HEADER IMMUNE SYSTEM 13-MAY-09 3HG1
TITLE GERMLINE-GOVERNED RECOGNITION OF A CANCER EPITOPE BY AN IMMUNODOMINANT
TITLE 2 HUMAN T CELL RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS I ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 25-300;
COMPND 5 SYNONYM: MHC CLASS I ANTIGEN A*2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 21-119;
COMPND 11 SYNONYM: BETA-2-MICROGLOBULIN;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CANCER/MART-1;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: MELAN-A, MART-1 PROTEIN, AUTOIMMUNOGENIC CANCER/TESTIS
COMPND 17 ANTIGEN NY-ESO-1;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: T-CELL RECEPTOR, ALPHA CHAIN;
COMPND 21 CHAIN: D;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: T-CELL RECEPTOR, BETA CHAIN;
COMPND 24 CHAIN: E
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEX078;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PEX050;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 MOL_ID: 4;
SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 28 ORGANISM_COMMON: HUMAN;
SOURCE 29 ORGANISM_TAXID: 9606;
SOURCE 30 MOL_ID: 5;
SOURCE 31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 32 ORGANISM_COMMON: HUMAN;
SOURCE 33 ORGANISM_TAXID: 9606
KEYWDS T-CELL RECEPTOR, CDR3, PHAGE DISPLAY, MELAN-1, MART-1, IMMUNE SYSTEM,
KEYWDS 2 DISULFIDE BOND, TRANSMEMBRANE, DISEASE MUTATION, GLYCATION,
KEYWDS 3 GLYCOPROTEIN, IMMUNE RESPONSE, IMMUNOGLOBULIN DOMAIN, MHC I,
KEYWDS 4 PYRROLIDONE CARBOXYLIC ACID, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR D.K.COLE,F.YUAN,P.J.RIZKALLAH,J.J.MILES,E.GOSTICK,D.A.PRICE,G.F.GAO,
AUTHOR 2 B.K.JAKOBSEN,A.K.SEWELL
REVDAT 4 09-APR-14 3HG1 1 SOURCE
REVDAT 3 13-JUL-11 3HG1 1 VERSN
REVDAT 2 20-OCT-09 3HG1 1 JRNL
REVDAT 1 28-JUL-09 3HG1 0
JRNL AUTH D.K.COLE,F.YUAN,P.J.RIZKALLAH,J.J.MILES,E.GOSTICK,D.A.PRICE,
JRNL AUTH 2 G.F.GAO,B.K.JAKOBSEN,A.K.SEWELL
JRNL TITL GERM LINE-GOVERNED RECOGNITION OF A CANCER EPITOPE BY AN
JRNL TITL 2 IMMUNODOMINANT HUMAN T-CELL RECEPTOR.
JRNL REF J.BIOL.CHEM. V. 284 27281 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19605354
JRNL DOI 10.1074/JBC.M109.022509
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 23740
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.304
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1211
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1656
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6583
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 44
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.30000
REMARK 3 B22 (A**2) : 1.30000
REMARK 3 B33 (A**2) : -2.60000
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): 0.506
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.904
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.817
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6779 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5807 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9213 ; 1.021 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13547 ; 1.016 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 819 ; 2.050 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 342 ;17.476 ;24.006
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1087 ; 8.917 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ; 7.347 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 969 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7617 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1427 ; 0.005 ; 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): 4107 ; 1.769 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1669 ; 0.000 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6627 ; 3.233 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2672 ; 4.550 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2586 ; 7.146 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 RIDING
REMARK 3 POSITIONS; U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3HG1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB053088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23764
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.16400
REMARK 200 R SYM (I) : 0.16400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.5120
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.73700
REMARK 200 R SYM FOR SHELL (I) : 0.73700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: MIXED ENTRIES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG 550 MME, 0.1M TRIS, 15%
REMARK 280 GLYCEROL, PH 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 40.99000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.48500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 20.49500
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, E
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 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 NE2 GLN A 218 CE1 HIS A 260 1.06
REMARK 500 O GLU B 16 ND2 ASN B 17 1.15
REMARK 500 O ASN D 184 N PHE D 186 1.48
REMARK 500 O ASP D 148 N ASP D 150 1.54
REMARK 500 NE2 GLN A 218 NE2 HIS A 260 1.63
REMARK 500 O MET D 161 CD ARG D 162 1.63
REMARK 500 O SER A 195 OD2 ASP A 196 1.68
REMARK 500 ND2 ASN D 184 N ALA D 185 1.77
REMARK 500 O GLN A 226 N THR A 228 1.79
REMARK 500 OG1 THR A 258 O LEU A 272 1.85
REMARK 500 O GLY A 252 N GLU A 254 1.88
REMARK 500 NE2 GLN A 218 ND1 HIS A 260 1.92
REMARK 500 NH2 ARG E 209 OE1 GLN E 211 1.92
REMARK 500 CD GLN A 218 CE1 HIS A 260 1.94
REMARK 500 CB MET D 161 O PHE D 166 1.97
REMARK 500 ND2 ASN D 22 OH TYR D 71 2.00
REMARK 500 O ASN E 220 O1 GOL E 802 2.02
REMARK 500 OG1 THR B 73 O LYS B 75 2.04
REMARK 500 OE1 GLN A 87 OH TYR A 118 2.05
REMARK 500 O GLN E 202 CD PRO E 204 2.09
REMARK 500 CE2 PHE D 166 OG SER D 168 2.11
REMARK 500 NH2 ARG A 14 O GLU A 19 2.15
REMARK 500 NE2 GLN D 2 OE2 GLU D 5 2.17
REMARK 500 NE ARG A 6 OH TYR A 113 2.18
REMARK 500 CA MET D 161 O PHE D 166 2.18
REMARK 500 CA PRO E 204 O GLY E 241 2.18
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 OE1 GLN D 140 O ASN D 176 4555 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 101 CB CYS A 101 SG -0.174
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 4 162.09 179.42
REMARK 500 ARG A 17 87.74 -155.70
REMARK 500 ASP A 29 -126.10 64.24
REMARK 500 SER A 38 -17.14 -46.76
REMARK 500 ARG A 48 21.01 -147.56
REMARK 500 PRO A 50 -70.78 -53.35
REMARK 500 LEU A 78 -36.85 -29.72
REMARK 500 ASN A 86 74.11 23.93
REMARK 500 TRP A 107 18.68 55.39
REMARK 500 ASP A 129 9.90 -66.87
REMARK 500 ARG A 131 -43.85 -141.32
REMARK 500 LYS A 176 -17.30 -47.49
REMARK 500 THR A 178 -70.52 -82.29
REMARK 500 ARG A 181 -154.64 -75.32
REMARK 500 THR A 182 87.78 171.53
REMARK 500 HIS A 191 -140.10 -80.31
REMARK 500 HIS A 192 76.05 124.73
REMARK 500 VAL A 194 30.71 -81.21
REMARK 500 SER A 195 121.52 70.09
REMARK 500 ASP A 196 161.11 39.46
REMARK 500 HIS A 197 -89.24 56.41
REMARK 500 ALA A 205 103.28 -176.10
REMARK 500 ILE A 213 142.13 -173.62
REMARK 500 ARG A 219 121.04 -177.04
REMARK 500 ASP A 220 -139.46 44.49
REMARK 500 GLN A 224 -158.20 122.03
REMARK 500 THR A 225 145.53 141.46
REMARK 500 GLN A 226 -92.58 -98.21
REMARK 500 ASP A 227 52.12 -27.94
REMARK 500 LYS A 243 156.54 167.77
REMARK 500 SER A 251 138.28 -14.30
REMARK 500 GLN A 253 5.66 -38.96
REMARK 500 GLN A 255 26.68 -60.76
REMARK 500 THR A 258 136.87 177.17
REMARK 500 PRO B 14 107.58 -51.64
REMARK 500 ASN B 17 132.42 81.73
REMARK 500 ASN B 21 -158.08 -162.87
REMARK 500 HIS B 31 132.19 -173.52
REMARK 500 ASP B 34 131.88 -38.07
REMARK 500 SER B 52 173.80 -55.41
REMARK 500 THR B 68 138.57 -172.07
REMARK 500 PRO B 72 -172.33 -44.29
REMARK 500 THR B 73 -167.84 -167.24
REMARK 500 LYS B 75 -163.71 -127.60
REMARK 500 ASP B 76 112.28 65.57
REMARK 500 ARG B 97 -83.94 -49.45
REMARK 500 ASP B 98 39.14 -69.60
REMARK 500 GLU D 3 -51.90 110.25
REMARK 500 SER D 8 -74.75 79.64
REMARK 500 ARG D 28 4.29 -69.13
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 802
DBREF 3HG1 A 1 276 UNP Q8WLS4 Q8WLS4_HUMAN 25 300
DBREF 3HG1 B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3HG1 C 1 10 PDB 3HG1 3HG1 1 10
DBREF 3HG1 D 2 195 PDB 3HG1 3HG1 2 195
DBREF 3HG1 E 1 244 PDB 3HG1 3HG1 1 244
SEQADV 3HG1 MET B 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 276 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 276 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 276 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 276 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 276 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 276 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 276 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 276 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 276 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 276 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 276 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 276 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 276 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 276 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 276 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 276 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 276 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 276 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 276 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 276 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 276 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 276 TRP GLU PRO
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 10 GLU LEU ALA GLY ILE GLY ILE LEU THR VAL
SEQRES 1 D 194 GLN GLU VAL GLU GLN ASN SER GLY PRO LEU SER VAL PRO
SEQRES 2 D 194 GLU GLY ALA ILE ALA SER LEU ASN CYS THR TYR SER ASP
SEQRES 3 D 194 ARG GLY SER GLN SER PHE PHE TRP TYR ARG GLN TYR SER
SEQRES 4 D 194 GLY LYS SER PRO GLU LEU ILE MET PHE ILE TYR SER ASN
SEQRES 5 D 194 GLY ASP LYS GLU ASP GLY ARG PHE THR ALA GLN LEU ASN
SEQRES 6 D 194 LYS ALA SER GLN TYR VAL SER LEU LEU ILE ARG ASP SER
SEQRES 7 D 194 GLN PRO SER ASP SER ALA THR TYR LEU CYS ALA VAL ASN
SEQRES 8 D 194 VAL ALA GLY LYS SER THR PHE GLY ASP GLY THR THR LEU
SEQRES 9 D 194 THR VAL LYS PRO ASN ILE GLN ASN PRO ASP PRO ALA VAL
SEQRES 10 D 194 TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER VAL
SEQRES 11 D 194 CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL SER
SEQRES 12 D 194 GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS CYS
SEQRES 13 D 194 VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN SER
SEQRES 14 D 194 ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS ALA
SEQRES 15 D 194 ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 1 E 244 SER GLN THR ILE HIS GLN TRP PRO ALA THR LEU VAL GLN
SEQRES 2 E 244 PRO VAL GLY SER PRO LEU SER LEU GLU CYS THR VAL GLU
SEQRES 3 E 244 GLY THR SER ASN PRO ASN LEU TYR TRP TYR ARG GLN ALA
SEQRES 4 E 244 ALA GLY ARG GLY LEU GLN LEU LEU PHE TYR SER VAL GLY
SEQRES 5 E 244 ILE GLY GLN ILE SER SER GLU VAL PRO GLN ASN LEU SER
SEQRES 6 E 244 ALA SER ARG PRO GLN ASP ARG GLN PHE ILE LEU SER SER
SEQRES 7 E 244 LYS LYS LEU LEU LEU SER ASP SER GLY PHE TYR LEU CYS
SEQRES 8 E 244 ALA TRP SER GLU THR GLY LEU GLY THR GLY GLU LEU PHE
SEQRES 9 E 244 PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP LEU
SEQRES 10 E 244 LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO
SEQRES 11 E 244 SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU
SEQRES 12 E 244 VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU
SEQRES 13 E 244 LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY
SEQRES 14 E 244 VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA
SEQRES 15 E 244 LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG
SEQRES 16 E 244 VAL SER ALA THR PHE TRP GLN ASP PRO ARG ASN HIS PHE
SEQRES 17 E 244 ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP
SEQRES 18 E 244 GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE
SEQRES 19 E 244 VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
HET GOL A 801 6
HET SO4 A 803 5
HET SO4 A 804 5
HET GOL E 802 6
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 7 SO4 2(O4 S 2-)
FORMUL 10 HOH *44(H2 O)
HELIX 1 1 ALA A 49 GLN A 54 1 6
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ASP A 137 ALA A 150 1 14
HELIX 4 4 HIS A 151 GLY A 162 1 12
HELIX 5 5 GLY A 162 GLY A 175 1 14
HELIX 6 6 GLN D 80 SER D 84 5 5
HELIX 7 7 LEU E 82 SER E 86 5 5
HELIX 8 8 ASP E 116 VAL E 120 5 5
HELIX 9 9 ALA E 198 ASP E 203 1 6
SHEET 1 A 8 GLU A 46 PRO A 47 0
SHEET 2 A 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N GLY A 26 O PHE A 33
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N VAL A 12 O ARG A 21
SHEET 5 A 8 THR A 94 VAL A 103 -1 O ARG A 97 N PHE A 9
SHEET 6 A 8 PHE A 109 TYR A 118 -1 O GLN A 115 N MET A 98
SHEET 7 A 8 LYS A 121 LEU A 126 -1 O LYS A 121 N TYR A 118
SHEET 8 A 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 B 4 MET A 189 THR A 190 0
SHEET 2 B 4 GLU A 198 PHE A 208 -1 O ARG A 202 N THR A 190
SHEET 3 B 4 PHE A 241 PRO A 250 -1 O VAL A 249 N ALA A 199
SHEET 4 B 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 C 4 MET A 189 THR A 190 0
SHEET 2 C 4 GLU A 198 PHE A 208 -1 O ARG A 202 N THR A 190
SHEET 3 C 4 PHE A 241 PRO A 250 -1 O VAL A 249 N ALA A 199
SHEET 4 C 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 D 2 THR A 214 GLN A 218 0
SHEET 2 D 2 THR A 258 GLN A 262 -1 O HIS A 260 N THR A 216
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 ARG B 45 0
SHEET 2 G 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 H 5 VAL D 4 GLN D 6 0
SHEET 2 H 5 ALA D 19 TYR D 25 -1 O THR D 24 N GLU D 5
SHEET 3 H 5 TYR D 71 ILE D 76 -1 O VAL D 72 N CYS D 23
SHEET 4 H 5 PHE D 61 ASN D 66 -1 N GLN D 64 O SER D 73
SHEET 5 H 5 GLY D 54 ASP D 58 -1 N ASP D 58 O PHE D 61
SHEET 1 I 5 SER D 8 PRO D 14 0
SHEET 2 I 5 THR D 103 LYS D 108 1 O THR D 104 N SER D 8
SHEET 3 I 5 ALA D 85 ASN D 92 -1 N ALA D 85 O LEU D 105
SHEET 4 I 5 PHE D 33 GLN D 38 -1 N TYR D 36 O LEU D 88
SHEET 5 I 5 GLU D 45 ILE D 50 -1 O GLU D 45 N ARG D 37
SHEET 1 J 4 SER D 8 PRO D 14 0
SHEET 2 J 4 THR D 103 LYS D 108 1 O THR D 104 N SER D 8
SHEET 3 J 4 ALA D 85 ASN D 92 -1 N ALA D 85 O LEU D 105
SHEET 4 J 4 SER D 97 PHE D 99 -1 O THR D 98 N VAL D 91
SHEET 1 K 4 ALA D 117 ARG D 122 0
SHEET 2 K 4 SER D 130 THR D 135 -1 O LEU D 133 N TYR D 119
SHEET 3 K 4 SER D 170 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 K 4 VAL D 151 ILE D 153 -1 N TYR D 152 O TRP D 174
SHEET 1 L 4 ILE E 4 TRP E 7 0
SHEET 2 L 4 LEU E 19 VAL E 25 -1 O THR E 24 N HIS E 5
SHEET 3 L 4 GLN E 73 SER E 78 -1 O LEU E 76 N LEU E 21
SHEET 4 L 4 LEU E 64 GLN E 70 -1 N SER E 65 O SER E 77
SHEET 1 M 5 THR E 10 PRO E 14 0
SHEET 2 M 5 SER E 109 LEU E 114 1 O THR E 112 N LEU E 11
SHEET 3 M 5 GLY E 87 SER E 94 -1 N TYR E 89 O SER E 109
SHEET 4 M 5 ASN E 32 GLN E 38 -1 N ASN E 32 O SER E 94
SHEET 5 M 5 GLN E 45 SER E 50 -1 O LEU E 47 N TRP E 35
SHEET 1 N 4 THR E 10 PRO E 14 0
SHEET 2 N 4 SER E 109 LEU E 114 1 O THR E 112 N LEU E 11
SHEET 3 N 4 GLY E 87 SER E 94 -1 N TYR E 89 O SER E 109
SHEET 4 N 4 PHE E 104 PHE E 105 -1 O PHE E 104 N TRP E 93
SHEET 1 O 4 GLU E 124 VAL E 125 0
SHEET 2 O 4 LYS E 140 PHE E 150 -1 O THR E 148 N GLU E 124
SHEET 3 O 4 TYR E 188 SER E 197 -1 O VAL E 196 N ALA E 141
SHEET 4 O 4 VAL E 170 THR E 172 -1 N CYS E 171 O ARG E 193
SHEET 1 P 4 GLU E 124 VAL E 125 0
SHEET 2 P 4 LYS E 140 PHE E 150 -1 O THR E 148 N GLU E 124
SHEET 3 P 4 TYR E 188 SER E 197 -1 O VAL E 196 N ALA E 141
SHEET 4 P 4 LEU E 177 LYS E 178 -1 N LEU E 177 O ALA E 189
SHEET 1 Q 3 VAL E 155 VAL E 161 0
SHEET 2 Q 3 PHE E 208 PHE E 214 -1 O GLN E 211 N SER E 158
SHEET 3 Q 3 GLN E 233 ALA E 239 -1 O ALA E 239 N PHE E 208
SSBOND 1 CYS A 101 CYS A 164 1555 1555 1.99
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.05
SSBOND 4 CYS D 23 CYS D 89 1555 1555 2.02
SSBOND 5 CYS D 132 CYS D 182 1555 1555 2.06
SSBOND 6 CYS D 157 CYS E 171 1555 1555 2.02
SSBOND 7 CYS E 23 CYS E 91 1555 1555 2.05
SSBOND 8 CYS E 145 CYS E 210 1555 1555 2.01
CISPEP 1 TYR A 209 PRO A 210 0 0.72
CISPEP 2 HIS B 31 PRO B 32 0 1.72
CISPEP 3 GLY D 9 PRO D 10 0 1.71
CISPEP 4 TRP E 7 PRO E 8 0 -0.28
CISPEP 5 TYR E 151 PRO E 152 0 3.17
SITE 1 AC1 2 SER A 105 TRP A 107
SITE 1 AC2 4 ARG A 6 TYR A 27 ASP A 29 ASP A 30
SITE 1 AC3 2 THR A 233 PHE A 241
SITE 1 AC4 4 GLN E 13 PRO E 14 GLU E 219 ASN E 220
CRYST1 120.898 120.898 81.980 90.00 90.00 90.00 P 43 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 0.008271 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END