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1906 lines (1906 loc) · 153 KB
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HEADER CELL ADHESION 31-JAN-03 1OBY
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH
TITLE 2 A SYNDECAN-4 PEPTIDE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNTENIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PDZ2, RESIDUES 197-270;
COMPND 5 SYNONYM: SYNDECAN BINDING PROTEIN 1, MELANOMA
COMPND 6 DIFFERENTIATION ASSOCIATED PROTEIN-9, MDA-9, SCAFFOLD
COMPND 7 PROTEIN PBP1, TACIP18, PRO-TGF-ALPHA CYTOPLASMIC
COMPND 8 DOMAIN-INTERACTING PROTEIN 18;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: SYNDECAN-4;
COMPND 12 CHAIN: P, Q;
COMPND 13 FRAGMENT: LAST 6 RESIDUES, RESIDUES 193-198;
COMPND 14 SYNONYM: AMPHIGLYCAN, SYND4, RYUDOCAN CORE PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ATCC: 72537;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PGST-PARALLEL1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS CELL ADHESION, ADHESION/COMPLEX, PDZ DOMAIN, SIGNAL
KEYWDS 2 TRANSDUCTION, NUCLEAR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.S.KANG,D.R.COOPER,Y.DEVEDJIEV,U.DEREWENDA,Z.S.DEREWENDA
REVDAT 3 24-FEB-09 1OBY 1 VERSN
REVDAT 2 14-OCT-03 1OBY 1 TITLE
REVDAT 1 11-JUL-03 1OBY 0
JRNL AUTH B.S.KANG,D.R.COOPER,Y.DEVEDJIEV,U.DEREWENDA,
JRNL AUTH 2 Z.S.DEREWENDA
JRNL TITL MOLECULAR ROOTS OF DEGENERATE SPECIFICITY IN
JRNL TITL 2 SYNTENIN'S PDZ2 DOMAIN: REASSESSMENT OF THE PDZ
JRNL TITL 3 RECOGNITION PARADIGM
JRNL REF STRUCTURE V. 11 845 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12842047
JRNL DOI 10.1016/S0969-2126(03)00125-4
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 12001
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 985
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 739
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.05000
REMARK 3 B22 (A**2) : 0.44000
REMARK 3 B33 (A**2) : -1.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.68000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.155
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.147
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.645
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1235 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1118 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1663 ; 1.815 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2610 ; 0.941 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 156 ; 5.762 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 205 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1342 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 222 ; 0.015 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 227 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1273 ; 0.257 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 732 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 96 ; 0.247 ; 0.200
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): 28 ; 0.668 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 72 ; 0.366 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.251 ; 0.200
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): 787 ; 1.120 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1275 ; 2.005 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 448 ; 3.160 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 388 ; 5.005 ; 4.500
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 : 2
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 197 A 270
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5350 0.0330 11.4090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0839 T22: 0.1013
REMARK 3 T33: 0.0164 T12: 0.0029
REMARK 3 T13: -0.0046 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 1.3204 L22: 2.7056
REMARK 3 L33: 4.8398 L12: 0.5960
REMARK 3 L13: -1.7543 L23: -0.6148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: -0.0468 S13: -0.0891
REMARK 3 S21: -0.1466 S22: -0.0233 S23: -0.0417
REMARK 3 S31: -0.1767 S32: 0.1682 S33: 0.0705
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 197 B 270
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8390 30.5630 12.2190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1082 T22: 0.1033
REMARK 3 T33: 0.0164 T12: -0.0029
REMARK 3 T13: 0.0412 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.1031 L22: 1.8190
REMARK 3 L33: 4.9443 L12: -0.6378
REMARK 3 L13: 1.2035 L23: -0.6651
REMARK 3 S TENSOR
REMARK 3 S11: -0.0677 S12: -0.0325 S13: 0.0211
REMARK 3 S21: 0.0309 S22: -0.1043 S23: -0.0475
REMARK 3 S31: 0.2779 S32: 0.0963 S33: 0.1720
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS 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 ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1OBY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-03.
REMARK 100 THE PDBE ID CODE IS EBI-12083.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46421
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.570
REMARK 200 R MERGE (I) : 0.49000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1N99
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP WITH 0.1 M HEPES,
REMARK 280 PH 6.8, 1.6 M AMMONIUM SULFATE, 20 MM COCL2, AND 0.2 MGSO4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 29.16850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.22050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 29.16850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.22050
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 GENERATING THE BIOMOLECULE
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, Q
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH A2034 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 MOL_ID 1: FUNCTIONS AS AN ADAPTER PROTEIN.
REMARK 400 MAY ALSO FUNCTION TO COUPLE SYNDECANS TO CYTOSKELETAL
REMARK 400 TRANSCRIPTION PROTEINS OR SIGNALING COMPONENTS. ALSO SEEMS
REMARK 400 TO COUPLE FACTOR SOX4 TO THE IL-5 RECEPTOR (IL5RA)
REMARK 400
REMARK 400 MOL_ID 2: CELL SURFACE PROTEOGLYCAN CONTAINING HEPARAN
REMARK 400 SULFATE
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 GLY A 192
REMARK 465 ALA A 193
REMARK 465 MET A 194
REMARK 465 ASP A 195
REMARK 465 GLY B 192
REMARK 465 ALA B 193
REMARK 465 MET B 194
REMARK 465 ASP B 195
REMARK 465 PRO B 196
REMARK 465 THR P 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2003 - O HOH A 2055 2.16
REMARK 500 O HOH B 2003 - O HOH B 2063 2.15
REMARK 500 O HOH B 2015 - O HOH B 2039 2.07
REMARK 500 O HOH B 2025 - O HOH B 2060 1.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 O1 SO4 A 1271 O3 SO4 A 1271 2555 1.53
REMARK 500 O2 SO4 A 1271 O4 SO4 A 1271 2555 1.31
REMARK 500 O3 SO4 A 1271 O1 SO4 A 1271 2555 1.53
REMARK 500 O3 SO4 A 1271 O3 SO4 A 1271 2555 1.67
REMARK 500 O3 SO4 A 1271 O4 SO4 A 1271 2555 2.16
REMARK 500 O4 SO4 A 1271 O2 SO4 A 1271 2555 1.31
REMARK 500 O4 SO4 A 1271 O3 SO4 A 1271 2555 2.16
REMARK 500 O4 SO4 A 1271 O4 SO4 A 1271 2555 1.26
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 229 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 224 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1271
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NTE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE SECOND PDZ
REMARK 900 DOMAIN OF SYNTENIN
REMARK 900 RELATED ID: 1OBX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2
REMARK 900 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR
REMARK 900 ALPHA PEPTIDE.
REMARK 900 RELATED ID: 1OBZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ TANDEM
REMARK 900 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR
REMARK 900 ALPHA PEPTIDE
REMARK 900 RELATED ID: 1EJP RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE SYNDECAN-4 WHOLE
REMARK 900 CYTOPLASMICDOMAIN
REMARK 900 RELATED ID: 1EJQ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE SYNDECAN-4 WHOLE
REMARK 900 CYTOPLASMIC DOMAIN IN THE PRESENCE OF
REMARK 900 PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE
DBREF 1OBY A 192 196 PDB 1OBY 1OBY 192 196
DBREF 1OBY A 197 270 UNP O00560 SDB1_HUMAN 197 270
DBREF 1OBY B 192 196 PDB 1OBY 1OBY 192 196
DBREF 1OBY B 197 270 UNP O00560 SDB1_HUMAN 197 270
DBREF 1OBY P 1 6 UNP P31431 SDC4_HUMAN 193 198
DBREF 1OBY Q 1 6 UNP P31431 SDC4_HUMAN 193 198
SEQRES 1 A 79 GLY ALA MET ASP PRO ARG THR ILE THR MET HIS LYS ASP
SEQRES 2 A 79 SER THR GLY HIS VAL GLY PHE ILE PHE LYS ASN GLY LYS
SEQRES 3 A 79 ILE THR SER ILE VAL LYS ASP SER SER ALA ALA ARG ASN
SEQRES 4 A 79 GLY LEU LEU THR GLU HIS ASN ILE CYS GLU ILE ASN GLY
SEQRES 5 A 79 GLN ASN VAL ILE GLY LEU LYS ASP SER GLN ILE ALA ASP
SEQRES 6 A 79 ILE LEU SER THR SER GLY THR VAL VAL THR ILE THR ILE
SEQRES 7 A 79 MET
SEQRES 1 B 79 GLY ALA MET ASP PRO ARG THR ILE THR MET HIS LYS ASP
SEQRES 2 B 79 SER THR GLY HIS VAL GLY PHE ILE PHE LYS ASN GLY LYS
SEQRES 3 B 79 ILE THR SER ILE VAL LYS ASP SER SER ALA ALA ARG ASN
SEQRES 4 B 79 GLY LEU LEU THR GLU HIS ASN ILE CYS GLU ILE ASN GLY
SEQRES 5 B 79 GLN ASN VAL ILE GLY LEU LYS ASP SER GLN ILE ALA ASP
SEQRES 6 B 79 ILE LEU SER THR SER GLY THR VAL VAL THR ILE THR ILE
SEQRES 7 B 79 MET
SEQRES 1 P 6 THR ASN GLU PHE TYR ALA
SEQRES 1 Q 6 THR ASN GLU PHE TYR ALA
HET SO4 A1271 5
HET SO4 A1272 5
HET SO4 B1271 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 8 HOH *145(H2 O1)
HELIX 1 1 SER A 225 GLY A 231 1 7
HELIX 2 2 LYS A 250 SER A 261 1 12
HELIX 3 3 SER B 225 GLY B 231 1 7
HELIX 4 4 LYS B 250 SER B 261 1 12
SHEET 1 AA 4 ARG A 197 HIS A 202 0
SHEET 2 AA 4 VAL A 264 MET A 270 -1 O VAL A 265 N MET A 201
SHEET 3 AA 4 ASN A 237 ILE A 241 -1 O ASN A 237 N MET A 270
SHEET 4 AA 4 GLN A 244 ASN A 245 -1 O GLN A 244 N ILE A 241
SHEET 1 AB 3 LYS A 217 ILE A 221 0
SHEET 2 AB 3 PHE A 211 LYS A 214 -1 O ILE A 212 N THR A 219
SHEET 3 AB 3 PHE P 4 ALA P 6 -1 O PHE P 4 N PHE A 213
SHEET 1 BA 6 THR B 198 HIS B 202 0
SHEET 2 BA 6 VAL B 264 MET B 270 -1 O VAL B 265 N MET B 201
SHEET 3 BA 6 HIS B 236 ILE B 241 -1 O ASN B 237 N MET B 270
SHEET 4 BA 6 LYS B 217 ILE B 221 -1 N ILE B 218 O HIS B 236
SHEET 5 BA 6 PHE B 211 LYS B 214 -1 O ILE B 212 N THR B 219
SHEET 6 BA 6 PHE Q 4 ALA Q 6 -1 O PHE Q 4 N PHE B 213
SHEET 1 BB 4 THR B 198 HIS B 202 0
SHEET 2 BB 4 VAL B 264 MET B 270 -1 O VAL B 265 N MET B 201
SHEET 3 BB 4 HIS B 236 ILE B 241 -1 O ASN B 237 N MET B 270
SHEET 4 BB 4 GLN B 244 ASN B 245 -1 O GLN B 244 N ILE B 241
SITE 1 AC1 5 PRO A 196 ARG A 197 LEU A 233 HIS A 236
SITE 2 AC1 5 MET A 270
SITE 1 AC2 8 HIS A 202 SER A 226 ARG A 229 ASN A 230
SITE 2 AC2 8 HOH A2008 HOH A2060 LYS B 250 GLN B 253
SITE 1 AC3 6 ASN A 242 SER A 261 GLY A 262 ASN B 215
SITE 2 AC3 6 LYS B 217 HOH B2022
CRYST1 58.337 54.441 50.219 90.00 98.65 90.00 C 1 2 1 8
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 0.017142 0.000000 0.002609 0.00000
SCALE2 0.000000 0.018368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020142 0.00000
ATOM 1 N PRO A 196 3.031 8.429 1.265 1.00 41.67 N
ATOM 2 CA PRO A 196 1.942 7.565 1.729 1.00 39.54 C
ATOM 3 C PRO A 196 1.490 7.834 3.133 1.00 36.24 C
ATOM 4 O PRO A 196 0.639 8.728 3.142 1.00 38.55 O
ATOM 5 CB PRO A 196 2.510 6.190 1.452 1.00 40.29 C
ATOM 6 CG PRO A 196 2.977 6.491 0.060 1.00 42.20 C
ATOM 7 CD PRO A 196 3.373 7.976 -0.088 1.00 42.73 C
ATOM 8 N ARG A 197 1.956 7.203 4.209 1.00 29.55 N
ATOM 9 CA ARG A 197 1.127 7.243 5.405 1.00 25.22 C
ATOM 10 C ARG A 197 1.892 7.101 6.721 1.00 20.48 C
ATOM 11 O ARG A 197 3.086 6.889 6.737 1.00 16.09 O
ATOM 12 CB ARG A 197 0.052 6.177 5.299 1.00 25.29 C
ATOM 13 CG ARG A 197 0.635 4.790 4.995 1.00 27.78 C
ATOM 14 CD ARG A 197 -0.393 3.709 4.644 1.00 29.23 C
ATOM 15 NE ARG A 197 -1.306 4.224 3.623 1.00 30.86 N
ATOM 16 CZ ARG A 197 -2.601 3.943 3.528 1.00 30.88 C
ATOM 17 NH1 ARG A 197 -3.197 3.113 4.377 1.00 26.24 N
ATOM 18 NH2 ARG A 197 -3.312 4.504 2.554 1.00 33.94 N
ATOM 19 N THR A 198 1.184 7.268 7.824 1.00 16.98 N
ATOM 20 CA THR A 198 1.807 7.430 9.139 1.00 16.22 C
ATOM 21 C THR A 198 1.038 6.550 10.095 1.00 16.73 C
ATOM 22 O THR A 198 -0.185 6.715 10.233 1.00 15.49 O
ATOM 23 CB THR A 198 1.699 8.897 9.562 1.00 16.44 C
ATOM 24 OG1 THR A 198 2.258 9.705 8.521 1.00 15.61 O
ATOM 25 CG2 THR A 198 2.540 9.212 10.791 1.00 16.28 C
ATOM 26 N ILE A 199 1.775 5.634 10.722 1.00 15.52 N
ATOM 27 CA ILE A 199 1.176 4.584 11.525 1.00 16.05 C
ATOM 28 C ILE A 199 1.806 4.665 12.923 1.00 15.64 C
ATOM 29 O ILE A 199 3.022 4.667 13.041 1.00 13.61 O
ATOM 30 CB ILE A 199 1.427 3.215 10.859 1.00 16.79 C
ATOM 31 CG1 ILE A 199 0.739 3.117 9.479 1.00 19.62 C
ATOM 32 CG2 ILE A 199 0.976 2.063 11.720 1.00 16.74 C
ATOM 33 CD1 ILE A 199 1.671 3.492 8.380 1.00 24.48 C
ATOM 34 N THR A 200 0.964 4.757 13.954 1.00 14.20 N
ATOM 35 CA THR A 200 1.405 4.733 15.345 1.00 14.27 C
ATOM 36 C THR A 200 1.128 3.381 15.968 1.00 13.54 C
ATOM 37 O THR A 200 0.009 2.861 15.922 1.00 12.96 O
ATOM 38 CB THR A 200 0.666 5.791 16.141 1.00 15.10 C
ATOM 39 OG1 THR A 200 0.979 7.067 15.583 1.00 14.38 O
ATOM 40 CG2 THR A 200 1.129 5.826 17.658 1.00 17.91 C
ATOM 41 N MET A 201 2.178 2.803 16.519 1.00 12.58 N
ATOM 42 CA MET A 201 2.139 1.467 17.122 1.00 11.85 C
ATOM 43 C MET A 201 2.651 1.533 18.575 1.00 13.91 C
ATOM 44 O MET A 201 3.287 2.514 18.956 1.00 13.76 O
ATOM 45 CB MET A 201 2.974 0.508 16.286 1.00 11.15 C
ATOM 46 CG MET A 201 2.373 0.196 14.909 1.00 12.07 C
ATOM 47 SD MET A 201 3.620 -0.366 13.673 1.00 14.23 S
ATOM 48 CE MET A 201 4.625 1.095 13.510 1.00 18.67 C
ATOM 49 N HIS A 202 2.339 0.487 19.343 1.00 12.91 N
ATOM 50 CA HIS A 202 2.740 0.274 20.737 1.00 14.26 C
ATOM 51 C HIS A 202 3.512 -1.036 20.852 1.00 11.84 C
ATOM 52 O HIS A 202 3.069 -2.063 20.347 1.00 13.43 O
ATOM 53 CB HIS A 202 1.498 0.234 21.624 1.00 14.13 C
ATOM 54 CG HIS A 202 0.825 1.562 21.790 1.00 19.96 C
ATOM 55 ND1 HIS A 202 0.281 2.266 20.737 1.00 25.04 N
ATOM 56 CD2 HIS A 202 0.532 2.278 22.902 1.00 27.38 C
ATOM 57 CE1 HIS A 202 -0.246 3.393 21.180 1.00 25.41 C
ATOM 58 NE2 HIS A 202 -0.127 3.414 22.496 1.00 27.92 N
ATOM 59 N LYS A 203 4.730 -0.996 21.403 1.00 11.41 N
ATOM 60 CA LYS A 203 5.450 -2.220 21.707 1.00 10.01 C
ATOM 61 C LYS A 203 4.646 -3.144 22.626 1.00 11.00 C
ATOM 62 O LYS A 203 3.944 -2.733 23.559 1.00 9.96 O
ATOM 63 CB LYS A 203 6.873 -1.969 22.255 1.00 10.79 C
ATOM 64 CG LYS A 203 7.812 -1.315 21.293 1.00 11.44 C
ATOM 65 CD LYS A 203 9.150 -0.941 21.923 1.00 12.14 C
ATOM 66 CE LYS A 203 10.056 -0.254 20.913 1.00 14.65 C
ATOM 67 NZ LYS A 203 11.471 -0.118 21.445 1.00 15.49 N
ATOM 68 N ASP A 204 4.687 -4.420 22.277 1.00 10.73 N
ATOM 69 CA ASP A 204 4.197 -5.491 23.109 1.00 12.10 C
ATOM 70 C ASP A 204 5.163 -5.840 24.227 1.00 11.35 C
ATOM 71 O ASP A 204 6.233 -5.218 24.406 1.00 12.97 O
ATOM 72 CB ASP A 204 3.729 -6.711 22.266 1.00 13.13 C
ATOM 73 CG ASP A 204 4.854 -7.538 21.682 1.00 14.09 C
ATOM 74 OD1 ASP A 204 6.021 -7.308 22.099 1.00 12.32 O
ATOM 75 OD2 ASP A 204 4.637 -8.444 20.794 1.00 12.76 O
ATOM 76 N SER A 205 4.774 -6.846 25.002 1.00 10.93 N
ATOM 77 CA SER A 205 5.514 -7.217 26.194 1.00 12.40 C
ATOM 78 C SER A 205 6.893 -7.829 25.939 1.00 14.01 C
ATOM 79 O SER A 205 7.655 -8.051 26.891 1.00 15.61 O
ATOM 80 CB SER A 205 4.625 -8.171 27.024 1.00 13.41 C
ATOM 81 OG SER A 205 4.528 -9.438 26.374 1.00 13.21 O
ATOM 82 N THR A 206 7.209 -8.131 24.684 1.00 12.60 N
ATOM 83 CA THR A 206 8.538 -8.511 24.228 1.00 13.84 C
ATOM 84 C THR A 206 9.342 -7.357 23.592 1.00 13.49 C
ATOM 85 O THR A 206 10.483 -7.550 23.149 1.00 12.88 O
ATOM 86 CB THR A 206 8.424 -9.672 23.168 1.00 14.05 C
ATOM 87 OG1 THR A 206 7.943 -9.185 21.892 1.00 13.58 O
ATOM 88 CG2 THR A 206 7.444 -10.762 23.659 1.00 16.06 C
ATOM 89 N GLY A 207 8.742 -6.175 23.512 1.00 11.55 N
ATOM 90 CA GLY A 207 9.393 -4.985 22.993 1.00 11.65 C
ATOM 91 C GLY A 207 9.286 -4.837 21.484 1.00 12.17 C
ATOM 92 O GLY A 207 10.090 -4.123 20.860 1.00 10.75 O
ATOM 93 N HIS A 208 8.297 -5.508 20.882 1.00 10.56 N
ATOM 94 CA HIS A 208 8.145 -5.506 19.436 1.00 11.47 C
ATOM 95 C HIS A 208 6.815 -4.942 18.931 1.00 10.87 C
ATOM 96 O HIS A 208 5.760 -5.109 19.567 1.00 11.15 O
ATOM 97 CB HIS A 208 8.267 -6.936 18.924 1.00 11.39 C
ATOM 98 CG HIS A 208 9.656 -7.478 19.042 1.00 13.92 C
ATOM 99 ND1 HIS A 208 9.934 -8.653 19.698 1.00 16.94 N
ATOM 100 CD2 HIS A 208 10.854 -6.931 18.727 1.00 19.94 C
ATOM 101 CE1 HIS A 208 11.234 -8.885 19.637 1.00 23.08 C
ATOM 102 NE2 HIS A 208 11.820 -7.842 19.080 1.00 18.29 N
ATOM 103 N VAL A 209 6.848 -4.225 17.823 1.00 11.47 N
ATOM 104 CA VAL A 209 5.601 -3.697 17.275 1.00 11.82 C
ATOM 105 C VAL A 209 4.940 -4.595 16.215 1.00 12.39 C
ATOM 106 O VAL A 209 3.736 -4.512 15.985 1.00 10.09 O
ATOM 107 CB VAL A 209 5.721 -2.262 16.728 1.00 12.85 C
ATOM 108 CG1 VAL A 209 5.990 -1.244 17.863 1.00 13.20 C
ATOM 109 CG2 VAL A 209 6.751 -2.136 15.673 1.00 14.91 C
ATOM 110 N GLY A 210 5.721 -5.499 15.626 1.00 11.63 N
ATOM 111 CA GLY A 210 5.190 -6.564 14.797 1.00 11.92 C
ATOM 112 C GLY A 210 5.444 -6.507 13.302 1.00 12.34 C
ATOM 113 O GLY A 210 4.535 -6.806 12.507 1.00 12.22 O
ATOM 114 N PHE A 211 6.655 -6.154 12.882 1.00 12.69 N
ATOM 115 CA PHE A 211 6.975 -6.250 11.437 1.00 12.04 C
ATOM 116 C PHE A 211 8.388 -6.743 11.181 1.00 9.93 C
ATOM 117 O PHE A 211 9.238 -6.746 12.077 1.00 11.33 O
ATOM 118 CB PHE A 211 6.659 -4.951 10.665 1.00 12.34 C
ATOM 119 CG PHE A 211 7.550 -3.784 11.002 1.00 12.49 C
ATOM 120 CD1 PHE A 211 7.207 -2.912 12.011 1.00 13.30 C
ATOM 121 CD2 PHE A 211 8.704 -3.535 10.277 1.00 11.63 C
ATOM 122 CE1 PHE A 211 8.012 -1.814 12.303 1.00 16.08 C
ATOM 123 CE2 PHE A 211 9.504 -2.447 10.572 1.00 12.25 C
ATOM 124 CZ PHE A 211 9.138 -1.593 11.567 1.00 14.00 C
ATOM 125 N ILE A 212 8.627 -7.256 9.987 1.00 9.19 N
ATOM 126 CA ILE A 212 9.986 -7.584 9.552 1.00 10.29 C
ATOM 127 C ILE A 212 10.380 -6.612 8.437 1.00 11.12 C
ATOM 128 O ILE A 212 9.545 -6.268 7.617 1.00 9.78 O
ATOM 129 CB ILE A 212 9.989 -9.065 9.081 1.00 10.82 C
ATOM 130 CG1 ILE A 212 9.639 -9.955 10.298 1.00 12.64 C
ATOM 131 CG2 ILE A 212 11.304 -9.494 8.459 1.00 11.92 C
ATOM 132 CD1 ILE A 212 9.226 -11.317 9.971 1.00 16.62 C
ATOM 133 N PHE A 213 11.653 -6.246 8.363 1.00 11.03 N
ATOM 134 CA PHE A 213 12.153 -5.395 7.303 1.00 11.28 C
ATOM 135 C PHE A 213 13.547 -5.824 6.839 1.00 11.85 C
ATOM 136 O PHE A 213 14.300 -6.564 7.509 1.00 12.58 O
ATOM 137 CB PHE A 213 12.106 -3.930 7.740 1.00 11.05 C
ATOM 138 CG PHE A 213 13.144 -3.548 8.762 1.00 12.33 C
ATOM 139 CD1 PHE A 213 14.364 -3.031 8.362 1.00 12.31 C
ATOM 140 CD2 PHE A 213 12.894 -3.694 10.120 1.00 13.90 C
ATOM 141 CE1 PHE A 213 15.320 -2.660 9.299 1.00 12.82 C
ATOM 142 CE2 PHE A 213 13.835 -3.311 11.063 1.00 16.52 C
ATOM 143 CZ PHE A 213 15.051 -2.783 10.637 1.00 12.45 C
ATOM 144 N LYS A 214 13.877 -5.356 5.644 1.00 11.40 N
ATOM 145 CA LYS A 214 15.177 -5.616 5.068 1.00 12.05 C
ATOM 146 C LYS A 214 15.371 -4.600 3.964 1.00 12.66 C
ATOM 147 O LYS A 214 14.421 -4.342 3.215 1.00 13.70 O
ATOM 148 CB LYS A 214 15.212 -7.006 4.452 1.00 12.45 C
ATOM 149 CG LYS A 214 16.548 -7.419 3.891 1.00 14.49 C
ATOM 150 CD LYS A 214 16.442 -8.686 3.050 1.00 19.71 C
ATOM 151 CE LYS A 214 17.730 -8.942 2.249 1.00 25.26 C
ATOM 152 NZ LYS A 214 18.459 -10.159 2.699 1.00 26.78 N
ATOM 153 N ASN A 215 16.581 -4.048 3.857 1.00 13.48 N
ATOM 154 CA ASN A 215 16.897 -3.049 2.837 1.00 13.59 C
ATOM 155 C ASN A 215 15.989 -1.837 3.025 1.00 13.83 C
ATOM 156 O ASN A 215 15.554 -1.215 2.069 1.00 11.55 O
ATOM 157 CB ASN A 215 16.744 -3.699 1.437 1.00 15.62 C
ATOM 158 CG ASN A 215 17.650 -3.073 0.360 1.00 19.06 C
ATOM 159 OD1 ASN A 215 18.628 -2.440 0.753 1.00 21.53 O
ATOM 160 ND2 ASN A 215 17.333 -3.201 -0.971 1.00 13.42 N
ATOM 161 N GLY A 216 15.649 -1.508 4.268 1.00 13.25 N
ATOM 162 CA GLY A 216 14.818 -0.359 4.567 1.00 14.10 C
ATOM 163 C GLY A 216 13.341 -0.481 4.241 1.00 14.64 C
ATOM 164 O GLY A 216 12.616 0.505 4.367 1.00 14.66 O
ATOM 165 N LYS A 217 12.913 -1.665 3.822 1.00 13.03 N
ATOM 166 CA LYS A 217 11.546 -1.882 3.396 1.00 14.31 C
ATOM 167 C LYS A 217 10.855 -2.927 4.280 1.00 14.12 C
ATOM 168 O LYS A 217 11.442 -3.956 4.610 1.00 13.58 O
ATOM 169 CB LYS A 217 11.618 -2.396 1.973 1.00 13.93 C
ATOM 170 CG LYS A 217 10.306 -2.743 1.347 1.00 18.58 C
ATOM 171 CD LYS A 217 10.549 -3.440 0.002 1.00 24.08 C
ATOM 172 CE LYS A 217 10.462 -2.449 -1.115 1.00 24.97 C
ATOM 173 NZ LYS A 217 10.591 -3.150 -2.416 1.00 27.83 N
ATOM 174 N ILE A 218 9.615 -2.664 4.653 1.00 14.38 N
ATOM 175 CA ILE A 218 8.817 -3.620 5.400 1.00 14.58 C
ATOM 176 C ILE A 218 8.441 -4.794 4.484 1.00 14.87 C
ATOM 177 O ILE A 218 7.873 -4.591 3.414 1.00 14.27 O
ATOM 178 CB ILE A 218 7.540 -2.910 5.888 1.00 15.18 C
ATOM 179 CG1 ILE A 218 7.875 -1.795 6.866 1.00 13.78 C
ATOM 180 CG2 ILE A 218 6.550 -3.855 6.560 1.00 15.80 C
ATOM 181 CD1 ILE A 218 6.987 -0.587 6.669 1.00 17.33 C
ATOM 182 N THR A 219 8.738 -6.022 4.897 1.00 15.00 N
ATOM 183 CA THR A 219 8.439 -7.194 4.074 1.00 16.50 C
ATOM 184 C THR A 219 7.336 -8.082 4.626 1.00 15.76 C
ATOM 185 O THR A 219 6.711 -8.826 3.860 1.00 15.15 O
ATOM 186 CB THR A 219 9.677 -8.085 3.837 1.00 17.06 C
ATOM 187 OG1 THR A 219 10.173 -8.543 5.098 1.00 21.39 O
ATOM 188 CG2 THR A 219 10.802 -7.315 3.229 1.00 20.13 C
ATOM 189 N SER A 220 7.060 -7.966 5.922 1.00 13.73 N
ATOM 190 CA SER A 220 6.096 -8.833 6.581 1.00 13.41 C
ATOM 191 C SER A 220 5.459 -8.125 7.769 1.00 12.05 C
ATOM 192 O SER A 220 6.114 -7.294 8.425 1.00 13.60 O
ATOM 193 CB SER A 220 6.814 -10.050 7.168 1.00 14.55 C
ATOM 194 OG SER A 220 7.570 -10.778 6.231 1.00 14.31 O
ATOM 195 N ILE A 221 4.218 -8.513 8.068 1.00 10.61 N
ATOM 196 CA ILE A 221 3.498 -8.080 9.253 1.00 11.54 C
ATOM 197 C ILE A 221 3.166 -9.330 10.075 1.00 10.55 C
ATOM 198 O ILE A 221 2.752 -10.371 9.561 1.00 10.28 O
ATOM 199 CB ILE A 221 2.161 -7.375 8.890 1.00 12.33 C
ATOM 200 CG1 ILE A 221 2.378 -6.178 7.946 1.00 14.88 C
ATOM 201 CG2 ILE A 221 1.403 -7.022 10.187 1.00 12.27 C
ATOM 202 CD1 ILE A 221 3.378 -5.121 8.399 1.00 16.14 C
ATOM 203 N VAL A 222 3.343 -9.199 11.374 1.00 9.30 N
ATOM 204 CA VAL A 222 3.052 -10.260 12.317 1.00 10.49 C
ATOM 205 C VAL A 222 1.582 -10.259 12.763 1.00 9.28 C
ATOM 206 O VAL A 222 1.022 -9.233 13.113 1.00 9.18 O
ATOM 207 CB VAL A 222 3.988 -10.165 13.532 1.00 10.28 C
ATOM 208 CG1 VAL A 222 3.584 -11.184 14.591 1.00 11.38 C
ATOM 209 CG2 VAL A 222 5.449 -10.283 13.064 1.00 10.77 C
ATOM 210 N LYS A 223 0.992 -11.437 12.704 1.00 10.88 N
ATOM 211 CA LYS A 223 -0.368 -11.676 13.138 1.00 11.69 C
ATOM 212 C LYS A 223 -0.558 -11.262 14.608 1.00 13.31 C
ATOM 213 O LYS A 223 0.292 -11.484 15.476 1.00 12.24 O
ATOM 214 CB LYS A 223 -0.699 -13.136 12.849 1.00 11.39 C
ATOM 215 CG LYS A 223 -2.040 -13.562 13.364 1.00 15.60 C
ATOM 216 CD LYS A 223 -2.663 -14.744 12.616 1.00 23.03 C
ATOM 217 CE LYS A 223 -3.176 -15.790 13.632 1.00 27.08 C
ATOM 218 NZ LYS A 223 -4.469 -16.457 13.284 1.00 29.26 N
ATOM 219 N ASP A 224 -1.660 -10.568 14.872 1.00 14.73 N
ATOM 220 CA ASP A 224 -2.064 -10.209 16.222 1.00 15.21 C
ATOM 221 C ASP A 224 -1.157 -9.203 16.900 1.00 14.71 C
ATOM 222 O ASP A 224 -1.111 -9.163 18.120 1.00 15.83 O
ATOM 223 CB ASP A 224 -2.254 -11.460 17.101 1.00 16.45 C
ATOM 224 CG ASP A 224 -3.368 -12.335 16.579 1.00 21.69 C
ATOM 225 OD1 ASP A 224 -4.488 -11.801 16.391 1.00 28.08 O
ATOM 226 OD2 ASP A 224 -3.200 -13.531 16.235 1.00 28.74 O
ATOM 227 N SER A 225 -0.490 -8.377 16.097 1.00 12.41 N
ATOM 228 CA SER A 225 0.502 -7.408 16.546 1.00 12.33 C
ATOM 229 C SER A 225 -0.022 -5.976 16.430 1.00 11.98 C
ATOM 230 O SER A 225 -1.060 -5.730 15.799 1.00 10.20 O
ATOM 231 CB SER A 225 1.759 -7.532 15.707 1.00 12.61 C
ATOM 232 OG SER A 225 1.518 -6.980 14.423 1.00 8.75 O
ATOM 233 N SER A 226 0.680 -5.031 17.046 1.00 11.67 N
ATOM 234 CA SER A 226 0.291 -3.630 16.914 1.00 11.89 C
ATOM 235 C SER A 226 0.387 -3.148 15.457 1.00 12.76 C
ATOM 236 O SER A 226 -0.456 -2.390 14.965 1.00 11.94 O
ATOM 237 CB SER A 226 1.150 -2.763 17.845 1.00 13.01 C
ATOM 238 OG SER A 226 0.698 -1.424 17.802 1.00 10.70 O
ATOM 239 N ALA A 227 1.413 -3.576 14.737 1.00 12.08 N
ATOM 240 CA ALA A 227 1.481 -3.297 13.300 1.00 12.93 C
ATOM 241 C ALA A 227 0.257 -3.784 12.546 1.00 12.40 C
ATOM 242 O ALA A 227 -0.225 -3.108 11.632 1.00 14.20 O
ATOM 243 CB ALA A 227 2.732 -3.926 12.682 1.00 12.89 C
ATOM 244 N ALA A 228 -0.234 -4.969 12.886 1.00 13.28 N
ATOM 245 CA ALA A 228 -1.467 -5.471 12.268 1.00 14.00 C
ATOM 246 C ALA A 228 -2.692 -4.628 12.627 1.00 14.57 C
ATOM 247 O ALA A 228 -3.486 -4.241 11.758 1.00 14.56 O
ATOM 248 CB ALA A 228 -1.719 -6.931 12.666 1.00 13.92 C
ATOM 249 N ARG A 229 -2.866 -4.366 13.921 1.00 12.87 N
ATOM 250 CA ARG A 229 -4.032 -3.620 14.404 1.00 13.12 C
ATOM 251 C ARG A 229 -4.090 -2.203 13.864 1.00 12.95 C
ATOM 252 O ARG A 229 -5.169 -1.624 13.729 1.00 12.73 O
ATOM 253 CB ARG A 229 -3.984 -3.550 15.931 1.00 13.35 C
ATOM 254 CG ARG A 229 -4.387 -4.839 16.632 1.00 12.11 C
ATOM 255 CD ARG A 229 -4.531 -4.663 18.094 1.00 13.56 C
ATOM 256 NE ARG A 229 -3.262 -4.340 18.749 1.00 13.84 N
ATOM 257 CZ ARG A 229 -2.346 -5.211 19.154 1.00 13.56 C
ATOM 258 NH1 ARG A 229 -2.454 -6.514 18.975 1.00 12.99 N
ATOM 259 NH2 ARG A 229 -1.295 -4.756 19.774 1.00 16.44 N
ATOM 260 N ASN A 230 -2.926 -1.639 13.565 1.00 12.98 N
ATOM 261 CA ASN A 230 -2.807 -0.241 13.190 1.00 13.64 C
ATOM 262 C ASN A 230 -2.610 -0.049 11.704 1.00 14.59 C
ATOM 263 O ASN A 230 -2.530 1.078 11.244 1.00 16.37 O
ATOM 264 CB ASN A 230 -1.720 0.419 14.017 1.00 14.15 C
ATOM 265 CG ASN A 230 -2.125 0.600 15.442 1.00 13.83 C
ATOM 266 OD1 ASN A 230 -2.970 1.442 15.734 1.00 16.59 O
ATOM 267 ND2 ASN A 230 -1.522 -0.161 16.353 1.00 10.42 N
ATOM 268 N GLY A 231 -2.571 -1.155 10.968 1.00 15.72 N
ATOM 269 CA GLY A 231 -2.666 -1.162 9.524 1.00 17.48 C
ATOM 270 C GLY A 231 -1.408 -0.871 8.737 1.00 17.41 C
ATOM 271 O GLY A 231 -1.459 -0.347 7.626 1.00 18.61 O
ATOM 272 N LEU A 232 -0.279 -1.203 9.326 1.00 16.09 N
ATOM 273 CA LEU A 232 1.023 -1.101 8.672 1.00 15.45 C
ATOM 274 C LEU A 232 1.038 -2.027 7.449 1.00 15.12 C
ATOM 275 O LEU A 232 0.494 -3.122 7.467 1.00 13.60 O
ATOM 276 CB LEU A 232 2.149 -1.421 9.667 1.00 14.48 C
ATOM 277 CG LEU A 232 3.547 -1.200 9.085 1.00 14.32 C
ATOM 278 CD1 LEU A 232 3.801 0.280 8.926 1.00 20.28 C
ATOM 279 CD2 LEU A 232 4.668 -1.764 9.921 1.00 14.77 C
ATOM 280 N LEU A 233 1.584 -1.519 6.349 1.00 15.53 N
ATOM 281 CA LEU A 233 1.485 -2.170 5.052 1.00 15.82 C
ATOM 282 C LEU A 233 2.845 -2.716 4.625 1.00 15.72 C
ATOM 283 O LEU A 233 3.883 -2.092 4.818 1.00 17.04 O
ATOM 284 CB LEU A 233 0.990 -1.141 4.022 1.00 15.38 C
ATOM 285 CG LEU A 233 -0.374 -0.528 4.345 1.00 18.17 C
ATOM 286 CD1 LEU A 233 -0.830 0.475 3.299 1.00 18.26 C
ATOM 287 CD2 LEU A 233 -1.385 -1.661 4.524 1.00 21.35 C
ATOM 288 N THR A 234 2.857 -3.891 4.010 1.00 15.92 N
ATOM 289 CA THR A 234 4.124 -4.430 3.531 1.00 14.68 C
ATOM 290 C THR A 234 4.448 -3.827 2.188 1.00 14.16 C
ATOM 291 O THR A 234 3.599 -3.205 1.550 1.00 12.85 O
ATOM 292 CB THR A 234 4.037 -5.937 3.379 1.00 15.59 C
ATOM 293 OG1 THR A 234 3.104 -6.245 2.322 1.00 16.94 O
ATOM 294 CG2 THR A 234 3.451 -6.513 4.629 1.00 14.35 C
ATOM 295 N GLU A 235 5.698 -4.052 1.801 1.00 14.97 N
ATOM 296 CA GLU A 235 6.296 -3.589 0.562 1.00 15.90 C
ATOM 297 C GLU A 235 6.331 -2.061 0.436 1.00 15.46 C
ATOM 298 O GLU A 235 6.317 -1.517 -0.661 1.00 15.81 O
ATOM 299 CB GLU A 235 5.633 -4.291 -0.628 1.00 17.30 C
ATOM 300 CG GLU A 235 6.007 -5.767 -0.663 1.00 24.18 C
ATOM 301 CD GLU A 235 7.512 -5.988 -0.849 1.00 31.19 C
ATOM 302 OE1 GLU A 235 8.077 -5.478 -1.846 1.00 36.64 O
ATOM 303 OE2 GLU A 235 8.151 -6.672 -0.013 1.00 33.26 O
ATOM 304 N HIS A 236 6.501 -1.404 1.569 1.00 14.43 N
ATOM 305 CA HIS A 236 6.638 0.040 1.667 1.00 14.74 C
ATOM 306 C HIS A 236 7.967 0.335 2.384 1.00 15.09 C
ATOM 307 O HIS A 236 8.318 -0.337 3.362 1.00 13.54 O
ATOM 308 CB HIS A 236 5.504 0.607 2.509 1.00 15.58 C
ATOM 309 CG HIS A 236 4.175 0.672 1.820 1.00 15.78 C
ATOM 310 ND1 HIS A 236 3.437 -0.449 1.497 1.00 15.70 N
ATOM 311 CD2 HIS A 236 3.411 1.735 1.471 1.00 21.48 C
ATOM 312 CE1 HIS A 236 2.336 -0.078 0.867 1.00 17.46 C
ATOM 313 NE2 HIS A 236 2.281 1.242 0.861 1.00 20.87 N
ATOM 314 N ASN A 237 8.725 1.288 1.849 1.00 14.78 N
ATOM 315 CA ASN A 237 9.960 1.770 2.458 1.00 15.68 C
ATOM 316 C ASN A 237 9.656 2.595 3.697 1.00 15.71 C
ATOM 317 O ASN A 237 8.681 3.346 3.741 1.00 16.46 O
ATOM 318 CB ASN A 237 10.737 2.666 1.475 1.00 16.64 C
ATOM 319 CG ASN A 237 11.363 1.875 0.350 1.00 18.63 C
ATOM 320 OD1 ASN A 237 11.247 2.246 -0.815 1.00 20.58 O
ATOM 321 ND2 ASN A 237 11.997 0.764 0.692 1.00 17.41 N
ATOM 322 N ILE A 238 10.480 2.453 4.720 1.00 15.99 N
ATOM 323 CA ILE A 238 10.334 3.241 5.946 1.00 17.41 C
ATOM 324 C ILE A 238 11.024 4.606 5.731 1.00 17.22 C
ATOM 325 O ILE A 238 12.175 4.610 5.361 1.00 17.36 O
ATOM 326 CB ILE A 238 10.980 2.474 7.133 1.00 17.82 C
ATOM 327 CG1 ILE A 238 10.447 1.043 7.283 1.00 18.60 C
ATOM 328 CG2 ILE A 238 10.834 3.237 8.429 1.00 20.17 C
ATOM 329 CD1 ILE A 238 11.334 0.152 8.165 1.00 19.04 C
ATOM 330 N CYS A 239 10.361 5.732 6.022 1.00 16.94 N
ATOM 331 CA CYS A 239 10.874 7.078 5.792 1.00 17.32 C
ATOM 332 C CYS A 239 11.331 7.741 7.080 1.00 16.54 C
ATOM 333 O CYS A 239 12.447 8.269 7.106 1.00 15.57 O
ATOM 334 CB CYS A 239 9.808 7.969 5.159 1.00 18.32 C
ATOM 335 SG CYS A 239 9.215 7.357 3.575 1.00 28.33 S
ATOM 336 N GLU A 240 10.462 7.691 8.099 1.00 15.43 N
ATOM 337 CA GLU A 240 10.657 8.316 9.398 1.00 15.93 C
ATOM 338 C GLU A 240 10.208 7.405 10.559 1.00 15.57 C
ATOM 339 O GLU A 240 9.210 6.700 10.463 1.00 14.86 O
ATOM 340 CB GLU A 240 9.948 9.680 9.490 1.00 16.67 C
ATOM 341 CG GLU A 240 10.401 10.722 8.480 1.00 21.41 C
ATOM 342 CD GLU A 240 10.074 12.133 8.943 1.00 27.15 C
ATOM 343 OE1 GLU A 240 9.870 12.328 10.163 1.00 26.28 O
ATOM 344 OE2 GLU A 240 10.003 13.027 8.071 1.00 32.99 O
ATOM 345 N ILE A 241 10.976 7.407 11.640 1.00 15.66 N
ATOM 346 CA ILE A 241 10.618 6.771 12.900 1.00 16.00 C
ATOM 347 C ILE A 241 10.800 7.798 14.032 1.00 17.05 C
ATOM 348 O ILE A 241 11.889 8.360 14.214 1.00 16.91 O
ATOM 349 CB ILE A 241 11.529 5.574 13.160 1.00 16.06 C
ATOM 350 CG1 ILE A 241 11.520 4.604 11.973 1.00 16.89 C
ATOM 351 CG2 ILE A 241 11.206 4.881 14.485 1.00 15.14 C
ATOM 352 CD1 ILE A 241 12.573 3.528 12.124 1.00 17.68 C
ATOM 353 N ASN A 242 9.718 8.014 14.769 1.00 18.01 N
ATOM 354 CA ASN A 242 9.668 8.997 15.839 1.00 19.05 C
ATOM 355 C ASN A 242 10.328 10.300 15.415 1.00 19.90 C
ATOM 356 O ASN A 242 11.105 10.885 16.174 1.00 20.68 O
ATOM 357 CB ASN A 242 10.259 8.386 17.103 1.00 18.62 C
ATOM 358 CG ASN A 242 9.354 7.318 17.680 1.00 19.76 C
ATOM 359 OD1 ASN A 242 8.297 7.080 17.116 1.00 18.08 O
ATOM 360 ND2 ASN A 242 9.658 6.810 18.878 1.00 23.58 N
ATOM 361 N GLY A 243 9.987 10.744 14.204 1.00 20.80 N
ATOM 362 CA GLY A 243 10.370 12.065 13.741 1.00 23.12 C
ATOM 363 C GLY A 243 11.748 12.136 13.101 1.00 23.64 C
ATOM 364 O GLY A 243 12.199 13.216 12.724 1.00 25.63 O
ATOM 365 N GLN A 244 12.386 10.979 12.931 1.00 22.81 N
ATOM 366 CA GLN A 244 13.771 10.876 12.506 1.00 20.85 C
ATOM 367 C GLN A 244 13.820 10.283 11.099 1.00 19.93 C
ATOM 368 O GLN A 244 13.267 9.211 10.878 1.00 17.73 O
ATOM 369 CB GLN A 244 14.485 9.967 13.512 1.00 22.34 C
ATOM 370 CG GLN A 244 15.913 9.655 13.153 1.00 24.33 C
ATOM 371 CD GLN A 244 16.806 9.316 14.325 1.00 27.43 C
ATOM 372 OE1 GLN A 244 18.027 9.399 14.170 1.00 30.32 O
ATOM 373 NE2 GLN A 244 16.234 8.959 15.476 1.00 26.49 N
ATOM 374 N ASN A 245 14.451 10.979 10.151 1.00 17.35 N
ATOM 375 CA ASN A 245 14.613 10.470 8.791 1.00 17.24 C
ATOM 376 C ASN A 245 15.537 9.256 8.772 1.00 16.45 C
ATOM 377 O ASN A 245 16.690 9.339 9.210 1.00 16.64 O
ATOM 378 CB ASN A 245 15.167 11.546 7.846 1.00 16.69 C
ATOM 379 CG ASN A 245 15.290 11.044 6.410 1.00 16.81 C
ATOM 380 OD1 ASN A 245 14.675 10.040 6.035 1.00 17.80 O
ATOM 381 ND2 ASN A 245 16.083 11.741 5.606 1.00 19.41 N
ATOM 382 N VAL A 246 15.007 8.129 8.293 1.00 15.67 N
ATOM 383 CA VAL A 246 15.777 6.907 8.163 1.00 14.83 C
ATOM 384 C VAL A 246 15.974 6.471 6.718 1.00 13.77 C
ATOM 385 O VAL A 246 16.525 5.395 6.472 1.00 11.27 O
ATOM 386 CB VAL A 246 15.188 5.776 9.040 1.00 14.96 C
ATOM 387 CG1 VAL A 246 15.100 6.283 10.477 1.00 15.65 C
ATOM 388 CG2 VAL A 246 13.814 5.351 8.566 1.00 16.05 C
ATOM 389 N ILE A 247 15.573 7.322 5.767 1.00 12.88 N
ATOM 390 CA ILE A 247 15.859 7.036 4.382 1.00 12.49 C
ATOM 391 C ILE A 247 17.376 6.991 4.203 1.00 11.65 C
ATOM 392 O ILE A 247 18.090 7.929 4.596 1.00 9.86 O
ATOM 393 CB ILE A 247 15.207 8.077 3.444 1.00 13.57 C
ATOM 394 CG1 ILE A 247 13.676 7.974 3.555 1.00 16.46 C
ATOM 395 CG2 ILE A 247 15.599 7.777 2.030 1.00 14.91 C
ATOM 396 CD1 ILE A 247 12.920 9.014 2.747 1.00 18.96 C
ATOM 397 N GLY A 248 17.845 5.904 3.597 1.00 9.72 N
ATOM 398 CA GLY A 248 19.266 5.677 3.409 1.00 10.53 C
ATOM 399 C GLY A 248 20.111 5.067 4.512 1.00 10.06 C
ATOM 400 O GLY A 248 21.278 4.766 4.255 1.00 9.60 O
ATOM 401 N LEU A 249 19.586 4.943 5.730 1.00 11.78 N
ATOM 402 CA LEU A 249 20.362 4.348 6.807 1.00 12.93 C
ATOM 403 C LEU A 249 20.464 2.836 6.570 1.00 13.25 C
ATOM 404 O LEU A 249 19.588 2.258 5.935 1.00 12.85 O
ATOM 405 CB LEU A 249 19.704 4.625 8.169 1.00 13.32 C
ATOM 406 CG LEU A 249 19.537 6.103 8.539 1.00 14.26 C
ATOM 407 CD1 LEU A 249 18.854 6.194 9.909 1.00 16.91 C
ATOM 408 CD2 LEU A 249 20.878 6.792 8.473 1.00 17.28 C
ATOM 409 N LYS A 250 21.540 2.219 7.052 1.00 13.10 N
ATOM 410 CA LYS A 250 21.672 0.766 7.124 1.00 13.09 C
ATOM 411 C LYS A 250 20.615 0.147 8.029 1.00 13.34 C
ATOM 412 O LYS A 250 20.157 0.766 9.007 1.00 13.28 O
ATOM 413 CB LYS A 250 23.038 0.369 7.686 1.00 14.09 C
ATOM 414 CG LYS A 250 24.252 0.830 6.893 1.00 17.57 C
ATOM 415 CD LYS A 250 24.319 0.248 5.496 1.00 22.12 C
ATOM 416 CE LYS A 250 25.460 -0.757 5.353 1.00 25.71 C
ATOM 417 NZ LYS A 250 25.392 -1.516 4.065 1.00 26.80 N
ATOM 418 N ASP A 251 20.263 -1.100 7.730 1.00 12.98 N
ATOM 419 CA ASP A 251 19.290 -1.832 8.534 1.00 14.05 C
ATOM 420 C ASP A 251 19.632 -1.910 10.022 1.00 13.82 C
ATOM 421 O ASP A 251 18.746 -1.810 10.872 1.00 14.14 O
ATOM 422 CB ASP A 251 19.151 -3.250 7.976 1.00 13.37 C
ATOM 423 CG ASP A 251 18.251 -3.313 6.767 1.00 13.00 C
ATOM 424 OD1 ASP A 251 17.572 -2.310 6.401 1.00 10.20 O
ATOM 425 OD2 ASP A 251 18.242 -4.356 6.095 1.00 12.40 O
ATOM 426 N SER A 252 20.899 -2.133 10.346 1.00 13.63 N
ATOM 427 CA SER A 252 21.316 -2.115 11.747 1.00 14.30 C
ATOM 428 C SER A 252 21.094 -0.753 12.428 1.00 13.53 C
ATOM 429 O SER A 252 20.756 -0.729 13.612 1.00 11.92 O
ATOM 430 CB SER A 252 22.755 -2.618 11.882 1.00 14.50 C
ATOM 431 OG SER A 252 23.618 -1.749 11.190 1.00 18.69 O
ATOM 432 N GLN A 253 21.228 0.363 11.706 1.00 13.19 N
ATOM 433 CA GLN A 253 20.985 1.698 12.251 1.00 12.71 C
ATOM 434 C GLN A 253 19.486 1.891 12.498 1.00 13.01 C
ATOM 435 O GLN A 253 19.079 2.470 13.529 1.00 12.42 O
ATOM 436 CB GLN A 253 21.463 2.821 11.321 1.00 13.28 C
ATOM 437 CG GLN A 253 22.943 3.146 11.328 1.00 13.81 C
ATOM 438 CD GLN A 253 23.330 4.161 10.267 1.00 16.52 C
ATOM 439 OE1 GLN A 253 23.759 5.265 10.592 1.00 19.21 O
ATOM 440 NE2 GLN A 253 23.190 3.790 8.989 1.00 19.06 N
ATOM 441 N ILE A 254 18.671 1.378 11.572 1.00 11.61 N
ATOM 442 CA ILE A 254 17.226 1.398 11.729 1.00 11.00 C
ATOM 443 C ILE A 254 16.792 0.567 12.946 1.00 12.66 C
ATOM 444 O ILE A 254 15.942 0.969 13.752 1.00 11.75 O
ATOM 445 CB ILE A 254 16.502 0.906 10.433 1.00 10.77 C
ATOM 446 CG1 ILE A 254 16.800 1.880 9.290 1.00 13.43 C
ATOM 447 CG2 ILE A 254 15.001 0.747 10.704 1.00 10.32 C
ATOM 448 CD1 ILE A 254 16.352 1.463 7.864 1.00 15.82 C
ATOM 449 N ALA A 255 17.395 -0.600 13.062 1.00 13.21 N
ATOM 450 CA ALA A 255 17.072 -1.521 14.137 1.00 14.53 C
ATOM 451 C ALA A 255 17.447 -0.923 15.485 1.00 15.39 C
ATOM 452 O ALA A 255 16.701 -1.083 16.458 1.00 14.15 O
ATOM 453 CB ALA A 255 17.776 -2.837 13.908 1.00 15.76 C
ATOM 454 N ASP A 256 18.584 -0.233 15.544 1.00 14.89 N
ATOM 455 CA ASP A 256 18.974 0.494 16.742 1.00 15.68 C
ATOM 456 C ASP A 256 18.001 1.603 17.128 1.00 15.37 C
ATOM 457 O ASP A 256 17.661 1.770 18.308 1.00 14.91 O
ATOM 458 CB ASP A 256 20.359 1.103 16.589 1.00 16.23 C
ATOM 459 CG ASP A 256 21.470 0.090 16.793 1.00 18.74 C
ATOM 460 OD1 ASP A 256 21.208 -1.097 17.105 1.00 20.67 O
ATOM 461 OD2 ASP A 256 22.657 0.418 16.635 1.00 25.48 O
ATOM 462 N ILE A 257 17.548 2.372 16.147 1.00 14.36 N
ATOM 463 CA ILE A 257 16.528 3.393 16.405 1.00 14.95 C
ATOM 464 C ILE A 257 15.252 2.751 16.991 1.00 14.19 C
ATOM 465 O ILE A 257 14.691 3.213 17.984 1.00 14.36 O
ATOM 466 CB ILE A 257 16.245 4.193 15.106 1.00 13.99 C
ATOM 467 CG1 ILE A 257 17.457 5.035 14.718 1.00 16.26 C
ATOM 468 CG2 ILE A 257 15.069 5.137 15.273 1.00 16.84 C
ATOM 469 CD1 ILE A 257 17.266 5.677 13.368 1.00 14.33 C
ATOM 470 N LEU A 258 14.811 1.646 16.397 1.00 16.05 N
ATOM 471 CA LEU A 258 13.585 0.993 16.842 1.00 16.18 C
ATOM 472 C LEU A 258 13.726 0.399 18.239 1.00 17.13 C
ATOM 473 O LEU A 258 12.809 0.469 19.063 1.00 16.76 O
ATOM 474 CB LEU A 258 13.168 -0.085 15.839 1.00 16.10 C
ATOM 475 CG LEU A 258 12.621 0.421 14.505 1.00 16.02 C
ATOM 476 CD1 LEU A 258 12.779 -0.633 13.418 1.00 20.11 C
ATOM 477 CD2 LEU A 258 11.172 0.856 14.656 1.00 18.37 C
ATOM 478 N SER A 259 14.902 -0.162 18.515 1.00 17.94 N
ATOM 479 CA SER A 259 15.120 -0.852 19.775 1.00 19.27 C
ATOM 480 C SER A 259 15.308 0.139 20.922 1.00 19.38 C
ATOM 481 O SER A 259 14.894 -0.154 22.037 1.00 20.01 O
ATOM 482 CB SER A 259 16.286 -1.852 19.688 1.00 19.90 C
ATOM 483 OG SER A 259 17.519 -1.174 19.710 1.00 23.62 O
ATOM 484 N THR A 260 15.886 1.302 20.641 1.00 19.44 N
ATOM 485 CA THR A 260 16.087 2.327 21.650 1.00 20.81 C
ATOM 486 C THR A 260 14.927 3.296 21.708 1.00 19.76 C
ATOM 487 O THR A 260 14.892 4.132 22.601 1.00 21.35 O