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3AYU.pdb
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3AYU.pdb
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HEADER HYDROLASE/HYDROLASE INHIBITOR 17-MAY-11 3AYU
TITLE CRYSTAL STRUCTURE OF MMP-2 ACTIVE SITE MUTANT IN COMPLEX WITH APP-
TITLE 2 DRIVED DECAPEPTIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 72 KDA TYPE IV COLLAGENASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 110-219 AND 394-450;
COMPND 5 SYNONYM: 72 KDA GELATINASE, GELATINASE A, MATRIX METALLOPROTEINASE-2,
COMPND 6 MMP-2;
COMPND 7 EC: 3.4.24.24;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: FUSION PROTEIN OF UNP RESIDUES 110-219 AND 394-450
COMPND 11 FROM 72 KDA TYPE IV COLLAGENASE;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: AMYLOID BETA A4 PROTEIN;
COMPND 14 CHAIN: B;
COMPND 15 FRAGMENT: UNP RESIDUES 586-595;
COMPND 16 SYNONYM: ABPP, APPI, APP, ALZHEIMER DISEASE AMYLOID PROTEIN, CEREBRAL
COMPND 17 VASCULAR AMYLOID PEPTIDE, CVAP, PREA4, PROTEASE NEXIN-II, PN-II;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MMP2, CLG4A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PFLAG-CTC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS PROTEASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HASHIMOTO,T.TAKEUCHI,K.KOMATSU,K.MIYAZAKI,M.SATO,S.HIGASHI
REVDAT 3 17-AUG-11 3AYU 1 JRNL
REVDAT 2 10-AUG-11 3AYU 1 AUTHOR
REVDAT 1 03-AUG-11 3AYU 0
JRNL AUTH H.HASHIMOTO,T.TAKEUCHI,K.KOMATSU,K.MIYAZAKI,M.SATO,S.HIGASHI
JRNL TITL STRUCTURAL BASIS FOR MATRIX METALLOPROTEINASE-2
JRNL TITL 2 (MMP-2)-SELECTIVE INHIBITORY ACTION OF {BETA}-AMYLOID
JRNL TITL 3 PRECURSOR PROTEIN-DERIVED INHIBITOR
JRNL REF J.BIOL.CHEM. 2011
JRNL REFN ESSN 1083-351X
JRNL PMID 21813640
JRNL DOI 10.1074/JBC.M111.264176
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0085
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 11476
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 578
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 819
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1710
REMARK 3 BIN FREE R VALUE SET COUNT : 36
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1392
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 263
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : -0.82000
REMARK 3 B33 (A**2) : 0.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.158
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.269
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1438 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 963 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1954 ; 1.091 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2324 ; 0.813 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 174 ; 6.121 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;33.943 ;23.784
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 207 ;14.400 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;11.069 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 193 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1650 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 321 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3733 -11.8568 -4.6990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0184 T22: 0.0270
REMARK 3 T33: 0.0106 T12: -0.0068
REMARK 3 T13: 0.0110 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.8147 L22: 1.3019
REMARK 3 L33: 0.6166 L12: -0.3359
REMARK 3 L13: 0.0468 L23: 0.0702
REMARK 3 S TENSOR
REMARK 3 S11: 0.0030 S12: 0.0001 S13: 0.0280
REMARK 3 S21: -0.0320 S22: 0.0356 S23: -0.0463
REMARK 3 S31: -0.0211 S32: 0.0282 S33: -0.0386
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3AYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB029865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : CU FINE FOCUS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54180
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12160
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 30.94050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.54100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 18.54100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.94050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.03000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ASP A 167
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 TRP A 67 -134.47 47.37
REMARK 500 ASP A 79 -170.07 77.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 416 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 NE2
REMARK 620 2 ASP A 71 OD2 112.0
REMARK 620 3 HIS A 84 NE2 111.8 116.8
REMARK 620 4 HIS A 97 ND1 109.9 91.5 113.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 415 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 120 NE2
REMARK 620 2 HIS A 130 NE2 109.3
REMARK 620 3 HIS A 124 NE2 101.8 102.2
REMARK 620 4 ASP B 6 OD1 143.4 88.3 105.4
REMARK 620 5 ASP B 6 OD2 93.1 145.4 98.2 59.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 417 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 81 O
REMARK 620 2 GLY A 77 O 177.0
REMARK 620 3 ASP A 79 O 92.0 90.6
REMARK 620 4 ASP A 99 OD2 91.8 85.5 175.9
REMARK 620 5 GLU A 102 OE2 88.7 90.4 82.0 99.2
REMARK 620 6 ASP A 76 OD2 92.9 88.6 85.9 92.8 167.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 418 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 93 O
REMARK 620 2 ASP A 59 O 94.6
REMARK 620 3 GLY A 91 O 96.6 166.6
REMARK 620 4 ASP A 95 OD1 91.5 85.1 101.7
REMARK 620 5 HOH A 303 O 82.3 85.1 89.3 167.9
REMARK 620 6 HOH A 212 O 171.4 87.5 80.3 97.0 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 419 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 102 O
REMARK 620 2 ASP A 100 O 89.3
REMARK 620 3 ASP A 25 OD2 87.8 168.2
REMARK 620 4 ASP A 100 OD1 113.4 78.7 91.9
REMARK 620 5 HOH A 215 O 100.2 103.6 88.2 146.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF AMYLOID BETA A4
REMARK 800 PROTEIN
DBREF 3AYU A 1 110 UNP P08253 MMP2_HUMAN 110 219
DBREF 3AYU A 111 167 UNP P08253 MMP2_HUMAN 394 450
DBREF 3AYU B 1 10 UNP P05067 A4_HUMAN 586 595
SEQADV 3AYU LYS A 108 UNP P08253 GLU 217 ENGINEERED MUTATION
SEQADV 3AYU VAL A 110 UNP P08253 GLN 219 ENGINEERED MUTATION
SEQADV 3AYU ALA A 121 UNP P08253 GLU 404 ENGINEERED MUTATION
SEQRES 1 A 167 TYR ASN PHE PHE PRO ARG LYS PRO LYS TRP ASP LYS ASN
SEQRES 2 A 167 GLN ILE THR TYR ARG ILE ILE GLY TYR THR PRO ASP LEU
SEQRES 3 A 167 ASP PRO GLU THR VAL ASP ASP ALA PHE ALA ARG ALA PHE
SEQRES 4 A 167 GLN VAL TRP SER ASP VAL THR PRO LEU ARG PHE SER ARG
SEQRES 5 A 167 ILE HIS ASP GLY GLU ALA ASP ILE MET ILE ASN PHE GLY
SEQRES 6 A 167 ARG TRP GLU HIS GLY ASP GLY TYR PRO PHE ASP GLY LYS
SEQRES 7 A 167 ASP GLY LEU LEU ALA HIS ALA PHE ALA PRO GLY THR GLY
SEQRES 8 A 167 VAL GLY GLY ASP SER HIS PHE ASP ASP ASP GLU LEU TRP
SEQRES 9 A 167 THR LEU GLY LYS GLY VAL GLY TYR SER LEU PHE LEU VAL
SEQRES 10 A 167 ALA ALA HIS ALA PHE GLY HIS ALA MET GLY LEU GLU HIS
SEQRES 11 A 167 SER GLN ASP PRO GLY ALA LEU MET ALA PRO ILE TYR THR
SEQRES 12 A 167 TYR THR LYS ASN PHE ARG LEU SER GLN ASP ASP ILE LYS
SEQRES 13 A 167 GLY ILE GLN GLU LEU TYR GLY ALA SER PRO ASP
SEQRES 1 B 10 ILE SER TYR GLY ASN ASP ALA LEU MET PRO
HET ZN A 415 1
HET ZN A 416 1
HET CA A 417 1
HET CA A 418 1
HET CA A 419 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 CA 3(CA 2+)
FORMUL 8 HOH *263(H2 O)
HELIX 1 1 ASP A 27 ASP A 44 1 18
HELIX 2 2 LEU A 114 MET A 126 1 13
HELIX 3 3 SER A 151 GLY A 163 1 13
SHEET 1 A 2 ASN A 2 PHE A 3 0
SHEET 2 A 2 LEU A 128 GLU A 129 -1 O GLU A 129 N ASN A 2
SHEET 1 B 6 ARG A 49 ARG A 52 0
SHEET 2 B 6 GLN A 14 ILE A 19 1 N ILE A 15 O ARG A 49
SHEET 3 B 6 ILE A 60 GLY A 65 1 O ILE A 62 N ARG A 18
SHEET 4 B 6 SER A 96 ASP A 99 1 O PHE A 98 N GLY A 65
SHEET 5 B 6 ALA A 83 PHE A 86 -1 N HIS A 84 O HIS A 97
SHEET 6 B 6 ALA B 7 LEU B 8 1 O LEU B 8 N ALA A 85
SHEET 1 C 2 TRP A 104 THR A 105 0
SHEET 2 C 2 TYR A 112 SER A 113 1 O TYR A 112 N THR A 105
LINK NE2 HIS A 69 ZN ZN A 416 1555 1555 2.01
LINK OD2 ASP A 71 ZN ZN A 416 1555 1555 2.02
LINK NE2 HIS A 84 ZN ZN A 416 1555 1555 2.04
LINK NE2 HIS A 120 ZN ZN A 415 1555 1555 2.05
LINK NE2 HIS A 130 ZN ZN A 415 1555 1555 2.08
LINK NE2 HIS A 124 ZN ZN A 415 1555 1555 2.11
LINK ND1 HIS A 97 ZN ZN A 416 1555 1555 2.13
LINK OD1 ASP B 6 ZN ZN A 415 1555 1555 2.17
LINK O LEU A 81 CA CA A 417 1555 1555 2.24
LINK O GLY A 77 CA CA A 417 1555 1555 2.27
LINK O GLY A 93 CA CA A 418 1555 1555 2.28
LINK O ASP A 79 CA CA A 417 1555 1555 2.28
LINK OD2 ASP A 99 CA CA A 417 1555 1555 2.29
LINK OD2 ASP B 6 ZN ZN A 415 1555 1555 2.30
LINK O GLU A 102 CA CA A 419 1555 1555 2.30
LINK O ASP A 59 CA CA A 418 1555 1555 2.33
LINK O GLY A 91 CA CA A 418 1555 1555 2.35
LINK O ASP A 100 CA CA A 419 1555 1555 2.35
LINK OE2 GLU A 102 CA CA A 417 1555 1555 2.35
LINK OD2 ASP A 25 CA CA A 419 1555 1555 2.36
LINK OD2 ASP A 76 CA CA A 417 1555 1555 2.39
LINK OD1 ASP A 100 CA CA A 419 1555 1555 2.43
LINK OD1 ASP A 95 CA CA A 418 1555 1555 2.43
LINK CA CA A 418 O HOH A 303 1555 1555 2.37
LINK CA CA A 418 O HOH A 212 1555 1555 2.40
LINK CA CA A 419 O HOH A 215 1555 1555 2.48
SITE 1 AC1 4 HIS A 120 HIS A 124 HIS A 130 ASP B 6
SITE 1 AC2 4 HIS A 69 ASP A 71 HIS A 84 HIS A 97
SITE 1 AC3 6 ASP A 76 GLY A 77 ASP A 79 LEU A 81
SITE 2 AC3 6 ASP A 99 GLU A 102
SITE 1 AC4 6 ASP A 59 GLY A 91 GLY A 93 ASP A 95
SITE 2 AC4 6 HOH A 212 HOH A 303
SITE 1 AC5 4 ASP A 25 ASP A 100 GLU A 102 HOH A 215
SITE 1 AC6 40 PHE A 4 ASP A 32 ARG A 52 HIS A 54
SITE 2 AC6 40 TYR A 73 ALA A 83 HIS A 84 ALA A 85
SITE 3 AC6 40 PHE A 86 ALA A 87 VAL A 92 GLY A 93
SITE 4 AC6 40 TYR A 112 HIS A 120 HIS A 124 HIS A 130
SITE 5 AC6 40 PRO A 140 ILE A 141 TYR A 142 ASN A 147
SITE 6 AC6 40 HOH A 208 HOH A 274 HOH A 280 HOH A 336
SITE 7 AC6 40 HOH A 345 HOH A 371 ZN A 415 HOH B 42
SITE 8 AC6 40 HOH B 46 HOH B 52 HOH B 79 HOH B 82
SITE 9 AC6 40 HOH B 104 HOH B 170 HOH B 178 HOH B 202
SITE 10 AC6 40 HOH B 226 HOH B 227 HOH B 264 HOH B 267
CRYST1 61.881 76.060 37.082 90.00 90.00 90.00 P 21 21 21 4
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 0.016160 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013148 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026967 0.00000
ATOM 1 N TYR A 1 12.613 1.466 -5.460 1.00 21.46 N
ANISOU 1 N TYR A 1 2376 2367 3411 -463 327 -101 N
ATOM 2 CA TYR A 1 11.468 0.714 -6.060 1.00 20.98 C
ANISOU 2 CA TYR A 1 2387 2353 3231 -417 345 -59 C
ATOM 3 C TYR A 1 11.510 0.833 -7.573 1.00 21.15 C
ANISOU 3 C TYR A 1 2434 2365 3237 -429 439 12 C
ATOM 4 O TYR A 1 12.119 1.757 -8.107 1.00 21.47 O
ANISOU 4 O TYR A 1 2456 2352 3350 -471 494 39 O
ATOM 5 CB TYR A 1 10.121 1.222 -5.526 1.00 20.62 C
ANISOU 5 CB TYR A 1 2410 2296 3129 -387 300 -63 C
ATOM 6 CG TYR A 1 9.913 2.713 -5.698 1.00 21.41 C
ANISOU 6 CG TYR A 1 2535 2320 3281 -413 317 -46 C
ATOM 7 CD1 TYR A 1 9.453 3.243 -6.904 1.00 21.61 C
ANISOU 7 CD1 TYR A 1 2609 2317 3286 -417 381 23 C
ATOM 8 CD2 TYR A 1 10.194 3.599 -4.656 1.00 22.04 C
ANISOU 8 CD2 TYR A 1 2595 2352 3429 -432 264 -101 C
ATOM 9 CE1 TYR A 1 9.277 4.614 -7.065 1.00 22.34 C
ANISOU 9 CE1 TYR A 1 2727 2331 3429 -440 396 43 C
ATOM 10 CE2 TYR A 1 10.021 4.970 -4.809 1.00 22.68 C
ANISOU 10 CE2 TYR A 1 2700 2354 3565 -457 278 -89 C
ATOM 11 CZ TYR A 1 9.562 5.472 -6.013 1.00 22.92 C
ANISOU 11 CZ TYR A 1 2776 2353 3579 -461 346 -14 C
ATOM 12 OH TYR A 1 9.387 6.834 -6.157 1.00 23.82 O
ANISOU 12 OH TYR A 1 2918 2382 3750 -483 359 3 O
ATOM 13 N ASN A 2 10.863 -0.110 -8.254 1.00 20.83 N
ANISOU 13 N ASN A 2 2438 2375 3103 -391 458 41 N
ATOM 14 CA ASN A 2 10.774 -0.089 -9.716 1.00 21.29 C
ANISOU 14 CA ASN A 2 2538 2431 3120 -390 540 107 C
ATOM 15 C ASN A 2 9.420 -0.586 -10.221 1.00 20.83 C
ANISOU 15 C ASN A 2 2560 2405 2949 -342 523 134 C
ATOM 16 O ASN A 2 8.688 -1.273 -9.498 1.00 20.10 O
ANISOU 16 O ASN A 2 2477 2348 2814 -311 458 102 O
ATOM 17 CB ASN A 2 11.874 -0.958 -10.327 1.00 21.68 C
ANISOU 17 CB ASN A 2 2539 2513 3185 -396 598 109 C
ATOM 18 CG ASN A 2 13.250 -0.363 -10.155 1.00 22.50 C
ANISOU 18 CG ASN A 2 2558 2580 3412 -448 635 96 C
ATOM 19 OD1 ASN A 2 13.560 0.680 -10.729 1.00 23.44 O
ANISOU 19 OD1 ASN A 2 2680 2645 3581 -485 697 137 O
ATOM 20 ND2 ASN A 2 14.088 -1.022 -9.365 1.00 22.60 N
ANISOU 20 ND2 ASN A 2 2491 2616 3478 -451 597 42 N
ATOM 21 N PHE A 3 9.123 -0.240 -11.475 1.00 21.08 N
ANISOU 21 N PHE A 3 2650 2423 2937 -337 581 194 N
ATOM 22 CA PHE A 3 7.893 -0.632 -12.162 1.00 20.74 C
ANISOU 22 CA PHE A 3 2682 2405 2791 -293 565 223 C
ATOM 23 C PHE A 3 8.227 -1.430 -13.420 1.00 21.06 C
ANISOU 23 C PHE A 3 2752 2481 2770 -276 624 253 C
ATOM 24 O PHE A 3 9.359 -1.403 -13.892 1.00 21.30 O
ANISOU 24 O PHE A 3 2751 2505 2838 -301 697 266 O
ATOM 25 CB PHE A 3 7.098 0.615 -12.561 1.00 20.91 C
ANISOU 25 CB PHE A 3 2764 2376 2804 -290 568 269 C
ATOM 26 CG PHE A 3 6.901 1.585 -11.434 1.00 20.79 C
ANISOU 26 CG PHE A 3 2726 2315 2858 -307 523 240 C
ATOM 27 CD1 PHE A 3 6.073 1.256 -10.366 1.00 19.98 C
ANISOU 27 CD1 PHE A 3 2616 2235 2740 -281 448 195 C
ATOM 28 CD2 PHE A 3 7.556 2.812 -11.426 1.00 21.40 C
ANISOU 28 CD2 PHE A 3 2790 2324 3018 -348 560 257 C
ATOM 29 CE1 PHE A 3 5.896 2.122 -9.311 1.00 19.97 C
ANISOU 29 CE1 PHE A 3 2599 2194 2793 -290 408 162 C
ATOM 30 CE2 PHE A 3 7.378 3.696 -10.373 1.00 21.40 C
ANISOU 30 CE2 PHE A 3 2773 2277 3080 -361 513 222 C
ATOM 31 CZ PHE A 3 6.542 3.349 -9.311 1.00 20.73 C
ANISOU 31 CZ PHE A 3 2687 2222 2970 -329 437 172 C
ATOM 32 N PHE A 4 7.229 -2.133 -13.951 1.00 21.02 N
ANISOU 32 N PHE A 4 2804 2510 2672 -234 594 261 N
ATOM 33 CA PHE A 4 7.345 -2.777 -15.257 1.00 21.87 C
ANISOU 33 CA PHE A 4 2961 2645 2702 -210 643 289 C
ATOM 34 C PHE A 4 7.440 -1.707 -16.346 1.00 23.09 C
ANISOU 34 C PHE A 4 3176 2761 2836 -215 711 357 C
ATOM 35 O PHE A 4 7.032 -0.558 -16.125 1.00 23.44 O
ANISOU 35 O PHE A 4 3237 2758 2911 -228 700 384 O
ATOM 36 CB PHE A 4 6.145 -3.696 -15.527 1.00 21.28 C
ANISOU 36 CB PHE A 4 2936 2609 2541 -164 578 276 C
ATOM 37 CG PHE A 4 6.125 -4.932 -14.674 1.00 20.63 C
ANISOU 37 CG PHE A 4 2805 2564 2470 -156 526 219 C
ATOM 38 CD1 PHE A 4 6.818 -6.067 -15.061 1.00 20.75 C
ANISOU 38 CD1 PHE A 4 2806 2611 2465 -145 553 197 C
ATOM 39 CD2 PHE A 4 5.403 -4.967 -13.489 1.00 20.08 C
ANISOU 39 CD2 PHE A 4 2706 2494 2429 -156 455 190 C
ATOM 40 CE1 PHE A 4 6.802 -7.208 -14.279 1.00 20.19 C
ANISOU 40 CE1 PHE A 4 2695 2568 2408 -136 506 150 C
ATOM 41 CE2 PHE A 4 5.383 -6.105 -12.705 1.00 19.70 C
ANISOU 41 CE2 PHE A 4 2620 2476 2388 -148 413 146 C
ATOM 42 CZ PHE A 4 6.083 -7.229 -13.101 1.00 19.69 C
ANISOU 42 CZ PHE A 4 2607 2503 2371 -139 436 127 C
ATOM 43 N PRO A 5 7.984 -2.071 -17.525 1.00 24.28 N
ANISOU 43 N PRO A 5 3365 2930 2931 -203 786 387 N
ATOM 44 CA PRO A 5 8.022 -1.137 -18.646 1.00 25.36 C
ANISOU 44 CA PRO A 5 3575 3033 3030 -201 857 461 C
ATOM 45 C PRO A 5 6.657 -0.536 -18.955 1.00 25.56 C
ANISOU 45 C PRO A 5 3680 3039 2991 -168 795 494 C
ATOM 46 O PRO A 5 5.676 -1.269 -19.046 1.00 25.16 O
ANISOU 46 O PRO A 5 3662 3024 2872 -127 721 469 O
ATOM 47 CB PRO A 5 8.488 -2.016 -19.812 1.00 25.87 C
ANISOU 47 CB PRO A 5 3683 3139 3008 -171 923 472 C
ATOM 48 CG PRO A 5 9.333 -3.043 -19.170 1.00 25.42 C
ANISOU 48 CG PRO A 5 3538 3116 3004 -183 927 411 C
ATOM 49 CD PRO A 5 8.655 -3.342 -17.861 1.00 24.29 C
ANISOU 49 CD PRO A 5 3346 2980 2905 -187 817 356 C
ATOM 50 N ARG A 6 6.618 0.784 -19.116 1.00 26.42 N
ANISOU 50 N ARG A 6 3818 3088 3133 -186 825 548 N
ATOM 51 CA ARG A 6 5.397 1.544 -19.402 1.00 26.95 C
ANISOU 51 CA ARG A 6 3959 3127 3155 -153 771 586 C
ATOM 52 C ARG A 6 4.417 1.627 -18.215 1.00 25.89 C
ANISOU 52 C ARG A 6 3784 2989 3065 -147 667 537 C
ATOM 53 O ARG A 6 3.273 2.066 -18.386 1.00 26.03 O
ANISOU 53 O ARG A 6 3852 2992 3046 -112 608 557 O
ATOM 54 CB ARG A 6 4.705 1.028 -20.671 1.00 27.97 C
ANISOU 54 CB ARG A 6 4188 3291 3149 -95 758 616 C
ATOM 55 CG ARG A 6 5.565 1.175 -21.926 1.00 29.48 C
ANISOU 55 CG ARG A 6 4442 3479 3281 -92 871 677 C
ATOM 56 CD ARG A 6 4.930 0.510 -23.128 1.00 30.38 C
ANISOU 56 CD ARG A 6 4658 3637 3250 -28 849 692 C
ATOM 57 NE ARG A 6 4.645 -0.893 -22.843 1.00 30.16 N
ANISOU 57 NE ARG A 6 4597 3670 3193 -9 784 616 N
ATOM 58 CZ ARG A 6 5.547 -1.876 -22.832 1.00 30.34 C
ANISOU 58 CZ ARG A 6 4577 3730 3221 -19 832 576 C
ATOM 59 NH1 ARG A 6 6.829 -1.642 -23.120 1.00 31.17 N
ANISOU 59 NH1 ARG A 6 4661 3825 3359 -49 952 603 N
ATOM 60 NH2 ARG A 6 5.159 -3.114 -22.538 1.00 29.81 N
ANISOU 60 NH2 ARG A 6 4485 3709 3132 0 762 508 N
ATOM 61 N LYS A 7 4.892 1.246 -17.023 1.00 24.58 N
ANISOU 61 N LYS A 7 3528 2834 2977 -179 647 476 N
ATOM 62 CA LYS A 7 4.136 1.364 -15.770 1.00 23.77 C
ANISOU 62 CA LYS A 7 3384 2727 2921 -177 565 429 C
ATOM 63 C LYS A 7 2.680 0.897 -15.876 1.00 23.01 C
ANISOU 63 C LYS A 7 3325 2661 2757 -126 484 421 C
ATOM 64 O LYS A 7 1.761 1.695 -15.689 1.00 22.87 O
ANISOU 64 O LYS A 7 3331 2612 2748 -107 444 436 O
ATOM 65 CB LYS A 7 4.178 2.807 -15.236 1.00 24.21 C
ANISOU 65 CB LYS A 7 3433 2709 3056 -202 571 445 C
ATOM 66 CG LYS A 7 5.567 3.286 -14.834 1.00 24.86 C
ANISOU 66 CG LYS A 7 3457 2756 3235 -261 632 437 C
ATOM 67 CD LYS A 7 5.593 4.766 -14.398 1.00 25.56 C
ANISOU 67 CD LYS A 7 3545 2760 3406 -288 636 453 C
ATOM 68 CE LYS A 7 5.062 4.978 -12.983 1.00 25.05 C
ANISOU 68 CE LYS A 7 3441 2687 3390 -284 557 388 C
ATOM 69 NZ LYS A 7 5.499 6.293 -12.391 1.00 25.67 N
ANISOU 69 NZ LYS A 7 3500 2682 3572 -323 565 382 N
ATOM 70 N PRO A 8 2.466 -0.397 -16.175 1.00 22.37 N
ANISOU 70 N PRO A 8 3246 2638 2616 -104 460 395 N
ATOM 71 CA PRO A 8 1.094 -0.910 -16.162 1.00 21.85 C
ANISOU 71 CA PRO A 8 3197 2598 2505 -63 379 380 C
ATOM 72 C PRO A 8 0.509 -0.877 -14.752 1.00 21.14 C
ANISOU 72 C PRO A 8 3048 2508 2478 -69 325 336 C
ATOM 73 O PRO A 8 1.231 -1.110 -13.772 1.00 20.52 O
ANISOU 73 O PRO A 8 2910 2433 2453 -99 338 299 O
ATOM 74 CB PRO A 8 1.243 -2.359 -16.656 1.00 21.72 C
ANISOU 74 CB PRO A 8 3185 2636 2431 -50 372 352 C
ATOM 75 CG PRO A 8 2.664 -2.723 -16.388 1.00 21.68 C
ANISOU 75 CG PRO A 8 3135 2638 2463 -85 438 334 C
ATOM 76 CD PRO A 8 3.438 -1.435 -16.572 1.00 22.35 C
ANISOU 76 CD PRO A 8 3228 2674 2591 -114 506 378 C
ATOM 77 N LYS A 9 -0.780 -0.568 -14.656 1.00 20.96 N
ANISOU 77 N LYS A 9 3040 2479 2447 -37 267 341 N
ATOM 78 CA LYS A 9 -1.489 -0.636 -13.384 1.00 20.65 C
ANISOU 78 CA LYS A 9 2947 2444 2455 -33 222 302 C
ATOM 79 C LYS A 9 -2.967 -0.915 -13.612 1.00 20.45 C
ANISOU 79 C LYS A 9 2932 2435 2403 8 156 304 C
ATOM 80 O LYS A 9 -3.459 -0.807 -14.737 1.00 20.56 O
ANISOU 80 O LYS A 9 2998 2447 2366 36 137 337 O
ATOM 81 CB LYS A 9 -1.278 0.636 -12.550 1.00 20.96 C
ANISOU 81 CB LYS A 9 2971 2432 2560 -49 238 301 C
ATOM 82 CG LYS A 9 -1.319 1.925 -13.329 1.00 21.94 C
ANISOU 82 CG LYS A 9 3149 2500 2686 -41 259 354 C
ATOM 83 CD LYS A 9 -2.662 2.594 -13.271 1.00 22.20 C
ANISOU 83 CD LYS A 9 3200 2511 2723 1 209 367 C
ATOM 84 CE LYS A 9 -2.917 3.295 -11.934 1.00 21.93 C
ANISOU 84 CE LYS A 9 3127 2448 2759 -1 197 330 C
ATOM 85 NZ LYS A 9 -4.382 3.404 -11.694 1.00 21.85 N
ANISOU 85 NZ LYS A 9 3110 2444 2750 47 143 325 N
ATOM 86 N TRP A 10 -3.648 -1.317 -12.546 1.00 19.90 N
ANISOU 86 N TRP A 10 2811 2383 2368 13 123 268 N
ATOM 87 CA TRP A 10 -5.082 -1.553 -12.592 1.00 20.43 C
ANISOU 87 CA TRP A 10 2867 2463 2433 48 64 266 C
ATOM 88 C TRP A 10 -5.773 -0.212 -12.774 1.00 21.15 C
ANISOU 88 C TRP A 10 2983 2511 2543 77 50 296 C
ATOM 89 O TRP A 10 -5.404 0.760 -12.120 1.00 20.75 O
ANISOU 89 O TRP A 10 2928 2423 2533 67 79 295 O
ATOM 90 CB TRP A 10 -5.559 -2.231 -11.309 1.00 19.76 C
ANISOU 90 CB TRP A 10 2718 2403 2387 43 50 225 C
ATOM 91 CG TRP A 10 -4.975 -3.600 -11.157 1.00 19.41 C
ANISOU 91 CG TRP A 10 2653 2395 2326 20 58 200 C
ATOM 92 CD1 TRP A 10 -4.053 -4.004 -10.243 1.00 18.99 C
ANISOU 92 CD1 TRP A 10 2573 2352 2290 -6 89 174 C
ATOM 93 CD2 TRP A 10 -5.255 -4.736 -11.982 1.00 19.49 C
ANISOU 93 CD2 TRP A 10 2673 2433 2300 26 28 197 C
ATOM 94 NE1 TRP A 10 -3.753 -5.336 -10.429 1.00 18.82 N
ANISOU 94 NE1 TRP A 10 2541 2361 2247 -16 84 159 N
ATOM 95 CE2 TRP A 10 -4.475 -5.805 -11.498 1.00 19.19 C
ANISOU 95 CE2 TRP A 10 2612 2418 2263 1 48 170 C
ATOM 96 CE3 TRP A 10 -6.101 -4.956 -13.075 1.00 19.89 C
ANISOU 96 CE3 TRP A 10 2751 2488 2317 52 -21 210 C
ATOM 97 CZ2 TRP A 10 -4.519 -7.076 -12.066 1.00 19.23 C
ANISOU 97 CZ2 TRP A 10 2620 2445 2240 1 26 156 C
ATOM 98 CZ3 TRP A 10 -6.141 -6.225 -13.642 1.00 19.93 C
ANISOU 98 CZ3 TRP A 10 2760 2518 2292 50 -47 191 C
ATOM 99 CH2 TRP A 10 -5.349 -7.263 -13.141 1.00 19.43 C
ANISOU 99 CH2 TRP A 10 2675 2474 2235 24 -21 165 C
ATOM 100 N ASP A 11 -6.765 -0.173 -13.659 1.00 22.29 N
ANISOU 100 N ASP A 11 3153 2656 2659 115 0 319 N
ATOM 101 CA ASP A 11 -7.468 1.073 -13.991 1.00 23.45 C
ANISOU 101 CA ASP A 11 3330 2760 2820 152 -22 353 C
ATOM 102 C ASP A 11 -8.633 1.375 -13.040 1.00 23.60 C
ANISOU 102 C ASP A 11 3292 2775 2900 178 -54 331 C
ATOM 103 O ASP A 11 -9.411 2.295 -13.283 1.00 23.83 O
ANISOU 103 O ASP A 11 3336 2771 2948 218 -82 354 O
ATOM 104 CB ASP A 11 -7.967 1.039 -15.442 1.00 24.61 C
ANISOU 104 CB ASP A 11 3538 2910 2903 188 -67 391 C
ATOM 105 CG ASP A 11 -8.986 -0.069 -15.697 1.00 25.08 C
ANISOU 105 CG ASP A 11 3566 3014 2950 209 -139 365 C
ATOM 106 OD1 ASP A 11 -9.457 -0.188 -16.849 1.00 26.32 O
ANISOU 106 OD1 ASP A 11 3771 3176 3053 242 -191 386 O
ATOM 107 OD2 ASP A 11 -9.313 -0.829 -14.756 1.00 25.10 O
ANISOU 107 OD2 ASP A 11 3498 3043 2998 192 -144 324 O
ATOM 108 N LYS A 12 -8.739 0.601 -11.963 1.00 23.14 N
ANISOU 108 N LYS A 12 3171 2747 2872 160 -45 288 N
ATOM 109 CA LYS A 12 -9.791 0.756 -10.967 1.00 23.20 C
ANISOU 109 CA LYS A 12 3121 2758 2936 184 -60 265 C
ATOM 110 C LYS A 12 -9.211 0.345 -9.612 1.00 21.90 C
ANISOU 110 C LYS A 12 2918 2610 2792 153 -15 226 C
ATOM 111 O LYS A 12 -8.218 -0.390 -9.568 1.00 20.91 O
ANISOU 111 O LYS A 12 2799 2505 2640 116 9 216 O
ATOM 112 CB LYS A 12 -10.961 -0.158 -11.324 1.00 24.19 C
ANISOU 112 CB LYS A 12 3206 2918 3066 205 -116 260 C
ATOM 113 CG LYS A 12 -10.608 -1.621 -11.130 1.00 24.66 C
ANISOU 113 CG LYS A 12 3239 3022 3110 169 -110 235 C
ATOM 114 CD LYS A 12 -11.310 -2.563 -12.089 1.00 25.70 C
ANISOU 114 CD LYS A 12 3364 3177 3223 178 -173 236 C
ATOM 115 CE LYS A 12 -10.542 -3.875 -12.183 1.00 25.64 C
ANISOU 115 CE LYS A 12 3360 3199 3184 141 -160 216 C
ATOM 116 NZ LYS A 12 -9.228 -3.672 -12.879 1.00 26.27 N
ANISOU 116 NZ LYS A 12 3509 3272 3202 125 -127 230 N
ATOM 117 N ASN A 13 -9.828 0.801 -8.523 1.00 21.17 N
ANISOU 117 N ASN A 13 2789 2509 2743 173 -3 205 N
ATOM 118 CA ASN A 13 -9.393 0.432 -7.165 1.00 20.48 C
ANISOU 118 CA ASN A 13 2675 2441 2668 153 35 168 C
ATOM 119 C ASN A 13 -10.073 -0.818 -6.587 1.00 19.95 C
ANISOU 119 C ASN A 13 2553 2421 2607 152 33 153 C
ATOM 120 O ASN A 13 -9.562 -1.404 -5.635 1.00 19.18 O
ANISOU 120 O ASN A 13 2442 2344 2501 132 62 130 O
ATOM 121 CB ASN A 13 -9.595 1.600 -6.197 1.00 20.82 C
ANISOU 121 CB ASN A 13 2717 2448 2744 178 57 148 C
ATOM 122 CG ASN A 13 -8.624 2.743 -6.450 1.00 21.10 C
ANISOU 122 CG ASN A 13 2804 2431 2783 164 69 154 C
ATOM 123 OD1 ASN A 13 -7.451 2.516 -6.722 1.00 20.98 O
ANISOU 123 OD1 ASN A 13 2810 2415 2747 124 84 156 O
ATOM 124 ND2 ASN A 13 -9.118 3.973 -6.375 1.00 21.35 N
ANISOU 124 ND2 ASN A 13 2850 2413 2848 198 66 157 N
ATOM 125 N GLN A 14 -11.235 -1.195 -7.127 1.00 20.20 N
ANISOU 125 N GLN A 14 2551 2464 2658 174 -3 167 N
ATOM 126 CA GLN A 14 -11.924 -2.425 -6.713 1.00 20.12 C
ANISOU 126 CA GLN A 14 2486 2493 2667 166 -6 158 C
ATOM 127 C GLN A 14 -11.451 -3.591 -7.593 1.00 19.30 C
ANISOU 127 C GLN A 14 2394 2408 2530 134 -33 163 C
ATOM 128 O GLN A 14 -11.789 -3.679 -8.780 1.00 19.58 O
ANISOU 128 O GLN A 14 2445 2441 2555 143 -83 178 O
ATOM 129 CB GLN A 14 -13.448 -2.261 -6.777 1.00 21.22 C
ANISOU 129 CB GLN A 14 2569 2631 2861 203 -32 165 C
ATOM 130 CG GLN A 14 -14.022 -1.112 -5.908 1.00 22.10 C
ANISOU 130 CG GLN A 14 2664 2721 3010 243 -1 156 C
ATOM 131 CD GLN A 14 -14.068 -1.391 -4.387 1.00 22.64 C
ANISOU 131 CD GLN A 14 2704 2809 3087 242 63 133 C
ATOM 132 OE1 GLN A 14 -14.226 -2.535 -3.941 1.00 22.90 O
ANISOU 132 OE1 GLN A 14 2703 2874 3124 220 81 132 O
ATOM 133 NE2 GLN A 14 -13.958 -0.316 -3.586 1.00 23.30 N
ANISOU 133 NE2 GLN A 14 2809 2871 3174 270 97 115 N
ATOM 134 N ILE A 15 -10.648 -4.467 -7.002 1.00 18.15 N
ANISOU 134 N ILE A 15 2249 2283 2365 103 -4 149 N
ATOM 135 CA ILE A 15 -10.009 -5.566 -7.714 1.00 17.66 C
ANISOU 135 CA ILE A 15 2204 2235 2270 74 -21 148 C
ATOM 136 C ILE A 15 -10.562 -6.877 -7.172 1.00 17.16 C
ANISOU 136 C ILE A 15 2091 2194 2233 60 -21 140 C
ATOM 137 O ILE A 15 -10.683 -7.040 -5.960 1.00 17.24 O
ANISOU 137 O ILE A 15 2076 2214 2263 59 18 135 O
ATOM 138 CB ILE A 15 -8.453 -5.515 -7.516 1.00 17.38 C
ANISOU 138 CB ILE A 15 2208 2198 2196 49 13 140 C
ATOM 139 CG1 ILE A 15 -7.909 -4.143 -7.955 1.00 17.59 C
ANISOU 139 CG1 ILE A 15 2278 2195 2211 58 23 151 C
ATOM 140 CG2 ILE A 15 -7.753 -6.643 -8.301 1.00 17.13 C
ANISOU 140 CG2 ILE A 15 2196 2182 2132 26 1 136 C
ATOM 141 CD1 ILE A 15 -6.796 -3.605 -7.095 1.00 17.55 C
ANISOU 141 CD1 ILE A 15 2285 2178 2205 42 62 135 C
ATOM 142 N THR A 16 -10.917 -7.804 -8.060 1.00 16.73 N
ANISOU 142 N THR A 16 2030 2146 2182 50 -65 140 N
ATOM 143 CA THR A 16 -11.394 -9.113 -7.626 1.00 16.33 C
ANISOU 143 CA THR A 16 1934 2106 2165 30 -66 134 C
ATOM 144 C THR A 16 -10.256 -10.122 -7.667 1.00 15.81 C
ANISOU 144 C THR A 16 1898 2047 2062 3 -55 123 C
ATOM 145 O THR A 16 -9.314 -9.993 -8.467 1.00 15.51 O
ANISOU 145 O THR A 16 1909 2007 1976 0 -63 118 O
ATOM 146 CB THR A 16 -12.569 -9.638 -8.482 1.00 16.70 C
ANISOU 146 CB THR A 16 1943 2150 2253 34 -129 132 C
ATOM 147 OG1 THR A 16 -12.198 -9.648 -9.866 1.00 16.57 O
ANISOU 147 OG1 THR A 16 1978 2128 2189 39 -182 126 O
ATOM 148 CG2 THR A 16 -13.810 -8.779 -8.287 1.00 17.02 C
ANISOU 148 CG2 THR A 16 1935 2185 2348 63 -140 142 C
ATOM 149 N TYR A 17 -10.337 -11.111 -6.780 1.00 15.51 N
ANISOU 149 N TYR A 17 1830 2015 2050 -15 -30 122 N
ATOM 150 CA TYR A 17 -9.484 -12.281 -6.856 1.00 15.30 C
ANISOU 150 CA TYR A 17 1822 1988 2002 -37 -29 112 C
ATOM 151 C TYR A 17 -10.284 -13.558 -6.697 1.00 15.63 C
ANISOU 151 C TYR A 17 1822 2022 2096 -56 -43 114 C
ATOM 152 O TYR A 17 -11.400 -13.545 -6.173 1.00 15.90 O
ANISOU 152 O TYR A 17 1803 2053 2183 -55 -35 127 O
ATOM 153 CB TYR A 17 -8.329 -12.228 -5.850 1.00 14.87 C
ANISOU 153 CB TYR A 17 1790 1942 1917 -40 18 111 C
ATOM 154 CG TYR A 17 -8.661 -12.402 -4.373 1.00 14.87 C
ANISOU 154 CG TYR A 17 1764 1948 1937 -37 62 123 C
ATOM 155 CD1 TYR A 17 -8.542 -13.648 -3.751 1.00 14.99 C
ANISOU 155 CD1 TYR A 17 1770 1962 1962 -52 76 131 C
ATOM 156 CD2 TYR A 17 -9.017 -11.309 -3.584 1.00 14.98 C
ANISOU 156 CD2 TYR A 17 1772 1968 1951 -17 91 128 C
ATOM 157 CE1 TYR A 17 -8.798 -13.801 -2.376 1.00 15.10 C
ANISOU 157 CE1 TYR A 17 1773 1983 1981 -45 122 148 C
ATOM 158 CE2 TYR A 17 -9.279 -11.451 -2.212 1.00 15.13 C
ANISOU 158 CE2 TYR A 17 1778 1996 1974 -8 136 138 C
ATOM 159 CZ TYR A 17 -9.168 -12.694 -1.618 1.00 15.15 C
ANISOU 159 CZ TYR A 17 1775 2000 1980 -22 153 151 C
ATOM 160 OH TYR A 17 -9.420 -12.833 -0.263 1.00 15.60 O
ANISOU 160 OH TYR A 17 1831 2067 2030 -9 203 166 O
ATOM 161 N ARG A 18 -9.707 -14.651 -7.184 1.00 15.72 N
ANISOU 161 N ARG A 18 1854 2025 2095 -73 -63 100 N
ATOM 162 CA ARG A 18 -10.305 -15.981 -7.060 1.00 16.34 C
ANISOU 162 CA ARG A 18 1898 2085 2227 -96 -78 100 C
ATOM 163 C ARG A 18 -9.224 -17.049 -6.875 1.00 16.08 C
ANISOU 163 C ARG A 18 1896 2044 2171 -108 -64 92 C
ATOM 164 O ARG A 18 -8.250 -17.085 -7.621 1.00 15.83 O
ANISOU 164 O ARG A 18 1910 2015 2090 -101 -78 71 O
ATOM 165 CB ARG A 18 -11.122 -16.306 -8.302 1.00 17.00 C
ANISOU 165 CB ARG A 18 1968 2154 2337 -100 -149 80 C
ATOM 166 CG ARG A 18 -11.828 -17.643 -8.225 1.00 17.57 C
ANISOU 166 CG ARG A 18 1998 2199 2480 -129 -171 75 C
ATOM 167 CD ARG A 18 -12.642 -17.891 -9.467 1.00 18.38 C
ANISOU 167 CD ARG A 18 2087 2286 2611 -131 -255 47 C
ATOM 168 NE ARG A 18 -13.209 -19.233 -9.454 1.00 19.01 N
ANISOU 168 NE ARG A 18 2128 2330 2765 -164 -282 36 N
ATOM 169 CZ ARG A 18 -13.640 -19.881 -10.532 1.00 19.88 C
ANISOU 169 CZ ARG A 18 2238 2418 2898 -172 -364 -2 C
ATOM 170 NH1 ARG A 18 -13.583 -19.317 -11.739 1.00 20.22 N
ANISOU 170 NH1 ARG A 18 2325 2475 2884 -145 -426 -30 N
ATOM 171 NH2 ARG A 18 -14.132 -21.106 -10.403 1.00 20.59 N
ANISOU 171 NH2 ARG A 18 2290 2467 3067 -207 -384 -12 N
ATOM 172 N ILE A 19 -9.415 -17.914 -5.882 1.00 16.15 N
ANISOU 172 N ILE A 19 1881 2039 2215 -123 -34 111 N
ATOM 173 CA ILE A 19 -8.493 -19.004 -5.608 1.00 16.12 C
ANISOU 173 CA ILE A 19 1903 2021 2199 -130 -24 108 C
ATOM 174 C ILE A 19 -9.051 -20.245 -6.304 1.00 16.86 C
ANISOU 174 C ILE A 19 1981 2078 2345 -154 -68 93 C
ATOM 175 O ILE A 19 -10.065 -20.812 -5.879 1.00 17.18 O
ANISOU 175 O ILE A 19 1976 2096 2454 -175 -63 112 O
ATOM 176 CB ILE A 19 -8.309 -19.221 -4.089 1.00 16.00 C
ANISOU 176 CB ILE A 19 1884 2009 2185 -128 33 142 C
ATOM 177 CG1 ILE A 19 -7.798 -17.933 -3.419 1.00 15.57 C
ANISOU 177 CG1 ILE A 19 1847 1988 2080 -104 65 146 C
ATOM 178 CG2 ILE A 19 -7.357 -20.382 -3.818 1.00 15.71 C
ANISOU 178 CG2 ILE A 19 1877 1954 2139 -131 36 141 C
ATOM 179 CD1 ILE A 19 -8.067 -17.862 -1.908 1.00 15.62 C
ANISOU 179 CD1 ILE A 19 1846 2002 2085 -94 120 178 C
ATOM 180 N ILE A 20 -8.397 -20.626 -7.397 1.00 17.17 N
ANISOU 180 N ILE A 20 2059 2110 2354 -149 -108 58 N
ATOM 181 CA ILE A 20 -8.877 -21.679 -8.288 1.00 18.17 C
ANISOU 181 CA ILE A 20 2183 2202 2520 -165 -164 29 C
ATOM 182 C ILE A 20 -8.469 -23.067 -7.802 1.00 18.42 C
ANISOU 182 C ILE A 20 2220 2195 2584 -180 -152 32 C
ATOM 183 O ILE A 20 -9.126 -24.057 -8.111 1.00 19.17 O
ANISOU 183 O ILE A 20 2296 2248 2741 -204 -188 19 O
ATOM 184 CB ILE A 20 -8.298 -21.507 -9.713 1.00 18.61 C
ANISOU 184 CB ILE A 20 2290 2266 2515 -146 -209 -15 C
ATOM 185 CG1 ILE A 20 -8.740 -20.168 -10.320 1.00 19.10 C
ANISOU 185 CG1 ILE A 20 2355 2359 2544 -129 -227 -14 C
ATOM 186 CG2 ILE A 20 -8.716 -22.680 -10.610 1.00 19.39 C
ANISOU 186 CG2 ILE A 20 2395 2325 2648 -159 -272 -55 C
ATOM 187 CD1 ILE A 20 -10.229 -20.026 -10.466 1.00 19.54 C
ANISOU 187 CD1 ILE A 20 2357 2404 2664 -141 -270 -10 C
ATOM 188 N GLY A 21 -7.365 -23.149 -7.071 1.00 17.76 N
ANISOU 188 N GLY A 21 2163 2121 2461 -165 -108 47 N
ATOM 189 CA GLY A 21 -6.908 -24.431 -6.594 1.00 17.94 C
ANISOU 189 CA GLY A 21 2198 2106 2511 -172 -99 53 C
ATOM 190 C GLY A 21 -6.070 -24.293 -5.350 1.00 17.58 C
ANISOU 190 C GLY A 21 2167 2079 2435 -154 -46 88 C
ATOM 191 O GLY A 21 -5.659 -23.183 -4.967 1.00 17.25 O
ANISOU 191 O GLY A 21 2129 2079 2345 -137 -21 96 O
ATOM 192 N TYR A 22 -5.780 -25.441 -4.753 1.00 17.68 N
ANISOU 192 N TYR A 22 2189 2054 2475 -157 -36 105 N
ATOM 193 CA TYR A 22 -5.160 -25.500 -3.447 1.00 17.67 C
ANISOU 193 CA TYR A 22 2202 2061 2450 -140 7 145 C
ATOM 194 C TYR A 22 -3.927 -26.409 -3.427 1.00 18.02 C
ANISOU 194 C TYR A 22 2282 2084 2480 -117 -4 132 C
ATOM 195 O TYR A 22 -3.677 -27.184 -4.364 1.00 18.16 O
ANISOU 195 O TYR A 22 2312 2070 2518 -118 -37 96 O
ATOM 196 CB TYR A 22 -6.208 -25.955 -2.428 1.00 17.97 C
ANISOU 196 CB TYR A 22 2215 2074 2538 -161 43 199 C
ATOM 197 CG TYR A 22 -7.176 -24.843 -2.089 1.00 17.79 C
ANISOU 197 CG TYR A 22 2158 2086 2517 -169 70 217 C
ATOM 198 CD1 TYR A 22 -8.329 -24.631 -2.854 1.00 17.89 C
ANISOU 198 CD1 TYR A 22 2126 2091 2583 -195 47 203 C
ATOM 199 CD2 TYR A 22 -6.915 -23.960 -1.032 1.00 17.44 C
ANISOU 199 CD2 TYR A 22 2125 2083 2419 -145 113 242 C
ATOM 200 CE1 TYR A 22 -9.204 -23.592 -2.555 1.00 17.75 C
ANISOU 200 CE1 TYR A 22 2071 2104 2570 -196 71 218 C
ATOM 201 CE2 TYR A 22 -7.788 -22.922 -0.731 1.00 17.24 C
ANISOU 201 CE2 TYR A 22 2069 2086 2394 -146 140 254 C
ATOM 202 CZ TYR A 22 -8.928 -22.741 -1.495 1.00 17.40 C
ANISOU 202 CZ TYR A 22 2041 2097 2472 -170 121 243 C
ATOM 203 OH TYR A 22 -9.796 -21.708 -1.203 1.00 17.27 O
ANISOU 203 OH TYR A 22 1991 2109 2463 -166 148 254 O
ATOM 204 N THR A 23 -3.157 -26.271 -2.351 1.00 17.96 N
ANISOU 204 N THR A 23 2292 2094 2436 -91 22 159 N
ATOM 205 CA THR A 23 -2.024 -27.131 -2.062 1.00 18.10 C
ANISOU 205 CA THR A 23 2339 2092 2446 -63 13 157 C
ATOM 206 C THR A 23 -2.389 -28.134 -0.956 1.00 18.77 C
ANISOU 206 C THR A 23 2437 2133 2560 -65 34 213 C
ATOM 207 O THR A 23 -3.102 -27.782 -0.014 1.00 18.79 O
ANISOU 207 O THR A 23 2433 2148 2556 -73 70 259 O
ATOM 208 CB THR A 23 -0.789 -26.296 -1.619 1.00 17.66 C
ANISOU 208 CB THR A 23 2294 2085 2332 -28 17 145 C
ATOM 209 OG1 THR A 23 0.255 -27.170 -1.181 1.00 17.68 O
ANISOU 209 OG1 THR A 23 2318 2066 2333 3 5 149 O
ATOM 210 CG2 THR A 23 -1.143 -25.318 -0.493 1.00 17.51 C
ANISOU 210 CG2 THR A 23 2272 2104 2278 -24 46 179 C
ATOM 211 N PRO A 24 -1.871 -29.379 -1.049 1.00 19.33 N
ANISOU 211 N PRO A 24 2530 2153 2662 -54 16 213 N
ATOM 212 CA PRO A 24 -2.019 -30.337 0.057 1.00 19.88 C
ANISOU 212 CA PRO A 24 2623 2178 2751 -48 37 273 C
ATOM 213 C PRO A 24 -1.206 -29.966 1.303 1.00 19.67 C
ANISOU 213 C PRO A 24 2625 2187 2660 -5 51 307 C
ATOM 214 O PRO A 24 -1.366 -30.603 2.351 1.00 20.23 O
ANISOU 214 O PRO A 24 2726 2231 2731 6 74 366 O
ATOM 215 CB PRO A 24 -1.481 -31.645 -0.536 1.00 20.42 C
ANISOU 215 CB PRO A 24 2711 2183 2866 -39 4 251 C
ATOM 216 CG PRO A 24 -0.488 -31.208 -1.570 1.00 19.98 C
ANISOU 216 CG PRO A 24 2652 2161 2781 -16 -27 181 C
ATOM 217 CD PRO A 24 -1.062 -29.939 -2.151 1.00 19.52 C
ANISOU 217 CD PRO A 24 2564 2157 2697 -39 -21 156 C
ATOM 218 N ASP A 25 -0.349 -28.953 1.193 1.00 18.90 N
ANISOU 218 N ASP A 25 2523 2148 2509 20 37 269 N
ATOM 219 CA ASP A 25 0.600 -28.617 2.258 1.00 18.87 C
ANISOU 219 CA ASP A 25 2544 2177 2448 64 31 284 C
ATOM 220 C ASP A 25 -0.042 -27.954 3.469 1.00 19.01 C
ANISOU 220 C ASP A 25 2578 2224 2419 67 68 331 C
ATOM 221 O ASP A 25 0.473 -28.074 4.584 1.00 18.92 O
ANISOU 221 O ASP A 25 2605 2223 2363 105 65 362 O
ATOM 222 CB ASP A 25 1.693 -27.680 1.726 1.00 18.19 C
ANISOU 222 CB ASP A 25 2439 2140 2333 83 4 226 C
ATOM 223 CG ASP A 25 2.483 -28.293 0.588 1.00 18.19 C
ANISOU 223 CG ASP A 25 2426 2118 2368 91 -23 178 C
ATOM 224 OD1 ASP A 25 2.377 -29.523 0.377 1.00 18.36 O
ANISOU 224 OD1 ASP A 25 2463 2083 2431 92 -30 188 O
ATOM 225 OD2 ASP A 25 3.203 -27.537 -0.100 1.00 17.61 O
ANISOU 225 OD2 ASP A 25 2329 2079 2282 96 -32 131 O
ATOM 226 N LEU A 26 -1.143 -27.244 3.236 1.00 18.93 N
ANISOU 226 N LEU A 26 2541 2231 2419 32 99 333 N
ATOM 227 CA LEU A 26 -1.816 -26.456 4.272 1.00 19.29 C
ANISOU 227 CA LEU A 26 2597 2311 2422 37 141 368 C
ATOM 228 C LEU A 26 -3.342 -26.645 4.182 1.00 19.98 C
ANISOU 228 C LEU A 26 2657 2374 2560 -5 189 403 C
ATOM 229 O LEU A 26 -3.873 -27.011 3.120 1.00 19.66 O
ANISOU 229 O LEU A 26 2580 2304 2586 -42 176 383 O
ATOM 230 CB LEU A 26 -1.453 -24.972 4.103 1.00 18.72 C
ANISOU 230 CB LEU A 26 2509 2296 2307 45 128 321 C
ATOM 231 CG LEU A 26 -0.017 -24.491 4.405 1.00 18.47 C
ANISOU 231 CG LEU A 26 2495 2297 2227 84 86 286 C
ATOM 232 CD1 LEU A 26 0.220 -23.064 3.881 1.00 17.98 C
ANISOU 232 CD1 LEU A 26 2405 2276 2151 75 75 235 C
ATOM 233 CD2 LEU A 26 0.292 -24.557 5.884 1.00 18.88 C
ANISOU 233 CD2 LEU A 26 2596 2361 2216 126 89 321 C
ATOM 234 N ASP A 27 -4.030 -26.406 5.302 1.00 20.72 N
ANISOU 234 N ASP A 27 2767 2480 2624 3 243 454 N
ATOM 235 CA ASP A 27 -5.494 -26.386 5.358 1.00 21.45 C
ANISOU 235 CA ASP A 27 2823 2560 2767 -33 300 489 C
ATOM 236 C ASP A 27 -5.984 -25.283 4.411 1.00 20.26 C
ANISOU 236 C ASP A 27 2620 2440 2636 -55 284 437 C
ATOM 237 O ASP A 27 -5.349 -24.233 4.331 1.00 19.53 O
ANISOU 237 O ASP A 27 2535 2393 2491 -33 261 396 O
ATOM 238 CB ASP A 27 -5.952 -26.083 6.804 1.00 22.90 C
ANISOU 238 CB ASP A 27 3042 2767 2893 -7 368 546 C
ATOM 239 CG ASP A 27 -7.450 -26.287 7.027 1.00 24.32 C
ANISOU 239 CG ASP A 27 3181 2925 3134 -42 442 596 C
ATOM 240 OD1 ASP A 27 -8.303 -25.560 6.445 1.00 25.07 O
ANISOU 240 OD1 ASP A 27 3217 3037 3272 -68 452 571 O
ATOM 241 OD2 ASP A 27 -7.791 -27.165 7.855 1.00 26.69 O
ANISOU 241 OD2 ASP A 27 3509 3191 3440 -42 496 666 O
ATOM 242 N PRO A 28 -7.102 -25.512 3.690 1.00 20.10 N
ANISOU 242 N PRO A 28 2546 2394 2698 -99 293 439 N
ATOM 243 CA PRO A 28 -7.606 -24.467 2.769 1.00 19.55 C
ANISOU 243 CA PRO A 28 2430 2352 2646 -114 272 393 C
ATOM 244 C PRO A 28 -7.888 -23.133 3.460 1.00 19.26 C
ANISOU 244 C PRO A 28 2393 2368 2557 -89 308 394 C
ATOM 245 O PRO A 28 -7.668 -22.074 2.867 1.00 18.28 O
ANISOU 245 O PRO A 28 2260 2275 2412 -82 279 349 O
ATOM 246 CB PRO A 28 -8.903 -25.065 2.198 1.00 20.05 C
ANISOU 246 CB PRO A 28 2434 2375 2810 -160 279 407 C
ATOM 247 CG PRO A 28 -9.119 -26.375 2.904 1.00 20.84 C
ANISOU 247 CG PRO A 28 2548 2423 2949 -174 316 464 C
ATOM 248 CD PRO A 28 -7.831 -26.785 3.536 1.00 20.69 C
ANISOU 248 CD PRO A 28 2599 2405 2859 -136 308 475 C
ATOM 249 N GLU A 29 -8.355 -23.193 4.709 1.00 19.73 N
ANISOU 249 N GLU A 29 2470 2434 2594 -74 375 446 N