE2 GLN A 150 3.750 -6.646 22.263 1.00 23.35 N
ANISOU 1278 NE2 GLN A 150 5243 1307 2322 1324 -1450 479 N
ATOM 1279 N ALA A 151 0.480 -0.643 21.484 1.00 7.48 N
ANISOU 1279 N ALA A 151 1089 835 917 286 100 -16 N
ATOM 1280 CA ALA A 151 -0.415 0.404 21.963 1.00 7.70 C
ANISOU 1280 CA ALA A 151 1220 895 810 377 152 33 C
ATOM 1281 C ALA A 151 -1.435 0.786 20.907 1.00 7.16 C
ANISOU 1281 C ALA A 151 1018 946 756 296 257 57 C
ATOM 1282 O ALA A 151 -2.572 1.083 21.260 1.00 6.91 O
ANISOU 1282 O ALA A 151 1011 779 835 185 321 49 O
ATOM 1283 CB ALA A 151 0.445 1.576 22.389 1.00 8.72 C
ANISOU 1283 CB ALA A 151 1245 975 1095 315 52 -107 C
ATOM 1284 N PHE A 152 -1.055 0.812 19.649 1.00 6.46 N
ANISOU 1284 N PHE A 152 996 689 768 221 290 63 N
ATOM 1285 CA PHE A 152 -1.995 1.137 18.585 1.00 5.78 C
ANISOU 1285 CA PHE A 152 893 549 755 228 235 -203 C
ATOM 1286 C PHE A 152 -3.169 0.188 18.602 1.00 6.05 C
ANISOU 1286 C PHE A 152 962 493 843 260 270 -12 C
ATOM 1287 O PHE A 152 -4.315 0.543 18.293 1.00 6.48 O
ANISOU 1287 O PHE A 152 876 787 799 98 229 48 O
ATOM 1288 CB PHE A 152 -1.308 1.094 17.222 1.00 5.72 C
ANISOU 1288 CB PHE A 152 844 578 750 288 158 -34 C
ATOM 1289 CG PHE A 152 -0.425 2.232 16.822 1.00 6.27 C
ANISOU 1289 CG PHE A 152 812 809 763 117 145 -33 C
ATOM 1290 CD1 PHE A 152 -0.334 3.382 17.557 1.00 6.23 C
ANISOU 1290 CD1 PHE A 152 749 780 839 109 301 53 C
ATOM 1291 CD2 PHE A 152 0.333 2.117 15.656 1.00 6.80 C
ANISOU 1291 CD2 PHE A 152 906 842 834 95 185 2 C
ATOM 1292 CE1 PHE A 152 0.471 4.440 17.169 1.00 7.56 C
ANISOU 1292 CE1 PHE A 152 848 784 1240 0 367 -183 C
ATOM 1293 CE2 PHE A 152 1.105 3.162 15.236 1.00 8.11 C
ANISOU 1293 CE2 PHE A 152 1180 873 1030 20 391 14 C
ATOM 1294 CZ PHE A 152 1.158 4.300 15.987 1.00 7.01 C
ANISOU 1294 CZ PHE A 152 892 780 991 -12 293 173 C
ATOM 1295 N ARG A 153 -2.907 -1.075 18.929 1.00 6.82 N
ANISOU 1295 N ARG A 153 943 621 1027 173 222 93 N
ATOM 1296 CA ARG A 153 -3.885 -2.160 18.868 1.00 6.72 C
ANISOU 1296 CA ARG A 153 1032 543 976 158 204 20 C
ATOM 1297 C ARG A 153 -4.687 -2.288 20.135 1.00 7.10 C
ANISOU 1297 C ARG A 153 1013 609 1073 167 264 -13 C
ATOM 1298 O ARG A 153 -4.972 -3.370 20.657 1.00 10.18 O
ANISOU 1298 O ARG A 153 1924 633 1311 258 750 124 O
ATOM 1299 CB ARG A 153 -3.197 -3.503 18.524 1.00 7.21 C
ANISOU 1299 CB ARG A 153 1201 649 890 259 240 43 C
ATOM 1300 CG ARG A 153 -2.608 -3.459 17.131 1.00 6.40 C
ANISOU 1300 CG ARG A 153 886 611 934 169 163 -17 C
ATOM 1301 CD ARG A 153 -1.738 -4.598 16.835 1.00 6.42 C
ANISOU 1301 CD ARG A 153 872 598 971 137 240 78 C
ATOM 1302 NE ARG A 153 -2.160 -5.949 17.007 1.00 5.90 N
ANISOU 1302 NE ARG A 153 810 562 870 182 18 72 N
ATOM 1303 CZ ARG A 153 -2.668 -6.753 16.077 1.00 6.26 C
ANISOU 1303 CZ ARG A 153 707 841 830 -110 145 67 C
ATOM 1304 NH1 ARG A 153 -2.918 -8.032 16.374 1.00 6.88 N
ANISOU 1304 NH1 ARG A 153 1039 651 924 53 505 -74 N
ATOM 1305 NH2 ARG A 153 -2.949 -6.311 14.867 1.00 6.52 N
ANISOU 1305 NH2 ARG A 153 855 967 655 233 318 -58 N
ATOM 1306 N THR A 154 -5.182 -1.157 20.621 1.00 7.85 N
ANISOU 1306 N THR A 154 1251 636 1095 123 432 -28 N
ATOM 1307 CA THR A 154 -6.056 -1.073 21.761 1.00 7.63 C
ANISOU 1307 CA THR A 154 1022 810 1069 172 386 -6 C
ATOM 1308 C THR A 154 -7.162 -0.051 21.487 1.00 7.46 C
ANISOU 1308 C THR A 154 987 777 1069 96 267 66 C
ATOM 1309 O THR A 154 -7.007 0.862 20.689 1.00 7.99 O
ANISOU 1309 O THR A 154 1266 870 900 106 408 54 O
ATOM 1310 CB THR A 154 -5.346 -0.676 23.075 1.00 7.72 C
ANISOU 1310 CB THR A 154 1130 747 1055 242 271 92 C
ATOM 1311 OG1 THR A 154 -4.758 0.618 22.907 1.00 7.56 O
ANISOU 1311 OG1 THR A 154 1301 621 950 278 299 35 O
ATOM 1312 CG2 THR A 154 -4.246 -1.665 23.438 1.00 8.57 C
ANISOU 1312 CG2 THR A 154 1277 793 1187 401 384 215 C
ATOM 1313 N ALA A 155 -8.256 -0.246 22.223 1.00 7.54 N
ANISOU 1313 N ALA A 155 952 916 998 165 335 58 N
ATOM 1314 CA ALA A 155 -9.476 0.540 22.003 1.00 8.12 C
ANISOU 1314 CA ALA A 155 1049 1087 949 208 363 -69 C
ATOM 1315 C ALA A 155 -9.389 1.850 22.730 1.00 7.98 C
ANISOU 1315 C ALA A 155 1152 942 938 239 391 34 C
ATOM 1316 O ALA A 155 -10.169 2.750 22.381 1.00 10.13 O
ANISOU 1316 O ALA A 155 1523 1246 1081 577 296 135 O
ATOM 1317 CB ALA A 155 -10.686 -0.242 22.481 1.00 10.94 C
ANISOU 1317 CB ALA A 155 922 1471 1762 -62 193 -196 C
ATOM 1318 N ASP A 156 -8.479 1.968 23.703 1.00 7.36 N
ANISOU 1318 N ASP A 156 867 830 1099 147 439 -22 N
ATOM 1319 CA ASP A 156 -8.332 3.215 24.442 1.00 7.55 C
ANISOU 1319 CA ASP A 156 1056 857 956 160 521 -44 C
ATOM 1320 C ASP A 156 -7.086 3.971 23.979 1.00 6.20 C
ANISOU 1320 C ASP A 156 1068 415 871 286 404 -108 C
ATOM 1321 O ASP A 156 -7.230 4.949 23.228 1.00 6.84 O
ANISOU 1321 O ASP A 156 1100 548 949 171 286 -8 O
ATOM 1322 CB ASP A 156 -8.366 2.993 25.962 1.00 9.39 C
ANISOU 1322 CB ASP A 156 1469 1103 997 -126 404 93 C
ATOM 1323 CG ASP A 156 -7.387 1.973 26.522 1.00 10.18 C
ANISOU 1323 CG ASP A 156 1515 1367 987 -118 395 246 C
ATOM 1324 OD1 ASP A 156 -6.767 1.195 25.781 1.00 9.83 O
ANISOU 1324 OD1 ASP A 156 1372 1271 1090 31 289 271 O
ATOM 1325 OD2 ASP A 156 -7.278 1.949 27.772 1.00 13.41 O
ANISOU 1325 OD2 ASP A 156 1737 2347 1010 16 196 133 O
ATOM 1326 N VAL A 157 -5.900 3.516 24.321 1.00 6.53 N
ANISOU 1326 N VAL A 157 1078 659 743 153 332 3 N
ATOM 1327 CA VAL A 157 -4.669 4.191 23.978 1.00 6.67 C
ANISOU 1327 CA VAL A 157 1071 608 857 85 234 -230 C
ATOM 1328 C VAL A 157 -4.493 4.292 22.477 1.00 6.22 C
ANISOU 1328 C VAL A 157 926 587 849 137 369 -113 C
ATOM 1329 O VAL A 157 -4.056 5.337 21.971 1.00 6.81 O
ANISOU 1329 O VAL A 157 875 644 1069 117 342 -68 O
ATOM 1330 CB VAL A 157 -3.482 3.515 24.676 1.00 7.43 C
ANISOU 1330 CB VAL A 157 1151 770 900 140 94 -241 C
ATOM 1331 CG1 VAL A 157 -2.183 4.113 24.185 1.00 8.92 C
ANISOU 1331 CG1 VAL A 157 1043 1334 1014 141 -74 123 C
ATOM 1332 CG2 VAL A 157 -3.631 3.665 26.173 1.00 10.27 C
ANISOU 1332 CG2 VAL A 157 1550 1452 899 155 134 -64 C
ATOM 1333 N GLY A 158 -4.873 3.244 21.740 1.00 5.57 N
ANISOU 1333 N GLY A 158 754 657 705 14 374 8 N
ATOM 1334 CA GLY A 158 -4.621 3.328 20.303 1.00 5.66 C
ANISOU 1334 CA GLY A 158 757 666 728 249 341 -26 C
ATOM 1335 C GLY A 158 -5.432 4.401 19.616 1.00 5.55 C
ANISOU 1335 C GLY A 158 745 550 813 115 351 77 C
ATOM 1336 O GLY A 158 -4.955 5.053 18.710 1.00 5.41 O
ANISOU 1336 O GLY A 158 833 563 661 126 430 -50 O
ATOM 1337 N ARG A 159 -6.676 4.547 20.081 1.00 5.39 N
ANISOU 1337 N ARG A 159 767 560 721 175 403 85 N
ATOM 1338 CA ARG A 159 -7.542 5.605 19.530 1.00 5.30 C
ANISOU 1338 CA ARG A 159 705 597 713 120 294 23 C
ATOM 1339 C ARG A 159 -7.060 6.964 19.941 1.00 5.21 C
ANISOU 1339 C ARG A 159 759 568 653 113 310 20 C
ATOM 1340 O ARG A 159 -7.041 7.892 19.139 1.00 5.79 O
ANISOU 1340 O ARG A 159 832 611 757 221 366 100 O
ATOM 1341 CB ARG A 159 -9.005 5.358 19.918 1.00 4.89 C
ANISOU 1341 CB ARG A 159 687 575 595 129 383 -21 C
ATOM 1342 CG ARG A 159 -9.575 4.088 19.325 1.00 5.50 C
ANISOU 1342 CG ARG A 159 799 646 644 68 345 -46 C
ATOM 1343 CD ARG A 159 -11.052 3.946 19.592 1.00 5.99 C
ANISOU 1343 CD ARG A 159 767 878 630 -48 273 19 C
ATOM 1344 NE ARG A 159 -11.893 4.896 18.867 1.00 6.52 N
ANISOU 1344 NE ARG A 159 869 854 753 179 225 -129 N
ATOM 1345 CZ ARG A 159 -12.227 4.781 17.575 1.00 5.49 C
ANISOU 1345 CZ ARG A 159 605 796 684 250 348 -117 C
ATOM 1346 NH1 ARG A 159 -11.740 3.799 16.820 1.00 5.85 N
ANISOU 1346 NH1 ARG A 159 740 502 981 48 579 -131 N
ATOM 1347 NH2 ARG A 159 -13.029 5.691 17.006 1.00 5.48 N
ANISOU 1347 NH2 ARG A 159 600 644 839 142 237 -114 N
ATOM 1348 N GLU A 160 -6.646 7.106 21.196 1.00 5.19 N
ANISOU 1348 N GLU A 160 727 646 599 87 401 -44 N
ATOM 1349 CA GLU A 160 -6.054 8.365 21.665 1.00 6.25 C
ANISOU 1349 CA GLU A 160 917 704 753 71 328 -69 C
ATOM 1350 C GLU A 160 -4.899 8.758 20.777 1.00 5.84 C
ANISOU 1350 C GLU A 160 834 567 817 42 273 44 C
ATOM 1351 O GLU A 160 -4.804 9.871 20.303 1.00 6.76 O
ANISOU 1351 O GLU A 160 1166 525 878 150 205 29 O
ATOM 1352 CB GLU A 160 -5.588 8.147 23.113 1.00 6.90 C
ANISOU 1352 CB GLU A 160 870 1044 708 88 288 -117 C
ATOM 1353 CG GLU A 160 -4.838 9.309 23.701 1.00 8.23 C
ANISOU 1353 CG GLU A 160 1123 1178 826 22 308 -226 C
ATOM 1354 CD GLU A 160 -4.233 9.052 25.058 1.00 8.77 C
ANISOU 1354 CD GLU A 160 1215 1353 763 12 294 -233 C
ATOM 1355 OE1 GLU A 160 -3.549 9.977 25.553 1.00 12.74 O
ANISOU 1355 OE1 GLU A 160 1636 2151 1054 -584 143 -271 O
ATOM 1356 OE2 GLU A 160 -4.401 7.952 25.643 1.00 13.47 O
ANISOU 1356 OE2 GLU A 160 1745 1986 1388 -314 176 507 O
ATOM 1357 N LEU A 161 -3.971 7.822 20.546 1.00 5.73 N
ANISOU 1357 N LEU A 161 926 577 676 79 309 69 N
ATOM 1358 CA LEU A 161 -2.758 8.179 19.828 1.00 5.85 C
ANISOU 1358 CA LEU A 161 883 640 700 -13 322 -85 C
ATOM 1359 C LEU A 161 -3.048 8.438 18.361 1.00 4.92 C
ANISOU 1359 C LEU A 161 545 607 719 -4 292 -77 C
ATOM 1360 O LEU A 161 -2.641 9.456 17.817 1.00 5.73 O
ANISOU 1360 O LEU A 161 881 593 703 -8 198 -47 O
ATOM 1361 CB LEU A 161 -1.712 7.071 19.980 1.00 7.08 C
ANISOU 1361 CB LEU A 161 925 960 805 191 402 118 C
ATOM 1362 CG LEU A 161 -1.167 6.795 21.384 1.00 8.75 C
ANISOU 1362 CG LEU A 161 1212 1056 1057 -110 60 262 C
ATOM 1363 CD1 LEU A 161 -0.267 5.555 21.357 1.00 12.11 C
ANISOU 1363 CD1 LEU A 161 1231 2221 1148 660 203 414 C
ATOM 1364 CD2 LEU A 161 -0.483 8.045 21.930 1.00 20.21 C
ANISOU 1364 CD2 LEU A 161 3656 2010 2015 -1188 -836 -10 C
ATOM 1365 N ILE A 162 -3.728 7.504 17.715 1.00 4.75 N
ANISOU 1365 N ILE A 162 703 495 605 104 296 -9 N
ATOM 1366 CA ILE A 162 -3.900 7.618 16.246 1.00 4.71 C
ANISOU 1366 CA ILE A 162 624 533 634 88 225 -65 C
ATOM 1367 C ILE A 162 -4.959 8.607 15.828 1.00 4.41 C
ANISOU 1367 C ILE A 162 680 369 627 48 302 -28 C
ATOM 1368 O ILE A 162 -4.759 9.393 14.892 1.00 5.19 O
ANISOU 1368 O ILE A 162 793 461 717 76 361 39 O
ATOM 1369 CB ILE A 162 -4.161 6.219 15.661 1.00 4.32 C
ANISOU 1369 CB ILE A 162 559 488 596 136 324 -53 C
ATOM 1370 CG1 ILE A 162 -2.950 5.313 15.806 1.00 5.07 C
ANISOU 1370 CG1 ILE A 162 508 613 806 135 261 -205 C
ATOM 1371 CG2 ILE A 162 -4.599 6.347 14.196 1.00 4.73 C
ANISOU 1371 CG2 ILE A 162 702 469 627 -10 284 -70 C
ATOM 1372 CD1 ILE A 162 -3.147 3.874 15.368 1.00 5.49 C
ANISOU 1372 CD1 ILE A 162 919 434 733 179 226 68 C
ATOM 1373 N ILE A 163 -6.105 8.593 16.517 1.00 4.76 N
ANISOU 1373 N ILE A 163 755 389 664 126 348 -25 N
ATOM 1374 CA ILE A 163 -7.211 9.437 16.107 1.00 4.86 C
ANISOU 1374 CA ILE A 163 682 553 613 120 254 4 C
ATOM 1375 C ILE A 163 -7.100 10.802 16.763 1.00 5.14 C
ANISOU 1375 C ILE A 163 807 461 685 160 311 31 C
ATOM 1376 O ILE A 163 -7.123 11.856 16.105 1.00 6.29 O
ANISOU 1376 O ILE A 163 1001 507 883 41 220 115 O
ATOM 1377 CB ILE A 163 -8.574 8.782 16.377 1.00 5.38 C
ANISOU 1377 CB ILE A 163 758 564 721 48 226 146 C
ATOM 1378 CG1 ILE A 163 -8.695 7.509 15.525 1.00 6.45 C
ANISOU 1378 CG1 ILE A 163 828 733 891 -43 235 -5 C
ATOM 1379 CG2 ILE A 163 -9.690 9.779 16.137 1.00 6.48 C
ANISOU 1379 CG2 ILE A 163 690 889 883 156 261 240 C
ATOM 1380 CD1 ILE A 163 -9.899 6.674 15.871 1.00 7.15 C
ANISOU 1380 CD1 ILE A 163 787 778 1154 -61 234 -149 C
ATOM 1381 N ASP A 164 -6.969 10.843 18.094 1.00 6.05 N
ANISOU 1381 N ASP A 164 1056 573 671 36 307 -17 N
ATOM 1382 CA ASP A 164 -6.960 12.134 18.765 1.00 6.32 C
ANISOU 1382 CA ASP A 164 938 642 822 139 76 -110 C
ATOM 1383 C ASP A 164 -5.657 12.900 18.578 1.00 6.86 C
ANISOU 1383 C ASP A 164 1052 592 963 92 119 -115 C
ATOM 1384 O ASP A 164 -5.722 14.139 18.512 1.00 7.98 O
ANISOU 1384 O ASP A 164 1183 653 1197 122 375 -27 O
ATOM 1385 CB ASP A 164 -7.283 11.954 20.241 1.00 6.69 C
ANISOU 1385 CB ASP A 164 1041 635 866 439 294 -191 C
ATOM 1386 CG ASP A 164 -8.657 11.344 20.496 1.00 7.39 C
ANISOU 1386 CG ASP A 164 1217 840 752 107 276 -348 C
ATOM 1387 OD1 ASP A 164 -9.625 11.600 19.756 1.00 8.06 O
ANISOU 1387 OD1 ASP A 164 1214 1017 831 -36 318 -107 O
ATOM 1388 OD2 ASP A 164 -8.737 10.675 21.560 1.00 9.52 O
ANISOU 1388 OD2 ASP A 164 1327 1111 1179 41 183 97 O
ATOM 1389 N GLN A 165 -4.523 12.240 18.467 1.00 6.66 N
ANISOU 1389 N GLN A 165 1081 569 880 113 424 -107 N
ATOM 1390 CA AGLN A 165 -3.226 12.866 18.356 0.60 6.74 C
ANISOU 1390 CA AGLN A 165 1132 529 900 59 368 -159 C
ATOM 1391 CA BGLN A 165 -3.240 12.913 18.345 0.40 6.80 C
ANISOU 1391 CA BGLN A 165 1129 535 922 66 388 -169 C
ATOM 1392 C GLN A 165 -2.532 12.723 16.997 1.00 6.20 C
ANISOU 1392 C GLN A 165 874 604 880 185 272 -132 C
ATOM 1393 O GLN A 165 -1.443 13.256 16.794 1.00 8.06 O
ANISOU 1393 O GLN A 165 919 996 1147 -27 380 -321 O
ATOM 1394 CB AGLN A 165 -2.239 12.286 19.375 0.60 6.50 C
ANISOU 1394 CB AGLN A 165 1070 553 849 191 413 -225 C
ATOM 1395 CB BGLN A 165 -2.295 12.452 19.457 0.40 8.46 C
ANISOU 1395 CB BGLN A 165 1215 1096 906 -13 270 -113 C
ATOM 1396 CG AGLN A 165 -2.652 12.481 20.808 0.60 8.36 C
ANISOU 1396 CG AGLN A 165 1507 855 814 -264 515 -153 C
ATOM 1397 CG BGLN A 165 -2.535 13.065 20.818 0.40 16.50 C
ANISOU 1397 CG BGLN A 165 1378 3544 1346 643 -180 -1234 C
ATOM 1398 CD AGLN A 165 -1.734 11.882 21.845 0.60 14.59 C
ANISOU 1398 CD AGLN A 165 1814 2821 909 -435 -600 -836 C
ATOM 1399 CD BGLN A 165 -2.450 14.567 20.920 0.40 19.17 C
ANISOU 1399 CD BGLN A 165 1702 3522 2060 1626 381 -2027 C
ATOM 1400 OE1AGLN A 165 -0.608 11.441 21.643 0.60 20.51 O
ANISOU 1400 OE1AGLN A 165 3132 3422 1241 1282 -304 -45 O
ATOM 1401 OE1BGLN A 165 -2.066 15.309 20.008 0.40 30.91 O
ANISOU 1401 OE1BGLN A 165 5373 3053 3316 990 483 -1359 O
ATOM 1402 NE2AGLN A 165 -2.220 11.863 23.066 0.60 17.59 N
ANISOU 1402 NE2AGLN A 165 2964 2648 1071 182 -204 -25 N
ATOM 1403 NE2BGLN A 165 -2.844 15.120 22.076 0.40 40.14 N
ANISOU 1403 NE2BGLN A 165 3914 6793 4545 -76 2584 -4620 N
ATOM 1404 N ASN A 166 -3.137 12.019 16.066 1.00 6.47 N
ANISOU 1404 N ASN A 166 1019 638 803 32 287 -61 N
ATOM 1405 CA ASN A 166 -2.601 11.819 14.721 1.00 5.65 C
ANISOU 1405 CA ASN A 166 805 606 737 142 276 35 C
ATOM 1406 C ASN A 166 -1.241 11.137 14.696 1.00 5.65 C
ANISOU 1406 C ASN A 166 822 703 622 94 127 -42 C
ATOM 1407 O ASN A 166 -0.416 11.430 13.807 1.00 5.65 O
ANISOU 1407 O ASN A 166 829 551 768 89 307 -82 O
ATOM 1408 CB ASN A 166 -2.546 13.110 13.903 1.00 6.01 C
ANISOU 1408 CB ASN A 166 955 477 850 147 389 -58 C
ATOM 1409 CG ASN A 166 -2.855 12.888 12.443 1.00 5.51 C
ANISOU 1409 CG ASN A 166 715 594 783 51 400 58 C
ATOM 1410 OD1 ASN A 166 -3.303 11.805 12.024 1.00 6.47 O
ANISOU 1410 OD1 ASN A 166 917 587 956 17 206 62 O
ATOM 1411 ND2 ASN A 166 -2.631 13.917 11.629 1.00 6.68 N
ANISOU 1411 ND2 ASN A 166 918 717 904 -53 364 149 N
ATOM 1412 N ALA A 167 -1.021 10.175 15.577 1.00 5.19 N
ANISOU 1412 N ALA A 167 654 540 779 -18 201 19 N
ATOM 1413 CA ALA A 167 0.303 9.582 15.688 1.00 5.67 C
ANISOU 1413 CA ALA A 167 579 751 823 -2 193 -11 C
ATOM 1414 C ALA A 167 0.709 8.792 14.481 1.00 5.09 C
ANISOU 1414 C ALA A 167 702 412 820 -40 184 115 C
ATOM 1415 O ALA A 167 1.931 8.635 14.268 1.00 6.85 O
ANISOU 1415 O ALA A 167 715 842 1044 81 183 -110 O
ATOM 1416 CB ALA A 167 0.335 8.638 16.895 1.00 7.21 C
ANISOU 1416 CB ALA A 167 970 973 795 154 -58 -2 C
ATOM 1417 N PHE A 168 -0.169 8.277 13.674 1.00 5.53 N
ANISOU 1417 N PHE A 168 660 741 702 -46 341 1 N
ATOM 1418 CA PHE A 168 0.259 7.487 12.513 1.00 5.01 C
ANISOU 1418 CA PHE A 168 563 519 822 57 321 -1 C
ATOM 1419 C PHE A 168 0.859 8.441 11.459 1.00 4.91 C
ANISOU 1419 C PHE A 168 756 480 630 134 324 -65 C
ATOM 1420 O PHE A 168 1.833 8.086 10.808 1.00 5.63 O
ANISOU 1420 O PHE A 168 623 692 825 110 366 -5 O
ATOM 1421 CB PHE A 168 -0.877 6.651 11.910 1.00 5.77 C
ANISOU 1421 CB PHE A 168 671 588 934 99 159 -66 C
ATOM 1422 CG PHE A 168 -0.403 5.260 11.561 1.00 5.19 C
ANISOU 1422 CG PHE A 168 594 590 787 66 195 -87 C
ATOM 1423 CD1 PHE A 168 0.540 5.029 10.579 1.00 6.26 C
ANISOU 1423 CD1 PHE A 168 746 517 1116 30 428 -30 C
ATOM 1424 CD2 PHE A 168 -0.895 4.144 12.216 1.00 5.64 C
ANISOU 1424 CD2 PHE A 168 716 647 781 136 344 19 C
ATOM 1425 CE1 PHE A 168 0.964 3.781 10.270 1.00 6.11 C
ANISOU 1425 CE1 PHE A 168 791 576 956 77 483 -55 C
ATOM 1426 CE2 PHE A 168 -0.439 2.886 11.935 1.00 6.67 C
ANISOU 1426 CE2 PHE A 168 1158 592 784 -50 398 59 C
ATOM 1427 CZ PHE A 168 0.510 2.704 10.979 1.00 6.20 C
ANISOU 1427 CZ PHE A 168 785 537 1034 182 310 29 C
ATOM 1428 N ILE A 169 0.310 9.616 11.255 1.00 5.49 N
ANISOU 1428 N ILE A 169 741 568 776 148 351 65 N
ATOM 1429 CA ILE A 169 0.782 10.609 10.310 1.00 5.55 C
ANISOU 1429 CA ILE A 169 1003 434 672 25 434 -128 C
ATOM 1430 C ILE A 169 2.001 11.323 10.855 1.00 6.15 C
ANISOU 1430 C ILE A 169 736 790 812 48 314 -30 C
ATOM 1431 O ILE A 169 2.983 11.477 10.136 1.00 6.37 O
ANISOU 1431 O ILE A 169 824 655 942 149 341 0 O
ATOM 1432 CB ILE A 169 -0.352 11.605 9.969 1.00 5.74 C
ANISOU 1432 CB ILE A 169 859 461 860 15 231 14 C
ATOM 1433 CG1 ILE A 169 -1.511 10.999 9.164 1.00 8.57 C
ANISOU 1433 CG1 ILE A 169 1282 901 1074 -594 85 169 C
ATOM 1434 CG2 ILE A 169 0.197 12.818 9.230 1.00 5.73 C
ANISOU 1434 CG2 ILE A 169 800 587 789 -122 117 33 C
ATOM 1435 CD1 ILE A 169 -1.166 10.661 7.719 1.00 9.48 C
ANISOU 1435 CD1 ILE A 169 1441 1081 1082 357 -234 -29 C
ATOM 1436 N GLU A 170 1.934 11.813 12.087 1.00 5.50 N
ANISOU 1436 N GLU A 170 754 642 693 59 198 72 N
ATOM 1437 CA GLU A 170 2.991 12.669 12.609 1.00 6.21 C
ANISOU 1437 CA GLU A 170 860 680 820 93 269 -88 C
ATOM 1438 C GLU A 170 4.146 11.882 13.168 1.00 6.07 C
ANISOU 1438 C GLU A 170 698 823 787 -1 255 -43 C
ATOM 1439 O GLU A 170 5.239 12.415 13.339 1.00 8.57 O
ANISOU 1439 O GLU A 170 829 1064 1362 -160 175 -175 O
ATOM 1440 CB GLU A 170 2.450 13.628 13.692 1.00 6.14 C
ANISOU 1440 CB GLU A 170 941 761 631 93 268 -35 C
ATOM 1441 CG GLU A 170 1.392 14.576 13.209 1.00 6.55 C
ANISOU 1441 CG GLU A 170 1054 553 880 117 169 -146 C
ATOM 1442 CD GLU A 170 1.871 15.636 12.267 1.00 7.12 C
ANISOU 1442 CD GLU A 170 1042 738 926 1 143 -2 C
ATOM 1443 OE1 GLU A 170 3.073 15.800 12.011 1.00 8.46 O
ANISOU 1443 OE1 GLU A 170 1158 867 1190 -116 150 87 O
ATOM 1444 OE2 GLU A 170 1.012 16.382 11.727 1.00 9.18 O
ANISOU 1444 OE2 GLU A 170 1237 1088 1165 -18 126 275 O
ATOM 1445 N GLY A 171 3.940 10.602 13.472 1.00 6.61 N
ANISOU 1445 N GLY A 171 732 770 1009 74 114 -22 N
ATOM 1446 CA GLY A 171 4.924 9.767 14.120 1.00 6.21 C
ANISOU 1446 CA GLY A 171 719 797 845 -72 -39 -119 C
ATOM 1447 C GLY A 171 5.373 8.608 13.280 1.00 6.67 C
ANISOU 1447 C GLY A 171 780 741 1013 92 184 40 C
ATOM 1448 O GLY A 171 6.495 8.575 12.805 1.00 8.18 O
ANISOU 1448 O GLY A 171 744 1295 1070 22 260 20 O
ATOM 1449 N ALA A 172 4.504 7.622 13.075 1.00 6.36 N
ANISOU 1449 N ALA A 172 703 694 1021 166 91 -109 N
ATOM 1450 CA ALA A 172 4.943 6.388 12.424 1.00 6.14 C
ANISOU 1450 CA ALA A 172 754 616 964 250 153 70 C
ATOM 1451 C ALA A 172 5.396 6.602 10.997 1.00 6.04 C
ANISOU 1451 C ALA A 172 628 742 926 226 55 -90 C
ATOM 1452 O ALA A 172 6.391 6.027 10.575 1.00 7.06 O
ANISOU 1452 O ALA A 172 878 775 1029 356 231 -151 O
ATOM 1453 CB ALA A 172 3.824 5.381 12.498 1.00 6.80 C
ANISOU 1453 CB ALA A 172 673 701 1208 186 219 -253 C
ATOM 1454 N LEU A 173 4.703 7.457 10.242 1.00 5.72 N
ANISOU 1454 N LEU A 173 758 526 888 176 241 -16 N
ATOM 1455 CA LEU A 173 5.067 7.687 8.844 1.00 5.90 C
ANISOU 1455 CA LEU A 173 732 645 865 -12 162 -55 C
ATOM 1456 C LEU A 173 6.474 8.245 8.739 1.00 5.67 C
ANISOU 1456 C LEU A 173 646 575 932 134 247 -65 C
ATOM 1457 O LEU A 173 7.364 7.611 8.130 1.00 6.42 O
ANISOU 1457 O LEU A 173 784 702 953 105 248 -205 O
ATOM 1458 CB LEU A 173 3.981 8.548 8.193 1.00 6.34 C
ANISOU 1458 CB LEU A 173 687 846 875 35 171 46 C
ATOM 1459 CG LEU A 173 4.332 9.198 6.869 1.00 6.13 C
ANISOU 1459 CG LEU A 173 776 706 847 136 295 -56 C
ATOM 1460 CD1 LEU A 173 4.587 8.127 5.797 1.00 8.39 C
ANISOU 1460 CD1 LEU A 173 1390 834 962 214 332 -141 C
ATOM 1461 CD2 LEU A 173 3.251 10.119 6.400 1.00 7.73 C
ANISOU 1461 CD2 LEU A 173 1210 809 919 316 318 171 C
ATOM 1462 N PRO A 174 6.796 9.408 9.303 1.00 6.34 N
ANISOU 1462 N PRO A 174 676 710 1023 60 218 -226 N
ATOM 1463 CA PRO A 174 8.181 9.895 9.139 1.00 7.85 C
ANISOU 1463 CA PRO A 174 689 937 1356 19 249 -520 C
ATOM 1464 C PRO A 174 9.194 9.014 9.827 1.00 7.39 C
ANISOU 1464 C PRO A 174 604 866 1340 -46 339 -452 C
ATOM 1465 O PRO A 174 10.338 8.966 9.379 1.00 8.48 O
ANISOU 1465 O PRO A 174 662 1288 1271 81 397 -296 O
ATOM 1466 CB PRO A 174 8.137 11.299 9.754 1.00 9.46 C
ANISOU 1466 CB PRO A 174 815 889 1891 -6 458 -615 C
ATOM 1467 CG PRO A 174 6.926 11.360 10.605 1.00 8.03 C
ANISOU 1467 CG PRO A 174 687 720 1645 28 344 -477 C
ATOM 1468 CD PRO A 174 5.975 10.411 9.959 1.00 6.51 C
ANISOU 1468 CD PRO A 174 790 813 871 69 304 -250 C
ATOM 1469 N LYS A 175 8.840 8.328 10.919 1.00 7.76 N
ANISOU 1469 N LYS A 175 659 1044 1243 -143 353 -442 N
ATOM 1470 CA LYS A 175 9.825 7.468 11.581 1.00 7.92 C
ANISOU 1470 CA LYS A 175 749 1092 1166 -238 280 -397 C
ATOM 1471 C LYS A 175 10.224 6.289 10.712 1.00 7.95 C
ANISOU 1471 C LYS A 175 830 1324 865 217 51 -378 C
ATOM 1472 O LYS A 175 11.231 5.602 10.904 1.00 12.21 O
ANISOU 1472 O LYS A 175 1109 2436 1094 819 -283 -576 O
ATOM 1473 CB LYS A 175 9.298 7.025 12.942 1.00 10.69 C
ANISOU 1473 CB LYS A 175 924 2010 1126 396 525 -262 C
ATOM 1474 CG LYS A 175 9.619 8.100 13.983 1.00 22.72 C
ANISOU 1474 CG LYS A 175 4489 2784 1359 652 342 -906 C
ATOM 1475 CD LYS A 175 8.930 7.890 15.320 1.00 42.82 C
ANISOU 1475 CD LYS A 175 7653 7268 1349 -673 1243 -1646 C
ATOM 1476 CE LYS A 175 8.967 9.143 16.194 1.00 48.64 C
ANISOU 1476 CE LYS A 175 9327 8230 924 1740 -281 -2228 C
ATOM 1477 NZ LYS A 175 7.686 9.292 16.962 1.00 74.51 N
ANISOU 1477 NZ LYS A 175 9969 15931 2409 3999 120 -4194 N
ATOM 1478 N CYS A 176 9.387 5.977 9.712 1.00 6.28 N
ANISOU 1478 N CYS A 176 685 755 947 266 -4 -190 N
ATOM 1479 CA CYS A 176 9.658 4.845 8.845 1.00 6.02 C
ANISOU 1479 CA CYS A 176 684 739 863 370 -32 -163 C
ATOM 1480 C CYS A 176 10.071 5.221 7.429 1.00 5.55 C
ANISOU 1480 C CYS A 176 415 815 879 219 -100 -206 C
ATOM 1481 O CYS A 176 9.941 4.430 6.475 1.00 5.81 O
ANISOU 1481 O CYS A 176 620 779 809 114 108 -135 O
ATOM 1482 CB CYS A 176 8.473 3.887 8.837 1.00 7.87 C
ANISOU 1482 CB CYS A 176 1266 768 956 3 97 -180 C
ATOM 1483 SG CYS A 176 8.209 3.039 10.405 1.00 11.64 S
ANISOU 1483 SG CYS A 176 1888 1245 1289 -18 224 155 S
ATOM 1484 N VAL A 177 10.630 6.422 7.316 1.00 6.06 N
ANISOU 1484 N VAL A 177 513 970 819 72 202 -372 N
ATOM 1485 CA VAL A 177 11.383 6.922 6.164 1.00 6.11 C
ANISOU 1485 CA VAL A 177 577 997 746 110 198 -359 C
ATOM 1486 C VAL A 177 12.769 7.270 6.660 1.00 5.83 C
ANISOU 1486 C VAL A 177 613 895 706 2 227 -72 C
ATOM 1487 O VAL A 177 12.862 7.919 7.696 1.00 7.69 O
ANISOU 1487 O VAL A 177 748 1223 952 -5 123 -418 O
ATOM 1488 CB VAL A 177 10.693 8.141 5.518 1.00 6.82 C
ANISOU 1488 CB VAL A 177 611 1040 940 -41 63 -243 C
ATOM 1489 CG1 VAL A 177 11.477 8.601 4.300 1.00 8.10 C
ANISOU 1489 CG1 VAL A 177 841 1209 1029 -248 112 -126 C
ATOM 1490 CG2 VAL A 177 9.249 7.849 5.146 1.00 7.48 C
ANISOU 1490 CG2 VAL A 177 563 1120 1158 17 90 -295 C
ATOM 1491 N VAL A 178 13.819 6.851 6.004 1.00 5.97 N
ANISOU 1491 N VAL A 178 476 864 927 6 57 -224 N
ATOM 1492 CA VAL A 178 15.176 7.148 6.479 1.00 6.51 C
ANISOU 1492 CA VAL A 178 494 1114 865 -206 127 -303 C
ATOM 1493 C VAL A 178 15.483 8.610 6.299 1.00 6.73 C
ANISOU 1493 C VAL A 178 359 1156 1044 -109 289 -197 C
ATOM 1494 O VAL A 178 15.915 9.294 7.237 1.00 8.00 O
ANISOU 1494 O VAL A 178 663 1000 1378 -35 -16 -328 O
ATOM 1495 CB VAL A 178 16.206 6.251 5.793 1.00 7.00 C
ANISOU 1495 CB VAL A 178 522 1095 1043 -74 149 -186 C
ATOM 1496 CG1 VAL A 178 17.633 6.638 6.184 1.00 8.03 C
ANISOU 1496 CG1 VAL A 178 477 1013 1562 -66 88 -122 C
ATOM 1497 CG2 VAL A 178 15.983 4.798 6.141 1.00 8.02 C
ANISOU 1497 CG2 VAL A 178 792 1077 1179 -269 364 -294 C
ATOM 1498 N ARG A 179 15.256 9.136 5.099 1.00 7.19 N
ANISOU 1498 N ARG A 179 552 1022 1159 39 194 -185 N
ATOM 1499 CA ARG A 179 15.481 10.562 4.885 1.00 8.10 C
ANISOU 1499 CA ARG A 179 845 1010 1221 -89 117 -240 C
ATOM 1500 C ARG A 179 14.366 11.350 5.551 1.00 8.55 C
ANISOU 1500 C ARG A 179 755 977 1517 83 33 -143 C
ATOM 1501 O ARG A 179 13.267 10.852 5.778 1.00 9.20 O
ANISOU 1501 O ARG A 179 767 1108 1619 112 -11 -6 O
ATOM 1502 CB ARG A 179 15.552 10.888 3.384 1.00 9.87 C
ANISOU 1502 CB ARG A 179 1369 1147 1235 -183 -64 -32 C
ATOM 1503 CG ARG A 179 14.219 10.726 2.722 1.00 12.41 C
ANISOU 1503 CG ARG A 179 1617 1688 1410 -341 -302 -178 C
ATOM 1504 CD ARG A 179 13.936 11.769 1.739 1.00 15.66 C
ANISOU 1504 CD ARG A 179 1684 967 3298 334 -1111 -154 C
ATOM 1505 NE ARG A 179 12.697 11.519 1.017 1.00 11.72 N
ANISOU 1505 NE ARG A 179 1362 748 2342 172 -509 -333 N
ATOM 1506 CZ ARG A 179 11.747 12.436 0.915 1.00 7.63 C
ANISOU 1506 CZ ARG A 179 803 675 1421 -51 201 -109 C
ATOM 1507 NH1 ARG A 179 11.855 13.616 1.483 1.00 7.94 N
ANISOU 1507 NH1 ARG A 179 1099 679 1237 -103 262 -124 N
ATOM 1508 NH2 ARG A 179 10.671 12.129 0.223 1.00 7.40 N
ANISOU 1508 NH2 ARG A 179 606 1024 1183 -182 412 -197 N
ATOM 1509 N PRO A 180 14.641 12.587 5.907 1.00 9.15 N
ANISOU 1509 N PRO A 180 670 1062 1745 156 52 -231 N
ATOM 1510 CA PRO A 180 13.576 13.393 6.503 1.00 8.86 C
ANISOU 1510 CA PRO A 180 917 1120 1329 199 -11 -273 C
ATOM 1511 C PRO A 180 12.548 13.812 5.459 1.00 8.34 C
ANISOU 1511 C PRO A 180 896 946 1326 328 -1 -390 C
ATOM 1512 O PRO A 180 12.906 14.317 4.379 1.00 11.45 O
ANISOU 1512 O PRO A 180 1103 1587 1661 -217 -317 193 O
ATOM 1513 CB PRO A 180 14.271 14.659 6.987 1.00 12.17 C
ANISOU 1513 CB PRO A 180 1316 1196 2112 171 -487 -449 C
ATOM 1514 CG PRO A 180 15.673 14.509 6.599 1.00 18.56 C
ANISOU 1514 CG PRO A 180 1445 1825 3784 -505 192 -1074 C
ATOM 1515 CD PRO A 180 15.932 13.274 5.828 1.00 12.37 C
ANISOU 1515 CD PRO A 180 731 1461 2508 -105 -217 -343 C
ATOM 1516 N LEU A 181 11.292 13.623 5.776 1.00 10.26 N
ANISOU 1516 N LEU A 181 929 1627 1345 328 57 -401 N
ATOM 1517 CA LEU A 181 10.184 14.144 4.976 1.00 8.95 C
ANISOU 1517 CA LEU A 181 819 1178 1405 136 97 -287 C
ATOM 1518 C LEU A 181 10.117 15.656 5.137 1.00 9.73 C
ANISOU 1518 C LEU A 181 1076 1187 1433 -48 131 -246 C
ATOM 1519 O LEU A 181 10.312 16.163 6.255 1.00 11.33 O
ANISOU 1519 O LEU A 181 1671 1181 1452 377 -170 -312 O
ATOM 1520 CB LEU A 181 8.827 13.495 5.342 1.00 8.31 C
ANISOU 1520 CB LEU A 181 947 1079 1132 96 158 -208 C
ATOM 1521 CG LEU A 181 8.702 12.005 5.003 1.00 7.66 C
ANISOU 1521 CG LEU A 181 959 923 1030 228 261 -15 C
ATOM 1522 CD1 LEU A 181 7.365 11.468 5.497 1.00 9.51 C
ANISOU 1522 CD1 LEU A 181 943 1230 1439 30 199 -6 C
ATOM 1523 CD2 LEU A 181 8.881 11.766 3.497 1.00 9.63 C
ANISOU 1523 CD2 LEU A 181 1322 1154 1183 -93 266 -286 C
ATOM 1524 N THR A 182 9.859 16.352 4.061 1.00 8.40 N
ANISOU 1524 N THR A 182 745 1098 1349 335 75 -465 N
ATOM 1525 CA THR A 182 9.744 17.799 4.162 1.00 8.50 C
ANISOU 1525 CA THR A 182 664 1007 1559 4 101 -497 C
ATOM 1526 C THR A 182 8.348 18.177 4.667 1.00 7.36 C
ANISOU 1526 C THR A 182 699 675 1424 108 41 -251 C
ATOM 1527 O THR A 182 7.404 17.380 4.621 1.00 7.00 O
ANISOU 1527 O THR A 182 744 582 1333 23 113 -188 O
ATOM 1528 CB THR A 182 10.014 18.527 2.833 1.00 10.07 C
ANISOU 1528 CB THR A 182 1117 984 1726 -23 350 -442 C
ATOM 1529 OG1 THR A 182 8.901 18.336 1.943 1.00 10.43 O
ANISOU 1529 OG1 THR A 182 1152 1239 1573 -126 337 -87 O
ATOM 1530 CG2 THR A 182 11.264 17.974 2.153 1.00 12.77 C
ANISOU 1530 CG2 THR A 182 1187 1543 2123 69 649 -174 C
ATOM 1531 N GLU A 183 8.207 19.411 5.079 1.00 8.45 N
ANISOU 1531 N GLU A 183 852 649 1711 -61 282 -298 N
ATOM 1532 CA AGLU A 183 6.898 19.848 5.547 0.60 9.34 C
ANISOU 1532 CA AGLU A 183 1018 1141 1389 218 196 -622 C
ATOM 1533 CA BGLU A 183 6.939 19.962 5.503 0.40 8.67 C
ANISOU 1533 CA BGLU A 183 942 873 1479 141 215 -309 C
ATOM 1534 C GLU A 183 5.913 19.920 4.385 1.00 7.42 C
ANISOU 1534 C GLU A 183 1015 447 1358 62 236 -54 C
ATOM 1535 O GLU A 183 4.725 19.669 4.632 1.00 7.88 O
ANISOU 1535 O GLU A 183 979 608 1406 -25 227 -36 O
ATOM 1536 CB AGLU A 183 6.931 21.165 6.328 0.60 10.05 C
ANISOU 1536 CB AGLU A 183 1209 992 1619 -169 545 -606 C
ATOM 1537 CB BGLU A 183 7.220 21.378 5.995 0.40 12.00 C
ANISOU 1537 CB BGLU A 183 1511 1078 1970 331 -47 -801 C
ATOM 1538 CG AGLU A 183 7.520 21.030 7.729 0.60 10.46 C
ANISOU 1538 CG AGLU A 183 446 1556 1971 42 163 -1107 C
ATOM 1539 CG BGLU A 183 6.321 21.954 7.003 0.40 21.22 C
ANISOU 1539 CG BGLU A 183 3216 2306 2540 -437 1234 -1636 C
ATOM 1540 CD AGLU A 183 6.923 19.961 8.600 0.60 13.14 C
ANISOU 1540 CD AGLU A 183 1110 2556 1326 269 152 -474 C
ATOM 1541 CD BGLU A 183 5.643 21.417 8.209 0.40 23.95 C
ANISOU 1541 CD BGLU A 183 3675 2720 2707 -754 1214 -1286 C
ATOM 1542 OE1AGLU A 183 5.704 19.960 8.888 0.60 18.09 O
ANISOU 1542 OE1AGLU A 183 1185 3122 2567 -805 449 -890 O
ATOM 1543 OE1BGLU A 183 5.948 20.298 8.668 0.40 18.95 O
ANISOU 1543 OE1BGLU A 183 2458 2545 2195 -498 1468 -1791 O
ATOM 1544 OE2AGLU A 183 7.629 19.035 9.071 0.60 23.42 O
ANISOU 1544 OE2AGLU A 183 3212 3573 2116 1177 -144 302 O
ATOM 1545 OE2BGLU A 183 4.777 22.174 8.767 0.40 13.42 O
ANISOU 1545 OE2BGLU A 183 708 2862 1528 -534 -48 549 O
ATOM 1546 N VAL A 184 6.330 20.191 3.160 1.00 8.06 N
ANISOU 1546 N VAL A 184 1114 519 1430 -137 328 -225 N
ATOM 1547 CA VAL A 184 5.375 20.149 2.040 1.00 7.50 C
ANISOU 1547 CA VAL A 184 1039 572 1239 -60 411 -146 C
ATOM 1548 C VAL A 184 4.861 18.725 1.862 1.00 6.42 C
ANISOU 1548 C VAL A 184 911 574 955 56 240 -81 C
ATOM 1549 O VAL A 184 3.679 18.479 1.669 1.00 6.39 O
ANISOU 1549 O VAL A 184 850 493 1087 90 295 -71 O
ATOM 1550 CB VAL A 184 6.050 20.690 0.774 1.00 8.99 C
ANISOU 1550 CB VAL A 184 1242 671 1505 82 554 91 C
ATOM 1551 CG1 VAL A 184 5.299 20.344 -0.499 1.00 12.44 C
ANISOU 1551 CG1 VAL A 184 2115 1338 1275 -183 523 257 C
ATOM 1552 CG2 VAL A 184 6.202 22.202 0.868 1.00 12.95 C
ANISOU 1552 CG2 VAL A 184 2367 716 1837 -107 730 229 C
ATOM 1553 N GLU A 185 5.772 17.742 1.918 1.00 6.68 N
ANISOU 1553 N GLU A 185 647 513 1381 -119 277 -229 N
ATOM 1554 CA GLU A 185 5.361 16.355 1.835 1.00 5.74 C
ANISOU 1554 CA GLU A 185 685 507 989 0 177 -135 C
ATOM 1555 C GLU A 185 4.439 15.969 2.992 1.00 5.96 C
ANISOU 1555 C GLU A 185 563 618 1083 4 256 -177 C
ATOM 1556 O GLU A 185 3.402 15.338 2.784 1.00 6.25 O
ANISOU 1556 O GLU A 185 751 579 1045 -62 102 -22 O
ATOM 1557 CB GLU A 185 6.588 15.421 1.813 1.00 5.69 C
ANISOU 1557 CB GLU A 185 605 514 1042 -2 256 -158 C
ATOM 1558 CG GLU A 185 7.432 15.601 0.575 1.00 7.60 C
ANISOU 1558 CG GLU A 185 755 1017 1117 -36 334 -200 C
ATOM 1559 CD GLU A 185 8.775 14.925 0.600 1.00 6.29 C
ANISOU 1559 CD GLU A 185 905 604 880 42 405 30 C
ATOM 1560 OE1 GLU A 185 9.412 14.922 1.664 1.00 8.37 O
ANISOU 1560 OE1 GLU A 185 999 1159 1021 103 241 -190 O
ATOM 1561 OE2 GLU A 185 9.199 14.440 -0.482 1.00 7.19 O
ANISOU 1561 OE2 GLU A 185 751 932 1047 -106 375 -262 O
ATOM 1562 N MET A 186 4.818 16.371 4.197 1.00 6.08 N
ANISOU 1562 N MET A 186 600 621 1089 -40 262 -177 N
ATOM 1563 CA MET A 186 3.955 16.098 5.346 1.00 6.29 C
ANISOU 1563 CA MET A 186 677 656 1056 153 288 -139 C
ATOM 1564 C MET A 186 2.563 16.711 5.160 1.00 5.70 C
ANISOU 1564 C MET A 186 640 527 998 48 241 -96 C
ATOM 1565 O MET A 186 1.547 16.086 5.501 1.00 6.21 O
ANISOU 1565 O MET A 186 703 655 1002 0 334 49 O
ATOM 1566 CB MET A 186 4.570 16.594 6.634 1.00 6.73 C
ANISOU 1566 CB MET A 186 611 827 1119 -3 198 -51 C
ATOM 1567 CG MET A 186 5.769 15.760 7.092 1.00 7.90 C
ANISOU 1567 CG MET A 186 942 1024 1036 195 185 229 C
ATOM 1568 SD MET A 186 5.386 14.059 7.496 1.00 8.43 S
ANISOU 1568 SD MET A 186 1027 967 1208 254 231 34 S
ATOM 1569 CE MET A 186 4.288 14.314 8.876 1.00 9.41 C
ANISOU 1569 CE MET A 186 1352 548 1676 135 680 69 C
ATOM 1570 N ASP A 187 2.487 17.936 4.644 1.00 5.69 N
ANISOU 1570 N ASP A 187 666 570 928 53 264 31 N
ATOM 1571 CA ASP A 187 1.158 18.524 4.420 1.00 5.23 C
ANISOU 1571 CA ASP A 187 583 555 849 2 313 -52 C
ATOM 1572 C ASP A 187 0.360 17.742 3.392 1.00 5.28 C
ANISOU 1572 C ASP A 187 770 504 733 58 166 75 C
ATOM 1573 O ASP A 187 -0.872 17.593 3.532 1.00 6.09 O
ANISOU 1573 O ASP A 187 665 566 1083 166 112 -82 O
ATOM 1574 CB ASP A 187 1.311 19.982 3.996 1.00 5.56 C
ANISOU 1574 CB ASP A 187 526 563 1025 63 163 37 C
ATOM 1575 CG ASP A 187 1.584 20.924 5.157 1.00 6.31 C
ANISOU 1575 CG ASP A 187 818 550 1032 51 55 35 C
ATOM 1576 OD1 ASP A 187 1.381 20.580 6.332 1.00 7.63 O
ANISOU 1576 OD1 ASP A 187 1204 678 1017 30 79 23 O
ATOM 1577 OD2 ASP A 187 2.005 22.067 4.871 1.00 7.88 O
ANISOU 1577 OD2 ASP A 187 1086 615 1292 -101 199 -34 O
ATOM 1578 N HIS A 188 0.965 17.175 2.359 1.00 5.58 N
ANISOU 1578 N HIS A 188 844 505 770 42 217 8 N
ATOM 1579 CA HIS A 188 0.195 16.306 1.454 1.00 5.56 C
ANISOU 1579 CA HIS A 188 741 416 955 88 305 -47 C
ATOM 1580 C HIS A 188 -0.353 15.087 2.172 1.00 4.79 C
ANISOU 1580 C HIS A 188 563 383 874 164 197 -135 C
ATOM 1581 O HIS A 188 -1.463 14.655 1.927 1.00 7.29 O
ANISOU 1581 O HIS A 188 722 903 1145 -147 30 293 O
ATOM 1582 CB HIS A 188 1.087 15.883 0.272 1.00 5.72 C
ANISOU 1582 CB HIS A 188 882 524 768 -34 204 -116 C
ATOM 1583 CG HIS A 188 1.211 16.923 -0.794 1.00 6.28 C
ANISOU 1583 CG HIS A 188 974 457 954 -6 230 -51 C
ATOM 1584 ND1 HIS A 188 0.245 17.047 -1.786 1.00 7.64 N
ANISOU 1584 ND1 HIS A 188 1030 778 1093 34 183 249 N
ATOM 1585 CD2 HIS A 188 2.171 17.818 -1.129 1.00 6.34 C
ANISOU 1585 CD2 HIS A 188 1036 413 960 85 372 -19 C
ATOM 1586 CE1 HIS A 188 0.581 17.999 -2.634 1.00 8.68 C
ANISOU 1586 CE1 HIS A 188 1296 824 1176 -87 170 278 C
ATOM 1587 NE2 HIS A 188 1.776 18.503 -2.255 1.00 7.33 N
ANISOU 1587 NE2 HIS A 188 1121 772 891 56 355 66 N
ATOM 1588 N TYR A 189 0.437 14.483 3.058 1.00 4.68 N
ANISOU 1588 N TYR A 189 553 370 857 126 277 -96 N
ATOM 1589 CA TYR A 189 -0.037 13.332 3.816 1.00 5.04 C
ANISOU 1589 CA TYR A 189 630 469 815 37 303 -48 C
ATOM 1590 C TYR A 189 -1.046 13.716 4.885 1.00 4.61 C
ANISOU 1590 C TYR A 189 583 498 669 -7 162 -112 C
ATOM 1591 O TYR A 189 -1.949 12.922 5.183 1.00 4.93 O
ANISOU 1591 O TYR A 189 558 533 782 -55 215 -109 O
ATOM 1592 CB TYR A 189 1.160 12.606 4.412 1.00 4.99 C
ANISOU 1592 CB TYR A 189 702 435 760 52 220 -16 C
ATOM 1593 CG TYR A 189 1.887 11.742 3.418 1.00 4.69 C
ANISOU 1593 CG TYR A 189 639 464 681 144 117 4 C
ATOM 1594 CD1 TYR A 189 1.270 10.735 2.730 1.00 5.61 C
ANISOU 1594 CD1 TYR A 189 549 714 870 23 228 -202 C
ATOM 1595 CD2 TYR A 189 3.256 11.932 3.192 1.00 5.16 C
ANISOU 1595 CD2 TYR A 189 608 375 977 98 124 -128 C
ATOM 1596 CE1 TYR A 189 1.943 9.929 1.826 1.00 5.79 C
ANISOU 1596 CE1 TYR A 189 699 568 934 -13 213 -215 C
ATOM 1597 CE2 TYR A 189 3.934 11.125 2.287 1.00 4.75 C
ANISOU 1597 CE2 TYR A 189 679 422 704 28 263 58 C
ATOM 1598 CZ TYR A 189 3.289 10.126 1.612 1.00 5.33 C
ANISOU 1598 CZ TYR A 189 730 385 910 148 335 -77 C
ATOM 1599 OH TYR A 189 3.940 9.321 0.701 1.00 6.08 O
ANISOU 1599 OH TYR A 189 766 532 1012 168 224 -188 O
ATOM 1600 N ARG A 190 -0.954 14.893 5.476 1.00 4.86 N
ANISOU 1600 N ARG A 190 568 391 889 -37 300 -48 N
ATOM 1601 CA ARG A 190 -1.891 15.358 6.466 1.00 4.95 C
ANISOU 1601 CA ARG A 190 548 537 797 -25 306 -65 C
ATOM 1602 C ARG A 190 -3.266 15.696 5.883 1.00 4.70 C
ANISOU 1602 C ARG A 190 622 486 677 -79 277 -71 C
ATOM 1603 O ARG A 190 -4.280 15.621 6.609 1.00 4.82 O
ANISOU 1603 O ARG A 190 613 488 733 89 330 -2 O
ATOM 1604 CB ARG A 190 -1.355 16.619 7.148 1.00 5.66 C
ANISOU 1604 CB ARG A 190 548 572 1032 90 170 -175 C
ATOM 1605 CG ARG A 190 -0.203 16.409 8.104 1.00 4.98 C
ANISOU 1605 CG ARG A 190 527 574 791 52 284 -160 C
ATOM 1606 CD ARG A 190 0.552 17.701 8.311 1.00 6.03 C
ANISOU 1606 CD ARG A 190 623 761 906 -82 141 -63 C
ATOM 1607 NE ARG A 190 1.678 17.538 9.218 1.00 7.05 N
ANISOU 1607 NE ARG A 190 793 747 1139 -49 -67 -94 N
ATOM 1608 CZ ARG A 190 2.796 18.248 9.197 1.00 6.58 C
ANISOU 1608 CZ ARG A 190 631 836 1034 -5 126 -36 C
ATOM 1609 NH1 ARG A 190 3.010 19.186 8.315 1.00 7.85 N
ANISOU 1609 NH1 ARG A 190 1224 753 1008 37 340 -75 N
ATOM 1610 NH2 ARG A 190 3.724 17.960 10.132 1.00 8.58 N
ANISOU 1610 NH2 ARG A 190 811 1079 1369 -14 -188 -91 N
ATOM 1611 N GLU A 191 -3.323 16.146 4.635 1.00 5.30 N
ANISOU 1611 N GLU A 191 633 722 658 30 363 -76 N
ATOM 1612 CA GLU A 191 -4.516 16.773 4.127 1.00 5.38 C
ANISOU 1612 CA GLU A 191 697 518 830 63 294 -36 C
ATOM 1613 C GLU A 191 -5.760 15.939 4.281 1.00 5.12 C
ANISOU 1613 C GLU A 191 650 541 755 104 195 -84 C
ATOM 1614 O GLU A 191 -6.776 16.533 4.704 1.00 5.73 O
ANISOU 1614 O GLU A 191 660 703 815 179 280 67 O
ATOM 1615 CB GLU A 191 -4.316 17.161 2.676 1.00 6.79 C
ANISOU 1615 CB GLU A 191 779 840 961 -139 176 172 C
ATOM 1616 CG GLU A 191 -5.451 18.024 2.131 1.00 13.00 C
ANISOU 1616 CG GLU A 191 1531 1703 1706 241 -489 426 C
ATOM 1617 CD GLU A 191 -5.005 18.443 0.733 1.00 16.66 C
ANISOU 1617 CD GLU A 191 2739 2072 1520 304 -680 633 C
ATOM 1618 OE1 GLU A 191 -4.777 19.635 0.584 1.00 31.72 O
ANISOU 1618 OE1 GLU A 191 7330 1957 2766 594 735 1111 O
ATOM 1619 OE2 GLU A 191 -4.785 17.637 -0.179 1.00 26.34 O
ANISOU 1619 OE2 GLU A 191 5470 2847 1693 -168 -141 129 O
ATOM 1620 N PRO A 192 -5.803 14.646 3.990 1.00 4.99 N
ANISOU 1620 N PRO A 192 612 506 777 102 12 -26 N
ATOM 1621 CA PRO A 192 -7.046 13.892 4.161 1.00 5.37 C
ANISOU 1621 CA PRO A 192 746 445 850 62 2 45 C
ATOM 1622 C PRO A 192 -7.535 13.833 5.581 1.00 5.41 C
ANISOU 1622 C PRO A 192 722 456 876 54 90 -47 C
ATOM 1623 O PRO A 192 -8.717 13.480 5.804 1.00 6.78 O
ANISOU 1623 O PRO A 192 658 844 1074 55 145 -104 O
ATOM 1624 CB PRO A 192 -6.702 12.471 3.635 1.00 6.30 C
ANISOU 1624 CB PRO A 192 791 566 1038 32 25 -248 C
ATOM 1625 CG PRO A 192 -5.503 12.710 2.751 1.00 6.37 C
ANISOU 1625 CG PRO A 192 1000 456 965 63 113 -109 C
ATOM 1626 CD PRO A 192 -4.731 13.807 3.443 1.00 5.94 C
ANISOU 1626 CD PRO A 192 701 694 860 120 98 -179 C
ATOM 1627 N PHE A 193 -6.674 14.056 6.555 1.00 4.74 N
ANISOU 1627 N PHE A 193 612 458 732 23 273 -17 N
ATOM 1628 CA PHE A 193 -6.919 13.711 7.952 1.00 4.89 C
ANISOU 1628 CA PHE A 193 523 601 734 53 283 -27 C
ATOM 1629 C PHE A 193 -6.879 14.943 8.867 1.00 5.20 C
ANISOU 1629 C PHE A 193 769 535 673 122 326 39 C
ATOM 1630 O PHE A 193 -6.757 14.812 10.066 1.00 6.52 O
ANISOU 1630 O PHE A 193 1013 838 628 59 289 40 O
ATOM 1631 CB PHE A 193 -5.905 12.654 8.422 1.00 5.58 C
ANISOU 1631 CB PHE A 193 924 478 718 146 262 -27 C
ATOM 1632 CG PHE A 193 -6.023 11.421 7.552 1.00 4.54 C
ANISOU 1632 CG PHE A 193 721 487 517 118 234 105 C
ATOM 1633 CD1 PHE A 193 -7.183 10.678 7.501 1.00 5.62 C
ANISOU 1633 CD1 PHE A 193 903 373 859 76 328 12 C
ATOM 1634 CD2 PHE A 193 -4.962 11.042 6.766 1.00 5.59 C
ANISOU 1634 CD2 PHE A 193 854 458 810 202 300 -24 C
ATOM 1635 CE1 PHE A 193 -7.290 9.588 6.679 1.00 6.29 C
ANISOU 1635 CE1 PHE A 193 1059 426 903 23 256 -41 C
ATOM 1636 CE2 PHE A 193 -5.066 9.930 5.958 1.00 6.73 C
ANISOU 1636 CE2 PHE A 193 1139 520 897 174 413 -103 C
ATOM 1637 CZ PHE A 193 -6.228 9.214 5.876 1.00 6.54 C
ANISOU 1637 CZ PHE A 193 1117 533 836 194 156 -119 C
ATOM 1638 N LEU A 194 -7.048 16.135 8.309 1.00 5.91 N
ANISOU 1638 N LEU A 194 929 514 801 -10 335 119 N
ATOM 1639 CA LEU A 194 -7.070 17.378 9.093 1.00 6.85 C
ANISOU 1639 CA LEU A 194 1101 569 933 24 347 31 C
ATOM 1640 C LEU A 194 -8.112 17.366 10.198 1.00 7.21 C
ANISOU 1640 C LEU A 194 1252 396 1091 48 461 5 C
ATOM 1641 O LEU A 194 -7.913 17.958 11.272 1.00 8.70 O
ANISOU 1641 O LEU A 194 1483 753 1069 -58 561 -93 O
ATOM 1642 CB LEU A 194 -7.290 18.568 8.167 1.00 7.09 C
ANISOU 1642 CB LEU A 194 1208 467 1017 92 493 -21 C
ATOM 1643 CG LEU A 194 -6.185 18.853 7.168 1.00 7.69 C
ANISOU 1643 CG LEU A 194 1157 967 797 128 389 122 C
ATOM 1644 CD1 LEU A 194 -6.555 20.019 6.245 1.00 8.32 C
ANISOU 1644 CD1 LEU A 194 1237 780 1142 -74 359 217 C
ATOM 1645 CD2 LEU A 194 -4.900 19.160 7.887 1.00 10.08 C
ANISOU 1645 CD2 LEU A 194 1277 1231 1321 -118 211 328 C
ATOM 1646 N LYS A 195 -9.220 16.689 9.950 1.00 7.46 N
ANISOU 1646 N LYS A 195 1176 542 1117 93 621 -99 N
ATOM 1647 CA LYS A 195 -10.230 16.553 10.994 1.00 7.87 C
ANISOU 1647 CA LYS A 195 1419 719 850 -26 657 -19 C
ATOM 1648 C LYS A 195 -10.052 15.211 11.724 1.00 7.28 C
ANISOU 1648 C LYS A 195 1081 638 1046 -38 372 -65 C
ATOM 1649 O LYS A 195 -10.105 14.169 11.089 1.00 6.93 O
ANISOU 1649 O LYS A 195 1042 718 873 -67 453 -30 O
ATOM 1650 CB LYS A 195 -11.615 16.583 10.367 1.00 10.17 C
ANISOU 1650 CB LYS A 195 1329 1354 1180 363 619 240 C
ATOM 1651 CG LYS A 195 -11.982 17.884 9.724 1.00 15.21 C
ANISOU 1651 CG LYS A 195 2108 1277 2393 669 434 336 C
ATOM 1652 CD ALYS A 195 -13.393 18.071 9.193 0.40 26.84 C
ANISOU 1652 CD ALYS A 195 3485 3212 3500 1667 -1401 -129 C
ATOM 1653 CD BLYS A 195 -11.778 19.127 10.597 0.60 23.39 C
ANISOU 1653 CD BLYS A 195 3022 1716 4149 1993 -566 -769 C
ATOM 1654 CE ALYS A 195 -13.582 19.537 8.801 0.40 29.74 C
ANISOU 1654 CE ALYS A 195 3901 3339 4060 1907 -1631 35 C
ATOM 1655 CE BLYS A 195 -12.506 19.258 11.907 0.60 29.85 C
ANISOU 1655 CE BLYS A 195 3225 3018 5100 1400 146 -2355 C
ATOM 1656 NZ ALYS A 195 -14.640 20.268 9.546 0.40 30.16 N
ANISOU 1656 NZ ALYS A 195 7015 897 3549 341 1307 119 N
ATOM 1657 NZ BLYS A 195 -13.956 19.628 11.827 0.60 19.52 N
ANISOU 1657 NZ BLYS A 195 3090 2463 1865 789 -424 218 N
ATOM 1658 N PRO A 196 -9.798 15.245 13.035 1.00 6.48 N
ANISOU 1658 N PRO A 196 935 556 973 130 602 -69 N
ATOM 1659 CA PRO A 196 -9.514 13.992 13.756 1.00 6.30 C
ANISOU 1659 CA PRO A 196 713 572 1108 135 460 -93 C
ATOM 1660 C PRO A 196 -10.509 12.862 13.523 1.00 5.96 C
ANISOU 1660 C PRO A 196 714 493 1060 190 420 -66 C
ATOM 1661 O PRO A 196 -10.076 11.695 13.362 1.00 5.75 O
ANISOU 1661 O PRO A 196 719 513 952 202 383 -127 O
ATOM 1662 CB PRO A 196 -9.484 14.486 15.196 1.00 6.98 C
ANISOU 1662 CB PRO A 196 854 729 1068 184 248 -98 C
ATOM 1663 CG PRO A 196 -8.950 15.896 15.107 1.00 8.18 C
ANISOU 1663 CG PRO A 196 1077 887 1144 -30 644 -371 C
ATOM 1664 CD PRO A 196 -9.647 16.440 13.878 1.00 8.51 C
ANISOU 1664 CD PRO A 196 1617 560 1057 -70 733 -150 C
ATOM 1665 N VAL A 197 -11.789 13.132 13.485 1.00 5.92 N
ANISOU 1665 N VAL A 197 733 531 984 259 367 38 N
ATOM 1666 CA VAL A 197 -12.734 12.004 13.334 1.00 7.00 C
ANISOU 1666 CA VAL A 197 855 832 971 53 255 35 C
ATOM 1667 C VAL A 197 -12.533 11.211 12.070 1.00 6.99 C
ANISOU 1667 C VAL A 197 819 920 915 -176 248 63 C
ATOM 1668 O VAL A 197 -12.935 10.056 11.969 1.00 7.58 O
ANISOU 1668 O VAL A 197 881 886 1113 -156 176 -31 O
ATOM 1669 CB VAL A 197 -14.170 12.557 13.432 1.00 8.50 C
ANISOU 1669 CB VAL A 197 760 976 1492 127 127 112 C
ATOM 1670 CG1 VAL A 197 -14.532 13.365 12.213 1.00 9.83 C
ANISOU 1670 CG1 VAL A 197 766 1613 1357 154 257 273 C
ATOM 1671 CG2 VAL A 197 -15.196 11.467 13.702 1.00 9.15 C
ANISOU 1671 CG2 VAL A 197 956 856 1665 86 393 -148 C
ATOM 1672 N ASP A 198 -11.959 11.817 11.020 1.00 6.29 N
ANISOU 1672 N ASP A 198 623 796 971 139 315 50 N
ATOM 1673 CA ASP A 198 -11.760 11.174 9.745 1.00 6.31 C
ANISOU 1673 CA ASP A 198 593 888 917 124 283 59 C
ATOM 1674 C ASP A 198 -10.596 10.187 9.797 1.00 5.38 C
ANISOU 1674 C ASP A 198 499 808 736 19 169 22 C
ATOM 1675 O ASP A 198 -10.280 9.552 8.755 1.00 6.14 O
ANISOU 1675 O ASP A 198 827 754 750 67 130 -71 O
ATOM 1676 CB ASP A 198 -11.497 12.252 8.672 1.00 7.43 C
ANISOU 1676 CB ASP A 198 837 1023 964 158 145 214 C
ATOM 1677 CG ASP A 198 -12.724 13.107 8.384 1.00 8.85 C
ANISOU 1677 CG ASP A 198 881 793 1687 108 -18 64 C
ATOM 1678 OD1 ASP A 198 -13.850 12.665 8.696 1.00 10.34 O
ANISOU 1678 OD1 ASP A 198 812 1585 1531 141 110 320 O
ATOM 1679 OD2 ASP A 198 -12.519 14.202 7.836 1.00 9.89 O
ANISOU 1679 OD2 ASP A 198 1082 1038 1638 250 171 300 O
ATOM 1680 N ARG A 199 -9.977 9.997 10.948 1.00 4.87 N
ANISOU 1680 N ARG A 199 659 567 625 191 260 -155 N
ATOM 1681 CA ARG A 199 -8.808 9.116 11.073 1.00 4.62 C
ANISOU 1681 CA ARG A 199 593 511 652 81 256 59 C
ATOM 1682 C ARG A 199 -9.139 7.675 11.393 1.00 5.06 C
ANISOU 1682 C ARG A 199 737 534 650 -17 126 146 C
ATOM 1683 O ARG A 199 -8.234 6.863 11.632 1.00 5.09 O
ANISOU 1683 O ARG A 199 664 521 747 92 -42 -24 O
ATOM 1684 CB ARG A 199 -7.835 9.712 12.101 1.00 5.07 C
ANISOU 1684 CB ARG A 199 614 534 778 16 162 131 C
ATOM 1685 CG ARG A 199 -7.282 11.034 11.698 1.00 5.11 C
ANISOU 1685 CG ARG A 199 679 529 733 12 163 138 C
ATOM 1686 CD ARG A 199 -6.616 11.807 12.795 1.00 5.43 C
ANISOU 1686 CD ARG A 199 737 518 811 43 338 -18 C
ATOM 1687 NE ARG A 199 -6.346 13.216 12.404 1.00 5.33 N
ANISOU 1687 NE ARG A 199 693 580 753 -24 321 5 N
ATOM 1688 CZ ARG A 199 -6.002 14.157 13.245 1.00 5.61 C
ANISOU 1688 CZ ARG A 199 696 600 834 -70 298 -110 C
ATOM 1689 NH1 ARG A 199 -5.902 13.899 14.536 1.00 6.75 N
ANISOU 1689 NH1 ARG A 199 901 827 834 136 190 -120 N
ATOM 1690 NH2 ARG A 199 -5.755 15.386 12.792 1.00 6.66 N
ANISOU 1690 NH2 ARG A 199 767 742 1022 -277 404 -42 N
ATOM 1691 N GLU A 200 -10.413 7.285 11.370 1.00 5.31 N
ANISOU 1691 N GLU A 200 596 530 893 140 278 -18 N
ATOM 1692 CA GLU A 200 -10.783 5.925 11.651 1.00 4.43 C
ANISOU 1692 CA GLU A 200 574 521 588 -10 119 -63 C
ATOM 1693 C GLU A 200 -10.001 4.882 10.864 1.00 4.55 C
ANISOU 1693 C GLU A 200 512 526 690 16 158 -68 C
ATOM 1694 O GLU A 200 -9.549 3.886 11.483 1.00 5.20 O
ANISOU 1694 O GLU A 200 731 439 803 -46 229 40 O
ATOM 1695 CB GLU A 200 -12.304 5.678 11.384 1.00 5.12 C
ANISOU 1695 CB GLU A 200 525 624 798 128 88 -55 C
ATOM 1696 CG GLU A 200 -12.777 4.405 12.085 1.00 6.05 C
ANISOU 1696 CG GLU A 200 687 815 798 -93 280 -124 C
ATOM 1697 CD GLU A 200 -12.852 4.497 13.586 1.00 5.57 C
ANISOU 1697 CD GLU A 200 500 844 772 328 275 -103 C
ATOM 1698 OE1 GLU A 200 -12.987 5.623 14.127 1.00 6.12 O
ANISOU 1698 OE1 GLU A 200 774 775 778 47 377 -92 O
ATOM 1699 OE2 GLU A 200 -12.784 3.405 14.228 1.00 6.52 O
ANISOU 1699 OE2 GLU A 200 880 751 847 186 130 -171 O
ATOM 1700 N PRO A 201 -9.800 5.009 9.537 1.00 4.43 N
ANISOU 1700 N PRO A 201 367 582 735 59 210 -6 N
ATOM 1701 CA PRO A 201 -9.060 3.952 8.852 1.00 5.10 C
ANISOU 1701 CA PRO A 201 610 553 775 32 247 -145 C
ATOM 1702 C PRO A 201 -7.634 3.807 9.386 1.00 4.67 C
ANISOU 1702 C PRO A 201 560 372 841 103 355 -173 C
ATOM 1703 O PRO A 201 -7.099 2.681 9.314 1.00 5.37 O
ANISOU 1703 O PRO A 201 693 387 959 88 365 -77 O
ATOM 1704 CB PRO A 201 -9.050 4.379 7.411 1.00 6.83 C
ANISOU 1704 CB PRO A 201 1032 776 786 93 206 -131 C
ATOM 1705 CG PRO A 201 -9.679 5.684 7.285 1.00 11.56 C
ANISOU 1705 CG PRO A 201 2848 735 808 489 542 4 C
ATOM 1706 CD PRO A 201 -10.254 6.038 8.600 1.00 5.60 C
ANISOU 1706 CD PRO A 201 485 887 755 207 124 30 C
ATOM 1707 N LEU A 202 -7.056 4.880 9.863 1.00 4.42 N
ANISOU 1707 N LEU A 202 551 399 727 179 122 -91 N
ATOM 1708 CA LEU A 202 -5.667 4.840 10.314 1.00 4.22 C
ANISOU 1708 CA LEU A 202 640 484 477 136 179 -80 C
ATOM 1709 C LEU A 202 -5.506 4.023 11.584 1.00 4.63 C
ANISOU 1709 C LEU A 202 535 622 600 106 197 39 C
ATOM 1710 O LEU A 202 -4.406 3.509 11.830 1.00 4.72 O
ANISOU 1710 O LEU A 202 596 542 658 71 219 113 O
ATOM 1711 CB LEU A 202 -5.180 6.251 10.549 1.00 4.44 C
ANISOU 1711 CB LEU A 202 378 533 775 123 240 -43 C
ATOM 1712 CG LEU A 202 -5.395 7.258 9.426 1.00 4.56 C
ANISOU 1712 CG LEU A 202 496 444 794 121 311 -13 C
ATOM 1713 CD1 LEU A 202 -4.629 8.546 9.714 1.00 6.45 C
ANISOU 1713 CD1 LEU A 202 744 582 1124 9 101 73 C
ATOM 1714 CD2 LEU A 202 -5.001 6.707 8.066 1.00 5.54 C
ANISOU 1714 CD2 LEU A 202 591 751 764 188 355 61 C
ATOM 1715 N TRP A 203 -6.538 3.920 12.409 1.00 4.35 N
ANISOU 1715 N TRP A 203 623 405 627 242 307 -40 N
ATOM 1716 CA TRP A 203 -6.586 3.111 13.601 1.00 4.65 C
ANISOU 1716 CA TRP A 203 659 559 548 81 166 -62 C
ATOM 1717 C TRP A 203 -7.029 1.685 13.300 1.00 4.55 C
ANISOU 1717 C TRP A 203 619 458 651 167 253 -33 C
ATOM 1718 O TRP A 203 -6.500 0.726 13.840 1.00 4.76 O
ANISOU 1718 O TRP A 203 757 531 519 173 276 38 O
ATOM 1719 CB TRP A 203 -7.470 3.791 14.667 1.00 4.65 C
ANISOU 1719 CB TRP A 203 734 507 526 74 204 -67 C
ATOM 1720 CG TRP A 203 -7.690 2.892 15.870 1.00 4.51 C
ANISOU 1720 CG TRP A 203 707 439 569 123 244 -76 C
ATOM 1721 CD1 TRP A 203 -6.919 2.747 16.956 1.00 4.78 C
ANISOU 1721 CD1 TRP A 203 689 458 670 211 231 18 C
ATOM 1722 CD2 TRP A 203 -8.778 2.000 16.073 1.00 4.86 C
ANISOU 1722 CD2 TRP A 203 776 545 527 61 380 -154 C
ATOM 1723 NE1 TRP A 203 -7.420 1.836 17.843 1.00 5.54 N
ANISOU 1723 NE1 TRP A 203 874 536 693 121 255 66 N
ATOM 1724 CE2 TRP A 203 -8.565 1.369 17.308 1.00 4.88 C
ANISOU 1724 CE2 TRP A 203 802 445 607 140 367 -77 C
ATOM 1725 CE3 TRP A 203 -9.912 1.669 15.340 1.00 6.30 C
ANISOU 1725 CE3 TRP A 203 758 845 791 -21 275 -77 C
ATOM 1726 CZ2 TRP A 203 -9.453 0.437 17.791 1.00 6.41 C
ANISOU 1726 CZ2 TRP A 203 1193 473 770 -60 359 -48 C
ATOM 1727 CZ3 TRP A 203 -10.805 0.739 15.823 1.00 6.18 C
ANISOU 1727 CZ3 TRP A 203 763 585 999 57 323 -212 C
ATOM 1728 CH2 TRP A 203 -10.562 0.133 17.062 1.00 6.94 C
ANISOU 1728 CH2 TRP A 203 1165 617 856 -189 485 -249 C
ATOM 1729 N ARG A 204 -8.036 1.522 12.446 1.00 4.43 N
ANISOU 1729 N ARG A 204 633 308 744 212 206 -131 N
ATOM 1730 CA ARG A 204 -8.489 0.155 12.207 1.00 4.45 C
ANISOU 1730 CA ARG A 204 692 392 608 84 318 -54 C
ATOM 1731 C ARG A 204 -7.390 -0.670 11.520 1.00 4.27 C
ANISOU 1731 C ARG A 204 757 307 557 54 304 -128 C
ATOM 1732 O ARG A 204 -7.211 -1.844 11.824 1.00 5.34 O
ANISOU 1732 O ARG A 204 759 352 919 122 211 22 O
ATOM 1733 CB ARG A 204 -9.799 0.119 11.442 1.00 6.34 C
ANISOU 1733 CB ARG A 204 694 573 1141 26 177 -54 C
ATOM 1734 CG ARG A 204 -10.361 -1.248 11.152 1.00 5.74 C
ANISOU 1734 CG ARG A 204 553 590 1037 125 245 -150 C
ATOM 1735 CD ARG A 204 -10.490 -2.164 12.380 1.00 6.56 C
ANISOU 1735 CD ARG A 204 938 522 1034 41 522 -200 C
ATOM 1736 NE ARG A 204 -11.559 -1.712 13.264 1.00 7.95 N
ANISOU 1736 NE ARG A 204 895 783 1343 184 620 -156 N
ATOM 1737 CZ ARG A 204 -11.929 -2.350 14.386 1.00 8.60 C
ANISOU 1737 CZ ARG A 204 978 989 1300 -93 671 -242 C
ATOM 1738 NH1 ARG A 204 -11.293 -3.450 14.792 1.00 10.38 N
ANISOU 1738 NH1 ARG A 204 1623 1057 1264 -117 331 -26 N
ATOM 1739 NH2 ARG A 204 -12.941 -1.846 15.091 1.00 12.75 N
ANISOU 1739 NH2 ARG A 204 1341 1723 1781 -199 1074 -631 N
ATOM 1740 N PHE A 205 -6.626 -0.062 10.612 1.00 4.54 N
ANISOU 1740 N PHE A 205 601 449 676 157 316 37 N
ATOM 1741 CA PHE A 205 -5.604 -0.813 9.887 1.00 4.88 C
ANISOU 1741 CA PHE A 205 625 471 758 144 278 -93 C
ATOM 1742 C PHE A 205 -4.600 -1.490 10.804 1.00 4.55 C
ANISOU 1742 C PHE A 205 502 446 781 45 270 -92 C
ATOM 1743 O PHE A 205 -4.414 -2.702 10.639 1.00 5.43 O
ANISOU 1743 O PHE A 205 744 461 857 165 215 -109 O
ATOM 1744 CB PHE A 205 -4.874 0.088 8.880 1.00 4.32 C
ANISOU 1744 CB PHE A 205 421 447 774 160 282 -146 C
ATOM 1745 CG PHE A 205 -5.442 0.101 7.466 1.00 5.29 C
ANISOU 1745 CG PHE A 205 540 713 756 161 294 -2 C
ATOM 1746 CD1 PHE A 205 -5.867 -1.019 6.838 1.00 5.92 C
ANISOU 1746 CD1 PHE A 205 745 786 719 192 205 -102 C
ATOM 1747 CD2 PHE A 205 -5.508 1.313 6.762 1.00 5.48 C
ANISOU 1747 CD2 PHE A 205 453 766 862 129 235 22 C
ATOM 1748 CE1 PHE A 205 -6.324 -1.061 5.552 1.00 6.65 C
ANISOU 1748 CE1 PHE A 205 551 1075 902 216 36 -120 C
ATOM 1749 CE2 PHE A 205 -5.933 1.300 5.440 1.00 6.05 C
ANISOU 1749 CE2 PHE A 205 362 1119 817 48 284 234 C
ATOM 1750 CZ PHE A 205 -6.312 0.138 4.828 1.00 7.39 C
ANISOU 1750 CZ PHE A 205 644 1381 784 -146 90 126 C
ATOM 1751 N PRO A 206 -3.962 -0.813 11.736 1.00 4.27 N
ANISOU 1751 N PRO A 206 490 484 647 250 365 -172 N
ATOM 1752 CA PRO A 206 -3.031 -1.588 12.587 1.00 4.85 C
ANISOU 1752 CA PRO A 206 516 568 758 235 228 -95 C
ATOM 1753 C PRO A 206 -3.720 -2.655 13.415 1.00 5.60 C
ANISOU 1753 C PRO A 206 782 589 758 114 170 -120 C
ATOM 1754 O PRO A 206 -3.082 -3.674 13.769 1.00 6.28 O
ANISOU 1754 O PRO A 206 975 682 728 210 353 87 O
ATOM 1755 CB PRO A 206 -2.355 -0.496 13.434 1.00 5.69 C
ANISOU 1755 CB PRO A 206 711 581 872 101 184 -43 C
ATOM 1756 CG PRO A 206 -3.250 0.688 13.410 1.00 5.48 C
ANISOU 1756 CG PRO A 206 702 599 780 113 265 -184 C
ATOM 1757 CD PRO A 206 -3.840 0.614 12.024 1.00 5.40 C
ANISOU 1757 CD PRO A 206 774 466 813 243 242 -199 C
ATOM 1758 N ASN A 207 -4.965 -2.448 13.758 1.00 5.84 N
ANISOU 1758 N ASN A 207 806 547 867 85 265 37 N
ATOM 1759 CA ASN A 207 -5.749 -3.432 14.481 1.00 5.76 C
ANISOU 1759 CA ASN A 207 940 496 752 152 286 70 C
ATOM 1760 C ASN A 207 -6.089 -4.644 13.640 1.00 5.32 C
ANISOU 1760 C ASN A 207 715 576 731 51 170 58 C
ATOM 1761 O ASN A 207 -6.390 -5.683 14.202 1.00 7.59 O
ANISOU 1761 O ASN A 207 1441 637 806 -120 407 125 O
ATOM 1762 CB ASN A 207 -7.016 -2.771 15.050 1.00 5.99 C
ANISOU 1762 CB ASN A 207 763 758 756 165 180 58 C
ATOM 1763 CG ASN A 207 -6.657 -2.039 16.333 1.00 6.26 C
ANISOU 1763 CG ASN A 207 887 717 775 270 193 5 C
ATOM 1764 OD1 ASN A 207 -6.653 -2.675 17.421 1.00 8.08 O
ANISOU 1764 OD1 ASN A 207 1455 956 661 55 322 81 O
ATOM 1765 ND2 ASN A 207 -6.329 -0.757 16.222 1.00 6.68 N
ANISOU 1765 ND2 ASN A 207 1027 661 850 247 384 -53 N
ATOM 1766 N GLU A 208 -5.999 -4.536 12.319 1.00 5.10 N
ANISOU 1766 N GLU A 208 859 356 724 117 200 160 N
ATOM 1767 CA GLU A 208 -6.201 -5.645 11.391 1.00 4.95 C
ANISOU 1767 CA GLU A 208 649 568 663 -55 410 125 C
ATOM 1768 C GLU A 208 -4.922 -6.412 11.057 1.00 4.72 C
ANISOU 1768 C GLU A 208 782 402 608 21 255 72 C
ATOM 1769 O GLU A 208 -5.003 -7.488 10.470 1.00 5.80 O
ANISOU 1769 O GLU A 208 978 356 871 -1 217 -12 O
ATOM 1770 CB GLU A 208 -6.822 -5.113 10.068 1.00 5.15 C
ANISOU 1770 CB GLU A 208 797 419 740 77 257 -2 C
ATOM 1771 CG GLU A 208 -8.245 -4.617 10.203 1.00 6.62 C
ANISOU 1771 CG GLU A 208 751 796 968 99 220 -77 C
ATOM 1772 CD GLU A 208 -9.282 -5.719 10.230 1.00 5.88 C
ANISOU 1772 CD GLU A 208 844 687 702 79 309 -68 C
ATOM 1773 OE1 GLU A 208 -9.413 -6.391 11.280 1.00 7.11 O
ANISOU 1773 OE1 GLU A 208 1047 779 873 301 281 142 O
ATOM 1774 OE2 GLU A 208 -9.916 -5.936 9.174 1.00 6.64 O
ANISOU 1774 OE2 GLU A 208 871 810 843 9 195 135 O
ATOM 1775 N LEU A 209 -3.753 -5.876 11.419 1.00 5.14 N
ANISOU 1775 N LEU A 209 722 417 815 111 233 -116 N
ATOM 1776 CA LEU A 209 -2.520 -6.528 11.011 1.00 5.01 C
ANISOU 1776 CA LEU A 209 739 452 714 151 330 2 C
ATOM 1777 C LEU A 209 -2.483 -7.952 11.579 1.00 5.10 C
ANISOU 1777 C LEU A 209 875 427 636 89 182 -14 C
ATOM 1778 O LEU A 209 -2.863 -8.148 12.734 1.00 5.63 O
ANISOU 1778 O LEU A 209 943 485 710 146 300 4 O
ATOM 1779 CB LEU A 209 -1.305 -5.758 11.537 1.00 5.38 C
ANISOU 1779 CB LEU A 209 696 386 962 116 407 22 C
ATOM 1780 CG LEU A 209 -0.936 -4.457 10.805 1.00 5.70 C
ANISOU 1780 CG LEU A 209 961 271 932 215 244 5 C
ATOM 1781 CD1 LEU A 209 0.034 -3.642 11.627 1.00 6.86 C
ANISOU 1781 CD1 LEU A 209 867 441 1297 85 235 -71 C
ATOM 1782 CD2 LEU A 209 -0.359 -4.776 9.439 1.00 6.95 C
ANISOU 1782 CD2 LEU A 209 879 862 901 -17 338 163 C
ATOM 1783 N PRO A 210 -2.008 -8.936 10.817 1.00 4.96 N
ANISOU 1783 N PRO A 210 710 440 733 214 284 26 N
ATOM 1784 CA PRO A 210 -2.018 -10.322 11.305 1.00 5.44 C
ANISOU 1784 CA PRO A 210 685 439 944 24 260 -21 C
ATOM 1785 C PRO A 210 -0.848 -10.616 12.216 1.00 5.36 C
ANISOU 1785 C PRO A 210 874 412 749 188 272 91 C
ATOM 1786 O PRO A 210 0.133 -11.266 11.775 1.00 8.49 O
ANISOU 1786 O PRO A 210 820 1677 730 469 225 -104 O
ATOM 1787 CB PRO A 210 -1.950 -11.100 9.997 1.00 5.59 C
ANISOU 1787 CB PRO A 210 741 424 958 189 213 -64 C
ATOM 1788 CG PRO A 210 -1.185 -10.230 9.061 1.00 5.44 C
ANISOU 1788 CG PRO A 210 792 429 846 144 243 -130 C
ATOM 1789 CD PRO A 210 -1.635 -8.816 9.416 1.00 5.76 C
ANISOU 1789 CD PRO A 210 892 503 792 154 283 -101 C
ATOM 1790 N ILE A 211 -0.913 -10.170 13.446 1.00 5.55 N
ANISOU 1790 N ILE A 211 939 317 853 162 275 -2 N
ATOM 1791 CA ILE A 211 0.179 -10.309 14.393 1.00 5.91 C
ANISOU 1791 CA ILE A 211 865 657 725 128 301 -52 C
ATOM 1792 C ILE A 211 -0.262 -11.200 15.541 1.00 6.03 C
ANISOU 1792 C ILE A 211 906 591 792 276 335 15 C
ATOM 1793 O ILE A 211 -1.308 -11.007 16.154 1.00 6.42 O
ANISOU 1793 O ILE A 211 1068 492 879 323 421 111 O
ATOM 1794 CB ILE A 211 0.636 -8.953 14.957 1.00 5.61 C
ANISOU 1794 CB ILE A 211 868 680 582 204 303 5 C
ATOM 1795 CG1 ILE A 211 0.922 -7.961 13.853 1.00 5.55 C
ANISOU 1795 CG1 ILE A 211 864 598 646 310 362 28 C
ATOM 1796 CG2 ILE A 211 1.834 -9.101 15.907 1.00 6.85 C
ANISOU 1796 CG2 ILE A 211 1114 704 786 100 35 -16 C
ATOM 1797 CD1 ILE A 211 1.101 -6.543 14.312 1.00 6.36 C
ANISOU 1797 CD1 ILE A 211 1172 681 564 178 136 104 C
ATOM 1798 N ALA A 212 0.542 -12.227 15.837 1.00 5.94 N
ANISOU 1798 N ALA A 212 950 565 741 294 400 -93 N
ATOM 1799 CA ALA A 212 0.283 -13.055 17.028 1.00 6.69 C
ANISOU 1799 CA ALA A 212 1072 674 795 162 245 54 C
ATOM 1800 C ALA A 212 -1.105 -13.670 16.976 1.00 6.34 C
ANISOU 1800 C ALA A 212 1008 448 952 265 303 75 C
ATOM 1801 O ALA A 212 -1.768 -13.788 18.002 1.00 7.52 O
ANISOU 1801 O ALA A 212 1263 681 912 83 423 81 O
ATOM 1802 CB ALA A 212 0.528 -12.250 18.292 1.00 8.28 C
ANISOU 1802 CB ALA A 212 1586 779 780 -96 363 14 C
ATOM 1803 N GLY A 213 -1.506 -14.110 15.788 1.00 6.78 N
ANISOU 1803 N GLY A 213 1162 475 939 164 305 32 N
ATOM 1804 CA GLY A 213 -2.728 -14.831 15.623 1.00 7.00 C
ANISOU 1804 CA GLY A 213 1261 686 714 61 236 126 C
ATOM 1805 C GLY A 213 -4.007 -14.054 15.542 1.00 7.50 C
ANISOU 1805 C GLY A 213 1243 774 833 2 97 172 C
ATOM 1806 O GLY A 213 -5.087 -14.641 15.378 1.00 8.70 O
ANISOU 1806 O GLY A 213 1207 810 1290 -82 308 27 O
ATOM 1807 N GLU A 214 -3.931 -12.722 15.669 1.00 7.32 N
ANISOU 1807 N GLU A 214 901 742 1139 63 259 69 N
ATOM 1808 CA AGLU A 214 -5.041 -11.814 15.839 0.50 7.35 C
ANISOU 1808 CA AGLU A 214 865 1105 822 223 218 147 C
ATOM 1809 CA BGLU A 214 -5.151 -11.934 15.693 0.50 8.05 C
ANISOU 1809 CA BGLU A 214 970 1147 943 262 316 312 C
ATOM 1810 C GLU A 214 -5.013 -10.677 14.832 1.00 6.67 C
ANISOU 1810 C GLU A 214 951 697 887 119 216 -63 C
ATOM 1811 O GLU A 214 -3.936 -10.077 14.731 1.00 7.77 O
ANISOU 1811 O GLU A 214 992 932 1026 21 97 8 O
ATOM 1812 CB AGLU A 214 -4.968 -11.208 17.235 0.50 5.75 C
ANISOU 1812 CB AGLU A 214 841 352 990 -30 158 168 C
ATOM 1813 CB BGLU A 214 -5.593 -11.635 17.110 0.50 8.90 C
ANISOU 1813 CB BGLU A 214 901 1513 969 220 254 137 C
ATOM 1814 CG AGLU A 214 -5.888 -10.069 17.549 0.50 9.46 C
ANISOU 1814 CG AGLU A 214 1361 1059 1174 685 49 83 C
ATOM 1815 CG BGLU A 214 -4.740 -10.664 17.880 0.50 12.44 C
ANISOU 1815 CG BGLU A 214 2248 1003 1474 -75 211 -22 C
ATOM 1816 CD AGLU A 214 -7.365 -10.337 17.565 0.50 10.94 C
ANISOU 1816 CD AGLU A 214 1397 952 1809 600 366 -698 C
ATOM 1817 CD BGLU A 214 -5.391 -10.360 19.222 0.50 16.07 C
ANISOU 1817 CD BGLU A 214 3893 1104 1109 -414 465 190 C
ATOM 1818 OE1AGLU A 214 -7.746 -11.496 17.801 0.50 14.09 O
ANISOU 1818 OE1AGLU A 214 1591 1305 2457 457 226 60 O
ATOM 1819 OE1BGLU A 214 -6.180 -11.199 19.719 0.50 14.70 O
ANISOU 1819 OE1BGLU A 214 2293 1216 2076 -69 714 -308 O
ATOM 1820 OE2AGLU A 214 -8.127 -9.344 17.389 0.50 11.54 O
ANISOU 1820 OE2AGLU A 214 1379 1441 1564 819 305 -251 O
ATOM 1821 OE2BGLU A 214 -5.086 -9.277 19.757 0.50 29.46 O
ANISOU 1821 OE2BGLU A 214 6545 2966 1681 -2810 1776 -1036 O
ATOM 1822 N PRO A 215 -6.103 -10.304 14.191 1.00 6.24 N
ANISOU 1822 N PRO A 215 902 643 825 -103 248 175 N
ATOM 1823 CA PRO A 215 -7.393 -10.989 14.201 1.00 6.40 C
ANISOU 1823 CA PRO A 215 922 529 982 -4 320 119 C
ATOM 1824 C PRO A 215 -7.379 -12.237 13.317 1.00 6.92 C
ANISOU 1824 C PRO A 215 1140 453 1037 2 331 98 C
ATOM 1825 O PRO A 215 -6.717 -12.315 12.288 1.00 7.46 O
ANISOU 1825 O PRO A 215 1209 735 890 -15 265 118 O
ATOM 1826 CB PRO A 215 -8.366 -9.964 13.610 1.00 7.59 C
ANISOU 1826 CB PRO A 215 868 672 1345 154 295 29 C
ATOM 1827 CG PRO A 215 -7.545 -8.916 12.997 1.00 9.68 C
ANISOU 1827 CG PRO A 215 1178 974 1526 95 151 564 C
ATOM 1828 CD PRO A 215 -6.135 -9.093 13.381 1.00 6.50 C
ANISOU 1828 CD PRO A 215 1041 523 907 -42 290 98 C
ATOM 1829 N ALA A 216 -8.112 -13.260 13.773 1.00 7.69 N
ANISOU 1829 N ALA A 216 1140 611 1172 -159 381 71 N
ATOM 1830 CA ALA A 216 -8.005 -14.559 13.154 1.00 7.83 C
ANISOU 1830 CA ALA A 216 1149 615 1211 -231 311 69 C
ATOM 1831 C ALA A 216 -8.431 -14.536 11.714 1.00 7.51 C
ANISOU 1831 C ALA A 216 1139 608 1106 -196 387 175 C
ATOM 1832 O ALA A 216 -7.859 -15.242 10.859 1.00 8.40 O
ANISOU 1832 O ALA A 216 1311 699 1183 -36 273 141 O
ATOM 1833 CB ALA A 216 -8.819 -15.567 13.982 1.00 11.77 C
ANISOU 1833 CB ALA A 216 2225 809 1436 -447 340 530 C
ATOM 1834 N ASN A 217 -9.431 -13.729 11.379 1.00 8.41 N
ANISOU 1834 N ASN A 217 1101 701 1392 -152 308 131 N
ATOM 1835 CA ASN A 217 -9.867 -13.738 9.979 1.00 7.83 C
ANISOU 1835 CA ASN A 217 904 620 1452 -29 276 55 C
ATOM 1836 C ASN A 217 -8.782 -13.237 9.044 1.00 6.97 C
ANISOU 1836 C ASN A 217 869 510 1270 16 199 6 C
ATOM 1837 O ASN A 217 -8.568 -13.747 7.944 1.00 8.21 O
ANISOU 1837 O ASN A 217 1077 626 1415 -119 296 -136 O
ATOM 1838 CB ASN A 217 -11.176 -12.936 9.784 1.00 9.71 C
ANISOU 1838 CB ASN A 217 817 1017 1856 44 173 -157 C
ATOM 1839 CG ASN A 217 -10.980 -11.436 9.973 1.00 9.45 C
ANISOU 1839 CG ASN A 217 718 975 1899 280 75 -237 C
ATOM 1840 OD1 ASN A 217 -10.408 -11.001 10.961 1.00 9.83 O
ANISOU 1840 OD1 ASN A 217 1199 1017 1518 53 295 -115 O
ATOM 1841 ND2 ASN A 217 -11.463 -10.642 9.019 1.00 12.22 N
ANISOU 1841 ND2 ASN A 217 1368 1177 2097 457 -178 -177 N
ATOM 1842 N ILE A 218 -8.068 -12.193 9.467 1.00 7.18 N
ANISOU 1842 N ILE A 218 843 672 1213 -60 230 -6 N
ATOM 1843 CA ILE A 218 -7.027 -11.642 8.601 1.00 7.04 C
ANISOU 1843 CA ILE A 218 939 498 1238 -40 291 -24 C
ATOM 1844 C ILE A 218 -5.845 -12.597 8.532 1.00 6.25 C
ANISOU 1844 C ILE A 218 961 514 900 -21 228 -49 C
ATOM 1845 O ILE A 218 -5.264 -12.819 7.472 1.00 6.66 O
ANISOU 1845 O ILE A 218 1083 528 918 3 324 -21 O
ATOM 1846 CB ILE A 218 -6.568 -10.256 9.075 1.00 6.55 C
ANISOU 1846 CB ILE A 218 973 553 962 -6 337 -88 C
ATOM 1847 CG1 ILE A 218 -7.767 -9.299 9.149 1.00 7.59 C
ANISOU 1847 CG1 ILE A 218 1007 596 1281 36 478 37 C
ATOM 1848 CG2 ILE A 218 -5.437 -9.726 8.212 1.00 7.07 C
ANISOU 1848 CG2 ILE A 218 947 519 1222 -89 394 -130 C
ATOM 1849 CD1 ILE A 218 -8.455 -9.016 7.820 1.00 9.76 C
ANISOU 1849 CD1 ILE A 218 1149 940 1618 190 107 35 C
ATOM 1850 N VAL A 219 -5.448 -13.180 9.675 1.00 6.48 N
ANISOU 1850 N VAL A 219 866 697 898 56 364 -5 N
ATOM 1851 CA VAL A 219 -4.364 -14.170 9.643 1.00 6.38 C
ANISOU 1851 CA VAL A 219 905 500 1021 1 400 55 C
ATOM 1852 C VAL A 219 -4.671 -15.264 8.644 1.00 6.55 C
ANISOU 1852 C VAL A 219 940 531 1018 74 240 31 C
ATOM 1853 O VAL A 219 -3.848 -15.645 7.811 1.00 7.15 O
ANISOU 1853 O VAL A 219 1002 594 1120 113 328 -16 O
ATOM 1854 CB VAL A 219 -4.140 -14.799 11.049 1.00 7.39 C
ANISOU 1854 CB VAL A 219 1015 830 961 106 307 65 C
ATOM 1855 CG1 VAL A 219 -3.218 -15.985 10.970 1.00 7.80 C
ANISOU 1855 CG1 VAL A 219 988 898 1078 169 207 -2 C
ATOM 1856 CG2 VAL A 219 -3.658 -13.730 11.998 1.00 7.64 C
ANISOU 1856 CG2 VAL A 219 1114 789 999 193 320 72 C
ATOM 1857 N ALA A 220 -5.901 -15.773 8.636 1.00 6.95 N
ANISOU 1857 N ALA A 220 1038 443 1159 48 437 -108 N
ATOM 1858 CA ALA A 220 -6.232 -16.858 7.712 1.00 7.66 C
ANISOU 1858 CA ALA A 220 1006 774 1129 -59 239 -91 C
ATOM 1859 C ALA A 220 -6.207 -16.401 6.265 1.00 6.75 C
ANISOU 1859 C ALA A 220 748 665 1151 -21 210 -82 C
ATOM 1860 O ALA A 220 -5.750 -17.126 5.374 1.00 8.09 O
ANISOU 1860 O ALA A 220 1221 693 1162 -99 425 -86 O
ATOM 1861 CB ALA A 220 -7.565 -17.479 8.118 1.00 10.75 C
ANISOU 1861 CB ALA A 220 1443 1084 1556 -546 418 22 C
ATOM 1862 N LEU A 221 -6.706 -15.189 5.985 1.00 8.01 N
ANISOU 1862 N LEU A 221 1091 755 1198 44 292 -27 N
ATOM 1863 CA ALEU A 221 -6.741 -14.628 4.649 0.50 7.15 C
ANISOU 1863 CA ALEU A 221 985 506 1227 -172 99 -88 C
ATOM 1864 CA BLEU A 221 -6.730 -14.869 4.549 0.50 7.90 C
ANISOU 1864 CA BLEU A 221 1029 745 1228 -251 66 22 C
ATOM 1865 C LEU A 221 -5.324 -14.467 4.105 1.00 6.34 C
ANISOU 1865 C LEU A 221 982 410 1019 -65 23 77 C
ATOM 1866 O LEU A 221 -5.034 -14.719 2.924 1.00 7.17 O
ANISOU 1866 O LEU A 221 1110 533 1080 75 58 -3 O
ATOM 1867 CB ALEU A 221 -7.520 -13.313 4.764 0.50 7.12 C
ANISOU 1867 CB ALEU A 221 1063 714 927 -13 8 -180 C
ATOM 1868 CB BLEU A 221 -7.751 -13.825 4.135 0.50 8.75 C
ANISOU 1868 CB BLEU A 221 1024 1101 1197 -18 22 -137 C
ATOM 1869 CG ALEU A 221 -7.888 -12.615 3.462 0.50 5.77 C
ANISOU 1869 CG ALEU A 221 801 671 719 7 299 -211 C
ATOM 1870 CG BLEU A 221 -7.472 -12.362 4.427 0.50 10.26 C
ANISOU 1870 CG BLEU A 221 1586 991 1323 290 93 -342 C
ATOM 1871 CD1ALEU A 221 -9.187 -11.854 3.596 0.50 6.29 C
ANISOU 1871 CD1ALEU A 221 965 739 687 149 444 -82 C
ATOM 1872 CD1BLEU A 221 -6.767 -11.646 3.294 0.50 10.82 C
ANISOU 1872 CD1BLEU A 221 1768 739 1606 175 89 -163 C
ATOM 1873 CD2ALEU A 221 -6.750 -11.685 3.095 0.50 8.93 C
ANISOU 1873 CD2ALEU A 221 1074 632 1686 -50 777 -225 C
ATOM 1874 CD2BLEU A 221 -8.787 -11.637 4.702 0.50 15.99 C
ANISOU 1874 CD2BLEU A 221 1603 1880 2591 368 290 -1229 C
ATOM 1875 N VAL A 222 -4.514 -13.904 4.963 1.00 7.03 N
ANISOU 1875 N VAL A 222 888 833 951 -124 119 51 N
ATOM 1876 CA VAL A 222 -3.130 -13.593 4.565 1.00 6.34 C
ANISOU 1876 CA VAL A 222 887 606 917 3 189 -24 C
ATOM 1877 C VAL A 222 -2.354 -14.873 4.417 1.00 6.51 C
ANISOU 1877 C VAL A 222 1029 589 855 2 190 -54 C
ATOM 1878 O VAL A 222 -1.600 -15.050 3.431 1.00 7.49 O
ANISOU 1878 O VAL A 222 974 751 1122 77 281 -49 O
ATOM 1879 CB VAL A 222 -2.497 -12.632 5.586 1.00 5.59 C
ANISOU 1879 CB VAL A 222 920 499 705 -14 227 81 C
ATOM 1880 CG1 VAL A 222 -1.010 -12.510 5.333 1.00 6.87 C
ANISOU 1880 CG1 VAL A 222 936 973 702 -125 244 136 C
ATOM 1881 CG2 VAL A 222 -3.191 -11.287 5.573 1.00 7.38 C
ANISOU 1881 CG2 VAL A 222 1331 557 915 94 174 34 C
ATOM 1882 N GLU A 223 -2.525 -15.854 5.296 1.00 8.11 N
ANISOU 1882 N GLU A 223 1450 450 1182 39 442 -89 N
ATOM 1883 CA GLU A 223 -1.924 -17.177 5.081 1.00 7.46 C
ANISOU 1883 CA GLU A 223 1041 547 1246 48 345 -122 C
ATOM 1884 C GLU A 223 -2.362 -17.744 3.726 1.00 7.38 C
ANISOU 1884 C GLU A 223 1120 471 1215 154 289 -96 C
ATOM 1885 O GLU A 223 -1.578 -18.344 2.971 1.00 8.22 O
ANISOU 1885 O GLU A 223 1431 424 1268 298 288 -117 O
ATOM 1886 CB GLU A 223 -2.358 -18.126 6.198 1.00 8.52 C
ANISOU 1886 CB GLU A 223 1186 727 1325 144 225 159 C
ATOM 1887 CG AGLU A 223 -1.608 -18.016 7.516 0.60 8.83 C
ANISOU 1887 CG AGLU A 223 1352 603 1400 634 129 -102 C
ATOM 1888 CG BGLU A 223 -1.935 -17.754 7.605 0.40 13.00 C
ANISOU 1888 CG BGLU A 223 2341 1282 1318 -83 123 122 C
ATOM 1889 CD AGLU A 223 -2.181 -18.688 8.739 0.60 10.07 C
ANISOU 1889 CD AGLU A 223 1810 661 1356 761 -90 198 C
ATOM 1890 CD BGLU A 223 -1.136 -18.802 8.344 0.40 16.67 C
ANISOU 1890 CD BGLU A 223 2038 2718 1577 941 -370 -334 C
ATOM 1891 OE1AGLU A 223 -1.467 -18.752 9.780 0.60 17.88 O
ANISOU 1891 OE1AGLU A 223 2878 2362 1555 907 -617 173 O
ATOM 1892 OE1BGLU A 223 -0.112 -19.276 7.815 0.40 24.22 O
ANISOU 1892 OE1BGLU A 223 1462 3277 4464 326 603 -168 O
ATOM 1893 OE2AGLU A 223 -3.341 -19.153 8.690 0.60 13.24 O
ANISOU 1893 OE2AGLU A 223 2509 852 1670 -159 26 423 O
ATOM 1894 OE2BGLU A 223 -1.515 -19.148 9.487 0.40 15.89 O
ANISOU 1894 OE2BGLU A 223 3060 758 2218 928 -84 264 O
ATOM 1895 N ALA A 224 -3.626 -17.569 3.363 1.00 7.18 N
ANISOU 1895 N ALA A 224 1108 511 1110 -41 287 82 N
ATOM 1896 CA ALA A 224 -4.078 -18.130 2.069 1.00 7.24 C
ANISOU 1896 CA ALA A 224 1134 507 1110 179 330 -26 C
ATOM 1897 C ALA A 224 -3.418 -17.463 0.886 1.00 6.59 C
ANISOU 1897 C ALA A 224 911 510 1084 78 213 -76 C
ATOM 1898 O ALA A 224 -2.994 -18.135 -0.050 1.00 7.46 O
ANISOU 1898 O ALA A 224 1196 556 1084 -3 287 -136 O
ATOM 1899 CB ALA A 224 -5.582 -18.021 1.933 1.00 7.88 C
ANISOU 1899 CB ALA A 224 1114 711 1171 -145 293 15 C
ATOM 1900 N TYR A 225 -3.295 -16.132 0.893 1.00 6.79 N
ANISOU 1900 N TYR A 225 1099 509 973 70 161 -20 N
ATOM 1901 CA TYR A 225 -2.651 -15.540 -0.284 1.00 6.54 C
ANISOU 1901 CA TYR A 225 1084 541 860 112 113 -18 C
ATOM 1902 C TYR A 225 -1.169 -15.818 -0.310 1.00 5.73 C
ANISOU 1902 C TYR A 225 1065 273 840 -2 90 -39 C
ATOM 1903 O TYR A 225 -0.565 -15.846 -1.383 1.00 6.64 O
ANISOU 1903 O TYR A 225 1112 575 835 89 210 -9 O
ATOM 1904 CB TYR A 225 -3.013 -14.069 -0.415 1.00 5.81 C
ANISOU 1904 CB TYR A 225 805 506 897 -9 348 -65 C
ATOM 1905 CG TYR A 225 -2.496 -12.978 0.448 1.00 5.88 C
ANISOU 1905 CG TYR A 225 931 450 852 32 149 43 C
ATOM 1906 CD1 TYR A 225 -1.148 -12.736 0.705 1.00 5.46 C
ANISOU 1906 CD1 TYR A 225 919 435 719 76 146 110 C
ATOM 1907 CD2 TYR A 225 -3.395 -12.093 1.032 1.00 6.16 C
ANISOU 1907 CD2 TYR A 225 823 495 1022 -69 258 -49 C
ATOM 1908 CE1 TYR A 225 -0.692 -11.730 1.496 1.00 6.13 C
ANISOU 1908 CE1 TYR A 225 877 624 828 58 80 -39 C
ATOM 1909 CE2 TYR A 225 -2.973 -11.028 1.824 1.00 5.60 C
ANISOU 1909 CE2 TYR A 225 910 393 825 125 67 98 C
ATOM 1910 CZ TYR A 225 -1.610 -10.859 2.042 1.00 5.48 C
ANISOU 1910 CZ TYR A 225 911 427 743 -46 141 36 C
ATOM 1911 OH TYR A 225 -1.196 -9.822 2.824 1.00 6.32 O
ANISOU 1911 OH TYR A 225 1051 537 813 -30 120 -69 O
ATOM 1912 N MET A 226 -0.532 -15.979 0.851 1.00 6.26 N
ANISOU 1912 N MET A 226 953 592 832 56 221 -15 N
ATOM 1913 CA MET A 226 0.892 -16.307 0.847 1.00 6.78 C
ANISOU 1913 CA MET A 226 976 546 1054 146 121 20 C
ATOM 1914 C MET A 226 1.098 -17.739 0.359 1.00 7.38 C
ANISOU 1914 C MET A 226 974 687 1142 131 177 -124 C
ATOM 1915 O MET A 226 2.071 -18.000 -0.336 1.00 7.75 O
ANISOU 1915 O MET A 226 1081 863 1000 335 145 -148 O
ATOM 1916 CB MET A 226 1.496 -16.088 2.232 1.00 7.04 C
ANISOU 1916 CB MET A 226 963 719 994 188 167 -29 C
ATOM 1917 CG MET A 226 1.686 -14.644 2.641 1.00 6.87 C
ANISOU 1917 CG MET A 226 1068 687 855 329 78 -13 C
ATOM 1918 SD MET A 226 2.528 -13.609 1.456 1.00 7.76 S
ANISOU 1918 SD MET A 226 1069 774 1105 32 137 -90 S
ATOM 1919 CE MET A 226 4.126 -14.402 1.396 1.00 9.30 C
ANISOU 1919 CE MET A 226 1255 1029 1249 303 273 -44 C
ATOM 1920 N ASN A 227 0.232 -18.678 0.701 1.00 7.12 N
ANISOU 1920 N ASN A 227 1090 584 1031 171 34 -48 N
ATOM 1921 CA ASN A 227 0.327 -20.016 0.132 1.00 7.86 C
ANISOU 1921 CA ASN A 227 1245 566 1175 217 108 -57 C
ATOM 1922 C ASN A 227 0.216 -19.945 -1.391 1.00 7.84 C
ANISOU 1922 C ASN A 227 1153 729 1096 73 132 -167 C
ATOM 1923 O ASN A 227 0.964 -20.600 -2.116 1.00 9.27 O
ANISOU 1923 O ASN A 227 1256 955 1310 211 193 -184 O
ATOM 1924 CB ASN A 227 -0.796 -20.863 0.722 1.00 10.02 C
ANISOU 1924 CB ASN A 227 1729 852 1227 -151 204 39 C
ATOM 1925 CG AASN A 227 -0.893 -22.259 0.173 0.50 9.57 C
ANISOU 1925 CG AASN A 227 1781 579 1277 75 400 320 C
ATOM 1926 CG BASN A 227 -0.618 -21.266 2.170 0.50 17.28 C
ANISOU 1926 CG BASN A 227 3380 1638 1547 143 170 757 C
ATOM 1927 OD1AASN A 227 -0.057 -23.091 0.496 0.50 12.96 O
ANISOU 1927 OD1AASN A 227 2206 1059 1658 403 232 431 O
ATOM 1928 OD1BASN A 227 0.486 -21.198 2.707 0.50 23.23 O
ANISOU 1928 OD1BASN A 227 4361 3100 1364 -752 -688 776 O
ATOM 1929 ND2AASN A 227 -1.907 -22.559 -0.632 0.50 9.73 N
ANISOU 1929 ND2AASN A 227 1879 184 1633 237 315 -175 N
ATOM 1930 ND2BASN A 227 -1.677 -21.691 2.852 0.50 20.37 N
ANISOU 1930 ND2BASN A 227 4129 1698 1913 334 779 1172 N
ATOM 1931 N TRP A 228 -0.720 -19.157 -1.867 1.00 7.66 N
ANISOU 1931 N TRP A 228 1219 663 1028 74 241 -40 N
ATOM 1932 CA TRP A 228 -0.873 -18.970 -3.313 1.00 7.49 C
ANISOU 1932 CA TRP A 228 1134 681 1029 -28 245 -80 C
ATOM 1933 C TRP A 228 0.399 -18.418 -3.921 1.00 7.52 C
ANISOU 1933 C TRP A 228 1122 688 1047 4 256 -144 C
ATOM 1934 O TRP A 228 0.944 -18.897 -4.929 1.00 8.62 O
ANISOU 1934 O TRP A 228 1173 955 1146 23 311 -234 O
ATOM 1935 CB TRP A 228 -2.107 -18.027 -3.555 1.00 9.17 C
ANISOU 1935 CB TRP A 228 1187 1190 1107 246 282 57 C
ATOM 1936 CG TRP A 228 -2.152 -17.690 -5.026 1.00 8.38 C
ANISOU 1936 CG TRP A 228 1120 981 1083 -3 151 -45 C
ATOM 1937 CD1 TRP A 228 -2.650 -18.450 -6.029 1.00 10.14 C
ANISOU 1937 CD1 TRP A 228 1521 970 1362 -126 -234 17 C
ATOM 1938 CD2 TRP A 228 -1.649 -16.498 -5.653 1.00 7.29 C
ANISOU 1938 CD2 TRP A 228 845 848 1079 137 180 -51 C
ATOM 1939 NE1 TRP A 228 -2.498 -17.818 -7.223 1.00 12.15 N
ANISOU 1939 NE1 TRP A 228 2478 930 1209 -57 -292 -75 N
ATOM 1940 CE2 TRP A 228 -1.881 -16.616 -7.040 1.00 8.19 C
ANISOU 1940 CE2 TRP A 228 1182 763 1167 357 -211 104 C
ATOM 1941 CE3 TRP A 228 -1.022 -15.344 -5.180 1.00 8.79 C
ANISOU 1941 CE3 TRP A 228 1259 714 1366 273 -215 10 C
ATOM 1942 CZ2 TRP A 228 -1.507 -15.631 -7.958 1.00 9.04 C
ANISOU 1942 CZ2 TRP A 228 1565 706 1163 639 54 99 C
ATOM 1943 CZ3 TRP A 228 -0.652 -14.367 -6.094 1.00 8.99 C
ANISOU 1943 CZ3 TRP A 228 927 774 1713 181 -127 109 C
ATOM 1944 CH2 TRP A 228 -0.902 -14.533 -7.431 1.00 10.03 C
ANISOU 1944 CH2 TRP A 228 1223 1008 1579 221 -16 323 C
ATOM 1945 N LEU A 229 0.903 -17.369 -3.292 1.00 7.35 N
ANISOU 1945 N LEU A 229 1020 579 1192 90 290 -157 N
ATOM 1946 CA LEU A 229 2.064 -16.675 -3.837 1.00 7.19 C
ANISOU 1946 CA LEU A 229 1245 443 1044 82 281 -15 C
ATOM 1947 C LEU A 229 3.285 -17.579 -3.924 1.00 7.01 C
ANISOU 1947 C LEU A 229 973 715 977 36 248 -18 C
ATOM 1948 O LEU A 229 4.045 -17.552 -4.888 1.00 8.17 O
ANISOU 1948 O LEU A 229 1446 586 1073 190 461 4 O
ATOM 1949 CB LEU A 229 2.402 -15.451 -3.003 1.00 6.63 C
ANISOU 1949 CB LEU A 229 729 864 927 -3 209 -192 C
ATOM 1950 CG LEU A 229 3.430 -14.487 -3.577 1.00 6.64 C
ANISOU 1950 CG LEU A 229 849 660 1014 83 348 -64 C
ATOM 1951 CD1 LEU A 229 2.866 -13.722 -4.759 1.00 6.73 C
ANISOU 1951 CD1 LEU A 229 922 477 1158 411 196 -200 C
ATOM 1952 CD2 LEU A 229 3.889 -13.493 -2.530 1.00 7.97 C
ANISOU 1952 CD2 LEU A 229 1023 726 1280 -59 81 -56 C
ATOM 1953 N HIS A 230 3.472 -18.411 -2.892 1.00 7.97 N
ANISOU 1953 N HIS A 230 1163 877 989 186 195 72 N
ATOM 1954 CA HIS A 230 4.621 -19.318 -2.870 1.00 8.36 C
ANISOU 1954 CA HIS A 230 1204 827 1144 203 388 138 C
ATOM 1955 C HIS A 230 4.532 -20.393 -3.947 1.00 9.97 C
ANISOU 1955 C HIS A 230 1574 976 1237 288 463 90 C
ATOM 1956 O HIS A 230 5.590 -20.947 -4.303 1.00 11.86 O
ANISOU 1956 O HIS A 230 1739 1179 1589 449 542 -149 O
ATOM 1957 CB HIS A 230 4.780 -19.955 -1.497 1.00 9.38 C
ANISOU 1957 CB HIS A 230 1301 1051 1214 316 446 302 C
ATOM 1958 CG HIS A 230 5.576 -19.147 -0.517 1.00 11.49 C
ANISOU 1958 CG HIS A 230 1739 1441 1184 226 228 339 C
ATOM 1959 ND1 HIS A 230 5.129 -18.400 0.547 1.00 16.91 N
ANISOU 1959 ND1 HIS A 230 1873 2437 2114 317 169 -687 N
ATOM 1960 CD2 HIS A 230 6.926 -19.001 -0.457 1.00 14.30 C
ANISOU 1960 CD2 HIS A 230 1649 2087 1699 458 -125 -223 C
ATOM 1961 CE1 HIS A 230 6.126 -17.817 1.216 1.00 12.33 C
ANISOU 1961 CE1 HIS A 230 1709 1900 1075 433 -19 315 C
ATOM 1962 NE2 HIS A 230 7.239 -18.201 0.580 1.00 16.84 N
ANISOU 1962 NE2 HIS A 230 1943 2423 2031 -24 372 -588 N
ATOM 1963 N GLN A 231 3.354 -20.684 -4.443 1.00 10.05 N
ANISOU 1963 N GLN A 231 1729 658 1430 132 268 11 N
ATOM 1964 CA GLN A 231 3.226 -21.691 -5.519 1.00 13.05 C
ANISOU 1964 CA GLN A 231 2869 625 1464 -16 245 38 C
ATOM 1965 C GLN A 231 2.930 -21.077 -6.881 1.00 11.85 C
ANISOU 1965 C GLN A 231 2355 715 1431 234 242 -79 C
ATOM 1966 O GLN A 231 2.857 -21.828 -7.867 1.00 14.52 O
ANISOU 1966 O GLN A 231 3211 907 1400 40 360 -173 O
ATOM 1967 CB AGLN A 231 2.096 -22.658 -5.194 0.60 17.15 C
ANISOU 1967 CB AGLN A 231 3814 782 1922 -654 308 -62 C
ATOM 1968 CB BGLN A 231 2.214 -22.769 -5.160 0.40 15.76 C
ANISOU 1968 CB BGLN A 231 3414 694 1880 -354 470 -147 C
ATOM 1969 CG AGLN A 231 2.360 -23.477 -3.928 0.60 13.53 C
ANISOU 1969 CG AGLN A 231 2110 930 2099 -276 502 79 C
ATOM 1970 CG BGLN A 231 0.770 -22.399 -4.942 0.40 22.70 C
ANISOU 1970 CG BGLN A 231 3251 2426 2948 -859 935 -1556 C
ATOM 1971 CD AGLN A 231 1.094 -24.277 -3.666 0.50 16.64 C
ANISOU 1971 CD AGLN A 231 2458 1047 2817 -437 1174 -167 C
ATOM 1972 CD BGLN A 231 0.013 -23.432 -4.134 0.40 26.03 C
ANISOU 1972 CD BGLN A 231 3635 2885 3369 -1208 1084 -1408 C
ATOM 1973 OE1AGLN A 231 0.687 -25.045 -4.540 0.60 43.30 O
ANISOU 1973 OE1AGLN A 231 5448 5868 5137 -4428 3171 -3184 O
ATOM 1974 OE1BGLN A 231 0.503 -24.543 -3.912 0.40 33.18 O
ANISOU 1974 OE1BGLN A 231 5762 2735 4111 -1230 370 -946 O
ATOM 1975 NE2AGLN A 231 0.491 -24.061 -2.512 0.60 28.08 N
ANISOU 1975 NE2AGLN A 231 4349 3619 2703 -1645 1884 -149 N
ATOM 1976 NE2BGLN A 231 -1.182 -23.111 -3.668 0.40 31.68 N
ANISOU 1976 NE2BGLN A 231 3442 6351 2244 -1238 965 -1411 N
ATOM 1977 N SER A 232 2.748 -19.775 -7.007 1.00 8.93 N
ANISOU 1977 N SER A 232 1361 713 1318 166 230 1 N
ATOM 1978 CA SER A 232 2.399 -19.150 -8.286 1.00 8.21 C
ANISOU 1978 CA SER A 232 1152 730 1238 107 165 -96 C
ATOM 1979 C SER A 232 3.587 -18.898 -9.173 1.00 7.57 C
ANISOU 1979 C SER A 232 1075 670 1133 184 74 -127 C
ATOM 1980 O SER A 232 4.613 -18.410 -8.690 1.00 7.30 O
ANISOU 1980 O SER A 232 1065 596 1113 210 52 -93 O
ATOM 1981 CB SER A 232 1.662 -17.834 -8.002 1.00 8.53 C
ANISOU 1981 CB SER A 232 1419 715 1107 178 436 124 C
ATOM 1982 OG ASER A 232 1.564 -17.138 -9.241 0.60 5.70 O
ANISOU 1982 OG ASER A 232 821 558 785 48 284 -163 O
ATOM 1983 OG BSER A 232 2.550 -16.764 -7.771 0.40 20.99 O
ANISOU 1983 OG BSER A 232 2301 1178 4497 -301 1168 -1291 O
ATOM 1984 N PRO A 233 3.506 -19.190 -10.472 1.00 7.73 N
ANISOU 1984 N PRO A 233 1275 530 1132 -125 50 -80 N
ATOM 1985 CA PRO A 233 4.604 -18.838 -11.390 1.00 7.40 C
ANISOU 1985 CA PRO A 233 1133 628 1051 279 47 74 C
ATOM 1986 C PRO A 233 4.635 -17.378 -11.780 1.00 6.87 C
ANISOU 1986 C PRO A 233 845 534 1231 65 176 -170 C
ATOM 1987 O PRO A 233 5.520 -16.982 -12.557 1.00 8.43 O
ANISOU 1987 O PRO A 233 1189 811 1204 66 349 -34 O
ATOM 1988 CB PRO A 233 4.349 -19.719 -12.623 1.00 12.05 C
ANISOU 1988 CB PRO A 233 2280 694 1603 36 497 -478 C
ATOM 1989 CG PRO A 233 2.853 -19.893 -12.599 1.00 15.39 C
ANISOU 1989 CG PRO A 233 2358 1965 1524 -557 95 -1024 C
ATOM 1990 CD PRO A 233 2.447 -19.915 -11.156 1.00 9.55 C
ANISOU 1990 CD PRO A 233 1396 742 1490 -116 -165 -136 C
ATOM 1991 N VAL A 234 3.690 -16.575 -11.298 1.00 7.61 N
ANISOU 1991 N VAL A 234 1026 550 1316 218 117 -94 N
ATOM 1992 CA VAL A 234 3.627 -15.200 -11.750 1.00 7.56 C
ANISOU 1992 CA VAL A 234 952 564 1356 173 176 -72 C
ATOM 1993 C VAL A 234 4.946 -14.470 -11.530 1.00 6.41 C
ANISOU 1993 C VAL A 234 880 621 937 182 312 -273 C
ATOM 1994 O VAL A 234 5.564 -14.616 -10.471 1.00 7.10 O
ANISOU 1994 O VAL A 234 1057 571 1069 107 157 28 O
ATOM 1995 CB VAL A 234 2.484 -14.448 -11.003 1.00 8.05 C
ANISOU 1995 CB VAL A 234 723 753 1583 315 -47 -213 C
ATOM 1996 CG1 VAL A 234 2.713 -14.309 -9.530 1.00 10.87 C
ANISOU 1996 CG1 VAL A 234 1068 1530 1534 165 200 -476 C
ATOM 1997 CG2 VAL A 234 2.283 -13.067 -11.603 1.00 11.73 C
ANISOU 1997 CG2 VAL A 234 1084 855 2518 595 113 50 C
ATOM 1998 N PRO A 235 5.389 -13.677 -12.477 1.00 6.47 N
ANISOU 1998 N PRO A 235 878 768 812 120 150 -223 N
ATOM 1999 CA PRO A 235 6.598 -12.896 -12.234 1.00 5.80 C
ANISOU 1999 CA PRO A 235 763 566 874 250 94 -156 C
ATOM 2000 C PRO A 235 6.450 -11.963 -11.042 1.00 5.28 C
ANISOU 2000 C PRO A 235 628 468 911 191 82 -115 C
ATOM 2001 O PRO A 235 5.444 -11.286 -10.927 1.00 5.51 O
ANISOU 2001 O PRO A 235 692 485 918 278 -11 -176 O
ATOM 2002 CB PRO A 235 6.783 -12.110 -13.531 1.00 6.62 C
ANISOU 2002 CB PRO A 235 947 625 942 206 148 -115 C
ATOM 2003 CG PRO A 235 6.171 -13.015 -14.571 1.00 6.94 C
ANISOU 2003 CG PRO A 235 1199 574 864 359 89 -43 C
ATOM 2004 CD PRO A 235 4.918 -13.548 -13.866 1.00 7.67 C
ANISOU 2004 CD PRO A 235 1105 822 989 48 -72 -154 C
ATOM 2005 N LYS A 236 7.474 -11.931 -10.199 1.00 5.01 N
ANISOU 2005 N LYS A 236 673 503 728 229 156 -99 N
ATOM 2006 CA LYS A 236 7.510 -11.084 -9.009 1.00 5.04 C
ANISOU 2006 CA LYS A 236 695 420 801 285 126 -144 C
ATOM 2007 C LYS A 236 8.772 -10.247 -8.973 1.00 5.31 C
ANISOU 2007 C LYS A 236 685 412 919 270 79 -64 C
ATOM 2008 O LYS A 236 9.870 -10.730 -9.317 1.00 6.39 O
ANISOU 2008 O LYS A 236 782 560 1087 250 307 -172 O
ATOM 2009 CB LYS A 236 7.458 -11.988 -7.764 1.00 5.24 C
ANISOU 2009 CB LYS A 236 847 489 657 154 207 -236 C
ATOM 2010 CG LYS A 236 6.273 -12.892 -7.711 1.00 5.69 C
ANISOU 2010 CG LYS A 236 832 666 665 161 278 -142 C
ATOM 2011 CD LYS A 236 6.375 -13.979 -6.665 1.00 6.27 C
ANISOU 2011 CD LYS A 236 1145 577 662 94 239 -145 C
ATOM 2012 CE LYS A 236 5.368 -15.118 -6.872 1.00 6.25 C
ANISOU 2012 CE LYS A 236 863 742 769 138 282 -106 C
ATOM 2013 NZ LYS A 236 5.730 -15.926 -8.072 1.00 6.32 N
ANISOU 2013 NZ LYS A 236 896 677 826 7 191 -236 N
ATOM 2014 N LEU A 237 8.614 -9.013 -8.514 1.00 4.76 N
ANISOU 2014 N LEU A 237 692 455 663 155 201 -63 N
ATOM 2015 CA LEU A 237 9.693 -8.060 -8.338 1.00 4.36 C
ANISOU 2015 CA LEU A 237 558 317 782 357 37 -78 C
ATOM 2016 C LEU A 237 9.590 -7.527 -6.903 1.00 4.98 C
ANISOU 2016 C LEU A 237 624 555 714 249 74 -114 C
ATOM 2017 O LEU A 237 8.599 -6.872 -6.606 1.00 6.42 O
ANISOU 2017 O LEU A 237 595 1046 799 377 121 -224 O
ATOM 2018 CB LEU A 237 9.607 -6.966 -9.404 1.00 4.81 C
ANISOU 2018 CB LEU A 237 756 365 705 265 164 -100 C
ATOM 2019 CG LEU A 237 10.686 -5.909 -9.419 1.00 5.99 C
ANISOU 2019 CG LEU A 237 939 584 752 47 55 -13 C
ATOM 2020 CD1 LEU A 237 12.033 -6.516 -9.747 1.00 8.82 C
ANISOU 2020 CD1 LEU A 237 828 687 1837 86 -10 128 C
ATOM 2021 CD2 LEU A 237 10.376 -4.819 -10.439 1.00 6.50 C
ANISOU 2021 CD2 LEU A 237 832 747 889 29 22 188 C
ATOM 2022 N LEU A 238 10.553 -7.817 -6.061 1.00 4.61 N
ANISOU 2022 N LEU A 238 507 545 700 234 195 -149 N
ATOM 2023 CA LEU A 238 10.521 -7.464 -4.650 1.00 5.09 C
ANISOU 2023 CA LEU A 238 689 571 674 36 113 -19 C
ATOM 2024 C LEU A 238 11.607 -6.466 -4.334 1.00 4.42 C
ANISOU 2024 C LEU A 238 488 587 605 151 201 -25 C
ATOM 2025 O LEU A 238 12.795 -6.793 -4.452 1.00 6.78 O
ANISOU 2025 O LEU A 238 540 775 1260 204 284 -181 O
ATOM 2026 CB LEU A 238 10.702 -8.734 -3.794 1.00 6.05 C
ANISOU 2026 CB LEU A 238 778 618 903 81 82 70 C
ATOM 2027 CG LEU A 238 10.873 -8.533 -2.299 1.00 7.02 C
ANISOU 2027 CG LEU A 238 977 897 794 231 215 236 C
ATOM 2028 CD1 LEU A 238 9.697 -7.782 -1.685 1.00 7.03 C
ANISOU 2028 CD1 LEU A 238 880 833 959 76 225 126 C
ATOM 2029 CD2 LEU A 238 11.084 -9.875 -1.623 1.00 10.69 C
ANISOU 2029 CD2 LEU A 238 1932 989 1141 491 113 327 C
ATOM 2030 N PHE A 239 11.220 -5.275 -3.957 1.00 4.61 N
ANISOU 2030 N PHE A 239 611 527 613 140 99 -127 N
ATOM 2031 CA PHE A 239 12.150 -4.262 -3.495 1.00 4.81 C
ANISOU 2031 CA PHE A 239 527 678 623 46 136 -37 C
ATOM 2032 C PHE A 239 12.301 -4.350 -1.999 1.00 4.49 C
ANISOU 2032 C PHE A 239 478 668 560 128 237 -213 C
ATOM 2033 O PHE A 239 11.304 -4.576 -1.318 1.00 5.60 O
ANISOU 2033 O PHE A 239 554 884 689 72 236 15 O
ATOM 2034 CB PHE A 239 11.618 -2.851 -3.848 1.00 5.26 C
ANISOU 2034 CB PHE A 239 641 588 768 -12 55 -101 C
ATOM 2035 CG PHE A 239 11.483 -2.651 -5.335 1.00 4.55 C
ANISOU 2035 CG PHE A 239 505 514 711 174 206 -94 C
ATOM 2036 CD1 PHE A 239 10.327 -2.938 -6.022 1.00 4.56 C
ANISOU 2036 CD1 PHE A 239 473 605 655 162 228 -194 C
ATOM 2037 CD2 PHE A 239 12.558 -2.167 -6.036 1.00 5.15 C
ANISOU 2037 CD2 PHE A 239 418 723 817 87 117 -112 C
ATOM 2038 CE1 PHE A 239 10.235 -2.766 -7.373 1.00 5.04 C
ANISOU 2038 CE1 PHE A 239 486 655 775 89 136 18 C
ATOM 2039 CE2 PHE A 239 12.472 -1.988 -7.412 1.00 5.41 C
ANISOU 2039 CE2 PHE A 239 506 798 752 28 210 32 C
ATOM 2040 CZ PHE A 239 11.311 -2.284 -8.089 1.00 4.96 C
ANISOU 2040 CZ PHE A 239 630 585 671 49 151 110 C
ATOM 2041 N TRP A 240 13.514 -4.191 -1.499 1.00 5.18 N
ANISOU 2041 N TRP A 240 590 825 554 103 119 -119 N
ATOM 2042 CA TRP A 240 13.764 -4.269 -0.083 1.00 5.27 C
ANISOU 2042 CA TRP A 240 614 827 561 133 153 -49 C
ATOM 2043 C TRP A 240 14.797 -3.208 0.307 1.00 5.07 C
ANISOU 2043 C TRP A 240 524 850 553 106 31 19 C
ATOM 2044 O TRP A 240 15.621 -2.785 -0.501 1.00 5.62 O
ANISOU 2044 O TRP A 240 640 763 732 152 231 -108 O
ATOM 2045 CB TRP A 240 14.202 -5.683 0.321 1.00 6.84 C
ANISOU 2045 CB TRP A 240 997 778 822 195 -28 -40 C
ATOM 2046 CG TRP A 240 15.479 -6.126 -0.326 1.00 7.13 C
ANISOU 2046 CG TRP A 240 1038 679 993 222 28 -12 C
ATOM 2047 CD1 TRP A 240 15.613 -6.682 -1.551 1.00 7.73 C
ANISOU 2047 CD1 TRP A 240 993 826 1118 177 83 -186 C
ATOM 2048 CD2 TRP A 240 16.813 -6.044 0.208 1.00 7.49 C
ANISOU 2048 CD2 TRP A 240 1008 984 852 219 41 126 C
ATOM 2049 NE1 TRP A 240 16.946 -6.949 -1.828 1.00 8.42 N
ANISOU 2049 NE1 TRP A 240 990 1000 1209 356 -50 -282 N
ATOM 2050 CE2 TRP A 240 17.697 -6.577 -0.762 1.00 8.07 C
ANISOU 2050 CE2 TRP A 240 988 895 1184 170 6 -208 C
ATOM 2051 CE3 TRP A 240 17.334 -5.564 1.416 1.00 8.27 C
ANISOU 2051 CE3 TRP A 240 1284 912 947 462 -127 -13 C
ATOM 2052 CZ2 TRP A 240 19.064 -6.653 -0.555 1.00 8.63 C
ANISOU 2052 CZ2 TRP A 240 973 755 1551 360 -40 -296 C
ATOM 2053 CZ3 TRP A 240 18.693 -5.641 1.624 1.00 9.50 C
ANISOU 2053 CZ3 TRP A 240 1366 936 1307 369 -414 -242 C
ATOM 2054 CH2 TRP A 240 19.522 -6.175 0.634 1.00 10.89 C
ANISOU 2054 CH2 TRP A 240 982 1543 1611 351 -294 -249 C
ATOM 2055 N GLY A 241 14.759 -2.812 1.586 1.00 5.79 N
ANISOU 2055 N GLY A 241 895 740 563 39 87 17 N
ATOM 2056 CA GLY A 241 15.754 -1.913 2.114 1.00 7.20 C
ANISOU 2056 CA GLY A 241 961 1183 590 74 -22 -212 C
ATOM 2057 C GLY A 241 16.382 -2.430 3.405 1.00 6.50 C
ANISOU 2057 C GLY A 241 807 859 803 324 -5 -189 C
ATOM 2058 O GLY A 241 15.974 -3.452 3.939 1.00 7.25 O
ANISOU 2058 O GLY A 241 968 764 1023 240 -40 -168 O
ATOM 2059 N THR A 242 17.354 -1.658 3.875 1.00 6.95 N
ANISOU 2059 N THR A 242 820 905 914 225 -108 -140 N
ATOM 2060 CA THR A 242 18.069 -1.969 5.115 1.00 8.28 C
ANISOU 2060 CA THR A 242 1072 1078 998 456 -282 -199 C
ATOM 2061 C THR A 242 17.852 -0.819 6.079 1.00 7.46 C
ANISOU 2061 C THR A 242 849 997 990 527 -316 -160 C
ATOM 2062 O THR A 242 18.189 0.322 5.693 1.00 8.37 O
ANISOU 2062 O THR A 242 839 1133 1209 260 -95 -275 O
ATOM 2063 CB THR A 242 19.583 -2.148 4.853 1.00 9.66 C
ANISOU 2063 CB THR A 242 1147 1151 1373 752 -317 -347 C
ATOM 2064 OG1 THR A 242 19.773 -3.272 3.982 1.00 11.69 O
ANISOU 2064 OG1 THR A 242 1433 1081 1928 656 -185 -545 O
ATOM 2065 CG2 THR A 242 20.356 -2.407 6.134 1.00 12.17 C
ANISOU 2065 CG2 THR A 242 1308 1475 1839 699 -707 -219 C
ATOM 2066 N PRO A 243 17.361 -1.056 7.283 1.00 8.48 N
ANISOU 2066 N PRO A 243 1060 1113 1048 490 -217 -186 N
ATOM 2067 CA PRO A 243 17.064 -2.376 7.862 1.00 9.59 C
ANISOU 2067 CA PRO A 243 1310 1327 1007 452 -261 28 C
ATOM 2068 C PRO A 243 15.723 -2.925 7.486 1.00 8.86 C
ANISOU 2068 C PRO A 243 1361 1029 975 404 -273 -29 C
ATOM 2069 O PRO A 243 15.421 -4.056 7.855 1.00 10.21 O
ANISOU 2069 O PRO A 243 1751 847 1281 551 -391 -68 O
ATOM 2070 CB PRO A 243 17.065 -2.103 9.370 1.00 11.08 C
ANISOU 2070 CB PRO A 243 1459 1724 1029 341 -415 -44 C
ATOM 2071 CG PRO A 243 16.578 -0.702 9.463 1.00 11.60 C
ANISOU 2071 CG PRO A 243 1662 1761 983 506 -82 -158 C
ATOM 2072 CD PRO A 243 17.164 0.052 8.275 1.00 9.49 C
ANISOU 2072 CD PRO A 243 1038 1398 1170 506 -34 -334 C
ATOM 2073 N GLY A 244 14.903 -2.146 6.744 1.00 7.86 N
ANISOU 2073 N GLY A 244 1105 1019 864 242 -63 97 N
ATOM 2074 CA GLY A 244 13.542 -2.618 6.503 1.00 7.29 C
ANISOU 2074 CA GLY A 244 1055 803 911 357 31 84 C
ATOM 2075 C GLY A 244 12.709 -2.568 7.758 1.00 7.12 C
ANISOU 2075 C GLY A 244 1069 845 790 281 -73 53 C
ATOM 2076 O GLY A 244 13.188 -2.191 8.806 1.00 7.99 O
ANISOU 2076 O GLY A 244 1238 892 907 24 -94 -139 O
ATOM 2077 N VAL A 245 11.454 -2.959 7.649 1.00 7.19 N
ANISOU 2077 N VAL A 245 1080 923 729 184 -23 -65 N
ATOM 2078 CA VAL A 245 10.509 -3.027 8.769 1.00 6.82 C
ANISOU 2078 CA VAL A 245 1233 774 586 163 33 -34 C
ATOM 2079 C VAL A 245 9.832 -4.386 8.637 1.00 8.34 C
ANISOU 2079 C VAL A 245 1721 792 654 -2 -164 283 C
ATOM 2080 O VAL A 245 10.209 -5.312 9.351 1.00 10.80 O
ANISOU 2080 O VAL A 245 2400 846 857 139 -243 362 O
ATOM 2081 CB VAL A 245 9.538 -1.835 8.824 1.00 7.68 C
ANISOU 2081 CB VAL A 245 1267 854 799 178 188 -184 C
ATOM 2082 CG1 VAL A 245 8.466 -2.056 9.878 1.00 8.06 C
ANISOU 2082 CG1 VAL A 245 1366 660 1037 158 250 -100 C
ATOM 2083 CG2 VAL A 245 10.334 -0.553 9.088 1.00 8.45 C
ANISOU 2083 CG2 VAL A 245 1529 816 865 94 216 78 C
ATOM 2084 N LEU A 246 8.867 -4.559 7.752 1.00 7.46 N
ANISOU 2084 N LEU A 246 1341 647 848 94 -11 -8 N
ATOM 2085 CA LEU A 246 8.155 -5.818 7.601 1.00 7.56 C
ANISOU 2085 CA LEU A 246 1330 612 929 73 301 -34 C
ATOM 2086 C LEU A 246 9.007 -6.879 6.921 1.00 7.26 C
ANISOU 2086 C LEU A 246 1263 646 850 109 111 -47 C
ATOM 2087 O LEU A 246 8.780 -8.076 7.165 1.00 8.13 O
ANISOU 2087 O LEU A 246 1369 632 1087 110 243 56 O
ATOM 2088 CB LEU A 246 6.860 -5.622 6.794 1.00 6.21 C
ANISOU 2088 CB LEU A 246 1264 309 788 -23 357 -11 C
ATOM 2089 CG LEU A 246 5.818 -4.693 7.442 1.00 6.65 C
ANISOU 2089 CG LEU A 246 1300 416 812 5 472 -10 C
ATOM 2090 CD1 LEU A 246 4.572 -4.620 6.570 1.00 7.61 C
ANISOU 2090 CD1 LEU A 246 1206 740 945 12 508 -8 C
ATOM 2091 CD2 LEU A 246 5.489 -5.098 8.865 1.00 8.75 C
ANISOU 2091 CD2 LEU A 246 1548 870 907 143 561 137 C
ATOM 2092 N ILE A 247 9.949 -6.461 6.072 1.00 6.96 N
ANISOU 2092 N ILE A 247 1096 602 946 265 108 83 N
ATOM 2093 CA ILE A 247 10.748 -7.421 5.275 1.00 7.08 C
ANISOU 2093 CA ILE A 247 1100 496 1094 318 75 31 C
ATOM 2094 C ILE A 247 12.211 -7.055 5.426 1.00 7.75 C
ANISOU 2094 C ILE A 247 1085 808 1050 236 26 -75 C
ATOM 2095 O ILE A 247 12.779 -6.360 4.605 1.00 8.22 O
ANISOU 2095 O ILE A 247 1088 745 1290 308 48 110 O
ATOM 2096 CB ILE A 247 10.299 -7.465 3.814 1.00 7.32 C
ANISOU 2096 CB ILE A 247 951 716 1113 325 41 -80 C
ATOM 2097 CG1 ILE A 247 8.808 -7.670 3.559 1.00 7.36 C
ANISOU 2097 CG1 ILE A 247 913 884 1000 31 360 -262 C
ATOM 2098 CG2 ILE A 247 11.099 -8.563 3.053 1.00 9.69 C
ANISOU 2098 CG2 ILE A 247 1177 1256 1249 484 210 -310 C
ATOM 2099 CD1 ILE A 247 8.195 -8.972 4.003 1.00 10.63 C
ANISOU 2099 CD1 ILE A 247 1577 988 1473 -135 556 -182 C
ATOM 2100 N PRO A 248 12.847 -7.510 6.501 1.00 8.01 N
ANISOU 2100 N PRO A 248 1271 710 1064 102 -113 -119 N
ATOM 2101 CA PRO A 248 14.261 -7.227 6.691 1.00 9.47 C
ANISOU 2101 CA PRO A 248 1193 1041 1366 248 -171 -31 C
ATOM 2102 C PRO A 248 15.120 -7.915 5.636 1.00 8.75 C
ANISOU 2102 C PRO A 248 1232 720 1375 329 -178 9 C
ATOM 2103 O PRO A 248 14.638 -8.845 4.959 1.00 9.63 O
ANISOU 2103 O PRO A 248 1279 742 1639 217 -250 10 O
ATOM 2104 CB PRO A 248 14.567 -7.870 8.048 1.00 13.76 C
ANISOU 2104 CB PRO A 248 1512 2468 1247 -57 -310 219 C
ATOM 2105 CG PRO A 248 13.273 -8.116 8.720 1.00 15.89 C
ANISOU 2105 CG PRO A 248 1565 3371 1100 217 -180 228 C
ATOM 2106 CD PRO A 248 12.246 -8.211 7.639 1.00 8.92 C
ANISOU 2106 CD PRO A 248 1352 1175 863 303 65 -203 C
ATOM 2107 N PRO A 249 16.340 -7.457 5.455 1.00 10.08 N
ANISOU 2107 N PRO A 249 1167 1025 1639 319 -115 -435 N
ATOM 2108 CA PRO A 249 17.226 -8.014 4.428 1.00 9.41 C
ANISOU 2108 CA PRO A 249 1148 770 1655 452 -124 -255 C
ATOM 2109 C PRO A 249 17.289 -9.526 4.387 1.00 8.91 C
ANISOU 2109 C PRO A 249 1130 770 1484 244 -101 -199 C
ATOM 2110 O PRO A 249 17.189 -10.094 3.304 1.00 10.61 O
ANISOU 2110 O PRO A 249 1539 845 1647 528 -206 -326 O
ATOM 2111 CB PRO A 249 18.592 -7.381 4.757 1.00 8.87 C
ANISOU 2111 CB PRO A 249 1207 698 1465 348 -163 -233 C
ATOM 2112 CG PRO A 249 18.197 -6.029 5.309 1.00 10.27 C
ANISOU 2112 CG PRO A 249 1259 752 1893 407 -34 -264 C
ATOM 2113 CD PRO A 249 16.993 -6.313 6.122 1.00 10.06 C
ANISOU 2113 CD PRO A 249 1068 1117 1637 362 -194 -457 C
ATOM 2114 N ALA A 250 17.446 -10.231 5.490 1.00 10.73 N
ANISOU 2114 N ALA A 250 1496 940 1641 516 -165 -91 N
ATOM 2115 CA ALA A 250 17.547 -11.669 5.460 1.00 11.27 C
ANISOU 2115 CA ALA A 250 1493 957 1831 725 -454 -154 C
ATOM 2116 C ALA A 250 16.252 -12.305 5.019 1.00 10.11 C
ANISOU 2116 C ALA A 250 1431 1013 1399 474 -70 -148 C
ATOM 2117 O ALA A 250 16.246 -13.368 4.383 1.00 10.12 O
ANISOU 2117 O ALA A 250 1580 924 1342 473 22 -55 O
ATOM 2118 CB ALA A 250 17.923 -12.250 6.833 1.00 13.68 C
ANISOU 2118 CB ALA A 250 2151 936 2110 299 -806 76 C
ATOM 2119 N GLU A 251 15.132 -11.687 5.338 1.00 9.22 N
ANISOU 2119 N GLU A 251 1451 854 1197 331 2 -113 N
ATOM 2120 CA GLU A 251 13.856 -12.240 4.852 1.00 9.00 C
ANISOU 2120 CA GLU A 251 1401 706 1313 415 -88 -69 C
ATOM 2121 C GLU A 251 13.650 -11.969 3.372 1.00 8.61 C
ANISOU 2121 C GLU A 251 1318 637 1315 434 -18 -17 C
ATOM 2122 O GLU A 251 13.063 -12.824 2.690 1.00 8.50 O
ANISOU 2122 O GLU A 251 1167 729 1335 304 -109 39 O
ATOM 2123 CB GLU A 251 12.730 -11.667 5.710 1.00 9.39 C
ANISOU 2123 CB GLU A 251 1445 823 1301 200 0 -274 C
ATOM 2124 CG GLU A 251 12.808 -12.157 7.155 1.00 10.53 C
ANISOU 2124 CG GLU A 251 1380 1137 1486 160 12 108 C
ATOM 2125 CD GLU A 251 12.722 -13.674 7.220 1.00 12.32 C
ANISOU 2125 CD GLU A 251 1752 1059 1868 332 58 4 C
ATOM 2126 OE1 GLU A 251 13.630 -14.295 7.829 1.00 13.69 O
ANISOU 2126 OE1 GLU A 251 1940 1133 2128 519 -48 -91 O
ATOM 2127 OE2 GLU A 251 11.722 -14.237 6.693 1.00 13.57 O
ANISOU 2127 OE2 GLU A 251 2132 1222 1804 -2 -78 20 O
ATOM 2128 N ALA A 252 14.088 -10.820 2.860 1.00 8.59 N
ANISOU 2128 N ALA A 252 1447 547 1268 336 111 -141 N
ATOM 2129 CA ALA A 252 14.053 -10.584 1.419 1.00 7.89 C
ANISOU 2129 CA ALA A 252 1066 633 1301 323 143 -120 C
ATOM 2130 C ALA A 252 14.868 -11.644 0.703 1.00 7.74 C
ANISOU 2130 C ALA A 252 1042 673 1224 343 80 -112 C
ATOM 2131 O ALA A 252 14.450 -12.164 -0.324 1.00 8.52 O
ANISOU 2131 O ALA A 252 1431 667 1138 365 76 -28 O
ATOM 2132 CB ALA A 252 14.542 -9.173 1.091 1.00 9.54 C
ANISOU 2132 CB ALA A 252 1512 613 1501 372 140 37 C
ATOM 2133 N ALA A 253 16.039 -12.001 1.255 1.00 9.12 N
ANISOU 2133 N ALA A 253 1129 884 1450 479 26 -125 N
ATOM 2134 CA ALA A 253 16.866 -13.018 0.626 1.00 9.63 C
ANISOU 2134 CA ALA A 253 882 946 1833 297 143 -254 C
ATOM 2135 C ALA A 253 16.207 -14.391 0.639 1.00 10.06 C
ANISOU 2135 C ALA A 253 1688 748 1386 299 -264 113 C
ATOM 2136 O ALA A 253 16.282 -15.139 -0.333 1.00 10.14 O
ANISOU 2136 O ALA A 253 1393 880 1581 142 -79 -14 O
ATOM 2137 CB ALA A 253 18.230 -13.077 1.313 1.00 11.42 C
ANISOU 2137 CB ALA A 253 1151 1159 2031 629 -146 -322 C
ATOM 2138 N ARG A 254 15.526 -14.699 1.745 1.00 9.20 N
ANISOU 2138 N ARG A 254 1574 564 1359 321 -300 47 N
ATOM 2139 CA ARG A 254 14.774 -15.941 1.793 1.00 8.76 C
ANISOU 2139 CA ARG A 254 1339 675 1314 324 -177 -136 C
ATOM 2140 C ARG A 254 13.663 -15.982 0.752 1.00 8.85 C
ANISOU 2140 C ARG A 254 1268 826 1269 349 -61 -68 C
ATOM 2141 O ARG A 254 13.433 -16.988 0.100 1.00 8.37 O
ANISOU 2141 O ARG A 254 1230 795 1155 117 -74 30 O
ATOM 2142 CB ARG A 254 14.198 -16.152 3.197 1.00 9.90 C
ANISOU 2142 CB ARG A 254 1574 813 1375 338 -131 62 C
ATOM 2143 CG ARG A 254 15.248 -16.723 4.137 1.00 9.95 C
ANISOU 2143 CG ARG A 254 1573 801 1407 250 -259 -19 C
ATOM 2144 CD ARG A 254 14.787 -16.668 5.584 1.00 12.45 C
ANISOU 2144 CD ARG A 254 2088 1186 1454 833 -142 -8 C
ATOM 2145 NE ARG A 254 15.320 -17.758 6.369 1.00 12.05 N
ANISOU 2145 NE ARG A 254 1935 1095 1547 451 -289 164 N
ATOM 2146 CZ ARG A 254 15.256 -17.916 7.664 1.00 14.30 C
ANISOU 2146 CZ ARG A 254 2641 1398 1394 972 -326 -122 C
ATOM 2147 NH1 ARG A 254 15.801 -19.017 8.228 1.00 13.31 N
ANISOU 2147 NH1 ARG A 254 2082 1307 1669 399 -346 252 N
ATOM 2148 NH2 ARG A 254 14.670 -17.014 8.448 1.00 20.06 N
ANISOU 2148 NH2 ARG A 254 3737 1701 2184 1016 -285 -885 N
ATOM 2149 N LEU A 255 12.948 -14.869 0.618 1.00 9.12 N
ANISOU 2149 N LEU A 255 1332 980 1153 458 -92 -104 N
ATOM 2150 CA LEU A 255 11.891 -14.765 -0.388 1.00 7.62 C
ANISOU 2150 CA LEU A 255 1109 698 1088 276 42 -26 C
ATOM 2151 C LEU A 255 12.415 -14.873 -1.821 1.00 7.86 C
ANISOU 2151 C LEU A 255 1086 775 1124 468 55 -146 C
ATOM 2152 O LEU A 255 11.725 -15.438 -2.648 1.00 8.83 O
ANISOU 2152 O LEU A 255 1229 1081 1044 481 11 -116 O
ATOM 2153 CB LEU A 255 11.102 -13.486 -0.186 1.00 7.77 C
ANISOU 2153 CB LEU A 255 1075 846 1033 364 156 -82 C
ATOM 2154 CG LEU A 255 10.217 -13.480 1.079 1.00 7.36 C
ANISOU 2154 CG LEU A 255 1335 495 965 316 161 104 C
ATOM 2155 CD1 LEU A 255 9.853 -12.070 1.454 1.00 8.96 C
ANISOU 2155 CD1 LEU A 255 1020 674 1712 497 204 -254 C
ATOM 2156 CD2 LEU A 255 8.982 -14.330 0.895 1.00 8.36 C
ANISOU 2156 CD2 LEU A 255 1484 669 1025 140 310 39 C
ATOM 2157 N ALA A 256 13.594 -14.349 -2.084 1.00 9.22 N
ANISOU 2157 N ALA A 256 1240 1047 1214 302 89 142 N
ATOM 2158 CA ALA A 256 14.188 -14.505 -3.406 1.00 11.13 C
ANISOU 2158 CA ALA A 256 1523 1351 1356 -125 252 -35 C
ATOM 2159 C ALA A 256 14.266 -15.981 -3.796 1.00 10.14 C
ANISOU 2159 C ALA A 256 1096 1404 1355 54 215 -136 C
ATOM 2160 O ALA A 256 14.160 -16.392 -4.941 1.00 12.70 O
ANISOU 2160 O ALA A 256 1771 1738 1316 455 330 -268 O
ATOM 2161 CB ALA A 256 15.576 -13.880 -3.415 1.00 12.65 C
ANISOU 2161 CB ALA A 256 1421 1238 2149 -24 398 83 C
ATOM 2162 N GLU A 257 14.522 -16.813 -2.775 1.00 11.08 N
ANISOU 2162 N GLU A 257 1299 1434 1477 113 8 -109 N
ATOM 2163 CA GLU A 257 14.698 -18.241 -2.963 1.00 11.73 C
ANISOU 2163 CA GLU A 257 1526 1517 1413 429 105 -156 C
ATOM 2164 C GLU A 257 13.366 -18.984 -2.928 1.00 10.16 C
ANISOU 2164 C GLU A 257 1488 808 1565 648 -96 -292 C
ATOM 2165 O GLU A 257 13.144 -19.923 -3.716 1.00 17.38 O
ANISOU 2165 O GLU A 257 2495 1486 2621 197 383 -1159 O
ATOM 2166 CB GLU A 257 15.667 -18.825 -1.929 1.00 12.88 C
ANISOU 2166 CB GLU A 257 1446 1837 1609 830 -107 -585 C
ATOM 2167 CG AGLU A 257 17.016 -18.229 -1.741 0.50 17.15 C
ANISOU 2167 CG AGLU A 257 1590 2622 2305 533 -170 -625 C
ATOM 2168 CG BGLU A 257 16.276 -20.173 -2.207 0.50 11.16 C
ANISOU 2168 CG BGLU A 257 642 1600 1999 360 372 -352 C
ATOM 2169 CD AGLU A 257 17.815 -18.134 -3.019 0.50 13.57 C
ANISOU 2169 CD AGLU A 257 1449 1482 2226 615 -304 -64 C
ATOM 2170 CD BGLU A 257 17.139 -20.378 -3.433 0.50 7.03 C
ANISOU 2170 CD BGLU A 257 680 365 1628 53 268 70 C
ATOM 2171 OE1AGLU A 257 17.528 -18.934 -3.934 0.50 15.52 O
ANISOU 2171 OE1AGLU A 257 1505 1731 2661 -173 695 -508 O
ATOM 2172 OE1BGLU A 257 17.390 -19.362 -4.132 0.50 10.49 O
ANISOU 2172 OE1BGLU A 257 2047 32 1907 185 60 58 O
ATOM 2173 OE2AGLU A 257 18.695 -17.265 -3.108 0.50 18.66 O
ANISOU 2173 OE2AGLU A 257 1953 2783 2354 -383 -721 -407 O
ATOM 2174 OE2BGLU A 257 17.562 -21.524 -3.743 0.50 5.45 O
ANISOU 2174 OE2BGLU A 257 1229 16 825 -122 193 307 O
ATOM 2175 N SER A 258 12.424 -18.569 -2.088 1.00 9.05 N
ANISOU 2175 N SER A 258 1573 715 1151 299 76 12 N
ATOM 2176 CA SER A 258 11.170 -19.302 -1.851 1.00 10.01 C
ANISOU 2176 CA SER A 258 1796 682 1325 104 -86 103 C
ATOM 2177 C SER A 258 9.972 -18.901 -2.698 1.00 12.55 C
ANISOU 2177 C SER A 258 1943 1069 1754 -206 -500 157 C
ATOM 2178 O SER A 258 8.978 -19.615 -2.749 1.00 15.28 O
ANISOU 2178 O SER A 258 2387 1654 1765 -712 -685 559 O
ATOM 2179 CB SER A 258 10.779 -19.165 -0.373 1.00 10.57 C
ANISOU 2179 CB SER A 258 1735 877 1405 329 145 270 C
ATOM 2180 OG SER A 258 10.372 -17.846 -0.030 1.00 10.71 O
ANISOU 2180 OG SER A 258 1567 944 1558 158 240 53 O
ATOM 2181 N LEU A 259 10.051 -17.752 -3.339 1.00 8.16 N
ANISOU 2181 N LEU A 259 1115 1017 970 208 136 -49 N
ATOM 2182 CA LEU A 259 9.010 -17.307 -4.247 1.00 8.27 C
ANISOU 2182 CA LEU A 259 1004 1175 964 -21 53 -138 C
ATOM 2183 C LEU A 259 9.430 -17.597 -5.686 1.00 7.72 C
ANISOU 2183 C LEU A 259 912 984 1039 168 124 -44 C
ATOM 2184 O LEU A 259 10.508 -17.158 -6.077 1.00 9.92 O
ANISOU 2184 O LEU A 259 1054 1562 1151 -158 183 59 O
ATOM 2185 CB LEU A 259 8.700 -15.812 -4.134 1.00 8.13 C
ANISOU 2185 CB LEU A 259 1110 1242 738 273 17 -29 C
ATOM 2186 CG LEU A 259 8.247 -15.315 -2.760 1.00 9.14 C
ANISOU 2186 CG LEU A 259 946 1606 922 575 136 -80 C
ATOM 2187 CD1 LEU A 259 8.116 -13.809 -2.809 1.00 12.57 C
ANISOU 2187 CD1 LEU A 259 1922 1631 1224 857 -64 -244 C
ATOM 2188 CD2 LEU A 259 6.951 -15.963 -2.327 1.00 12.61 C
ANISOU 2188 CD2 LEU A 259 1062 2501 1230 313 341 -347 C
ATOM 2189 N PRO A 260 8.595 -18.289 -6.445 1.00 6.66 N
ANISOU 2189 N PRO A 260 940 700 892 164 136 56 N
ATOM 2190 CA PRO A 260 8.968 -18.536 -7.843 1.00 7.14 C
ANISOU 2190 CA PRO A 260 1049 733 932 120 248 61 C
ATOM 2191 C PRO A 260 9.119 -17.283 -8.686 1.00 5.89 C
ANISOU 2191 C PRO A 260 834 670 734 261 124 -12 C
ATOM 2192 O PRO A 260 8.373 -16.323 -8.486 1.00 6.76 O
ANISOU 2192 O PRO A 260 934 671 966 207 187 -110 O
ATOM 2193 CB PRO A 260 7.822 -19.370 -8.394 1.00 8.47 C
ANISOU 2193 CB PRO A 260 1496 844 876 -87 137 63 C
ATOM 2194 CG PRO A 260 7.236 -20.034 -7.187 1.00 7.56 C
ANISOU 2194 CG PRO A 260 1148 679 1043 110 358 32 C
ATOM 2195 CD PRO A 260 7.351 -18.990 -6.077 1.00 6.98 C
ANISOU 2195 CD PRO A 260 992 688 973 173 287 68 C
ATOM 2196 N ASN A 261 10.048 -17.314 -9.643 1.00 6.39 N
ANISOU 2196 N ASN A 261 973 497 957 177 294 -37 N
ATOM 2197 CA ASN A 261 10.223 -16.257 -10.644 1.00 6.74 C
ANISOU 2197 CA ASN A 261 1010 644 907 147 144 75 C
ATOM 2198 C ASN A 261 10.253 -14.888 -9.980 1.00 5.79 C
ANISOU 2198 C ASN A 261 659 602 941 167 199 43 C
ATOM 2199 O ASN A 261 9.600 -13.940 -10.408 1.00 7.21 O
ANISOU 2199 O ASN A 261 903 799 1039 382 143 1 O
ATOM 2200 CB ASN A 261 9.146 -16.345 -11.718 1.00 7.92 C
ANISOU 2200 CB ASN A 261 1138 618 1255 66 -81 -70 C
ATOM 2201 CG ASN A 261 9.311 -17.627 -12.510 1.00 7.81 C
ANISOU 2201 CG ASN A 261 1140 792 1035 22 351 -125 C
ATOM 2202 OD1 ASN A 261 10.411 -18.048 -12.786 1.00 9.36 O
ANISOU 2202 OD1 ASN A 261 1088 1055 1412 13 292 -121 O
ATOM 2203 ND2 ASN A 261 8.194 -18.239 -12.851 1.00 8.47 N
ANISOU 2203 ND2 ASN A 261 1165 939 1113 -41 421 -438 N
ATOM 2204 N CYS A 262 11.067 -14.760 -8.965 1.00 6.60 N
ANISOU 2204 N CYS A 262 909 568 1029 251 97 61 N
ATOM 2205 CA CYS A 262 11.192 -13.576 -8.140 1.00 7.92 C
ANISOU 2205 CA CYS A 262 1046 793 1169 54 29 -84 C
ATOM 2206 C CYS A 262 12.575 -12.936 -8.335 1.00 8.18 C
ANISOU 2206 C CYS A 262 854 787 1466 183 88 -116 C
ATOM 2207 O CYS A 262 13.631 -13.595 -8.190 1.00 10.79 O
ANISOU 2207 O CYS A 262 1063 862 2174 408 -18 -248 O
ATOM 2208 CB CYS A 262 10.992 -13.916 -6.685 1.00 9.25 C
ANISOU 2208 CB CYS A 262 1415 953 1148 -12 204 -199 C
ATOM 2209 SG CYS A 262 11.029 -12.487 -5.595 1.00 10.85 S
ANISOU 2209 SG CYS A 262 1740 1046 1336 183 272 -335 S
ATOM 2210 N LYS A 263 12.578 -11.679 -8.675 1.00 6.83 N
ANISOU 2210 N LYS A 263 560 775 1259 284 280 -275 N
ATOM 2211 CA LYS A 263 13.726 -10.820 -8.776 1.00 7.59 C
ANISOU 2211 CA LYS A 263 763 816 1306 122 210 -289 C
ATOM 2212 C LYS A 263 13.709 -9.855 -7.592 1.00 6.90 C
ANISOU 2212 C LYS A 263 732 709 1182 167 261 -158 C
ATOM 2213 O LYS A 263 12.674 -9.229 -7.355 1.00 7.96 O
ANISOU 2213 O LYS A 263 765 1094 1167 374 130 -275 O
ATOM 2214 CB LYS A 263 13.741 -10.045 -10.089 1.00 8.09 C
ANISOU 2214 CB LYS A 263 1156 730 1188 106 347 -391 C
ATOM 2215 CG LYS A 263 14.882 -9.039 -10.193 1.00 9.11 C
ANISOU 2215 CG LYS A 263 1167 1104 1190 -31 423 -246 C
ATOM 2216 CD LYS A 263 14.869 -8.324 -11.540 1.00 11.02 C
ANISOU 2216 CD LYS A 263 1566 1307 1316 16 478 -60 C
ATOM 2217 CE LYS A 263 15.786 -7.131 -11.586 1.00 12.53 C
ANISOU 2217 CE LYS A 263 1791 1268 1700 -10 618 11 C
ATOM 2218 NZ LYS A 263 17.214 -7.430 -11.530 1.00 14.65 N
ANISOU 2218 NZ LYS A 263 1685 1904 1978 -278 119 -212 N
ATOM 2219 N THR A 264 14.783 -9.782 -6.826 1.00 7.58 N
ANISOU 2219 N THR A 264 703 720 1457 309 163 -357 N
ATOM 2220 CA THR A 264 14.847 -8.842 -5.743 1.00 7.60 C
ANISOU 2220 CA THR A 264 874 785 1229 219 193 -275 C
ATOM 2221 C THR A 264 15.731 -7.663 -6.140 1.00 7.27 C
ANISOU 2221 C THR A 264 538 930 1296 225 159 -378 C
ATOM 2222 O THR A 264 16.702 -7.813 -6.870 1.00 9.91 O
ANISOU 2222 O THR A 264 917 1354 1492 12 555 -809 O
ATOM 2223 CB THR A 264 15.359 -9.441 -4.424 1.00 10.29 C
ANISOU 2223 CB THR A 264 1300 1068 1541 459 -153 -62 C
ATOM 2224 OG1 THR A 264 16.648 -10.009 -4.591 1.00 13.68 O
ANISOU 2224 OG1 THR A 264 1475 1725 1999 728 -198 -312 O
ATOM 2225 CG2 THR A 264 14.415 -10.572 -4.009 1.00 13.65 C
ANISOU 2225 CG2 THR A 264 1792 1276 2121 394 -120 554 C
ATOM 2226 N VAL A 265 15.373 -6.505 -5.614 1.00 6.56 N
ANISOU 2226 N VAL A 265 605 807 1079 154 296 -248 N
ATOM 2227 CA VAL A 265 16.124 -5.282 -5.844 1.00 6.12 C
ANISOU 2227 CA VAL A 265 464 900 961 180 275 -199 C
ATOM 2228 C VAL A 265 16.376 -4.600 -4.496 1.00 5.33 C
ANISOU 2228 C VAL A 265 554 692 778 15 343 -37 C
ATOM 2229 O VAL A 265 15.441 -4.206 -3.822 1.00 6.84 O
ANISOU 2229 O VAL A 265 462 1159 979 106 328 -155 O
ATOM 2230 CB VAL A 265 15.378 -4.299 -6.773 1.00 7.56 C
ANISOU 2230 CB VAL A 265 907 1083 882 66 160 -22 C
ATOM 2231 CG1 VAL A 265 16.115 -2.955 -6.835 1.00 8.61 C
ANISOU 2231 CG1 VAL A 265 982 1081 1208 16 195 58 C
ATOM 2232 CG2 VAL A 265 15.149 -4.879 -8.169 1.00 10.17 C
ANISOU 2232 CG2 VAL A 265 1385 1496 984 -8 -25 -182 C
ATOM 2233 N ASP A 266 17.661 -4.440 -4.185 1.00 6.86 N
ANISOU 2233 N ASP A 266 492 1035 1081 168 303 -344 N
ATOM 2234 CA ASP A 266 18.176 -3.713 -3.031 1.00 6.44 C
ANISOU 2234 CA ASP A 266 657 943 848 116 200 -99 C
ATOM 2235 C ASP A 266 18.094 -2.217 -3.264 1.00 6.70 C
ANISOU 2235 C ASP A 266 494 928 1123 70 232 -111 C
ATOM 2236 O ASP A 266 18.748 -1.705 -4.206 1.00 7.23 O
ANISOU 2236 O ASP A 266 600 1224 921 59 83 90 O
ATOM 2237 CB ASP A 266 19.625 -4.149 -2.786 1.00 7.14 C
ANISOU 2237 CB ASP A 266 601 897 1213 54 144 -111 C
ATOM 2238 CG ASP A 266 20.298 -3.572 -1.575 1.00 7.96 C
ANISOU 2238 CG ASP A 266 854 1062 1108 284 -14 -67 C
ATOM 2239 OD1 ASP A 266 19.685 -2.716 -0.909 1.00 8.92 O
ANISOU 2239 OD1 ASP A 266 1038 1182 1170 461 -195 -126 O
ATOM 2240 OD2 ASP A 266 21.474 -3.944 -1.311 1.00 10.10 O
ANISOU 2240 OD2 ASP A 266 807 1578 1454 361 -118 -350 O
ATOM 2241 N ILE A 267 17.275 -1.506 -2.497 1.00 5.94 N
ANISOU 2241 N ILE A 267 651 806 801 31 100 -120 N
ATOM 2242 CA ILE A 267 17.162 -0.068 -2.723 1.00 5.91 C
ANISOU 2242 CA ILE A 267 752 790 703 23 75 24 C
ATOM 2243 C ILE A 267 18.114 0.779 -1.870 1.00 5.30 C
ANISOU 2243 C ILE A 267 630 753 633 197 214 -195 C
ATOM 2244 O ILE A 267 18.112 1.996 -2.015 1.00 6.37 O
ANISOU 2244 O ILE A 267 696 833 890 -25 176 -69 O
ATOM 2245 CB ILE A 267 15.734 0.464 -2.476 1.00 7.10 C
ANISOU 2245 CB ILE A 267 720 845 1133 41 201 84 C
ATOM 2246 CG1 ILE A 267 15.293 0.538 -0.989 1.00 8.40 C
ANISOU 2246 CG1 ILE A 267 653 1302 1237 167 336 276 C
ATOM 2247 CG2 ILE A 267 14.787 -0.304 -3.377 1.00 9.33 C
ANISOU 2247 CG2 ILE A 267 780 1009 1758 46 20 -185 C
ATOM 2248 CD1 ILE A 267 14.630 1.822 -0.601 1.00 9.72 C
ANISOU 2248 CD1 ILE A 267 1180 1322 1191 -65 308 -275 C
ATOM 2249 N GLY A 268 18.911 0.136 -1.035 1.00 6.53 N
ANISOU 2249 N GLY A 268 740 1023 718 305 33 -215 N
ATOM 2250 CA GLY A 268 19.768 0.821 -0.090 1.00 6.60 C
ANISOU 2250 CA GLY A 268 409 1222 878 134 151 -180 C
ATOM 2251 C GLY A 268 19.060 1.129 1.207 1.00 5.72 C
ANISOU 2251 C GLY A 268 383 1009 782 101 32 -140 C
ATOM 2252 O GLY A 268 18.224 0.327 1.643 1.00 7.15 O
ANISOU 2252 O GLY A 268 703 1245 768 -98 164 -180 O
ATOM 2253 N PRO A 269 19.363 2.252 1.860 1.00 6.38 N
ANISOU 2253 N PRO A 269 521 1040 863 103 160 -158 N
ATOM 2254 CA PRO A 269 18.670 2.550 3.109 1.00 6.69 C
ANISOU 2254 CA PRO A 269 492 1162 887 125 172 -212 C
ATOM 2255 C PRO A 269 17.159 2.624 2.936 1.00 5.90 C
ANISOU 2255 C PRO A 269 526 908 808 54 145 -60 C
ATOM 2256 O PRO A 269 16.625 3.218 2.014 1.00 6.42 O
ANISOU 2256 O PRO A 269 657 824 960 68 43 18 O
ATOM 2257 CB PRO A 269 19.284 3.910 3.481 1.00 8.17 C
ANISOU 2257 CB PRO A 269 645 1259 1199 22 192 -456 C
ATOM 2258 CG PRO A 269 20.663 3.892 2.859 1.00 8.70 C
ANISOU 2258 CG PRO A 269 734 1327 1244 -105 286 -484 C
ATOM 2259 CD PRO A 269 20.401 3.274 1.512 1.00 6.90 C
ANISOU 2259 CD PRO A 269 445 1061 1115 35 204 -314 C
ATOM 2260 N GLY A 270 16.471 2.000 3.879 1.00 5.66 N
ANISOU 2260 N GLY A 270 499 1001 651 167 199 -191 N
ATOM 2261 CA GLY A 270 15.011 2.027 3.854 1.00 5.15 C
ANISOU 2261 CA GLY A 270 451 906 601 94 178 -150 C
ATOM 2262 C GLY A 270 14.438 1.363 5.082 1.00 5.24 C
ANISOU 2262 C GLY A 270 574 832 586 73 177 -138 C
ATOM 2263 O GLY A 270 15.061 0.482 5.662 1.00 7.16 O
ANISOU 2263 O GLY A 270 812 1033 874 187 31 -21 O
ATOM 2264 N LEU A 271 13.252 1.819 5.452 1.00 5.31 N
ANISOU 2264 N LEU A 271 557 698 764 -86 296 -126 N
ATOM 2265 CA LEU A 271 12.515 1.274 6.579 1.00 4.48 C
ANISOU 2265 CA LEU A 271 441 590 673 225 212 -144 C
ATOM 2266 C LEU A 271 11.221 0.685 6.026 1.00 4.02 C
ANISOU 2266 C LEU A 271 499 620 406 40 232 -8 C
ATOM 2267 O LEU A 271 11.274 -0.408 5.498 1.00 5.38 O
ANISOU 2267 O LEU A 271 671 609 765 120 75 -70 O
ATOM 2268 CB LEU A 271 12.354 2.341 7.662 1.00 4.57 C
ANISOU 2268 CB LEU A 271 541 513 683 150 159 -99 C
ATOM 2269 CG LEU A 271 13.621 2.581 8.489 1.00 6.76 C
ANISOU 2269 CG LEU A 271 850 711 1008 -5 -182 8 C
ATOM 2270 CD1 LEU A 271 13.591 3.960 9.133 1.00 8.40 C
ANISOU 2270 CD1 LEU A 271 900 900 1391 41 -180 -339 C
ATOM 2271 CD2 LEU A 271 13.794 1.515 9.550 1.00 8.97 C
ANISOU 2271 CD2 LEU A 271 1382 1079 945 379 -165 137 C
ATOM 2272 N HIS A 272 10.120 1.442 6.102 1.00 4.85 N
ANISOU 2272 N HIS A 272 502 788 555 119 109 -53 N
ATOM 2273 CA HIS A 272 8.848 0.904 5.571 1.00 4.55 C
ANISOU 2273 CA HIS A 272 543 609 575 79 169 -106 C
ATOM 2274 C HIS A 272 8.412 1.585 4.275 1.00 3.86 C
ANISOU 2274 C HIS A 272 213 474 779 91 145 -54 C
ATOM 2275 O HIS A 272 8.043 0.880 3.308 1.00 4.52 O
ANISOU 2275 O HIS A 272 615 504 598 29 101 -10 O
ATOM 2276 CB HIS A 272 7.736 0.992 6.601 1.00 4.66 C
ANISOU 2276 CB HIS A 272 519 501 751 129 216 -136 C
ATOM 2277 CG HIS A 272 6.443 0.422 6.084 1.00 4.72 C
ANISOU 2277 CG HIS A 272 555 589 647 13 196 -40 C
ATOM 2278 ND1 HIS A 272 6.270 -0.923 5.788 1.00 4.66 N
ANISOU 2278 ND1 HIS A 272 485 695 589 -11 197 -112 N
ATOM 2279 CD2 HIS A 272 5.268 1.032 5.820 1.00 5.60 C
ANISOU 2279 CD2 HIS A 272 545 796 785 63 180 18 C
ATOM 2280 CE1 HIS A 272 5.004 -1.063 5.349 1.00 5.54 C
ANISOU 2280 CE1 HIS A 272 598 766 740 4 32 -12 C
ATOM 2281 NE2 HIS A 272 4.365 0.108 5.355 1.00 6.06 N
ANISOU 2281 NE2 HIS A 272 508 897 899 140 161 -126 N
ATOM 2282 N TYR A 273 8.394 2.912 4.227 1.00 4.42 N
ANISOU 2282 N TYR A 273 609 484 585 26 238 -73 N
ATOM 2283 CA TYR A 273 7.904 3.654 3.051 1.00 4.27 C
ANISOU 2283 CA TYR A 273 474 475 673 91 29 -119 C
ATOM 2284 C TYR A 273 9.037 3.794 2.040 1.00 4.34 C
ANISOU 2284 C TYR A 273 526 565 560 129 35 -26 C
ATOM 2285 O TYR A 273 9.590 4.879 1.835 1.00 5.44 O
ANISOU 2285 O TYR A 273 718 670 677 39 169 37 O
ATOM 2286 CB TYR A 273 7.320 5.009 3.516 1.00 5.22 C
ANISOU 2286 CB TYR A 273 714 354 916 73 222 -130 C
ATOM 2287 CG TYR A 273 6.195 4.773 4.480 1.00 5.63 C
ANISOU 2287 CG TYR A 273 711 638 789 128 221 -23 C
ATOM 2288 CD1 TYR A 273 4.903 4.496 4.085 1.00 5.57 C
ANISOU 2288 CD1 TYR A 273 777 817 524 43 160 -176 C
ATOM 2289 CD2 TYR A 273 6.431 4.807 5.840 1.00 5.23 C
ANISOU 2289 CD2 TYR A 273 339 778 872 99 97 -87 C
ATOM 2290 CE1 TYR A 273 3.886 4.288 5.002 1.00 6.03 C
ANISOU 2290 CE1 TYR A 273 757 849 684 124 238 -96 C
ATOM 2291 CE2 TYR A 273 5.444 4.563 6.764 1.00 4.71 C
ANISOU 2291 CE2 TYR A 273 489 570 732 373 268 -225 C
ATOM 2292 CZ TYR A 273 4.176 4.299 6.335 1.00 4.97 C
ANISOU 2292 CZ TYR A 273 560 672 655 54 264 -198 C
ATOM 2293 OH TYR A 273 3.212 4.042 7.288 1.00 6.17 O
ANISOU 2293 OH TYR A 273 633 1017 695 99 261 -2 O
ATOM 2294 N LEU A 274 9.453 2.666 1.457 1.00 5.19 N
ANISOU 2294 N LEU A 274 582 694 697 20 192 -163 N
ATOM 2295 CA LEU A 274 10.638 2.663 0.581 1.00 4.78 C
ANISOU 2295 CA LEU A 274 563 721 532 83 70 -136 C
ATOM 2296 C LEU A 274 10.531 3.640 -0.570 1.00 4.49 C
ANISOU 2296 C LEU A 274 528 589 590 44 202 -200 C
ATOM 2297 O LEU A 274 11.556 4.147 -1.032 1.00 5.17 O
ANISOU 2297 O LEU A 274 470 754 742 -5 212 -94 O
ATOM 2298 CB LEU A 274 10.858 1.264 0.054 1.00 5.16 C
ANISOU 2298 CB LEU A 274 538 672 750 95 141 -82 C
ATOM 2299 CG LEU A 274 10.949 0.116 1.083 1.00 5.01 C
ANISOU 2299 CG LEU A 274 516 714 674 235 241 -90 C
ATOM 2300 CD1 LEU A 274 11.356 -1.154 0.347 1.00 5.50 C
ANISOU 2300 CD1 LEU A 274 605 519 966 -88 429 -119 C
ATOM 2301 CD2 LEU A 274 11.906 0.453 2.227 1.00 6.45 C
ANISOU 2301 CD2 LEU A 274 913 806 731 125 54 -3 C
ATOM 2302 N GLN A 275 9.300 3.890 -1.003 1.00 4.57 N
ANISOU 2302 N GLN A 275 473 582 680 110 202 -94 N
ATOM 2303 CA GLN A 275 9.087 4.830 -2.077 1.00 4.67 C
ANISOU 2303 CA GLN A 275 578 578 620 105 249 -143 C
ATOM 2304 C GLN A 275 9.557 6.249 -1.763 1.00 3.98 C
ANISOU 2304 C GLN A 275 362 521 630 325 -37 -15 C
ATOM 2305 O GLN A 275 9.763 7.013 -2.711 1.00 5.03 O
ANISOU 2305 O GLN A 275 718 603 591 117 56 37 O
ATOM 2306 CB GLN A 275 7.580 4.899 -2.395 1.00 5.23 C
ANISOU 2306 CB GLN A 275 594 575 818 43 117 58 C
ATOM 2307 CG GLN A 275 6.901 3.572 -2.652 1.00 5.68 C
ANISOU 2307 CG GLN A 275 673 682 805 -22 162 -39 C
ATOM 2308 CD GLN A 275 6.343 2.915 -1.417 1.00 5.28 C
ANISOU 2308 CD GLN A 275 626 571 809 -42 253 -158 C
ATOM 2309 OE1 GLN A 275 6.776 3.108 -0.294 1.00 5.92 O
ANISOU 2309 OE1 GLN A 275 568 905 778 -43 93 -12 O
ATOM 2310 NE2 GLN A 275 5.279 2.150 -1.640 1.00 8.38 N
ANISOU 2310 NE2 GLN A 275 1141 1239 804 -640 314 -287 N
ATOM 2311 N GLU A 276 9.672 6.569 -0.500 1.00 4.44 N
ANISOU 2311 N GLU A 276 581 493 614 4 106 -43 N
ATOM 2312 CA GLU A 276 10.119 7.925 -0.123 1.00 4.61 C
ANISOU 2312 CA GLU A 276 474 623 653 5 94 -91 C
ATOM 2313 C GLU A 276 11.627 7.976 -0.018 1.00 5.73 C
ANISOU 2313 C GLU A 276 484 663 1029 84 37 -251 C
ATOM 2314 O GLU A 276 12.185 9.087 -0.048 1.00 8.99 O
ANISOU 2314 O GLU A 276 594 658 2164 -87 140 -248 O
ATOM 2315 CB GLU A 276 9.438 8.383 1.140 1.00 4.95 C
ANISOU 2315 CB GLU A 276 658 573 651 147 116 -178 C
ATOM 2316 CG GLU A 276 7.954 8.644 1.032 1.00 4.72 C
ANISOU 2316 CG GLU A 276 543 752 499 -100 126 -107 C
ATOM 2317 CD GLU A 276 7.561 9.766 0.104 1.00 5.36 C
ANISOU 2317 CD GLU A 276 581 605 849 87 248 -77 C
ATOM 2318 OE1 GLU A 276 8.426 10.369 -0.560 1.00 5.69 O
ANISOU 2318 OE1 GLU A 276 701 677 783 5 230 22 O
ATOM 2319 OE2 GLU A 276 6.340 10.052 0.017 1.00 6.91 O
ANISOU 2319 OE2 GLU A 276 611 1137 876 119 180 58 O
ATOM 2320 N ASP A 277 12.311 6.846 0.107 1.00 4.75 N
ANISOU 2320 N ASP A 277 451 653 701 30 185 12 N
ATOM 2321 CA ASP A 277 13.761 6.841 0.169 1.00 5.01 C
ANISOU 2321 CA ASP A 277 446 582 876 105 305 -111 C
ATOM 2322 C ASP A 277 14.390 6.655 -1.215 1.00 5.16 C
ANISOU 2322 C ASP A 277 458 741 761 23 210 -142 C
ATOM 2323 O ASP A 277 15.393 7.305 -1.491 1.00 6.48 O
ANISOU 2323 O ASP A 277 590 1017 854 -153 310 -244 O
ATOM 2324 CB ASP A 277 14.217 5.771 1.150 1.00 5.71 C
ANISOU 2324 CB ASP A 277 510 882 777 59 171 -38 C
ATOM 2325 CG ASP A 277 14.163 6.275 2.571 1.00 6.61 C
ANISOU 2325 CG ASP A 277 559 1117 833 -64 236 -204 C
ATOM 2326 OD1 ASP A 277 14.766 7.355 2.825 1.00 6.95 O
ANISOU 2326 OD1 ASP A 277 849 919 872 -50 188 -107 O
ATOM 2327 OD2 ASP A 277 13.536 5.594 3.411 1.00 6.29 O
ANISOU 2327 OD2 ASP A 277 716 962 713 -36 119 -171 O
ATOM 2328 N ASN A 278 13.851 5.825 -2.088 1.00 5.34 N
ANISOU 2328 N ASN A 278 501 688 840 -23 218 -132 N
ATOM 2329 CA ASN A 278 14.453 5.625 -3.380 1.00 5.54 C
ANISOU 2329 CA ASN A 278 486 781 838 69 101 -254 C
ATOM 2330 C ASN A 278 13.418 5.393 -4.478 1.00 5.09 C
ANISOU 2330 C ASN A 278 393 710 829 2 173 -123 C
ATOM 2331 O ASN A 278 13.336 4.350 -5.101 1.00 5.12 O
ANISOU 2331 O ASN A 278 599 604 743 2 4 -101 O
ATOM 2332 CB ASN A 278 15.433 4.440 -3.342 1.00 5.55 C
ANISOU 2332 CB ASN A 278 454 838 817 70 121 -12 C
ATOM 2333 CG ASN A 278 16.403 4.450 -4.508 1.00 6.05 C
ANISOU 2333 CG ASN A 278 623 935 741 149 105 -275 C
ATOM 2334 OD1 ASN A 278 16.243 5.175 -5.490 1.00 6.76 O
ANISOU 2334 OD1 ASN A 278 766 1011 792 48 155 -84 O
ATOM 2335 ND2 ASN A 278 17.410 3.632 -4.370 1.00 6.12 N
ANISOU 2335 ND2 ASN A 278 638 875 812 79 345 -15 N
ATOM 2336 N PRO A 279 12.598 6.426 -4.758 1.00 5.33 N
ANISOU 2336 N PRO A 279 493 665 867 57 148 -139 N
ATOM 2337 CA PRO A 279 11.575 6.259 -5.791 1.00 5.22 C
ANISOU 2337 CA PRO A 279 451 654 880 23 176 -48 C
ATOM 2338 C PRO A 279 12.148 6.047 -7.181 1.00 5.85 C
ANISOU 2338 C PRO A 279 719 683 819 76 147 -8 C
ATOM 2339 O PRO A 279 11.562 5.350 -7.997 1.00 6.14 O
ANISOU 2339 O PRO A 279 853 621 861 54 160 -80 O
ATOM 2340 CB PRO A 279 10.829 7.583 -5.735 1.00 6.00 C
ANISOU 2340 CB PRO A 279 746 696 836 104 142 -18 C
ATOM 2341 CG PRO A 279 11.789 8.570 -5.146 1.00 6.06 C
ANISOU 2341 CG PRO A 279 755 629 920 9 174 54 C
ATOM 2342 CD PRO A 279 12.585 7.742 -4.160 1.00 5.47 C
ANISOU 2342 CD PRO A 279 831 622 623 -35 228 8 C
ATOM 2343 N ASP A 280 13.326 6.652 -7.501 1.00 5.78 N
ANISOU 2343 N ASP A 280 869 686 643 -17 241 24 N
ATOM 2344 CA ASP A 280 13.801 6.523 -8.873 1.00 6.20 C
ANISOU 2344 CA ASP A 280 964 728 664 27 197 3 C
ATOM 2345 C ASP A 280 14.237 5.102 -9.188 1.00 6.13 C
ANISOU 2345 C ASP A 280 748 770 810 64 226 -34 C
ATOM 2346 O ASP A 280 13.987 4.641 -10.287 1.00 6.58 O
ANISOU 2346 O ASP A 280 987 808 704 0 184 -19 O
ATOM 2347 CB ASP A 280 14.911 7.547 -9.165 1.00 9.32 C
ANISOU 2347 CB ASP A 280 1600 916 1024 -328 792 -225 C
ATOM 2348 CG ASP A 280 14.311 8.936 -9.390 1.00 15.35 C
ANISOU 2348 CG ASP A 280 3158 942 1734 -417 -557 563 C
ATOM 2349 OD1 ASP A 280 13.157 9.114 -9.876 1.00 14.97 O
ANISOU 2349 OD1 ASP A 280 3054 1078 1554 -87 -324 174 O
ATOM 2350 OD2 ASP A 280 15.090 9.882 -9.083 1.00 18.59 O
ANISOU 2350 OD2 ASP A 280 2929 966 3170 -293 -163 -66 O
ATOM 2351 N LEU A 281 14.891 4.387 -8.237 1.00 5.58 N
ANISOU 2351 N LEU A 281 688 746 687 44 207 -145 N
ATOM 2352 CA LEU A 281 15.284 3.029 -8.542 1.00 5.45 C
ANISOU 2352 CA LEU A 281 582 754 735 81 255 -130 C
ATOM 2353 C LEU A 281 14.021 2.128 -8.599 1.00 4.85 C
ANISOU 2353 C LEU A 281 559 690 593 108 134 -23 C
ATOM 2354 O LEU A 281 13.924 1.245 -9.432 1.00 5.44 O
ANISOU 2354 O LEU A 281 647 782 637 93 132 -99 O
ATOM 2355 CB LEU A 281 16.224 2.495 -7.498 1.00 6.66 C
ANISOU 2355 CB LEU A 281 698 854 978 -41 2 -82 C
ATOM 2356 CG LEU A 281 16.743 1.094 -7.779 1.00 6.63 C
ANISOU 2356 CG LEU A 281 446 884 1190 15 40 -73 C
ATOM 2357 CD1 LEU A 281 17.590 0.982 -9.052 1.00 9.10 C
ANISOU 2357 CD1 LEU A 281 751 1509 1197 51 107 -347 C
ATOM 2358 CD2 LEU A 281 17.584 0.633 -6.607 1.00 9.15 C
ANISOU 2358 CD2 LEU A 281 973 1206 1297 89 -87 207 C
ATOM 2359 N ILE A 282 13.060 2.361 -7.698 1.00 5.14 N
ANISOU 2359 N ILE A 282 590 771 592 8 178 -86 N
ATOM 2360 CA ILE A 282 11.829 1.567 -7.759 1.00 4.45 C
ANISOU 2360 CA ILE A 282 619 503 569 116 175 -153 C
ATOM 2361 C ILE A 282 11.156 1.766 -9.088 1.00 5.04 C
ANISOU 2361 C ILE A 282 711 570 634 10 113 -82 C
ATOM 2362 O ILE A 282 10.763 0.814 -9.759 1.00 4.94 O
ANISOU 2362 O ILE A 282 785 478 614 75 74 -32 O
ATOM 2363 CB ILE A 282 10.936 1.880 -6.544 1.00 4.95 C
ANISOU 2363 CB ILE A 282 587 684 611 91 230 -105 C
ATOM 2364 CG1 ILE A 282 11.617 1.409 -5.259 1.00 5.09 C
ANISOU 2364 CG1 ILE A 282 764 591 580 54 215 -183 C
ATOM 2365 CG2 ILE A 282 9.586 1.231 -6.707 1.00 5.00 C
ANISOU 2365 CG2 ILE A 282 705 543 652 44 172 -20 C
ATOM 2366 CD1 ILE A 282 11.000 2.043 -3.986 1.00 6.28 C
ANISOU 2366 CD1 ILE A 282 676 1130 579 162 302 -221 C
ATOM 2367 N GLY A 283 10.926 3.027 -9.505 1.00 4.91 N
ANISOU 2367 N GLY A 283 689 546 632 -54 160 -32 N
ATOM 2368 CA GLY A 283 10.270 3.267 -10.758 1.00 4.89 C
ANISOU 2368 CA GLY A 283 595 630 631 -32 130 -109 C
ATOM 2369 C GLY A 283 11.023 2.747 -11.957 1.00 4.92 C
ANISOU 2369 C GLY A 283 689 604 577 148 78 -1 C
ATOM 2370 O GLY A 283 10.448 2.147 -12.863 1.00 4.81 O
ANISOU 2370 O GLY A 283 669 505 655 148 178 -141 O
ATOM 2371 N SER A 284 12.337 3.009 -11.999 1.00 5.28 N
ANISOU 2371 N SER A 284 787 721 498 -75 219 -133 N
ATOM 2372 CA SER A 284 13.102 2.559 -13.173 1.00 5.88 C
ANISOU 2372 CA SER A 284 1010 657 565 53 372 30 C
ATOM 2373 C SER A 284 13.154 1.041 -13.269 1.00 5.42 C
ANISOU 2373 C SER A 284 791 681 588 179 95 -49 C
ATOM 2374 O SER A 284 13.072 0.498 -14.365 1.00 5.93 O
ANISOU 2374 O SER A 284 837 793 622 22 122 42 O
ATOM 2375 CB SER A 284 14.467 3.197 -13.170 1.00 7.41 C
ANISOU 2375 CB SER A 284 912 1076 828 -49 369 -298 C
ATOM 2376 OG SER A 284 15.248 2.713 -12.113 1.00 10.24 O
ANISOU 2376 OG SER A 284 1315 1349 1226 -271 36 154 O
ATOM 2377 N GLU A 285 13.255 0.335 -12.140 1.00 4.83 N
ANISOU 2377 N GLU A 285 665 526 643 46 249 -78 N
ATOM 2378 CA GLU A 285 13.292 -1.124 -12.182 1.00 5.24 C
ANISOU 2378 CA GLU A 285 764 598 628 -98 239 -80 C
ATOM 2379 C GLU A 285 11.926 -1.694 -12.531 1.00 4.64 C
ANISOU 2379 C GLU A 285 669 393 702 62 235 -13 C
ATOM 2380 O GLU A 285 11.827 -2.666 -13.280 1.00 5.37 O
ANISOU 2380 O GLU A 285 586 561 892 121 194 -183 O
ATOM 2381 CB GLU A 285 13.785 -1.660 -10.841 1.00 5.80 C
ANISOU 2381 CB GLU A 285 697 694 812 80 189 83 C
ATOM 2382 CG AGLU A 285 15.271 -1.468 -10.575 0.50 8.53 C
ANISOU 2382 CG AGLU A 285 742 1638 862 1 104 -470 C
ATOM 2383 CG BGLU A 285 15.293 -1.455 -10.672 0.50 6.13 C
ANISOU 2383 CG BGLU A 285 679 847 804 3 250 109 C
ATOM 2384 CD AGLU A 285 16.080 -2.611 -11.157 0.50 10.29 C
ANISOU 2384 CD AGLU A 285 728 1953 1231 276 347 -294 C
ATOM 2385 CD BGLU A 285 16.152 -2.171 -11.692 0.50 9.46 C
ANISOU 2385 CD BGLU A 285 779 1402 1411 173 338 -258 C
ATOM 2386 OE1AGLU A 285 17.253 -2.787 -10.798 0.50 14.69 O
ANISOU 2386 OE1AGLU A 285 1076 2451 2056 577 -266 -317 O
ATOM 2387 OE1BGLU A 285 16.948 -1.493 -12.389 0.50 12.01 O
ANISOU 2387 OE1BGLU A 285 1248 1770 1544 274 922 -263 O
ATOM 2388 OE2AGLU A 285 15.546 -3.353 -12.004 0.50 20.08 O
ANISOU 2388 OE2AGLU A 285 1201 2733 3695 1735 -930 -2107 O
ATOM 2389 OE2BGLU A 285 16.067 -3.412 -11.823 0.50 9.33 O
ANISOU 2389 OE2BGLU A 285 392 1427 1725 410 -5 -436 O
ATOM 2390 N ILE A 286 10.829 -1.109 -12.038 1.00 4.88 N
ANISOU 2390 N ILE A 286 708 482 663 232 144 -60 N
ATOM 2391 CA ILE A 286 9.519 -1.553 -12.521 1.00 4.45 C
ANISOU 2391 CA ILE A 286 723 246 721 223 94 -144 C
ATOM 2392 C ILE A 286 9.402 -1.359 -14.028 1.00 4.47 C
ANISOU 2392 C ILE A 286 544 385 768 199 88 -15 C
ATOM 2393 O ILE A 286 9.009 -2.258 -14.770 1.00 5.17 O
ANISOU 2393 O ILE A 286 655 472 838 36 136 -190 O
ATOM 2394 CB ILE A 286 8.373 -0.838 -11.797 1.00 4.97 C
ANISOU 2394 CB ILE A 286 681 463 742 271 67 -135 C
ATOM 2395 CG1 ILE A 286 8.333 -1.224 -10.322 1.00 4.88 C
ANISOU 2395 CG1 ILE A 286 341 680 834 -43 150 -50 C
ATOM 2396 CG2 ILE A 286 7.045 -1.143 -12.466 1.00 5.41 C
ANISOU 2396 CG2 ILE A 286 660 604 794 196 178 -65 C
ATOM 2397 CD1 ILE A 286 7.446 -0.371 -9.476 1.00 6.37 C
ANISOU 2397 CD1 ILE A 286 628 957 836 -74 116 -404 C
ATOM 2398 N ALA A 287 9.763 -0.186 -14.531 1.00 4.98 N
ANISOU 2398 N ALA A 287 754 387 750 99 50 -18 N
ATOM 2399 CA ALA A 287 9.647 0.069 -15.970 1.00 5.39 C
ANISOU 2399 CA ALA A 287 796 541 712 172 -62 25 C
ATOM 2400 C ALA A 287 10.449 -0.931 -16.791 1.00 5.33 C
ANISOU 2400 C ALA A 287 837 428 760 -1 34 23 C
ATOM 2401 O ALA A 287 9.962 -1.429 -17.815 1.00 6.63 O
ANISOU 2401 O ALA A 287 1083 743 694 216 -139 -51 O
ATOM 2402 CB ALA A 287 10.071 1.505 -16.267 1.00 6.46 C
ANISOU 2402 CB ALA A 287 1222 531 701 290 171 29 C
ATOM 2403 N ARG A 288 11.660 -1.238 -16.351 1.00 4.73 N
ANISOU 2403 N ARG A 288 671 594 533 47 241 -67 N
ATOM 2404 CA ARG A 288 12.497 -2.128 -17.094 1.00 5.77 C
ANISOU 2404 CA ARG A 288 931 533 729 33 377 -147 C
ATOM 2405 C ARG A 288 11.944 -3.550 -17.097 1.00 5.22 C
ANISOU 2405 C ARG A 288 640 601 743 -35 227 -80 C
ATOM 2406 O ARG A 288 12.159 -4.304 -18.057 1.00 6.08 O
ANISOU 2406 O ARG A 288 778 607 926 -18 322 -178 O
ATOM 2407 CB ARG A 288 13.902 -2.133 -16.486 1.00 10.45 C
ANISOU 2407 CB ARG A 288 515 802 2652 -108 509 -758 C
ATOM 2408 CG AARG A 288 14.890 -2.836 -17.427 0.60 16.29 C
ANISOU 2408 CG AARG A 288 1179 890 4119 31 1100 -1340 C
ATOM 2409 CG BARG A 288 14.793 -1.105 -17.182 0.40 21.65 C
ANISOU 2409 CG BARG A 288 2043 2596 3586 -1639 574 -310 C
ATOM 2410 CD AARG A 288 16.285 -2.365 -17.069 0.60 30.02 C
ANISOU 2410 CD AARG A 288 682 4461 6264 939 703 -3752 C
ATOM 2411 CD BARG A 288 15.926 -0.589 -16.334 0.40 31.39 C
ANISOU 2411 CD BARG A 288 3578 4355 3995 -3376 819 -1570 C
ATOM 2412 NE AARG A 288 16.540 -2.818 -15.687 0.60 38.36 N
ANISOU 2412 NE AARG A 288 1988 6180 6407 1412 -468 -3935 N
ATOM 2413 NE BARG A 288 16.028 0.882 -16.380 0.40 34.58 N
ANISOU 2413 NE BARG A 288 4754 4175 4211 -2719 1528 -2598 N
ATOM 2414 CZ AARG A 288 17.780 -2.993 -15.254 0.60 44.38 C
ANISOU 2414 CZ AARG A 288 1836 8548 6479 782 -726 -4891 C
ATOM 2415 CZ BARG A 288 17.098 1.479 -15.883 0.40 26.99 C
ANISOU 2415 CZ BARG A 288 3106 2868 4280 -2074 2758 -2265 C
ATOM 2416 NH1AARG A 288 18.755 -2.744 -16.115 0.60 46.14 N
ANISOU 2416 NH1AARG A 288 2024 7305 8203 -1032 -689 -3966 N
ATOM 2417 NH1BARG A 288 18.034 0.687 -15.368 0.40 41.21 N
ANISOU 2417 NH1BARG A 288 5100 4355 6205 -54 1072 -4004 N
ATOM 2418 NH2AARG A 288 18.000 -3.398 -14.025 0.60 47.30 N
ANISOU 2418 NH2AARG A 288 1891 10777 5306 3505 -453 -6685 N
ATOM 2419 NH2BARG A 288 17.274 2.791 -15.883 0.40 33.87 N
ANISOU 2419 NH2BARG A 288 6021 3100 3749 -3038 3027 -1626 N
ATOM 2420 N TRP A 289 11.245 -3.950 -16.059 1.00 5.65 N
ANISOU 2420 N TRP A 289 875 459 814 31 298 -82 N
ATOM 2421 CA TRP A 289 10.692 -5.298 -15.863 1.00 5.17 C
ANISOU 2421 CA TRP A 289 574 502 887 54 325 -50 C
ATOM 2422 C TRP A 289 9.392 -5.538 -16.615 1.00 4.84 C
ANISOU 2422 C TRP A 289 687 535 618 107 313 -180 C
ATOM 2423 O TRP A 289 9.024 -6.682 -16.900 1.00 6.51 O
ANISOU 2423 O TRP A 289 899 565 1011 -28 13 13 O
ATOM 2424 CB TRP A 289 10.515 -5.501 -14.377 1.00 5.94 C
ANISOU 2424 CB TRP A 289 701 683 873 -86 52 69 C
ATOM 2425 CG TRP A 289 9.749 -6.631 -13.757 1.00 5.03 C
ANISOU 2425 CG TRP A 289 653 479 777 116 184 -49 C
ATOM 2426 CD1 TRP A 289 10.113 -7.929 -13.566 1.00 5.78 C
ANISOU 2426 CD1 TRP A 289 885 505 806 6 249 -50 C
ATOM 2427 CD2 TRP A 289 8.421 -6.488 -13.199 1.00 5.08 C
ANISOU 2427 CD2 TRP A 289 634 689 609 -9 99 -95 C
ATOM 2428 NE1 TRP A 289 9.099 -8.605 -12.933 1.00 5.73 N
ANISOU 2428 NE1 TRP A 289 795 587 794 33 257 -31 N
ATOM 2429 CE2 TRP A 289 8.050 -7.748 -12.693 1.00 5.74 C
ANISOU 2429 CE2 TRP A 289 721 687 772 26 176 -51 C
ATOM 2430 CE3 TRP A 289 7.544 -5.421 -13.092 1.00 5.83 C
ANISOU 2430 CE3 TRP A 289 699 826 688 106 238 60 C
ATOM 2431 CZ2 TRP A 289 6.830 -7.960 -12.089 1.00 6.08 C
ANISOU 2431 CZ2 TRP A 289 798 785 727 -23 230 -67 C
ATOM 2432 CZ3 TRP A 289 6.316 -5.624 -12.478 1.00 6.07 C
ANISOU 2432 CZ3 TRP A 289 543 859 905 42 72 15 C
ATOM 2433 CH2 TRP A 289 5.991 -6.887 -11.988 1.00 5.82 C
ANISOU 2433 CH2 TRP A 289 718 835 657 -30 237 -92 C
ATOM 2434 N LEU A 290 8.639 -4.480 -16.942 1.00 4.78 N
ANISOU 2434 N LEU A 290 612 572 632 27 260 -97 N
ATOM 2435 CA LEU A 290 7.346 -4.719 -17.541 1.00 4.46 C
ANISOU 2435 CA LEU A 290 530 510 657 41 362 -90 C
ATOM 2436 C LEU A 290 7.356 -5.400 -18.899 1.00 5.42 C
ANISOU 2436 C LEU A 290 538 850 671 34 231 -180 C
ATOM 2437 O LEU A 290 6.445 -6.235 -19.138 1.00 5.62 O
ANISOU 2437 O LEU A 290 553 810 772 46 182 -195 O
ATOM 2438 CB LEU A 290 6.585 -3.390 -17.627 1.00 5.28 C
ANISOU 2438 CB LEU A 290 591 700 717 101 299 -86 C
ATOM 2439 CG LEU A 290 6.175 -2.784 -16.300 1.00 5.05 C
ANISOU 2439 CG LEU A 290 619 606 693 256 154 -183 C
ATOM 2440 CD1 LEU A 290 5.732 -1.355 -16.506 1.00 6.30 C
ANISOU 2440 CD1 LEU A 290 978 507 908 70 155 -147 C
ATOM 2441 CD2 LEU A 290 5.090 -3.587 -15.610 1.00 7.08 C
ANISOU 2441 CD2 LEU A 290 1402 522 765 281 677 -146 C
ATOM 2442 N PRO A 291 8.227 -5.086 -19.839 1.00 5.54 N
ANISOU 2442 N PRO A 291 772 566 766 22 363 -168 N
ATOM 2443 CA PRO A 291 8.003 -5.629 -21.189 1.00 5.42 C
ANISOU 2443 CA PRO A 291 776 614 669 120 268 -101 C
ATOM 2444 C PRO A 291 7.964 -7.147 -21.294 1.00 5.35 C
ANISOU 2444 C PRO A 291 649 608 775 34 236 -119 C
ATOM 2445 O PRO A 291 7.148 -7.673 -22.038 1.00 6.05 O
ANISOU 2445 O PRO A 291 789 753 757 22 155 -91 O
ATOM 2446 CB PRO A 291 9.162 -5.039 -21.996 1.00 6.79 C
ANISOU 2446 CB PRO A 291 1074 765 740 -54 331 62 C
ATOM 2447 CG PRO A 291 9.428 -3.739 -21.302 1.00 6.62 C
ANISOU 2447 CG PRO A 291 862 891 764 -88 373 -104 C
ATOM 2448 CD PRO A 291 9.313 -4.109 -19.820 1.00 6.28 C
ANISOU 2448 CD PRO A 291 1090 402 894 -139 313 -2 C
ATOM 2449 N ALA A 292 8.811 -7.858 -20.568 1.00 5.28 N
ANISOU 2449 N ALA A 292 664 657 687 120 260 -180 N
ATOM 2450 CA ALA A 292 8.866 -9.317 -20.688 1.00 5.99 C
ANISOU 2450 CA ALA A 292 905 642 729 133 248 -87 C
ATOM 2451 C ALA A 292 7.643 -9.952 -20.044 1.00 5.88 C
ANISOU 2451 C ALA A 292 773 574 886 191 250 -164 C
ATOM 2452 O ALA A 292 7.445 -11.156 -20.238 1.00 6.73 O
ANISOU 2452 O ALA A 292 909 627 1019 199 469 -190 O
ATOM 2453 CB ALA A 292 10.156 -9.881 -20.111 1.00 7.46 C
ANISOU 2453 CB ALA A 292 837 649 1347 150 168 -140 C
ATOM 2454 N LEU A 293 6.791 -9.221 -19.329 1.00 4.97 N
ANISOU 2454 N LEU A 293 690 417 782 117 223 -85 N
ATOM 2455 CA LEU A 293 5.547 -9.754 -18.803 1.00 6.34 C
ANISOU 2455 CA LEU A 293 725 691 994 87 298 -105 C
ATOM 2456 C LEU A 293 4.455 -9.823 -19.848 1.00 6.68 C
ANISOU 2456 C LEU A 293 726 841 972 50 302 -248 C
ATOM 2457 O LEU A 293 3.423 -10.465 -19.642 1.00 7.61 O
ANISOU 2457 O LEU A 293 768 1107 1017 -68 330 -194 O
ATOM 2458 CB LEU A 293 4.995 -8.853 -17.668 1.00 7.01 C
ANISOU 2458 CB LEU A 293 766 1130 767 199 319 -98 C
ATOM 2459 CG LEU A 293 5.959 -8.448 -16.546 1.00 7.11 C
ANISOU 2459 CG LEU A 293 948 778 975 231 153 -94 C
ATOM 2460 CD1 LEU A 293 5.245 -7.544 -15.535 1.00 7.32 C
ANISOU 2460 CD1 LEU A 293 948 1039 793 189 287 -45 C
ATOM 2461 CD2 LEU A 293 6.566 -9.654 -15.869 1.00 8.00 C
ANISOU 2461 CD2 LEU A 293 1138 955 946 199 321 281 C
ATOM 2462 N HIS A 294 4.626 -9.120 -20.953 1.00 6.48 N
ANISOU 2462 N HIS A 294 717 823 922 104 260 -268 N
ATOM 2463 CA HIS A 294 3.503 -8.994 -21.869 1.00 7.22 C
ANISOU 2463 CA HIS A 294 699 1067 979 147 265 -244 C
ATOM 2464 C HIS A 294 3.024 -10.291 -22.491 1.00 8.37 C
ANISOU 2464 C HIS A 294 810 1421 950 -51 177 -401 C
ATOM 2465 O HIS A 294 1.815 -10.553 -22.574 1.00 9.49 O
ANISOU 2465 O HIS A 294 831 1333 1442 -152 157 -142 O
ATOM 2466 CB HIS A 294 3.898 -8.036 -23.000 1.00 8.26 C
ANISOU 2466 CB HIS A 294 720 1255 1162 338 270 -31 C
ATOM 2467 CG HIS A 294 2.776 -7.898 -23.990 1.00 10.14 C
ANISOU 2467 CG HIS A 294 1016 1585 1251 156 97 97 C
ATOM 2468 ND1 HIS A 294 2.702 -8.450 -25.251 1.00 14.09 N
ANISOU 2468 ND1 HIS A 294 1508 2275 1569 -255 -174 -317 N
ATOM 2469 CD2 HIS A 294 1.606 -7.205 -23.791 1.00 10.42 C
ANISOU 2469 CD2 HIS A 294 751 1456 1753 42 -145 388 C
ATOM 2470 CE1 HIS A 294 1.537 -8.101 -25.808 1.00 15.56 C
ANISOU 2470 CE1 HIS A 294 1431 2867 1617 -663 -254 273 C
ATOM 2471 NE2 HIS A 294 0.889 -7.357 -24.941 1.00 17.49 N
ANISOU 2471 NE2 HIS A 294 1507 2892 2244 212 -723 185 N
ATOM 2472 N HIS A 295 3.968 -11.056 -23.006 1.00 8.29 N
ANISOU 2472 N HIS A 295 941 1100 1110 131 17 -313 N
ATOM 2473 CA HIS A 295 3.586 -12.202 -23.832 1.00 7.61 C
ANISOU 2473 CA HIS A 295 774 1043 1075 -48 177 -197 C
ATOM 2474 C HIS A 295 2.802 -13.205 -23.013 1.00 10.19 C
ANISOU 2474 C HIS A 295 1128 1518 1227 -300 360 -111 C
ATOM 2475 O HIS A 295 3.183 -13.496 -21.893 1.00 11.47 O
ANISOU 2475 O HIS A 295 1757 1313 1288 -263 331 8 O
ATOM 2476 CB HIS A 295 4.851 -12.834 -24.418 1.00 7.45 C
ANISOU 2476 CB HIS A 295 920 839 1070 46 260 41 C
ATOM 2477 CG HIS A 295 4.484 -13.916 -25.369 1.00 7.65 C
ANISOU 2477 CG HIS A 295 773 1113 1020 51 437 -50 C
ATOM 2478 ND1 HIS A 295 3.880 -13.637 -26.572 1.00 11.45 N
ANISOU 2478 ND1 HIS A 295 1446 2021 885 84 325 -97 N
ATOM 2479 CD2 HIS A 295 4.608 -15.263 -25.292 1.00 9.84 C
ANISOU 2479 CD2 HIS A 295 1439 1054 1247 -155 604 -318 C
ATOM 2480 CE1 HIS A 295 3.655 -14.788 -27.193 1.00 14.03 C
ANISOU 2480 CE1 HIS A 295 1259 2554 1517 59 140 -697 C
ATOM 2481 NE2 HIS A 295 4.081 -15.780 -26.452 1.00 12.95 N
ANISOU 2481 NE2 HIS A 295 1590 1830 1499 -663 556 -544 N
ATOM 2482 N HIS A 296 1.746 -13.750 -23.635 1.00 13.40 N
ANISOU 2482 N HIS A 296 1631 1760 1701 -820 304 -362 N
ATOM 2483 CA HIS A 296 1.000 -14.809 -22.963 1.00 22.60 C
ANISOU 2483 CA HIS A 296 2835 2481 3271 -1704 1581 -719 C
ATOM 2484 C HIS A 296 1.442 -16.201 -23.432 1.00 29.20 C
ANISOU 2484 C HIS A 296 5193 2062 3840 -2407 2346 -975 C
ATOM 2485 O HIS A 296 1.093 -16.447 -24.810 1.00 37.86 O
ANISOU 2485 O HIS A 296 3773 6011 4602 -1893 2111 -2986 O
ATOM 2486 CB HIS A 296 -0.505 -14.618 -23.181 1.00 35.20 C
ANISOU 2486 CB HIS A 296 2514 6170 4689 -2376 1780 -1543 C
ATOM 2487 CG HIS A 296 -1.313 -15.695 -22.529 1.00 52.56 C
ANISOU 2487 CG HIS A 296 4997 9110 5862 -5650 2858 -2429 C
ATOM 2488 ND1 HIS A 296 -1.573 -16.934 -23.107 1.00 53.26 N
ANISOU 2488 ND1 HIS A 296 6738 7718 5780 -4937 2616 -1260 N
ATOM 2489 CD2 HIS A 296 -1.935 -15.697 -21.323 1.00 59.03 C
ANISOU 2489 CD2 HIS A 296 6140 10211 6078 -6160 3378 -2366 C
ATOM 2490 CE1 HIS A 296 -2.318 -17.649 -22.278 1.00 57.33 C
ANISOU 2490 CE1 HIS A 296 6569 8807 6408 -5465 2814 -1198 C
ATOM 2491 NE2 HIS A 296 -2.542 -16.918 -21.194 1.00 60.72 N
ANISOU 2491 NE2 HIS A 296 5793 10307 6970 -6078 3571 -2004 N
TER 2492 HIS A 296
HETATM 2493 C1 IPA A1001 2.402 0.721 8.347 1.00 12.83 C
ANISOU 2493 C1 IPA A1001 2287 908 1679 255 155 -58 C
HETATM 2494 C2 IPA A1001 2.327 -0.578 9.070 1.00 10.19 C
ANISOU 2494 C2 IPA A1001 1546 964 1362 276 273 -113 C
HETATM 2495 C3 IPA A1001 3.747 -1.226 8.974 1.00 12.17 C
ANISOU 2495 C3 IPA A1001 1625 1106 1893 386 389 -202 C
HETATM 2496 O2 IPA A1001 1.335 -1.417 8.395 1.00 11.95 O
ANISOU 2496 O2 IPA A1001 1629 1298 1614 -56 471 -101 O
HETATM 2497 C ACT A1002 2.272 -5.671 -20.519 1.00 8.59 C
ANISOU 2497 C ACT A1002 756 1165 1343 186 171 -78 C
HETATM 2498 O ACT A1002 2.746 -4.745 -21.248 1.00 10.50 O
ANISOU 2498 O ACT A1002 1457 941 1589 86 182 14 O
HETATM 2499 OXT ACT A1002 1.475 -6.470 -21.025 1.00 10.58 O
ANISOU 2499 OXT ACT A1002 1037 1387 1596 -54 76 -95 O
HETATM 2500 CH3 ACT A1002 2.798 -5.859 -19.093 1.00 9.76 C
ANISOU 2500 CH3 ACT A1002 1358 1094 1257 458 102 -241 C
HETATM 2501 C ACT A1003 6.776 -22.150 -10.757 1.00 16.71 C
ANISOU 2501 C ACT A1003 2595 1357 2397 338 -331 559 C
HETATM 2502 O ACT A1003 6.829 -22.249 -12.340 1.00 20.09 O
ANISOU 2502 O ACT A1003 3632 1627 2373 134 -545 477 O
HETATM 2503 OXT ACT A1003 8.178 -22.374 -10.726 1.00 18.87 O
ANISOU 2503 OXT ACT A1003 2669 2291 2209 613 -50 -146 O
HETATM 2504 CH3 ACT A1003 5.683 -22.114 -9.906 1.00 20.98 C
ANISOU 2504 CH3 ACT A1003 2909 1554 3510 520 324 -1153 C
HETATM 2505 CL CL A1004 -1.178 -0.479 9.734 1.00 8.33 CL
ANISOU 2505 CL CL A1004 1115 938 1112 186 252 -109 CL
HETATM 2506 O HOH A2001 -2.261 10.576 3.769 1.00 5.20 O
HETATM 2507 O HOH A2002 12.252 -4.079 3.065 1.00 5.89 O
HETATM 2508 O HOH A2003 10.452 -5.181 1.153 1.00 5.83 O
HETATM 2509 O HOH A2004 -2.835 9.180 12.834 1.00 5.68 O
HETATM 2510 O HOH A2005 8.818 9.560 -3.270 1.00 5.15 O
HETATM 2511 O HOH A2006 -1.540 16.473 12.562 1.00 8.38 O
HETATM 2512 O HOH A2007 1.667 2.855 2.159 1.00 6.30 O
HETATM 2513 O HOH A2008 -3.616 15.340 9.371 1.00 7.13 O
HETATM 2514 O HOH A2009 11.179 5.326 -17.863 1.00 8.73 O
HETATM 2515 O HOH A2010 6.863 8.407 -5.032 1.00 6.06 O
HETATM 2516 O HOH A2011 -10.450 0.791 -0.376 1.00 7.04 O
HETATM 2517 O HOH A2012 10.216 -11.207 -12.102 1.00 7.44 O
HETATM 2518 O HOH A2013 -4.522 9.259 2.754 1.00 5.71 O
HETATM 2519 O HOH A2014 12.959 -3.269 -20.552 1.00 8.44 O
HETATM 2520 O HOH A2015 -2.451 4.096 -4.949 1.00 7.95 O
HETATM 2521 O HOH A2016 -2.546 19.410 4.858 1.00 8.95 O
HETATM 2522 O HOH A2017 8.236 -0.684 -19.773 1.00 7.92 O
HETATM 2523 O HOH A2018 12.992 4.825 -15.846 1.00 10.74 O
HETATM 2524 O HOH A2019 6.675 -10.212 -23.232 1.00 7.30 O
HETATM 2525 O HOH A2020 -3.192 17.793 10.791 1.00 9.27 O
HETATM 2526 O HOH A2021 8.105 3.322 -19.091 1.00 7.66 O
HETATM 2527 O HOH A2022 8.008 10.669 -17.288 1.00 8.45 O
HETATM 2528 O HOH A2023 -8.844 1.048 7.294 1.00 5.91 O
HETATM 2529 O HOH A2024 -22.860 3.817 -6.242 1.00 10.08 O
HETATM 2530 O HOH A2025 4.387 -8.505 7.030 1.00 10.26 O
HETATM 2531 O HOH A2026 -1.404 20.488 7.067 1.00 9.66 O
HETATM 2532 O HOH A2027 -13.061 0.899 13.162 1.00 9.56 O
HETATM 2533 O HOH A2028 -0.318 -13.915 13.173 1.00 7.84 O
HETATM 2534 O HOH A2029 17.582 4.200 -0.360 1.00 6.79 O
HETATM 2535 O HOH A2030 -4.272 11.335 -13.284 1.00 7.01 O
HETATM 2536 O HOH A2031 11.761 3.743 3.983 1.00 7.37 O
HETATM 2537 O HOH A2032 6.150 -2.702 -23.197 1.00 13.57 O
HETATM 2538 O HOH A2033 10.088 -13.451 -13.850 1.00 10.34 O
HETATM 2539 O HOH A2034 -3.256 0.489 -21.294 1.00 8.11 O
HETATM 2540 O HOH A2035 -2.319 -6.567 19.878 1.00 10.79 O
HETATM 2541 O HOH A2036 3.469 4.670 -24.940 1.00 11.61 O
HETATM 2542 O HOH A2037 -13.939 8.145 13.621 0.70 4.76 O
HETATM 2543 O HOH A2038 1.112 -0.312 -22.559 1.00 9.11 O
HETATM 2544 O HOH A2039 -10.158 15.304 7.426 1.00 9.81 O
HETATM 2545 O HOH A2040 -12.505 -6.673 -9.110 1.00 9.15 O
HETATM 2546 O HOH A2041 -9.455 6.411 23.868 1.00 11.69 O
HETATM 2547 O HOH A2042 -13.706 -8.687 11.332 1.00 13.25 O
HETATM 2548 O HOH A2043 -9.347 -5.288 13.738 1.00 8.74 O
HETATM 2549 O HOH A2044 2.125 1.647 4.498 1.00 6.84 O
HETATM 2550 O HOH A2045 10.186 -7.891 10.389 1.00 9.92 O
HETATM 2551 O HOH A2046 -12.969 15.854 14.413 1.00 9.02 O
HETATM 2552 O HOH A2047 -8.538 -7.752 -2.310 1.00 7.26 O
HETATM 2553 O HOH A2048 -17.309 -5.230 -4.143 1.00 9.88 O
HETATM 2554 O HOH A2049 3.386 -13.272 20.320 1.00 9.31 O
HETATM 2555 O HOH A2050 -2.894 13.521 -14.966 1.00 13.47 O
HETATM 2556 O HOH A2051 0.622 -17.089 15.057 1.00 12.14 O
HETATM 2557 O HOH A2052 0.830 -3.154 -22.330 1.00 11.33 O
HETATM 2558 O HOH A2053 -11.049 -8.413 11.706 1.00 10.37 O
HETATM 2559 O HOH A2054 -5.347 14.323 -8.298 1.00 10.28 O
HETATM 2560 O HOH A2055 -15.515 6.160 10.109 1.00 9.64 O
HETATM 2561 O HOH A2056 2.101 22.740 2.141 1.00 10.99 O
HETATM 2562 O HOH A2057 -0.831 -11.376 22.014 1.00 11.98 O
HETATM 2563 O HOH A2058 0.372 -16.386 12.313 1.00 12.58 O
HETATM 2564 O HOH A2059 6.678 -9.084 8.548 1.00 10.49 O
HETATM 2565 O HOH A2060 -0.696 -0.148 -20.464 1.00 7.98 O
HETATM 2566 O HOH A2061 17.226 7.994 2.023 1.00 10.27 O
HETATM 2567 O HOH A2062 -23.773 6.550 0.309 1.00 9.94 O
HETATM 2568 O HOH A2063 -4.637 19.802 -15.747 1.00 13.67 O
HETATM 2569 O HOH A2064 -8.184 10.017 24.469 1.00 12.97 O
HETATM 2570 O HOH A2065 -21.508 6.825 5.792 1.00 11.32 O
HETATM 2571 O HOH A2066 -8.470 -2.321 19.627 1.00 15.88 O
HETATM 2572 O HOH A2067 -6.483 6.321 26.405 1.00 11.02 O
HETATM 2573 O HOH A2068 7.623 -8.224 11.101 1.00 11.65 O
HETATM 2574 O HOH A2069 -10.232 11.025 2.152 1.00 11.18 O
HETATM 2575 O HOH A2070 -8.473 -2.646 23.831 1.00 13.24 O
HETATM 2576 O HOH A2071 2.240 8.553 -20.742 1.00 10.96 O
HETATM 2577 O HOH A2072 -2.077 11.666 1.114 1.00 13.33 O
HETATM 2578 O HOH A2073 21.796 -5.168 4.346 1.00 14.20 O
HETATM 2579 O HOH A2074 -10.735 9.756 22.806 1.00 10.19 O
HETATM 2580 O HOH A2075 -20.362 0.304 2.357 1.00 12.88 O
HETATM 2581 O HOH A2076 5.469 13.372 -10.163 1.00 15.71 O
HETATM 2582 O AHOH A2077 -11.122 9.620 6.230 0.70 6.49 O
HETATM 2583 O BHOH A2077 -11.692 8.309 6.707 0.30 7.57 O
HETATM 2584 O HOH A2078 -10.128 -5.815 -3.454 1.00 8.72 O
HETATM 2585 O HOH A2079 -11.745 -7.463 7.802 1.00 9.49 O
HETATM 2586 O HOH A2080 -6.421 -14.580 0.486 1.00 8.44 O
HETATM 2587 O HOH A2081 4.850 -15.275 21.624 1.00 11.15 O
HETATM 2588 O HOH A2082 2.003 20.524 0.588 1.00 11.66 O
HETATM 2589 O HOH A2083 6.484 -11.891 8.837 1.00 12.03 O
HETATM 2590 O HOH A2084 8.867 21.368 -2.102 1.00 18.19 O
HETATM 2591 O HOH A2085 -8.982 17.915 3.977 1.00 13.25 O
HETATM 2592 O HOH A2086 11.742 -19.653 -9.861 1.00 9.84 O
HETATM 2593 O HOH A2087 6.605 14.759 -7.632 1.00 10.63 O
HETATM 2594 O HOH A2088 -7.023 -4.517 -18.249 1.00 12.56 O
HETATM 2595 O HOH A2089 11.613 15.590 -1.240 1.00 10.22 O
HETATM 2596 O HOH A2090 -9.188 15.918 -14.042 1.00 13.19 O
HETATM 2597 O HOH A2091 -4.318 8.162 -22.434 1.00 14.62 O
HETATM 2598 O HOH A2092 -9.531 -12.893 16.260 1.00 18.99 O
HETATM 2599 O HOH A2093 11.384 -20.441 -12.493 1.00 13.98 O
HETATM 2600 O HOH A2094 13.229 -2.801 11.480 1.00 13.24 O
HETATM 2601 O HOH A2095 8.020 -20.776 -14.291 1.00 14.49 O
HETATM 2602 O HOH A2096 -14.311 -7.908 8.743 1.00 11.94 O
HETATM 2603 O HOH A2097 18.517 -15.081 4.308 1.00 14.39 O
HETATM 2604 O HOH A2098 15.180 8.233 -5.857 1.00 11.40 O
HETATM 2605 O HOH A2099 9.750 -10.564 8.398 1.00 14.51 O
HETATM 2606 O HOH A2100 19.515 -5.814 -5.980 1.00 12.25 O
HETATM 2607 O HOH A2101 5.517 -13.209 -20.487 1.00 9.78 O
HETATM 2608 O HOH A2102 -4.840 13.285 -0.568 1.00 17.64 O
HETATM 2609 O HOH A2103 4.756 -0.275 -24.032 1.00 14.79 O
HETATM 2610 O HOH A2104 -21.727 2.829 -8.589 1.00 12.92 O
HETATM 2611 O HOH A2105 -11.569 -12.825 13.230 1.00 14.61 O
HETATM 2612 O HOH A2106 -10.441 -15.344 6.695 1.00 16.92 O
HETATM 2613 O HOH A2107 -3.607 17.011 -8.380 1.00 15.29 O
HETATM 2614 O HOH A2108 12.142 -8.060 12.227 1.00 13.83 O
HETATM 2615 O HOH A2109 -4.386 11.592 -2.646 1.00 13.08 O
HETATM 2616 O HOH A2110 16.785 9.434 -0.381 1.00 12.41 O
HETATM 2617 O HOH A2111 9.337 -1.583 21.414 1.00 13.53 O
HETATM 2618 O HOH A2112 11.809 -8.905 14.882 1.00 13.40 O
HETATM 2619 O HOH A2113 -13.242 5.293 21.754 1.00 12.57 O
HETATM 2620 O HOH A2114 -5.428 18.579 12.120 1.00 15.11 O
HETATM 2621 O HOH A2115 11.318 10.998 7.717 1.00 12.28 O
HETATM 2622 O HOH A2116 -1.856 15.336 -2.819 1.00 17.74 O
HETATM 2623 O HOH A2117 0.816 -19.387 4.146 1.00 17.45 O
HETATM 2624 O HOH A2118 -13.996 -8.782 -8.417 1.00 15.56 O
HETATM 2625 O HOH A2119 -1.773 -9.347 18.823 1.00 13.03 O
HETATM 2626 O HOH A2120 -12.416 3.424 23.757 1.00 14.89 O
HETATM 2627 O AHOH A2121 -6.350 -5.457 20.483 0.50 6.02 O
HETATM 2628 O BHOH A2121 -8.076 -4.268 21.437 0.50 9.73 O
HETATM 2629 O HOH A2122 -17.116 -5.719 -6.980 1.00 13.47 O
HETATM 2630 O HOH A2123 -18.035 -2.005 -9.931 1.00 12.49 O
HETATM 2631 O HOH A2124 5.493 20.771 -4.440 1.00 11.99 O
HETATM 2632 O HOH A2125 10.574 21.106 5.429 1.00 15.24 O
HETATM 2633 O HOH A2126 8.967 -23.075 -8.481 1.00 12.70 O
HETATM 2634 O HOH A2127 9.704 19.084 -5.583 1.00 17.45 O
HETATM 2635 O HOH A2128 13.788 1.977 -16.560 1.00 13.25 O
HETATM 2636 O HOH A2129 19.673 -2.239 1.654 1.00 14.30 O
HETATM 2637 O HOH A2130 -10.333 6.808 -16.090 1.00 11.97 O
HETATM 2638 O HOH A2131 6.448 -19.631 -15.952 1.00 21.62 O
HETATM 2639 O HOH A2132 -4.383 0.129 26.715 1.00 15.36 O
HETATM 2640 O HOH A2133 -1.999 -4.815 21.956 1.00 17.08 O
HETATM 2641 O HOH A2134 -5.789 -0.048 -19.966 1.00 12.84 O
HETATM 2642 O HOH A2135 -2.965 17.059 -4.851 1.00 16.38 O
HETATM 2643 O HOH A2136 4.973 -15.303 7.881 1.00 15.02 O
HETATM 2644 O HOH A2137 0.440 0.529 -25.077 1.00 17.93 O
HETATM 2645 O HOH A2138 13.431 -7.062 16.186 1.00 15.84 O
HETATM 2646 O HOH A2139 9.966 -11.367 11.185 1.00 15.47 O
HETATM 2647 O HOH A2140 1.025 10.908 19.669 1.00 22.89 O
HETATM 2648 O HOH A2141 3.115 -12.307 -17.317 1.00 15.51 O
HETATM 2649 O HOH A2142 18.914 9.579 3.438 1.00 14.90 O
HETATM 2650 O HOH A2143 11.331 -14.635 4.091 1.00 14.76 O
HETATM 2651 O HOH A2144 -21.133 0.344 -7.168 1.00 12.48 O
HETATM 2652 O HOH A2145 -16.091 -7.755 -3.290 1.00 14.25 O
HETATM 2653 O HOH A2146 -7.520 -2.056 -19.296 1.00 15.95 O
HETATM 2654 O HOH A2147 -13.526 8.099 9.698 1.00 18.74 O
HETATM 2655 O HOH A2148 -11.417 -9.452 5.638 0.50 9.74 O
HETATM 2656 O HOH A2149 17.073 -11.404 -7.833 1.00 16.69 O
HETATM 2657 O HOH A2150 4.135 -8.545 -28.639 1.00 18.44 O
HETATM 2658 O HOH A2151 -14.507 1.877 16.213 1.00 22.29 O
HETATM 2659 O HOH A2152 8.096 -13.339 10.453 1.00 18.42 O
HETATM 2660 O HOH A2153 2.939 -4.367 -25.807 1.00 16.88 O
HETATM 2661 O HOH A2154 1.303 19.442 -6.271 1.00 21.60 O
HETATM 2662 O HOH A2155 -4.876 12.228 -16.384 1.00 11.93 O
HETATM 2663 O HOH A2156 -18.836 7.093 -11.631 1.00 16.74 O
HETATM 2664 O HOH A2157 -22.591 -1.997 -6.592 1.00 9.82 O
HETATM 2665 O HOH A2158 1.322 6.304 -25.344 1.00 10.71 O
HETATM 2666 O HOH A2159 -0.093 5.738 -27.666 1.00 10.35 O
HETATM 2667 O HOH A2160 12.589 -0.642 -20.977 1.00 9.70 O
HETATM 2668 O HOH A2161 10.011 0.167 -21.578 1.00 10.76 O
HETATM 2669 O HOH A2162 -2.056 20.093 9.746 1.00 10.07 O
HETATM 2670 O HOH A2163 9.920 2.955 -21.155 1.00 10.98 O
HETATM 2671 O HOH A2164 -8.636 7.899 26.020 1.00 10.67 O
HETATM 2672 O HOH A2165 4.458 -4.623 -23.469 1.00 13.34 O
HETATM 2673 O HOH A2166 -2.082 -12.090 24.401 1.00 12.47 O
HETATM 2674 O HOH A2167 -4.453 2.056 -3.330 1.00 10.82 O
HETATM 2675 O HOH A2168 13.841 -4.603 -13.158 1.00 12.84 O
HETATM 2676 O HOH A2169 -7.441 18.943 16.192 1.00 18.85 O
HETATM 2677 O HOH A2170 12.143 3.795 -19.860 1.00 13.52 O
HETATM 2678 O HOH A2171 -0.708 22.650 1.550 1.00 13.17 O
HETATM 2679 O HOH A2172 -2.478 -11.835 19.931 1.00 12.22 O
HETATM 2680 O HOH A2173 11.214 -21.522 -7.859 1.00 13.49 O
HETATM 2681 O HOH A2174 -11.031 2.437 -17.750 1.00 13.86 O
HETATM 2682 O HOH A2175 -2.268 12.791 -3.743 1.00 14.87 O
HETATM 2683 O HOH A2176 -10.521 17.840 6.259 1.00 14.43 O
HETATM 2684 O HOH A2177 13.176 1.312 -19.045 1.00 16.77 O
HETATM 2685 O HOH A2178 18.318 -9.258 0.959 1.00 16.32 O
HETATM 2686 O HOH A2179 4.384 -15.820 4.981 1.00 12.24 O
HETATM 2687 O HOH A2180 17.746 7.109 -2.866 1.00 12.76 O
HETATM 2688 O HOH A2181 3.961 23.247 6.324 1.00 15.41 O
HETATM 2689 O HOH A2182 -16.495 -8.195 -7.878 1.00 18.07 O
HETATM 2690 O HOH A2183 3.247 -5.790 -28.105 1.00 18.14 O
HETATM 2691 O AHOH A2184 22.868 -5.659 -2.613 0.50 8.27 O
HETATM 2692 O BHOH A2184 22.767 -5.227 -3.612 0.50 10.69 O
HETATM 2693 O AHOH A2185 -19.803 0.114 -9.541 0.60 13.17 O
HETATM 2694 O BHOH A2185 -19.705 0.003 -11.007 0.40 15.37 O
HETATM 2695 O HOH A2186 14.236 -2.857 15.707 1.00 14.87 O
HETATM 2696 O HOH A2187 5.281 -13.653 -17.936 1.00 13.94 O
HETATM 2697 O HOH A2188 7.807 1.123 19.740 1.00 14.78 O
HETATM 2698 O HOH A2189 18.518 -15.380 -1.797 1.00 17.77 O
HETATM 2699 O HOH A2190 13.729 -5.726 12.011 1.00 17.62 O
HETATM 2700 O HOH A2191 15.901 -5.344 10.244 1.00 16.27 O
HETATM 2701 O HOH A2192 -6.386 4.608 28.731 1.00 13.99 O
HETATM 2702 O HOH A2193 -5.787 -19.842 5.271 1.00 16.21 O
HETATM 2703 O HOH A2194 10.813 -17.158 2.607 1.00 15.80 O
HETATM 2704 O HOH A2195 -2.059 18.692 -10.741 1.00 15.98 O
HETATM 2705 O HOH A2196 -11.421 -8.316 14.430 1.00 20.81 O
HETATM 2706 O HOH A2197 -6.814 9.214 -18.093 1.00 19.60 O
HETATM 2707 O HOH A2198 -4.094 -20.463 -0.972 1.00 14.84 O
HETATM 2708 O HOH A2199 2.675 8.969 19.938 1.00 19.78 O
HETATM 2709 O HOH A2200 14.720 -5.254 14.534 1.00 19.62 O
HETATM 2710 O HOH A2201 -0.818 -1.956 24.584 1.00 19.66 O
HETATM 2711 O HOH A2202 10.175 -22.931 -12.266 1.00 16.13 O
HETATM 2712 O AHOH A2203 7.196 17.322 -7.857 0.50 13.72 O
HETATM 2713 O BHOH A2203 7.679 18.590 -7.334 0.50 14.98 O
HETATM 2714 O HOH A2204 -22.028 4.249 6.774 1.00 15.09 O
HETATM 2715 O HOH A2205 -13.405 11.749 -13.229 1.00 16.51 O
HETATM 2716 O HOH A2206 -10.119 18.428 -13.266 1.00 17.49 O
HETATM 2717 O HOH A2207 21.107 8.046 3.424 1.00 18.00 O
HETATM 2718 O HOH A2208 -1.792 0.543 25.437 1.00 15.27 O
HETATM 2719 O HOH A2209 1.351 3.889 -28.911 1.00 22.72 O
HETATM 2720 O HOH A2210 -0.558 19.948 0.501 1.00 15.81 O
HETATM 2721 O HOH A2211 17.884 -9.167 8.237 1.00 15.57 O
HETATM 2722 O HOH A2212 -10.936 -15.691 -0.810 1.00 19.15 O
HETATM 2723 O HOH A2213 14.388 -6.109 -15.282 1.00 15.40 O
HETATM 2724 O HOH A2214 9.645 20.536 0.345 1.00 14.91 O
HETATM 2725 O AHOH A2215 -5.770 17.662 14.564 0.50 10.98 O
HETATM 2726 O BHOH A2215 -5.261 16.528 15.519 0.25 5.91 O
HETATM 2727 O CHOH A2215 -4.475 15.942 16.119 0.25 6.25 O
HETATM 2728 O HOH A2216 -18.926 -4.282 -8.337 1.00 15.36 O
HETATM 2729 O AHOH A2217 -18.081 -0.702 8.072 0.70 12.50 O
HETATM 2730 O BHOH A2217 -19.147 -1.620 6.089 0.30 13.69 O
HETATM 2731 O HOH A2218 -1.096 -14.645 -11.637 1.00 16.06 O
HETATM 2732 O HOH A2219 18.603 -7.893 -4.113 1.00 16.39 O
HETATM 2733 O HOH A2220 -0.634 -20.535 -9.104 1.00 22.62 O
HETATM 2734 O HOH A2221 4.212 19.571 -13.521 1.00 19.97 O
HETATM 2735 O HOH A2222 -22.254 8.917 7.465 1.00 18.55 O
HETATM 2736 O AHOH A2223 -22.426 9.430 0.087 0.60 15.22 O
HETATM 2737 O BHOH A2223 -23.616 8.372 -1.438 0.40 3.30 O
HETATM 2738 O HOH A2224 21.668 -5.936 7.018 1.00 25.32 O
HETATM 2739 O HOH A2225 -15.326 -0.291 14.816 1.00 19.26 O
HETATM 2740 O HOH A2226 3.382 11.718 16.602 1.00 19.07 O
HETATM 2741 O HOH A2227 -13.566 -5.656 -15.443 1.00 18.33 O
HETATM 2742 O HOH A2228 -3.043 15.470 -0.297 1.00 19.81 O
HETATM 2743 O HOH A2229 2.338 2.333 -26.026 1.00 25.34 O
HETATM 2744 O HOH A2230 -4.891 -13.031 20.789 1.00 18.32 O
HETATM 2745 O HOH A2231 17.073 -13.105 -10.100 1.00 19.16 O
HETATM 2746 O HOH A2232 -18.763 -2.661 -12.415 1.00 20.25 O
HETATM 2747 O HOH A2233 -11.608 -11.003 15.324 1.00 24.02 O
HETATM 2748 O HOH A2234 -0.422 -20.667 -6.783 1.00 22.00 O
HETATM 2749 O HOH A2235 7.486 -24.124 -6.365 1.00 16.61 O
HETATM 2750 O HOH A2236 0.393 -4.006 -24.955 1.00 17.49 O
HETATM 2751 O HOH A2237 -2.502 22.914 6.255 1.00 17.85 O
HETATM 2752 O HOH A2238 -6.198 -6.936 16.564 1.00 23.43 O
HETATM 2753 O HOH A2239 5.566 15.017 12.554 1.00 16.53 O
HETATM 2754 O HOH A2240 3.670 6.819 16.363 1.00 16.94 O
HETATM 2755 O HOH A2241 -9.844 -0.298 -18.815 1.00 17.48 O
HETATM 2756 O HOH A2242 5.956 -8.338 -30.597 1.00 15.87 O
HETATM 2757 O HOH A2243 14.653 15.281 2.670 1.00 19.26 O
HETATM 2758 O AHOH A2244 20.377 1.616 6.444 0.50 10.70 O
HETATM 2759 O CHOH A2244 21.075 1.398 5.258 0.50 10.89 O
HETATM 2760 O HOH A2245 -8.105 -19.247 -0.310 1.00 30.31 O
HETATM 2761 O HOH A2246 2.408 -19.430 11.817 1.00 26.96 O
HETATM 2762 O AHOH A2247 9.848 10.487 -11.149 0.50 11.61 O
HETATM 2763 O BHOH A2247 11.134 10.200 -9.939 0.50 24.62 O
HETATM 2764 O HOH A2248 -1.443 -5.894 -23.290 1.00 20.55 O
HETATM 2765 O HOH A2249 5.207 4.521 -27.039 1.00 18.28 O
HETATM 2766 O HOH A2250 1.122 12.413 17.560 1.00 19.02 O
HETATM 2767 O HOH A2251 -14.244 15.687 6.596 1.00 26.19 O
HETATM 2768 O HOH A2252 -5.073 -5.603 22.459 1.00 24.80 O
HETATM 2769 O HOH A2253 -4.903 -6.909 19.231 1.00 21.98 O
HETATM 2770 O HOH A2254 -17.699 -4.853 4.416 1.00 19.27 O
HETATM 2771 O HOH A2255 -20.526 6.050 13.606 1.00 20.64 O
HETATM 2772 O HOH A2256 3.862 24.965 2.230 1.00 17.45 O
HETATM 2773 O HOH A2257 1.388 19.059 12.646 1.00 19.89 O
HETATM 2774 O HOH A2258 22.110 -7.572 3.196 1.00 21.06 O
HETATM 2775 O HOH A2259 -17.480 -6.840 -13.599 1.00 28.66 O
HETATM 2776 O HOH A2260 -12.339 -13.967 5.544 1.00 21.15 O
HETATM 2777 O HOH A2261 6.802 -13.340 20.970 1.00 18.04 O
HETATM 2778 O AHOH A2262 11.749 12.252 -7.301 0.50 10.11 O
HETATM 2779 O BHOH A2262 11.412 13.184 -8.219 0.50 16.68 O
HETATM 2780 O HOH A2263 4.758 -10.505 -26.725 1.00 16.49 O
HETATM 2781 O HOH A2264 -8.661 20.435 2.904 1.00 21.89 O
HETATM 2782 O HOH A2265 -5.832 19.898 -18.125 1.00 25.88 O
HETATM 2783 O HOH A2266 9.088 12.923 -9.964 1.00 21.53 O
HETATM 2784 O HOH A2267 16.987 0.941 -13.121 1.00 22.48 O
HETATM 2785 O HOH A2268 18.559 -16.179 6.825 1.00 21.91 O
HETATM 2786 O HOH A2269 8.800 21.878 2.841 1.00 17.96 O
HETATM 2787 O HOH A2270 3.453 -3.392 25.179 1.00 28.70 O
HETATM 2788 O HOH A2271 -7.208 -4.955 18.394 1.00 24.97 O
HETATM 2789 O HOH A2272 8.663 -16.155 18.287 1.00 22.90 O
HETATM 2790 O HOH A2273 -13.815 -11.413 11.742 1.00 23.97 O
HETATM 2791 O HOH A2274 20.649 -13.530 4.394 1.00 25.37 O
HETATM 2792 O HOH A2275 15.593 -13.363 9.516 1.00 21.49 O
HETATM 2793 O HOH A2276 -7.372 -14.705 17.091 1.00 20.41 O
HETATM 2794 O HOH A2277 6.239 -11.345 22.811 1.00 27.21 O
HETATM 2795 O HOH A2278 -6.278 -1.984 -22.922 1.00 20.02 O
HETATM 2796 O HOH A2279 1.262 -18.033 10.046 1.00 22.94 O
HETATM 2797 O HOH A2280 17.734 -10.710 -1.715 1.00 26.08 O
HETATM 2798 O HOH A2281 -11.471 7.160 22.294 1.00 17.16 O
HETATM 2799 O HOH A2282 18.355 5.852 -7.204 1.00 22.49 O
HETATM 2800 O AHOH A2283 -11.674 14.982 -3.303 0.50 10.81 O
HETATM 2801 O BHOH A2283 -11.067 15.690 -4.452 0.50 16.82 O
HETATM 2802 O HOH A2284 11.026 10.576 -13.722 1.00 23.90 O
HETATM 2803 O HOH A2285 -20.623 0.610 8.063 1.00 27.62 O
HETATM 2804 O HOH A2286 -13.613 8.542 6.956 0.50 9.68 O
HETATM 2805 O AHOH A2287 6.459 -16.810 -15.140 0.70 14.52 O
HETATM 2806 O BHOH A2287 4.909 -17.583 -15.140 0.30 14.52 O
HETATM 2807 O HOH A2288 -17.244 12.005 1.934 1.00 25.68 O
HETATM 2808 O HOH A2289 -12.563 13.337 0.823 1.00 26.34 O
HETATM 2809 O HOH A2290 -6.184 -19.143 -6.753 1.00 24.09 O
HETATM 2810 O HOH A2291 4.862 -14.493 24.268 1.00 20.61 O
HETATM 2811 O HOH A2292 21.960 -4.027 -6.161 0.50 11.51 O
HETATM 2812 O HOH A2293 12.821 -16.981 -7.947 1.00 17.02 O
HETATM 2813 O HOH A2294 -19.591 10.183 2.321 1.00 24.11 O
HETATM 2814 O HOH A2295 14.981 -15.638 -7.284 1.00 21.90 O
HETATM 2815 O HOH A2296 14.116 4.401 -21.488 1.00 20.10 O
HETATM 2816 O HOH A2297 9.163 -0.178 -24.215 1.00 12.72 O
HETATM 2817 O HOH A2298 -4.536 -12.104 23.569 1.00 14.86 O
HETATM 2818 O HOH A2299 -4.792 6.887 -18.911 0.70 10.62 O
HETATM 2819 O HOH A2300 2.905 6.269 18.809 1.00 17.03 O
HETATM 2820 O HOH A2301 -23.520 -2.710 -8.995 1.00 18.79 O
HETATM 2821 O HOH A2302 -9.723 19.917 14.744 1.00 19.36 O
HETATM 2822 O HOH A2303 5.689 23.846 4.293 1.00 23.82 O
HETATM 2823 O HOH A2304 -7.841 -12.975 19.640 1.00 19.54 O
HETATM 2824 O HOH A2305 6.555 -16.011 3.552 1.00 14.77 O
HETATM 2825 O HOH A2306 -4.191 12.582 24.405 1.00 18.17 O
HETATM 2826 O HOH A2307 2.630 -0.650 24.419 0.50 12.14 O
HETATM 2827 O HOH A2308 0.001 2.172 26.576 1.00 24.28 O
HETATM 2828 O HOH A2309 -4.324 4.846 -25.876 1.00 18.02 O
HETATM 2829 O HOH A2310 -12.276 17.902 -11.459 1.00 19.39 O
HETATM 2830 O HOH A2311 19.339 -12.923 -2.566 1.00 25.05 O
HETATM 2831 O HOH A2312 -2.275 4.259 -27.400 1.00 21.11 O
HETATM 2832 O HOH A2313 19.773 -4.927 8.546 1.00 24.09 O
HETATM 2833 O HOH A2314 18.012 -6.758 9.924 1.00 25.25 O
HETATM 2834 O HOH A2315 13.937 15.894 0.048 1.00 21.37 O
HETATM 2835 O HOH A2316 14.402 -9.622 11.772 1.00 22.80 O
HETATM 2836 O HOH A2317 17.791 -15.059 9.056 1.00 22.13 O
HETATM 2837 O HOH A2318 2.659 -24.292 -8.565 1.00 21.69 O
HETATM 2838 O HOH A2319 -12.587 -9.554 2.953 0.50 14.37 O
HETATM 2839 O HOH A2320 -3.975 22.079 10.333 1.00 23.87 O
HETATM 2840 O HOH A2321 -15.540 -7.860 13.092 1.00 22.89 O
HETATM 2841 O AHOH A2322 5.736 25.884 0.401 0.50 14.16 O
HETATM 2842 O BHOH A2322 5.260 25.254 -0.561 0.50 17.21 O
HETATM 2843 O HOH A2323 -13.856 -10.348 -10.547 1.00 27.22 O
HETATM 2844 O HOH A2324 -7.949 14.806 0.991 0.50 12.33 O
HETATM 2845 O HOH A2325 -10.724 19.638 -15.482 1.00 42.00 O
HETATM 2846 O HOH A2326 18.429 -11.219 -11.736 1.00 23.42 O
HETATM 2847 O HOH A2327 15.854 -10.717 9.855 1.00 25.10 O
HETATM 2848 O HOH A2328 -14.416 -12.702 -3.591 1.00 25.12 O
HETATM 2849 O HOH A2329 -14.640 2.783 18.741 1.00 24.86 O
HETATM 2850 O HOH A2330 19.010 -6.135 -8.855 1.00 28.35 O
HETATM 2851 O HOH A2331 12.643 -11.684 14.508 1.00 27.78 O
HETATM 2852 O HOH A2332 10.543 3.793 -23.690 1.00 23.01 O
HETATM 2853 O HOH A2333 -22.909 3.556 -10.829 1.00 24.55 O
HETATM 2854 O AHOH A2334 10.141 11.488 -15.904 0.50 13.47 O
HETATM 2855 O BHOH A2334 9.381 12.470 -15.805 0.50 16.39 O
HETATM 2856 O HOH A2335 -3.588 17.391 -18.250 1.00 29.82 O
HETATM 2857 O HOH A2336 -4.043 21.036 3.273 1.00 31.00 O
HETATM 2858 O HOH A2337 15.147 -1.588 12.890 1.00 20.02 O
HETATM 2859 O AHOH A2338 3.186 -17.764 8.140 0.50 12.43 O
HETATM 2860 O BHOH A2338 4.409 -17.730 8.869 0.50 20.12 O
HETATM 2861 O HOH A2339 22.655 -7.942 -1.571 1.00 29.90 O
HETATM 2862 O HOH A2340 5.907 23.350 -3.887 1.00 25.86 O
HETATM 2863 O HOH A2341 -6.699 14.483 -17.361 1.00 24.90 O
HETATM 2864 O HOH A2342 -14.464 -9.047 -14.565 1.00 24.07 O
HETATM 2865 O HOH A2343 -13.682 -7.208 15.412 1.00 26.16 O
HETATM 2866 O HOH A2344 -19.752 -0.452 -14.028 1.00 34.82 O
HETATM 2867 O HOH A2345 -11.277 20.363 1.567 1.00 21.80 O
HETATM 2868 O HOH A2346 -6.844 -0.082 29.430 1.00 24.62 O
HETATM 2869 O HOH A2347 20.384 -9.722 2.108 1.00 33.23 O
HETATM 2870 O HOH A2348 10.971 -20.747 -5.527 1.00 24.14 O
HETATM 2871 O HOH A2349 8.051 24.053 3.588 1.00 31.25 O
HETATM 2872 O HOH A2350 -10.586 20.402 7.204 1.00 30.25 O
HETATM 2873 O HOH A2351 -12.400 -10.356 -6.897 1.00 22.43 O
HETATM 2874 O HOH A2352 15.499 14.785 -1.595 1.00 27.39 O
HETATM 2875 O HOH A2353 -2.719 -21.928 -5.235 1.00 30.99 O
HETATM 2876 O HOH A2354 17.013 12.111 -0.623 1.00 24.60 O
HETATM 2877 O HOH A2355 -0.471 -17.660 -10.646 1.00 28.63 O
HETATM 2878 O HOH A2356 3.583 -1.705 -26.008 1.00 22.75 O
HETATM 2879 O HOH A2357 4.881 -24.833 -7.124 1.00 23.47 O
HETATM 2880 O HOH A2358 2.157 -17.597 5.526 1.00 29.27 O
HETATM 2881 O HOH A2359 -2.451 22.683 3.441 1.00 22.77 O
HETATM 2882 O HOH A2360 -16.903 -8.724 -1.131 1.00 35.13 O
HETATM 2883 O HOH A2361 17.521 -4.371 12.226 1.00 35.82 O
HETATM 2884 O HOH A2362 -6.414 -4.398 24.737 1.00 27.11 O
HETATM 2885 O HOH A2363 -2.514 18.969 -0.965 1.00 26.74 O
HETATM 2886 O HOH A2364 14.575 11.390 -7.005 1.00 24.40 O
HETATM 2887 O AHOH A2365 21.003 -2.864 9.832 0.70 20.83 O
HETATM 2888 O BHOH A2365 20.633 -0.887 9.817 0.30 16.15 O
HETATM 2889 O HOH A2366 -4.533 16.602 19.088 1.00 29.66 O
HETATM 2890 O HOH A2367 -0.992 -8.578 22.026 1.00 22.57 O
HETATM 2891 O HOH A2368 0.023 -22.553 -11.236 1.00 24.75 O
HETATM 2892 O HOH A2369 2.724 15.152 -14.582 1.00 28.47 O
HETATM 2893 O HOH A2370 -20.873 9.736 -3.955 0.50 12.63 O
HETATM 2894 O HOH A2371 -22.381 -1.432 -10.979 1.00 30.72 O
HETATM 2895 O HOH A2372 -14.614 17.080 -7.412 1.00 30.07 O
HETATM 2896 O HOH A2373 -20.275 10.215 -0.945 1.00 23.97 O
HETATM 2897 O HOH A2374 -13.867 12.241 -2.993 1.00 32.18 O
HETATM 2898 O HOH A2375 7.642 -9.534 22.068 1.00 27.26 O
HETATM 2899 O HOH A2376 4.583 9.624 17.962 1.00 30.48 O
HETATM 2900 O HOH A2377 12.481 18.364 -1.045 1.00 29.43 O
HETATM 2901 O HOH A2378 -8.636 -18.639 -12.916 1.00 39.98 O
HETATM 2902 O HOH A2379 4.155 -19.768 -15.976 1.00 43.18 O
HETATM 2903 O HOH A2380 17.150 14.028 2.185 1.00 30.16 O
HETATM 2904 O HOH A2381 -11.320 -17.161 8.538 1.00 24.48 O
HETATM 2905 O HOH A2382 4.613 -16.210 -17.018 1.00 38.03 O
HETATM 2906 O HOH A2383 -17.624 9.870 -11.986 1.00 28.37 O
HETATM 2907 O HOH A2384 -0.556 15.845 17.044 1.00 31.78 O
HETATM 2908 O HOH A2385 -14.878 -12.487 9.591 1.00 32.91 O
HETATM 2909 O HOH A2386 15.351 5.882 -16.484 1.00 29.43 O
HETATM 2910 O HOH A2387 -17.757 10.753 -9.430 1.00 23.75 O
HETATM 2911 O HOH A2388 -14.878 -11.485 -0.738 1.00 31.20 O
HETATM 2912 O AHOH A2389 13.524 7.295 10.652 0.50 23.45 O
HETATM 2913 O BHOH A2389 13.123 9.136 10.113 0.50 17.42 O
HETATM 2914 O HOH A2390 -5.829 9.406 -20.676 1.00 30.20 O
HETATM 2915 O HOH A2391 -1.659 17.639 -13.623 1.00 28.41 O
HETATM 2916 O AHOH A2392 -4.410 -20.187 -8.629 0.50 19.21 O
HETATM 2917 O BHOH A2392 -3.530 -19.801 -9.400 0.50 19.72 O
HETATM 2918 O HOH A2393 -9.422 -17.180 4.723 1.00 27.30 O
HETATM 2919 O AHOH A2394 18.263 -4.968 -12.117 0.40 21.05 O
HETATM 2920 O BHOH A2394 18.460 -4.775 -10.830 0.60 17.97 O
HETATM 2921 O HOH A2395 0.473 -6.571 23.081 1.00 29.58 O
HETATM 2922 O HOH A2396 -0.163 13.517 -15.821 1.00 45.24 O
HETATM 2923 O AHOH A2397 -7.695 0.821 -26.378 0.50 19.07 O
HETATM 2924 O BHOH A2397 -6.722 1.719 -26.968 0.50 19.21 O
HETATM 2925 O HOH A2398 -10.153 -19.443 9.858 1.00 24.60 O
HETATM 2926 O HOH A2399 11.350 -16.960 7.602 1.00 24.95 O
HETATM 2927 O HOH A2400 -7.296 -13.150 -18.314 1.00 34.61 O
HETATM 2928 O HOH A2401 -17.299 -9.341 -5.414 1.00 28.12 O
HETATM 2929 O HOH A2402 -4.166 18.702 -2.919 1.00 28.82 O
HETATM 2930 O HOH A2403 0.093 20.147 -10.599 0.50 17.63 O
HETATM 2931 O HOH A2404 3.134 -19.116 2.954 1.00 26.21 O
HETATM 2932 O HOH A2405 20.870 -9.073 -3.143 1.00 31.69 O
HETATM 2933 O HOH A2406 20.938 -10.157 4.957 1.00 35.63 O
HETATM 2934 O HOH A2407 -19.071 2.716 -10.906 1.00 25.37 O
HETATM 2935 O HOH A2408 -11.491 -13.241 -12.239 1.00 27.66 O
HETATM 2936 O HOH A2409 0.924 -5.503 -29.112 1.00 37.87 O
HETATM 2937 O HOH A2410 6.846 -4.928 23.888 1.00 29.09 O
HETATM 2938 O HOH A2411 -2.715 -22.146 5.731 0.50 32.28 O
HETATM 2939 O AHOH A2412 -1.830 18.552 -8.271 0.50 7.79 O
HETATM 2940 O BHOH A2412 -1.684 18.590 -6.692 0.50 14.64 O
HETATM 2941 O HOH A2413 2.052 3.901 20.284 1.00 25.68 O
HETATM 2942 O HOH A2414 1.666 20.390 -12.691 1.00 24.03 O
HETATM 2943 O HOH A2415 6.509 -18.317 15.312 1.00 24.23 O
HETATM 2944 O HOH A2416 0.204 20.978 10.829 1.00 26.73 O
HETATM 2945 O HOH A2417 -1.789 17.332 15.212 1.00 30.88 O
HETATM 2946 O HOH A2418 -1.645 -10.078 26.172 1.00 26.86 O
HETATM 2947 O HOH A2419 2.791 1.327 25.707 1.00 29.86 O
HETATM 2948 O HOH A2420 -16.346 -11.893 -5.016 1.00 33.13 O
HETATM 2949 O HOH A2421 8.176 -22.367 -4.235 1.00 39.43 O
HETATM 2950 O HOH A2422 -10.033 -10.418 -17.529 1.00 33.13 O
HETATM 2951 O HOH A2423 -14.073 -11.535 16.632 1.00 41.25 O
HETATM 2952 O AHOH A2424 10.903 13.327 8.519 0.70 18.88 O
HETATM 2953 O BHOH A2424 11.720 12.670 9.918 0.30 8.56 O
HETATM 2954 O AHOH A2425 -12.254 15.018 -12.086 0.50 19.49 O
HETATM 2955 O BHOH A2425 -12.048 13.985 -13.560 0.50 15.73 O
HETATM 2956 O HOH A2426 -13.428 -3.025 -20.209 1.00 36.19 O
HETATM 2957 O HOH A2427 -14.103 7.733 -13.899 1.00 28.62 O
HETATM 2958 O HOH A2428 -9.075 20.089 12.239 1.00 29.19 O
HETATM 2959 O HOH A2429 -9.540 22.110 4.815 1.00 26.15 O
HETATM 2960 O HOH A2430 -16.434 -6.134 8.412 1.00 24.19 O
HETATM 2961 O HOH A2431 -6.312 21.648 2.461 1.00 30.42 O
HETATM 2962 O HOH A2432 5.905 21.070 -7.167 1.00 30.85 O
HETATM 2963 O HOH A2433 -7.583 18.248 -17.489 1.00 33.58 O
HETATM 2964 O HOH A2434 -4.170 -20.283 -11.548 1.00 25.80 O
HETATM 2965 O HOH A2435 -3.267 1.337 29.197 1.00 29.61 O
HETATM 2966 O HOH A2436 17.915 -8.122 -9.233 1.00 33.18 O
HETATM 2967 O HOH A2437 0.232 1.543 -28.838 1.00 38.65 O
HETATM 2968 O HOH A2438 -12.146 5.093 -17.113 1.00 31.17 O
HETATM 2969 O HOH A2439 -13.740 1.479 20.783 1.00 28.33 O
HETATM 2970 O HOH A2440 7.419 23.981 -2.141 1.00 32.61 O
HETATM 2971 O HOH A2441 12.695 -12.301 12.013 1.00 32.69 O
HETATM 2972 O HOH A2442 5.576 13.513 16.720 1.00 34.99 O
HETATM 2973 O HOH A2443 -9.121 21.948 8.567 1.00 31.99 O
HETATM 2974 O HOH A2444 15.130 -7.831 18.031 1.00 34.88 O
HETATM 2975 O HOH A2445 1.731 -15.550 -19.618 1.00 35.18 O
HETATM 2976 O HOH A2446 7.633 -17.327 11.096 1.00 33.93 O
HETATM 2977 O HOH A2447 14.784 -14.170 11.661 1.00 39.93 O
HETATM 2978 O HOH A2448 8.722 13.675 -13.967 1.00 45.07 O
HETATM 2979 O HOH A2449 -9.520 -13.049 -17.448 1.00 33.27 O
HETATM 2980 O HOH A2450 -21.585 6.247 -11.515 1.00 37.68 O
HETATM 2981 O HOH A2451 -6.518 22.825 9.300 1.00 34.59 O
HETATM 2982 O HOH A2452 -9.046 -21.038 7.700 1.00 37.82 O
HETATM 2983 O HOH A2453 12.553 18.109 6.828 1.00 29.07 O
HETATM 2984 O HOH A2454 13.048 20.930 3.427 1.00 40.78 O
HETATM 2985 O HOH A2455 -10.267 -6.781 15.677 1.00 31.35 O
HETATM 2986 O HOH A2456 -11.180 -2.805 19.110 1.00 24.45 O
HETATM 2987 O HOH A2457 -10.257 -5.308 18.152 1.00 30.76 O
HETATM 2988 O HOH A2458 0.554 -21.563 5.311 1.00 38.31 O
HETATM 2989 O HOH A2459 -12.603 -11.775 6.538 1.00 19.13 O
HETATM 2990 O HOH A2460 0.371 -8.787 -28.232 1.00 27.80 O
HETATM 2991 O HOH A2461 7.020 1.326 -24.721 1.00 15.11 O
HETATM 2992 O HOH A2462 8.306 14.854 9.425 1.00 31.56 O
HETATM 2993 O HOH A2463 -19.952 2.276 10.665 1.00 28.37 O
HETATM 2994 O HOH A2464 -18.885 -2.828 9.720 1.00 28.02 O
HETATM 2995 O HOH A2465 -17.467 10.435 7.380 1.00 27.10 O
HETATM 2996 O HOH A2466 -20.039 10.872 8.287 1.00 31.11 O
HETATM 2997 O HOH A2467 12.059 -17.548 10.356 1.00 35.74 O
HETATM 2998 O HOH A2468 2.886 3.944 22.668 1.00 30.34 O
HETATM 2999 O HOH A2469 1.185 -2.239 27.954 1.00 28.51 O
HETATM 3000 O HOH A2470 14.538 18.678 -0.075 1.00 42.69 O
HETATM 3001 O HOH A2471 -20.448 0.133 12.227 1.00 28.66 O
HETATM 3002 O HOH A2472 14.495 -18.231 10.973 1.00 30.91 O
HETATM 3003 O HOH A2473 11.493 20.147 7.305 1.00 48.10 O
HETATM 3004 O HOH A2474 11.454 3.010 18.949 1.00 30.60 O
HETATM 3005 O HOH A2475 6.615 24.376 10.158 1.00 40.94 O
HETATM 3006 O HOH A2476 -14.836 17.055 12.096 1.00 24.13 O
HETATM 3007 O HOH A2477 -15.412 -7.935 1.705 0.50 13.59 O
HETATM 3008 O HOH A2478 -22.165 9.649 -2.500 0.50 15.40 O
HETATM 3009 O HOH A2479 -12.689 -11.395 0.830 1.00 22.77 O
HETATM 3010 O HOH A2480 -19.931 10.271 4.591 1.00 26.82 O
HETATM 3011 O HOH A2481 6.538 14.282 -12.148 1.00 29.73 O
HETATM 3012 O HOH A2482 -5.992 7.866 -24.712 1.00 35.25 O
HETATM 3013 O HOH A2483 1.433 -13.342 -19.061 1.00 34.81 O
HETATM 3014 O HOH A2484 -4.261 -21.102 7.007 0.50 14.61 O
HETATM 3015 O HOH A2485 1.697 -1.925 25.344 0.50 23.07 O
HETATM 3016 O HOH A2486 16.434 8.314 9.816 1.00 30.56 O
HETATM 3017 O HOH A2487 -6.642 23.998 5.077 1.00 40.68 O
HETATM 3018 O AHOH A2488 7.426 16.807 -11.947 0.50 19.70 O
HETATM 3019 O BHOH A2488 5.885 17.502 -13.183 0.50 26.03 O
HETATM 3020 O HOH A2489 8.456 24.222 7.982 1.00 47.37 O
HETATM 3021 O HOH A2490 18.965 -0.034 11.901 0.50 21.21 O
HETATM 3022 O HOH A2491 4.953 18.773 -9.229 1.00 36.71 O
HETATM 3023 O HOH A2492 -0.129 6.420 25.743 1.00 43.58 O
HETATM 3024 O HOH A2493 21.982 -6.032 -5.162 0.50 16.45 O
HETATM 3025 O HOH A2494 17.969 -19.449 -6.633 1.00 34.93 O
HETATM 3026 O HOH A2495 -4.239 -6.732 -20.656 1.00 25.44 O
HETATM 3027 O HOH A2496 -7.458 -1.415 26.045 1.00 29.71 O
HETATM 3028 O HOH A2497 -13.396 -4.838 16.726 1.00 37.31 O
HETATM 3029 O HOH A2498 19.989 -13.440 9.837 1.00 35.20 O
HETATM 3030 O HOH A2499 -11.910 -16.964 -2.624 1.00 30.57 O
HETATM 3031 O HOH A2500 -0.296 20.088 -8.464 0.50 17.14 O
HETATM 3032 O HOH A2501 1.581 -19.490 14.736 1.00 27.83 O
HETATM 3033 O HOH A2502 17.856 9.454 -8.473 1.00 36.49 O
HETATM 3034 O HOH A2503 -10.072 -17.883 -4.116 1.00 24.15 O
HETATM 3035 O HOH A2504 2.275 -16.408 -14.987 1.00 26.56 O
HETATM 3036 O HOH A2505 -5.899 15.524 -0.420 0.50 22.76 O
HETATM 3037 O HOH A2506 7.777 12.620 14.750 1.00 37.77 O
HETATM 3038 O HOH A2507 -12.048 10.889 -15.575 1.00 32.83 O
HETATM 3039 O HOH A2508 -13.672 -15.683 -3.480 1.00 39.83 O
HETATM 3040 O HOH A2509 -17.039 13.337 -9.120 0.65 16.66 O
HETATM 3041 O HOH A2510 18.599 10.600 6.410 1.00 25.50 O
HETATM 3042 O HOH A2511 21.764 0.130 4.576 0.50 12.25 O
HETATM 3043 O HOH A2512 17.293 3.307 9.524 1.00 25.07 O
HETATM 3044 O HOH A2513 5.320 5.241 19.811 1.00 27.72 O
HETATM 3045 O HOH A2514 -5.932 -21.711 0.804 1.00 44.17 O
HETATM 3046 O HOH A2515 -9.889 16.420 1.790 1.00 36.05 O
HETATM 3047 O HOH A2516 6.080 5.884 15.586 1.00 34.40 O
HETATM 3048 O AHOH A2517 -23.188 4.777 9.295 0.50 17.93 O
HETATM 3049 O BHOH A2517 -23.032 5.988 10.024 0.50 29.28 O
HETATM 3050 O HOH A2518 -2.775 -12.475 -17.266 1.00 38.23 O
HETATM 3051 O HOH A2519 10.265 23.359 6.372 1.00 38.77 O
HETATM 3052 O HOH A2520 -14.719 14.492 1.959 1.00 35.16 O
HETATM 3053 O HOH A2521 6.921 3.561 14.808 1.00 34.16 O
HETATM 3054 O HOH A2522 2.343 -22.579 -0.880 1.00 46.98 O
HETATM 3055 O HOH A2523 18.457 3.777 6.859 1.00 99.51 O
HETATM 3056 O HOH A2524 -4.815 -20.523 -3.913 1.00 29.12 O
HETATM 3057 O HOH A2525 -13.740 15.691 -12.659 0.50 16.80 O
HETATM 3058 O HOH A2526 16.553 5.833 10.570 1.00 40.27 O
HETATM 3059 O HOH A2527 -17.979 1.329 -15.347 1.00 34.56 O
HETATM 3060 O HOH A2528 -16.968 20.062 11.304 1.00 43.62 O
HETATM 3061 O HOH A2529 19.537 13.052 6.728 1.00 45.11 O
HETATM 3062 O HOH A2530 -18.823 3.570 -13.676 1.00 50.68 O
HETATM 3063 O HOH A2531 19.030 12.449 4.131 1.00 39.11 O
HETATM 3064 O HOH A2532 -14.901 -10.360 7.327 0.50 28.52 O
HETATM 3065 O HOH A2533 -17.483 -2.923 14.933 1.00 42.60 O
HETATM 3066 O HOH A2534 -10.239 8.995 -17.629 1.00 35.65 O
HETATM 3067 O HOH A2535 15.616 2.188 -22.899 1.00 34.35 O
HETATM 3068 O HOH A2536 0.190 4.722 27.549 1.00 37.70 O
HETATM 3069 O HOH A2537 18.216 -16.815 -4.165 0.50 13.08 O
HETATM 3070 O HOH A2538 -11.832 2.375 -20.310 1.00 38.53 O
HETATM 3071 O HOH A2539 17.134 -5.897 14.017 1.00 37.20 O
HETATM 3072 O HOH A2540 -2.375 3.387 29.714 1.00 34.76 O
HETATM 3073 O HOH A2541 5.053 -19.462 11.444 1.00 28.54 O
HETATM 3074 O HOH A2542 8.897 -3.537 23.388 1.00 35.65 O
CONECT 2493 2494
CONECT 2494 2493 2495 2496
CONECT 2495 2494
CONECT 2496 2494
CONECT 2497 2498 2499 2500
CONECT 2498 2497
CONECT 2499 2497
CONECT 2500 2497
CONECT 2501 2502 2503 2504
CONECT 2502 2501
CONECT 2503 2501
CONECT 2504 2501
MASTER 281 0 4 19 8 0 7 6 2914 1 12 23
END