HEADER IMMUNE SYSTEM 05-JUN-07 2Q6W
TITLE THE STRUCTURE OF HLA-DRA, DRB3*0101 (DR52A) WITH BOUND
TITLE 2 PLATELET INTEGRIN PEPTIDE ASSOCIATED WITH FETAL AND
TITLE 3 NEONATAL ALLOIMMUNE THROMBOCYTOPENIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR
COMPND 3 ALPHA CHAIN;
COMPND 4 CHAIN: A, D;
COMPND 5 FRAGMENT: SEQUENCE DATABASE RESIDUES 26-207;
COMPND 6 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB3-1
COMPND 10 BETA CHAIN;
COMPND 11 CHAIN: B, E;
COMPND 12 FRAGMENT: SEQUENCE DATABASE RESIDUES 30-219;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: INTEGRIN BETA-3;
COMPND 16 CHAIN: C, F;
COMPND 17 FRAGMENT: SEQUENCE DATABASE RESIDUES 50-61;
COMPND 18 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61
COMPND 19 ANTIGEN;
COMPND 20 ENGINEERED: YES;
COMPND 21 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-DRA;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: S2;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HLA-DRB3;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: S2;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 OTHER_DETAILS: THE INTEGRIN PEPTIDE IS NATURALLY FOUND
SOURCE 24 HOMO SAPIENS (HUMAN).
KEYWDS DRB3, PEPTIDE-CLASS II MHC COMPLEX, FETAL-MATERNAL
KEYWDS 2 ALLOIMMUNE THROMBOCYTOPENIA, THROMBOCYTOPENIA PURPURA,
KEYWDS 3 MYASTHENIA GRAVIS, BETA 11 ARGININE, AUTOIMMUNITY, IMMUNE
KEYWDS 4 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.PARRY
REVDAT 2 24-FEB-09 2Q6W 1 VERSN
REVDAT 1 24-JUL-07 2Q6W 0
JRNL AUTH C.S.PARRY,J.GORSKI,L.J.STERN
JRNL TITL CRYSTALLOGRAPHIC STRUCTURE OF THE HUMAN LEUKOCYTE
JRNL TITL 2 ANTIGEN DRA, DRB3*0101: MODELS OF A DIRECTIONAL
JRNL TITL 3 ALLOIMMUNE RESPONSE AND AUTOIMMUNITY
JRNL REF J.MOL.BIOL. V. 371 435 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17583734
JRNL DOI 10.1016/J.JMB.2007.05.025
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 44561
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 3684
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1757
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.3770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6043
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 487
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.82000
REMARK 3 B22 (A**2) : 0.82000
REMARK 3 B33 (A**2) : -1.64000
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): 0.295
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.240
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.910
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6214 ; 0.029 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8463 ; 2.478 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 751 ; 8.266 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 307 ;34.671 ;23.257
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 945 ;18.375 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;22.268 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 910 ; 0.159 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4857 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4017 ; 0.278 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4312 ; 0.340 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 730 ; 0.235 ; 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): 58 ; 0.243 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.267 ; 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): 3823 ; 1.677 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6107 ; 2.551 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2697 ; 3.834 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2356 ; 5.641 ; 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 : 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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2Q6W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-07.
REMARK 100 THE RCSB ID CODE IS RCSB043224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48049
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 15.800
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.040
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 1DLH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% PEG 8000, 0.1M SODIUM
REMARK 280 ACETATE, 10% (V/V) GLYCEROL, 0.01M CD2+, PH 4.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 297.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 124.27750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 46.08450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.08450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.13875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.08450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.08450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 186.41625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.08450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.08450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.13875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.08450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.08450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 186.41625
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 124.27750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ILE A 1
REMARK 465 LYS A 2
REMARK 465 GLY B 1
REMARK 465 ASP B 2
REMARK 465 SER C 35
REMARK 465 ILE D 1
REMARK 465 LYS D 2
REMARK 465 GLY E 1
REMARK 465 ASP E 2
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 GLU A 46 CD OE1 OE2
REMARK 470 GLU A 47 CD OE1 OE2
REMARK 470 ARG A 50 CZ NH1 NH2
REMARK 470 PHE A 51 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 55 CG CD OE1 OE2
REMARK 470 GLN A 57 OE1 NE2
REMARK 470 LYS A 126 NZ
REMARK 470 GLU A 141 CG CD OE1 OE2
REMARK 470 GLU A 166 CD OE1 OE2
REMARK 470 ASP A 171 CG OD1 OD2
REMARK 470 ALA A 182 N CA C O CB
REMARK 470 GLY B 20 O
REMARK 470 GLU B 35 CG CD OE1 OE2
REMARK 470 LEU B 53 CG CD1 CD2
REMARK 470 ARG B 55 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 59 CD OE1 OE2
REMARK 470 SER B 63 OG
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 470 ASP B 66 CG OD1 OD2
REMARK 470 GLU B 69 O
REMARK 470 ARG B 94 NE CZ NH1 NH2
REMARK 470 HIS B 96 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 98 CG CD OE1 NE2
REMARK 470 GLN B 107 CD OE1 NE2
REMARK 470 GLN B 110 CD OE1 NE2
REMARK 470 HIS B 111 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 128 CD OE1 OE2
REMARK 470 ARG B 130 NE CZ NH1 NH2
REMARK 470 GLU B 176 CD OE1 OE2
REMARK 470 VAL B 180 CG1 CG2
REMARK 470 ALA B 190 O
REMARK 470 ILE D 7 CD1
REMARK 470 GLU D 46 C O
REMARK 470 ILE D 82 CG2
REMARK 470 ASN D 94 CG OD1 ND2
REMARK 470 GLU D 98 CG CD OE1 OE2
REMARK 470 ARG D 100 CZ NH1 NH2
REMARK 470 ILE D 106 CD1
REMARK 470 LYS D 111 NZ
REMARK 470 ALA D 182 O
REMARK 470 ASN E 19 CB CG OD1 ND2
REMARK 470 GLU E 22 CG CD OE1 OE2
REMARK 470 ARG E 23 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 52 CG CD OE1 OE2
REMARK 470 GLU E 59 CG CD OE1 OE2
REMARK 470 SER E 60 CB OG
REMARK 470 ASP E 66 CG OD1 OD2
REMARK 470 LEU E 67 CG CD1 CD2
REMARK 470 GLU E 69 CG CD OE1 OE2
REMARK 470 GLU E 128 CG CD OE1 OE2
REMARK 470 ARG E 133 CD NE CZ NH1 NH2
REMARK 470 ASN E 134 CG OD1 ND2
REMARK 470 GLN E 136 CB CG CD OE1 NE2
REMARK 470 GLU E 138 CD OE1 OE2
REMARK 470 LYS E 139 CB CG CD CE NZ
REMARK 470 ALA E 140 CB
REMARK 470 ARG E 166 CD NE CZ NH1 NH2
REMARK 470 SER E 167 CB OG
REMARK 470 VAL E 170 CB CG1 CG2
REMARK 470 ALA E 190 O
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET D 36 CG SD CE
REMARK 480 SER F 35 CB OG
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 SD MET D 36 O HOH D 293 1.00
REMARK 500 CE MET D 36 O HOH D 301 1.11
REMARK 500 SD MET D 36 O HOH D 301 1.20
REMARK 500 CE MET D 36 O HOH D 293 1.38
REMARK 500 N GLY E 125 O HOH E 278 1.38
REMARK 500 CG MET D 36 O HOH D 293 1.42
REMARK 500 O HOH D 293 O HOH D 301 1.51
REMARK 500 CA GLY E 125 O HOH E 278 1.57
REMARK 500 O MET D 36 O HOH D 253 1.74
REMARK 500 C GLY E 125 O HOH E 278 1.76
REMARK 500 N SER E 126 O HOH E 278 1.77
REMARK 500 CG2 THR E 3 O HOH E 279 1.87
REMARK 500 CB LEU B 53 O HOH B 304 1.87
REMARK 500 CD2 LEU D 92 CE1 PHE D 108 1.92
REMARK 500 C PRO E 124 O HOH E 278 1.93
REMARK 500 ND2 ASN D 118 O HOH D 295 1.95
REMARK 500 C MET D 36 O HOH D 253 1.95
REMARK 500 OH TYR E 26 OD2 ASP F 28 1.96
REMARK 500 O HOH B 290 O HOH B 313 2.03
REMARK 500 N GLU D 47 O HOH D 294 2.07
REMARK 500 CE3 TRP F 25 O HOH D 303 2.10
REMARK 500 OD2 ASP E 43 O HOH E 267 2.11
REMARK 500 O LEU E 109 O HOH E 261 2.13
REMARK 500 CD2 TRP F 25 O HOH E 280 2.15
REMARK 500 OE1 GLU A 21 O HOH A 283 2.16
REMARK 500 O HOH A 224 O HOH A 294 2.16
REMARK 500 O HOH B 256 O HOH B 311 2.17
REMARK 500 CE2 TRP F 25 O HOH E 280 2.17
REMARK 500 O HOH B 246 O HOH B 300 2.19
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 163 CB CYS A 163 SG -0.114
REMARK 500 SER B 13 CB SER B 13 OG -0.088
REMARK 500 GLU B 52 CG GLU B 52 CD 0.105
REMARK 500 GLN B 70 C GLN B 70 O 0.116
REMARK 500 TYR B 78 CZ TYR B 78 CE2 -0.093
REMARK 500 GLU B 87 CB GLU B 87 CG -0.124
REMARK 500 TYR D 150 CE2 TYR D 150 CD2 -0.107
REMARK 500 SER F 35 CA SER F 35 CB 0.176
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 44 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 LYS A 176 CD - CE - NZ ANGL. DEV. = -16.1 DEGREES
REMARK 500 GLY B 20 CA - C - N ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG B 23 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLU B 69 CA - C - N ANGL. DEV. = -18.6 DEGREES
REMARK 500 LEU B 158 CB - CG - CD2 ANGL. DEV. = -12.4 DEGREES
REMARK 500 CYS B 173 CA - CB - SG ANGL. DEV. = -10.9 DEGREES
REMARK 500 MET D 36 CA - CB - CG ANGL. DEV. = -17.7 DEGREES
REMARK 500 LEU D 92 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG D 146 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG E 29 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG E 29 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG E 93 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 SER E 126 N - CA - CB ANGL. DEV. = -12.0 DEGREES
REMARK 500 SER F 35 N - CA - CB ANGL. DEV. = 13.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 36 -74.28 -60.52
REMARK 500 ALA A 37 123.75 -34.13
REMARK 500 LYS A 38 -16.28 89.80
REMARK 500 HIS A 143 -7.71 80.07
REMARK 500 SER A 156 139.00 -172.46
REMARK 500 ASN B 19 65.00 63.05
REMARK 500 ASN B 33 -128.81 58.03
REMARK 500 TYR B 78 -61.27 -136.37
REMARK 500 THR B 90 -74.43 -122.83
REMARK 500 GLN B 110 -14.73 84.94
REMARK 500 ASN B 134 54.54 32.96
REMARK 500 TRP B 153 31.88 70.53
REMARK 500 SER B 167 129.91 -35.07
REMARK 500 LYS D 39 53.06 36.00
REMARK 500 ARG D 100 7.33 82.30
REMARK 500 HIS D 143 -3.67 66.31
REMARK 500 ARG E 4 142.06 -34.88
REMARK 500 ASN E 33 -114.42 56.51
REMARK 500 ALA E 58 -73.88 -40.62
REMARK 500 ASN E 62 2.29 -58.83
REMARK 500 TYR E 78 -65.65 -138.69
REMARK 500 THR E 90 -79.22 -123.40
REMARK 500 GLN E 110 -14.25 76.86
REMARK 500 SER E 126 118.90 -37.66
REMARK 500 ASN E 134 71.48 -150.42
REMARK 500 TRP E 153 32.13 70.04
REMARK 500 SER E 182 -147.33 -77.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 87 GLU A 88 148.10
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 250 DISTANCE = 5.70 ANGSTROMS
DBREF 2Q6W A 1 182 UNP P01903 2DRA_HUMAN 26 207
DBREF 2Q6W B 1 190 UNP P79483 2B31_HUMAN 30 219
DBREF 2Q6W C 24 35 UNP P05106 ITB3_HUMAN 50 61
DBREF 2Q6W D 1 182 UNP P01903 2DRA_HUMAN 26 207
DBREF 2Q6W E 1 190 UNP P79483 2B31_HUMAN 30 219
DBREF 2Q6W F 24 35 UNP P05106 ITB3_HUMAN 50 61
SEQADV 2Q6W ARG C 26 UNP P05106 CYS 52 ENGINEERED
SEQADV 2Q6W ARG F 26 UNP P05106 CYS 52 ENGINEERED
SEQRES 1 A 182 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 182 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 182 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 182 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 182 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 182 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 182 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 182 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 182 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 182 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 182 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 182 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 182 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 182 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES 1 B 190 GLY ASP THR ARG PRO ARG PHE LEU GLU LEU ARG LYS SER
SEQRES 2 B 190 GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG TYR
SEQRES 3 B 190 LEU ASP ARG TYR PHE HIS ASN GLN GLU GLU PHE LEU ARG
SEQRES 4 B 190 PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES 5 B 190 LEU GLY ARG PRO VAL ALA GLU SER TRP ASN SER GLN LYS
SEQRES 6 B 190 ASP LEU LEU GLU GLN LYS ARG GLY ARG VAL ASP ASN TYR
SEQRES 7 B 190 CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES 8 B 190 GLN ARG ARG VAL HIS PRO GLN VAL THR VAL TYR PRO ALA
SEQRES 9 B 190 LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES 10 B 190 SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES 11 B 190 TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES 12 B 190 SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES 13 B 190 THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES 14 B 190 VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES 15 B 190 ALA LEU THR VAL GLU TRP ARG ALA
SEQRES 1 C 12 ALA TRP ARG SER ASP GLU ALA LEU PRO LEU GLY SER
SEQRES 1 D 182 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 D 182 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 D 182 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 D 182 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 D 182 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 D 182 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 D 182 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 D 182 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 D 182 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 D 182 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 D 182 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 D 182 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 D 182 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 D 182 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES 1 E 190 GLY ASP THR ARG PRO ARG PHE LEU GLU LEU ARG LYS SER
SEQRES 2 E 190 GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG TYR
SEQRES 3 E 190 LEU ASP ARG TYR PHE HIS ASN GLN GLU GLU PHE LEU ARG
SEQRES 4 E 190 PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES 5 E 190 LEU GLY ARG PRO VAL ALA GLU SER TRP ASN SER GLN LYS
SEQRES 6 E 190 ASP LEU LEU GLU GLN LYS ARG GLY ARG VAL ASP ASN TYR
SEQRES 7 E 190 CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES 8 E 190 GLN ARG ARG VAL HIS PRO GLN VAL THR VAL TYR PRO ALA
SEQRES 9 E 190 LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES 10 E 190 SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES 11 E 190 TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES 12 E 190 SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES 13 E 190 THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES 14 E 190 VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES 15 E 190 ALA LEU THR VAL GLU TRP ARG ALA
SEQRES 1 F 12 ALA TRP ARG SER ASP GLU ALA LEU PRO LEU GLY SER
FORMUL 7 HOH *487(H2 O)
HELIX 1 1 GLU A 47 ALA A 52 1 6
HELIX 2 2 GLU A 55 SER A 77 1 23
HELIX 3 3 THR B 51 LEU B 53 5 3
HELIX 4 4 GLY B 54 SER B 63 1 10
HELIX 5 5 GLN B 64 ARG B 72 1 9
HELIX 6 6 GLY B 73 TYR B 78 1 6
HELIX 7 7 TYR B 78 GLU B 87 1 10
HELIX 8 8 GLU D 47 PHE D 51 5 5
HELIX 9 9 GLU D 55 SER D 77 1 23
HELIX 10 10 THR E 51 LEU E 53 5 3
HELIX 11 11 GLY E 54 SER E 63 1 10
HELIX 12 12 GLN E 64 GLY E 73 1 10
HELIX 13 13 GLY E 73 TYR E 78 1 6
HELIX 14 14 TYR E 78 GLU E 87 1 10
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 N ASP A 35 O GLU A 40
SHEET 3 A 8 SER A 19 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 4 A 8 HIS A 5 ASN A 15 -1 N LEU A 14 O SER A 19
SHEET 5 A 8 PHE B 7 PHE B 18 -1 O PHE B 7 N ASN A 15
SHEET 6 A 8 ARG B 23 HIS B 32 -1 O ARG B 25 N HIS B 16
SHEET 7 A 8 GLU B 35 ASP B 41 -1 O GLU B 35 N HIS B 32
SHEET 8 A 8 TYR B 47 ALA B 49 -1 O ARG B 48 N ARG B 39
SHEET 1 B 4 GLU A 88 THR A 93 0
SHEET 2 B 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 B 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 B 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 C 4 GLU A 88 THR A 93 0
SHEET 2 C 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 C 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 C 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 D 4 LYS A 126 VAL A 128 0
SHEET 2 D 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 D 4 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 D 4 LEU A 174 TRP A 178 -1 O LYS A 176 N CYS A 163
SHEET 1 E 4 GLN B 98 PRO B 103 0
SHEET 2 E 4 ASN B 113 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 E 4 PHE B 155 THR B 163 -1 O THR B 163 N ASN B 113
SHEET 4 E 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 F 4 GLN B 98 PRO B 103 0
SHEET 2 F 4 ASN B 113 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 F 4 PHE B 155 THR B 163 -1 O THR B 163 N ASN B 113
SHEET 4 F 4 ILE B 148 GLN B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 G 4 GLN B 136 GLU B 138 0
SHEET 2 G 4 GLU B 128 ARG B 133 -1 N TRP B 131 O GLU B 138
SHEET 3 G 4 VAL B 170 GLU B 176 -1 O GLU B 176 N GLU B 128
SHEET 4 G 4 LEU B 184 ARG B 189 -1 O LEU B 184 N VAL B 175
SHEET 1 H 8 GLU D 40 TRP D 43 0
SHEET 2 H 8 ASP D 29 ASP D 35 -1 N HIS D 33 O VAL D 42
SHEET 3 H 8 SER D 19 PHE D 26 -1 N PHE D 26 O ASP D 29
SHEET 4 H 8 HIS D 5 ASN D 15 -1 N LEU D 14 O SER D 19
SHEET 5 H 8 PHE E 7 PHE E 18 -1 O PHE E 7 N ASN D 15
SHEET 6 H 8 ARG E 23 HIS E 32 -1 O LEU E 27 N GLU E 14
SHEET 7 H 8 GLU E 35 ASP E 41 -1 O GLU E 35 N HIS E 32
SHEET 8 H 8 TYR E 47 ALA E 49 -1 O ARG E 48 N ARG E 39
SHEET 1 I 4 GLU D 88 THR D 93 0
SHEET 2 I 4 ASN D 103 PHE D 112 -1 O ILE D 106 N LEU D 92
SHEET 3 I 4 PHE D 145 PHE D 153 -1 O LEU D 151 N LEU D 105
SHEET 4 I 4 SER D 133 GLU D 134 -1 N SER D 133 O TYR D 150
SHEET 1 J 4 GLU D 88 THR D 93 0
SHEET 2 J 4 ASN D 103 PHE D 112 -1 O ILE D 106 N LEU D 92
SHEET 3 J 4 PHE D 145 PHE D 153 -1 O LEU D 151 N LEU D 105
SHEET 4 J 4 LEU D 138 PRO D 139 -1 N LEU D 138 O ARG D 146
SHEET 1 K 4 LYS D 126 VAL D 128 0
SHEET 2 K 4 ASN D 118 ARG D 123 -1 N ARG D 123 O LYS D 126
SHEET 3 K 4 VAL D 160 GLU D 166 -1 O ARG D 164 N THR D 120
SHEET 4 K 4 LEU D 174 GLU D 179 -1 O TRP D 178 N TYR D 161
SHEET 1 L 4 GLN E 98 PRO E 103 0
SHEET 2 L 4 ASN E 113 PHE E 122 -1 O SER E 120 N GLN E 98
SHEET 3 L 4 PHE E 155 THR E 163 -1 O VAL E 159 N CYS E 117
SHEET 4 L 4 VAL E 142 SER E 144 -1 N VAL E 143 O MET E 160
SHEET 1 M 4 GLN E 98 PRO E 103 0
SHEET 2 M 4 ASN E 113 PHE E 122 -1 O SER E 120 N GLN E 98
SHEET 3 M 4 PHE E 155 THR E 163 -1 O VAL E 159 N CYS E 117
SHEET 4 M 4 ILE E 148 GLN E 149 -1 N ILE E 148 O GLN E 156
SHEET 1 N 4 GLU E 137 GLU E 138 0
SHEET 2 N 4 GLU E 128 PHE E 132 -1 N TRP E 131 O GLU E 138
SHEET 3 N 4 VAL E 170 GLU E 176 -1 O THR E 172 N PHE E 132
SHEET 4 N 4 LEU E 184 ARG E 189 -1 O VAL E 186 N CYS E 173
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.02
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.20
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.00
SSBOND 4 CYS D 107 CYS D 163 1555 1555 2.10
SSBOND 5 CYS E 15 CYS E 79 1555 1555 2.23
SSBOND 6 CYS E 117 CYS E 173 1555 1555 2.01
CISPEP 1 ASN A 15 PRO A 16 0 1.84
CISPEP 2 THR A 113 PRO A 114 0 -0.30
CISPEP 3 TYR B 123 PRO B 124 0 1.72
CISPEP 4 ASN D 15 PRO D 16 0 4.20
CISPEP 5 THR D 113 PRO D 114 0 -5.41
CISPEP 6 TYR E 123 PRO E 124 0 1.28
CRYST1 92.169 92.169 248.555 90.00 90.00 90.00 P 41 21 2 16
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 0.010850 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010850 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004023 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
