HEADER IMMUNE SYSTEM 29-MAR-11 3RBG
TITLE CRYSTAL STRUCTURE ANALYSIS OF CLASS-I MHC RESTRICTED T-CELL ASSOCIATED
TITLE 2 MOLECULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOTOXIC AND REGULATORY T-CELL MOLECULE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CLASS-I MHC-RESTRICTED T-CELL-ASSOCIATED MOLECULE;
COMPND 5 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: CRTAM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(AI);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A+
KEYWDS IGV, CRTAM, STRUCTURAL GENOMICS, PSI-BIOLOGY, NEW YORK STRUCTURAL
KEYWDS 2 GENOMICS RESEARCH CONSORTIUM, NYSGRC, ATOMS-TO-ANIMALS: THE IMMUNE
KEYWDS 3 FUNCTION NETWORK, IFN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.RUBINSTEIN,U.A.RAMAGOPAL,R.TORO,S.G.NATHENSON,A.FISER,S.C.ALMO,NEW
AUTHOR 2 YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NYSGRC),ATOMS-TO-
AUTHOR 3 ANIMALS: THE IMMUNE FUNCTION NETWORK (IFN)
REVDAT 4 13-SEP-23 3RBG 1 REMARK SEQADV
REVDAT 3 25-OCT-17 3RBG 1 REMARK
REVDAT 2 07-AUG-13 3RBG 1 JRNL VERSN
REVDAT 1 25-MAY-11 3RBG 0
JRNL AUTH R.RUBINSTEIN,U.A.RAMAGOPAL,S.G.NATHENSON,S.C.ALMO,A.FISER
JRNL TITL FUNCTIONAL CLASSIFICATION OF IMMUNE REGULATORY PROTEINS.
JRNL REF STRUCTURE V. 21 766 2013
JRNL REFN ISSN 0969-2126
JRNL PMID 23583034
JRNL DOI 10.1016/J.STR.2013.02.022
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 23571
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1190
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1430
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3146
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.73000
REMARK 3 B22 (A**2) : -10.00000
REMARK 3 B33 (A**2) : 23.72000
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): 0.045
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.227
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3270 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4473 ; 1.442 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 409 ; 6.622 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 125 ;41.054 ;25.680
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 579 ;15.978 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;23.554 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 557 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2334 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2030 ; 0.732 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3347 ; 1.413 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1240 ; 1.960 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1124 ; 3.313 ; 4.500
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.551
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.449
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 : 1.40
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 RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3RBG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23676
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.46200
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1Z9M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.49 M SODIUM PHOSPHATE, 0.91M
REMARK 280 POTASIUM PHOSPHATE PH 6.9, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 39.50900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.50900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.01000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.14550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.01000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.14550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.50900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.01000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.14550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.50900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.01000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.14550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 REMARK: ANALYTICAL ULTRA CENTRIFUGATION STUDIES SUGGESTS IT IS
REMARK 300 DIMER IN SOLUTION.
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: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
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: 1880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -116.02000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -39.50900
REMARK 350
REMARK 350 BIOMOLECULE: 3
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: 1780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -39.50900
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 16
REMARK 465 GLY A 17
REMARK 465 SER A 18
REMARK 465 MET A 118
REMARK 465 LYS A 119
REMARK 465 GLY A 120
REMARK 465 GLU A 121
REMARK 465 PHE A 122
REMARK 465 CYS A 123
REMARK 465 ARG A 124
REMARK 465 TYR A 125
REMARK 465 PRO A 126
REMARK 465 SER A 127
REMARK 465 HIS A 128
REMARK 465 TRP A 129
REMARK 465 ARG A 130
REMARK 465 PRO A 131
REMARK 465 LEU A 132
REMARK 465 GLU A 133
REMARK 465 HIS A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 MET B 16
REMARK 465 GLY B 17
REMARK 465 THR B 117
REMARK 465 MET B 118
REMARK 465 LYS B 119
REMARK 465 GLY B 120
REMARK 465 GLU B 121
REMARK 465 PHE B 122
REMARK 465 CYS B 123
REMARK 465 ARG B 124
REMARK 465 TYR B 125
REMARK 465 PRO B 126
REMARK 465 SER B 127
REMARK 465 HIS B 128
REMARK 465 TRP B 129
REMARK 465 ARG B 130
REMARK 465 PRO B 131
REMARK 465 LEU B 132
REMARK 465 GLU B 133
REMARK 465 HIS B 134
REMARK 465 HIS B 135
REMARK 465 HIS B 136
REMARK 465 HIS B 137
REMARK 465 HIS B 138
REMARK 465 HIS B 139
REMARK 465 MET C 16
REMARK 465 GLY C 17
REMARK 465 MET C 118
REMARK 465 LYS C 119
REMARK 465 GLY C 120
REMARK 465 GLU C 121
REMARK 465 PHE C 122
REMARK 465 CYS C 123
REMARK 465 ARG C 124
REMARK 465 TYR C 125
REMARK 465 PRO C 126
REMARK 465 SER C 127
REMARK 465 HIS C 128
REMARK 465 TRP C 129
REMARK 465 ARG C 130
REMARK 465 PRO C 131
REMARK 465 LEU C 132
REMARK 465 GLU C 133
REMARK 465 HIS C 134
REMARK 465 HIS C 135
REMARK 465 HIS C 136
REMARK 465 HIS C 137
REMARK 465 HIS C 138
REMARK 465 HIS C 139
REMARK 465 MET D 16
REMARK 465 GLY D 17
REMARK 465 GLU D 121
REMARK 465 PHE D 122
REMARK 465 CYS D 123
REMARK 465 ARG D 124
REMARK 465 TYR D 125
REMARK 465 PRO D 126
REMARK 465 SER D 127
REMARK 465 HIS D 128
REMARK 465 TRP D 129
REMARK 465 ARG D 130
REMARK 465 PRO D 131
REMARK 465 LEU D 132
REMARK 465 GLU D 133
REMARK 465 HIS D 134
REMARK 465 HIS D 135
REMARK 465 HIS D 136
REMARK 465 HIS D 137
REMARK 465 HIS D 138
REMARK 465 HIS D 139
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 LYS D 44 CD CE NZ
REMARK 470 ASN D 68 CG OD1 ND2
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 ASN A 61 -141.90 52.65
REMARK 500 SER A 102 -148.75 -123.03
REMARK 500 SER A 102 -148.55 -123.27
REMARK 500 ASN B 61 -130.24 50.68
REMARK 500 SER B 102 -120.74 -126.28
REMARK 500 SER B 102 -147.40 -131.30
REMARK 500 SER B 104 -167.51 -123.46
REMARK 500 ASN C 61 -139.16 50.14
REMARK 500 SER C 102 -139.05 -128.12
REMARK 500 SER C 102 -134.36 -128.16
REMARK 500 ASN D 61 -127.18 49.53
REMARK 500 ASN D 87 41.77 39.51
REMARK 500 SER D 102 -126.23 -132.22
REMARK 500 SER D 102 -155.26 -134.37
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 PO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-005622 RELATED DB: TARGETDB
DBREF 3RBG A 18 117 UNP O95727 CRTAM_HUMAN 18 117
DBREF 3RBG B 18 117 UNP O95727 CRTAM_HUMAN 18 117
DBREF 3RBG C 18 117 UNP O95727 CRTAM_HUMAN 18 117
DBREF 3RBG D 18 117 UNP O95727 CRTAM_HUMAN 18 117
SEQADV 3RBG MET A 16 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY A 17 UNP O95727 EXPRESSION TAG
SEQADV 3RBG VAL A 65 UNP O95727 ALA 65 CONFLICT
SEQADV 3RBG MET A 118 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LYS A 119 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY A 120 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU A 121 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PHE A 122 UNP O95727 EXPRESSION TAG
SEQADV 3RBG CYS A 123 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG A 124 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TYR A 125 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO A 126 UNP O95727 EXPRESSION TAG
SEQADV 3RBG SER A 127 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS A 128 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TRP A 129 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG A 130 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO A 131 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LEU A 132 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU A 133 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS A 134 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS A 135 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS A 136 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS A 137 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS A 138 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS A 139 UNP O95727 EXPRESSION TAG
SEQADV 3RBG MET B 16 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY B 17 UNP O95727 EXPRESSION TAG
SEQADV 3RBG VAL B 65 UNP O95727 ALA 65 ENGINEERED MUTATION
SEQADV 3RBG MET B 118 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LYS B 119 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY B 120 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU B 121 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PHE B 122 UNP O95727 EXPRESSION TAG
SEQADV 3RBG CYS B 123 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG B 124 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TYR B 125 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO B 126 UNP O95727 EXPRESSION TAG
SEQADV 3RBG SER B 127 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS B 128 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TRP B 129 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG B 130 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO B 131 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LEU B 132 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU B 133 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS B 134 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS B 135 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS B 136 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS B 137 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS B 138 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS B 139 UNP O95727 EXPRESSION TAG
SEQADV 3RBG MET C 16 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY C 17 UNP O95727 EXPRESSION TAG
SEQADV 3RBG VAL C 65 UNP O95727 ALA 65 ENGINEERED MUTATION
SEQADV 3RBG MET C 118 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LYS C 119 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY C 120 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU C 121 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PHE C 122 UNP O95727 EXPRESSION TAG
SEQADV 3RBG CYS C 123 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG C 124 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TYR C 125 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO C 126 UNP O95727 EXPRESSION TAG
SEQADV 3RBG SER C 127 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS C 128 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TRP C 129 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG C 130 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO C 131 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LEU C 132 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU C 133 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS C 134 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS C 135 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS C 136 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS C 137 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS C 138 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS C 139 UNP O95727 EXPRESSION TAG
SEQADV 3RBG MET D 16 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY D 17 UNP O95727 EXPRESSION TAG
SEQADV 3RBG VAL D 65 UNP O95727 ALA 65 ENGINEERED MUTATION
SEQADV 3RBG MET D 118 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LYS D 119 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLY D 120 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU D 121 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PHE D 122 UNP O95727 EXPRESSION TAG
SEQADV 3RBG CYS D 123 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG D 124 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TYR D 125 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO D 126 UNP O95727 EXPRESSION TAG
SEQADV 3RBG SER D 127 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS D 128 UNP O95727 EXPRESSION TAG
SEQADV 3RBG TRP D 129 UNP O95727 EXPRESSION TAG
SEQADV 3RBG ARG D 130 UNP O95727 EXPRESSION TAG
SEQADV 3RBG PRO D 131 UNP O95727 EXPRESSION TAG
SEQADV 3RBG LEU D 132 UNP O95727 EXPRESSION TAG
SEQADV 3RBG GLU D 133 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS D 134 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS D 135 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS D 136 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS D 137 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS D 138 UNP O95727 EXPRESSION TAG
SEQADV 3RBG HIS D 139 UNP O95727 EXPRESSION TAG
SEQRES 1 A 124 MET GLY SER LEU THR ASN HIS THR GLU THR ILE THR VAL
SEQRES 2 A 124 GLU GLU GLY GLN THR LEU THR LEU LYS CYS VAL THR SER
SEQRES 3 A 124 LEU ARG LYS ASN SER SER LEU GLN TRP LEU THR PRO SER
SEQRES 4 A 124 GLY PHE THR ILE PHE LEU ASN GLU TYR PRO VAL LEU LYS
SEQRES 5 A 124 ASN SER LYS TYR GLN LEU LEU HIS HIS SER ALA ASN GLN
SEQRES 6 A 124 LEU SER ILE THR VAL PRO ASN VAL THR LEU GLN ASP GLU
SEQRES 7 A 124 GLY VAL TYR LYS CYS LEU HIS TYR SER ASP SER VAL SER
SEQRES 8 A 124 THR LYS GLU VAL LYS VAL ILE VAL LEU ALA THR MET LYS
SEQRES 9 A 124 GLY GLU PHE CYS ARG TYR PRO SER HIS TRP ARG PRO LEU
SEQRES 10 A 124 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 124 MET GLY SER LEU THR ASN HIS THR GLU THR ILE THR VAL
SEQRES 2 B 124 GLU GLU GLY GLN THR LEU THR LEU LYS CYS VAL THR SER
SEQRES 3 B 124 LEU ARG LYS ASN SER SER LEU GLN TRP LEU THR PRO SER
SEQRES 4 B 124 GLY PHE THR ILE PHE LEU ASN GLU TYR PRO VAL LEU LYS
SEQRES 5 B 124 ASN SER LYS TYR GLN LEU LEU HIS HIS SER ALA ASN GLN
SEQRES 6 B 124 LEU SER ILE THR VAL PRO ASN VAL THR LEU GLN ASP GLU
SEQRES 7 B 124 GLY VAL TYR LYS CYS LEU HIS TYR SER ASP SER VAL SER
SEQRES 8 B 124 THR LYS GLU VAL LYS VAL ILE VAL LEU ALA THR MET LYS
SEQRES 9 B 124 GLY GLU PHE CYS ARG TYR PRO SER HIS TRP ARG PRO LEU
SEQRES 10 B 124 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 124 MET GLY SER LEU THR ASN HIS THR GLU THR ILE THR VAL
SEQRES 2 C 124 GLU GLU GLY GLN THR LEU THR LEU LYS CYS VAL THR SER
SEQRES 3 C 124 LEU ARG LYS ASN SER SER LEU GLN TRP LEU THR PRO SER
SEQRES 4 C 124 GLY PHE THR ILE PHE LEU ASN GLU TYR PRO VAL LEU LYS
SEQRES 5 C 124 ASN SER LYS TYR GLN LEU LEU HIS HIS SER ALA ASN GLN
SEQRES 6 C 124 LEU SER ILE THR VAL PRO ASN VAL THR LEU GLN ASP GLU
SEQRES 7 C 124 GLY VAL TYR LYS CYS LEU HIS TYR SER ASP SER VAL SER
SEQRES 8 C 124 THR LYS GLU VAL LYS VAL ILE VAL LEU ALA THR MET LYS
SEQRES 9 C 124 GLY GLU PHE CYS ARG TYR PRO SER HIS TRP ARG PRO LEU
SEQRES 10 C 124 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 124 MET GLY SER LEU THR ASN HIS THR GLU THR ILE THR VAL
SEQRES 2 D 124 GLU GLU GLY GLN THR LEU THR LEU LYS CYS VAL THR SER
SEQRES 3 D 124 LEU ARG LYS ASN SER SER LEU GLN TRP LEU THR PRO SER
SEQRES 4 D 124 GLY PHE THR ILE PHE LEU ASN GLU TYR PRO VAL LEU LYS
SEQRES 5 D 124 ASN SER LYS TYR GLN LEU LEU HIS HIS SER ALA ASN GLN
SEQRES 6 D 124 LEU SER ILE THR VAL PRO ASN VAL THR LEU GLN ASP GLU
SEQRES 7 D 124 GLY VAL TYR LYS CYS LEU HIS TYR SER ASP SER VAL SER
SEQRES 8 D 124 THR LYS GLU VAL LYS VAL ILE VAL LEU ALA THR MET LYS
SEQRES 9 D 124 GLY GLU PHE CYS ARG TYR PRO SER HIS TRP ARG PRO LEU
SEQRES 10 D 124 GLU HIS HIS HIS HIS HIS HIS
HET PO4 A 3 5
HET PO4 B 2 5
HET PO4 C 4 5
HET PO4 D 1 5
HETNAM PO4 PHOSPHATE ION
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 9 HOH *116(H2 O)
HELIX 1 1 THR A 89 GLU A 93 5 5
HELIX 2 2 THR B 89 GLU B 93 5 5
HELIX 3 3 THR C 89 GLU C 93 5 5
HELIX 4 4 THR D 89 GLU D 93 5 5
SHEET 1 A 9 TYR A 63 PRO A 64 0
SHEET 2 A 9 THR A 57 LEU A 60 -1 N LEU A 60 O TYR A 63
SHEET 3 A 9 SER A 47 LEU A 51 -1 N TRP A 50 O ILE A 58
SHEET 4 A 9 GLY A 94 TYR A 101 -1 O LEU A 99 N GLN A 49
SHEET 5 A 9 VAL A 105 LEU A 115 -1 O VAL A 110 N TYR A 96
SHEET 6 A 9 THR A 23 GLU A 29 1 N GLU A 24 O LYS A 111
SHEET 7 A 9 GLN B 72 SER B 77 -1 O HIS B 76 N THR A 25
SHEET 8 A 9 GLN B 80 VAL B 85 -1 O GLN B 80 N SER B 77
SHEET 9 A 9 LEU B 34 VAL B 39 -1 N LEU B 36 O ILE B 83
SHEET 1 B 9 LEU A 34 VAL A 39 0
SHEET 2 B 9 GLN A 80 VAL A 85 -1 O ILE A 83 N LEU A 36
SHEET 3 B 9 GLN A 72 SER A 77 -1 N HIS A 75 O SER A 82
SHEET 4 B 9 THR D 23 GLU D 29 -1 O THR D 25 N HIS A 76
SHEET 5 B 9 VAL D 105 LEU D 115 1 O LEU D 115 N VAL D 28
SHEET 6 B 9 GLY D 94 TYR D 101 -1 N TYR D 96 O VAL D 110
SHEET 7 B 9 SER D 47 LEU D 51 -1 N LEU D 51 O LYS D 97
SHEET 8 B 9 THR D 57 LEU D 60 -1 O ILE D 58 N TRP D 50
SHEET 9 B 9 TYR D 63 PRO D 64 -1 O TYR D 63 N LEU D 60
SHEET 1 C 9 TYR B 63 PRO B 64 0
SHEET 2 C 9 THR B 57 LEU B 60 -1 N LEU B 60 O TYR B 63
SHEET 3 C 9 SER B 47 LEU B 51 -1 N TRP B 50 O ILE B 58
SHEET 4 C 9 GLY B 94 TYR B 101 -1 O LEU B 99 N GLN B 49
SHEET 5 C 9 VAL B 105 LEU B 115 -1 O VAL B 110 N TYR B 96
SHEET 6 C 9 THR B 23 GLU B 29 1 N VAL B 28 O LEU B 115
SHEET 7 C 9 GLN C 72 SER C 77 -1 O HIS C 76 N THR B 25
SHEET 8 C 9 GLN C 80 VAL C 85 -1 O SER C 82 N HIS C 75
SHEET 9 C 9 LEU C 34 VAL C 39 -1 N LEU C 34 O VAL C 85
SHEET 1 D 9 TYR C 63 PRO C 64 0
SHEET 2 D 9 THR C 57 LEU C 60 -1 N LEU C 60 O TYR C 63
SHEET 3 D 9 SER C 47 LEU C 51 -1 N TRP C 50 O ILE C 58
SHEET 4 D 9 GLY C 94 TYR C 101 -1 O LYS C 97 N LEU C 51
SHEET 5 D 9 VAL C 105 LEU C 115 -1 O VAL C 110 N TYR C 96
SHEET 6 D 9 THR C 23 GLU C 29 1 N VAL C 28 O LEU C 115
SHEET 7 D 9 GLN D 72 SER D 77 -1 O HIS D 76 N THR C 25
SHEET 8 D 9 GLN D 80 VAL D 85 -1 O GLN D 80 N SER D 77
SHEET 9 D 9 LEU D 34 VAL D 39 -1 N LEU D 36 O ILE D 83
SSBOND 1 CYS A 38 CYS A 98 1555 1555 2.08
SSBOND 2 CYS B 38 CYS B 98 1555 1555 2.10
SSBOND 3 CYS C 38 CYS C 98 1555 1555 2.08
SSBOND 4 CYS D 38 CYS D 98 1555 1555 2.09
SITE 1 AC1 5 THR A 40 SER A 41 HIS A 100 SER A 106
SITE 2 AC1 5 LYS A 108
SITE 1 AC2 5 THR B 40 SER B 41 ARG B 43 HIS B 100
SITE 2 AC2 5 SER B 106
SITE 1 AC3 5 SER C 41 ARG C 43 HIS C 100 SER C 106
SITE 2 AC3 5 LYS C 108
SITE 1 AC4 6 THR D 40 SER D 41 ARG D 43 HIS D 100
SITE 2 AC4 6 SER D 106 LYS D 108
CRYST1 116.020 116.291 79.018 90.00 90.00 90.00 C 2 2 21 32
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 0.008619 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012655 0.00000
(ATOM LINES ARE NOT SHOWN.)
END