HEADER IMMUNE SYSTEM 17-JAN-11 3QCU
TITLE CRYSTAL STRUCTURE OF THE LT3015 ANTIBODY FAB FRAGMENT IN COMPLEX WITH
TITLE 2 LYSOPHOSPHATIDIC ACID (14:0)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LT3015 ANTIBODY FAB FRAGMENT, HEAVY CHAIN;
COMPND 3 CHAIN: H, I;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: LT3015 ANTIBODY FAB FRAGMENT, LIGHT CHAIN;
COMPND 7 CHAIN: L, M;
COMPND 8 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: DKFZP686P15220;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: IGKC;
SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS ANTIBODY, LYSOPHOSPHATIDIC ACID BINDING, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.FLEMING,J.M.WOJCIAK,M.-A.CAMPBELL,T.HUXFORD
REVDAT 5 13-SEP-23 3QCU 1 REMARK HETSYN
REVDAT 4 08-NOV-17 3QCU 1 REMARK
REVDAT 3 26-JUL-17 3QCU 1 SOURCE REMARK
REVDAT 2 27-APR-11 3QCU 1 JRNL
REVDAT 1 30-MAR-11 3QCU 0
JRNL AUTH J.K.FLEMING,J.M.WOJCIAK,M.A.CAMPBELL,T.HUXFORD
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF
JRNL TITL 2 LYSOPHOSPHATIDIC ACID BINDING BY A HUMANIZED MONOCLONAL
JRNL TITL 3 ANTIBODY.
JRNL REF J.MOL.BIOL. V. 408 462 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21392506
JRNL DOI 10.1016/J.JMB.2011.02.061
REMARK 2
REMARK 2 RESOLUTION. 1.98 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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 72488
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3653
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) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5017
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 275
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6686
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 284
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.46000
REMARK 3 B22 (A**2) : -0.51000
REMARK 3 B33 (A**2) : 0.98000
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): 0.185
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.162
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.329
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6910 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9390 ; 1.288 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 868 ; 6.374 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 276 ;35.781 ;24.710
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1088 ;13.692 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;22.426 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1034 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5202 ; 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): 4340 ; 0.619 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7020 ; 1.144 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2570 ; 1.713 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2370 ; 2.757 ; 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 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 : H -10 H 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9087 -34.2621 13.0430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0598 T22: 0.1073
REMARK 3 T33: 0.0276 T12: -0.0178
REMARK 3 T13: 0.0069 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 2.6433 L22: 1.1439
REMARK 3 L33: 0.7806 L12: -1.2744
REMARK 3 L13: 0.1308 L23: -0.0123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0257 S13: -0.1268
REMARK 3 S21: 0.0192 S22: 0.0015 S23: 0.0994
REMARK 3 S31: 0.0358 S32: -0.2797 S33: -0.0001
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 : L -10 L 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5167 -18.8294 21.6458
REMARK 3 T TENSOR
REMARK 3 T11: 0.0433 T22: 0.1266
REMARK 3 T33: 0.0424 T12: 0.0341
REMARK 3 T13: 0.0079 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.2473 L22: 0.3583
REMARK 3 L33: 0.9348 L12: -0.4714
REMARK 3 L13: -0.1583 L23: 0.3358
REMARK 3 S TENSOR
REMARK 3 S11: 0.0436 S12: -0.1535 S13: 0.1473
REMARK 3 S21: 0.0329 S22: -0.0411 S23: 0.0229
REMARK 3 S31: -0.0657 S32: -0.3071 S33: -0.0025
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I -10 I 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6404 -31.6494 -12.8709
REMARK 3 T TENSOR
REMARK 3 T11: 0.1055 T22: 0.0342
REMARK 3 T33: 0.0600 T12: -0.0045
REMARK 3 T13: 0.0523 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 2.1063 L22: 1.1094
REMARK 3 L33: 0.4954 L12: 1.0528
REMARK 3 L13: 0.4307 L23: 0.2212
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: 0.0459 S13: -0.0796
REMARK 3 S21: 0.0003 S22: 0.0391 S23: -0.1467
REMARK 3 S31: 0.0485 S32: 0.0943 S33: -0.0001
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M -10 M 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 47.0607 -14.1229 -16.8001
REMARK 3 T TENSOR
REMARK 3 T11: 0.1485 T22: 0.0405
REMARK 3 T33: 0.0424 T12: -0.0144
REMARK 3 T13: 0.0274 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 2.9536 L22: 0.8324
REMARK 3 L33: 0.4115 L12: 0.8510
REMARK 3 L13: -0.2053 L23: -0.3265
REMARK 3 S TENSOR
REMARK 3 S11: -0.0290 S12: 0.2469 S13: 0.0543
REMARK 3 S21: -0.1297 S22: 0.0192 S23: -0.0478
REMARK 3 S31: 0.0283 S32: 0.0631 S33: 0.0098
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 : RESIDUAL ONLY
REMARK 4
REMARK 4 3QCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063483.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 1.0000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72518
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.979
REMARK 200 RESOLUTION RANGE LOW (A) : 46.749
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
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) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.48200
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: PHASER 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 3QCT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.095 M SODIUM CITRATE PH 5.6, 19%
REMARK 280 (V/V) ISOPROPANOL, 19% (W/V) PEG 4000, AND 5% (V/V) GLYCEROL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 65.00000
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 65.00000
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 43.26300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 92.17550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.26300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 92.17550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.26300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 92.17550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 65.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.26300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 92.17550
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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
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: 3570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M
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 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 LYS I 129
REMARK 465 SER I 130
REMARK 465 THR I 131
REMARK 465 SER I 132
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 PRO H 41 99.83 -26.38
REMARK 500 GLN H 43 -160.77 -129.81
REMARK 500 ASP H 144 62.14 67.65
REMARK 500 VAL L 51 -48.60 73.89
REMARK 500 SER L 52 -2.28 -141.79
REMARK 500 ASN L 152 -4.93 71.41
REMARK 500 GLN I 43 -168.22 -113.07
REMARK 500 ALA I 88 169.48 178.54
REMARK 500 ASP I 101 57.65 -141.49
REMARK 500 THR I 191 -62.47 -120.18
REMARK 500 VAL M 2 74.57 62.91
REMARK 500 VAL M 51 -49.17 73.30
REMARK 500 ASN M 138 61.48 63.17
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 NKN H 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NKN I 215
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QCT RELATED DB: PDB
REMARK 900 RELATED ID: 3QCV RELATED DB: PDB
DBREF 3QCU H 1 109 PDB 3QCT 3QCT 1 118
DBREF 3QCU H 110 214 UNP Q6N089 Q6N089_HUMAN 139 243
DBREF 3QCU L 1 108 PDB 3QCT 3QCT 1 113
DBREF 3QCU L 109 213 UNP P01834 IGKC_HUMAN 1 105
DBREF 3QCU I 1 109 PDB 3QCT 3QCT 1 118
DBREF 3QCU I 110 214 UNP Q6N089 Q6N089_HUMAN 139 243
DBREF 3QCU M 1 108 PDB 3QCT 3QCT 1 113
DBREF 3QCU M 109 213 UNP P01834 IGKC_HUMAN 1 105
SEQRES 1 H 223 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 223 PRO GLY GLU SER LEU LYS ILE SER CYS GLN ALA PHE GLY
SEQRES 3 H 223 TYR GLY PHE ILE ASN TYR LEU ILE GLU TRP ILE ARG GLN
SEQRES 4 H 223 MET PRO GLY GLN GLY LEU GLU TRP ILE GLY LEU ILE ASN
SEQRES 5 H 223 PRO GLY SER ASP TYR THR ASN TYR ASN GLU ASN PHE LYS
SEQRES 6 H 223 GLY GLN ALA THR LEU SER ALA ASP LYS SER SER SER THR
SEQRES 7 H 223 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR
SEQRES 8 H 223 ALA MET TYR PHE CYS ALA ARG ARG PHE GLY TYR TYR GLY
SEQRES 9 H 223 SER GLY ASN TYR PHE ASP TYR TRP GLY GLN GLY THR MET
SEQRES 10 H 223 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL
SEQRES 11 H 223 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY
SEQRES 12 H 223 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO
SEQRES 13 H 223 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR
SEQRES 14 H 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER
SEQRES 15 H 223 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER
SEQRES 16 H 223 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN
SEQRES 17 H 223 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU
SEQRES 18 H 223 PRO LYS
SEQRES 1 L 218 ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 L 218 THR PRO GLY GLU PRO ALA SER ILE SER CYS THR SER GLY
SEQRES 3 L 218 GLN SER LEU VAL HIS ILE ASN GLY ASN THR TYR LEU HIS
SEQRES 4 L 218 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU
SEQRES 5 L 218 ILE TYR LYS VAL SER ASN LEU PHE SER GLY VAL PRO ASP
SEQRES 6 L 218 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 L 218 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR
SEQRES 8 L 218 PHE CYS SER GLN SER THR HIS PHE PRO PHE THR PHE GLY
SEQRES 9 L 218 GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA
SEQRES 10 L 218 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU
SEQRES 11 L 218 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN
SEQRES 12 L 218 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP
SEQRES 13 L 218 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR
SEQRES 14 L 218 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER
SEQRES 15 L 218 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS
SEQRES 16 L 218 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER
SEQRES 17 L 218 PRO VAL THR LYS SER PHE ASN ARG GLY GLU
SEQRES 1 I 223 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 I 223 PRO GLY GLU SER LEU LYS ILE SER CYS GLN ALA PHE GLY
SEQRES 3 I 223 TYR GLY PHE ILE ASN TYR LEU ILE GLU TRP ILE ARG GLN
SEQRES 4 I 223 MET PRO GLY GLN GLY LEU GLU TRP ILE GLY LEU ILE ASN
SEQRES 5 I 223 PRO GLY SER ASP TYR THR ASN TYR ASN GLU ASN PHE LYS
SEQRES 6 I 223 GLY GLN ALA THR LEU SER ALA ASP LYS SER SER SER THR
SEQRES 7 I 223 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR
SEQRES 8 I 223 ALA MET TYR PHE CYS ALA ARG ARG PHE GLY TYR TYR GLY
SEQRES 9 I 223 SER GLY ASN TYR PHE ASP TYR TRP GLY GLN GLY THR MET
SEQRES 10 I 223 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL
SEQRES 11 I 223 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY
SEQRES 12 I 223 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO
SEQRES 13 I 223 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR
SEQRES 14 I 223 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER
SEQRES 15 I 223 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER
SEQRES 16 I 223 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN
SEQRES 17 I 223 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU
SEQRES 18 I 223 PRO LYS
SEQRES 1 M 218 ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 M 218 THR PRO GLY GLU PRO ALA SER ILE SER CYS THR SER GLY
SEQRES 3 M 218 GLN SER LEU VAL HIS ILE ASN GLY ASN THR TYR LEU HIS
SEQRES 4 M 218 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU
SEQRES 5 M 218 ILE TYR LYS VAL SER ASN LEU PHE SER GLY VAL PRO ASP
SEQRES 6 M 218 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 M 218 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR
SEQRES 8 M 218 PHE CYS SER GLN SER THR HIS PHE PRO PHE THR PHE GLY
SEQRES 9 M 218 GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA
SEQRES 10 M 218 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU
SEQRES 11 M 218 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN
SEQRES 12 M 218 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP
SEQRES 13 M 218 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR
SEQRES 14 M 218 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER
SEQRES 15 M 218 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS
SEQRES 16 M 218 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER
SEQRES 17 M 218 PRO VAL THR LYS SER PHE ASN ARG GLY GLU
HET NKN H 215 25
HET NKN I 215 25
HETNAM NKN (2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL TETRADECANOATE
HETSYN NKN 14:0 LPA; MYRISTOYL LYSOPHOSPHATIDIC ACID
FORMUL 5 NKN 2(C17 H35 O7 P)
FORMUL 7 HOH *284(H2 O)
HELIX 1 1 GLY H 28 TYR H 32 5 5
HELIX 2 2 GLU H 61 LYS H 64 5 4
HELIX 3 3 LYS H 83 THR H 87 5 5
HELIX 4 4 SER H 187 THR H 191 5 5
HELIX 5 5 LYS H 201 ASN H 204 5 4
HELIX 6 6 GLU L 79 VAL L 83 5 5
HELIX 7 7 SER L 121 SER L 127 1 7
HELIX 8 8 LYS L 183 GLU L 187 1 5
HELIX 9 9 GLY I 28 TYR I 32 5 5
HELIX 10 10 GLU I 61 LYS I 64 5 4
HELIX 11 11 LYS I 83 THR I 87 5 5
HELIX 12 12 SER I 156 ALA I 158 5 3
HELIX 13 13 SER I 187 LEU I 189 5 3
HELIX 14 14 LYS I 201 ASN I 204 5 4
HELIX 15 15 GLU M 79 VAL M 83 5 5
HELIX 16 16 SER M 121 LYS M 126 1 6
HELIX 17 17 LYS M 183 LYS M 188 1 6
SHEET 1 A 4 GLN H 3 GLN H 6 0
SHEET 2 A 4 LEU H 18 PHE H 25 -1 O GLN H 23 N VAL H 5
SHEET 3 A 4 THR H 77 TRP H 82 -1 O ALA H 78 N CYS H 22
SHEET 4 A 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77
SHEET 1 B 6 GLU H 10 LYS H 12 0
SHEET 2 B 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12
SHEET 3 B 6 ALA H 88 PHE H 96 -1 N ALA H 88 O VAL H 109
SHEET 4 B 6 ILE H 34 GLN H 39 -1 N ILE H 37 O PHE H 91
SHEET 5 B 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 B 6 THR H 57 TYR H 59 -1 O ASN H 58 N LEU H 50
SHEET 1 C 4 GLU H 10 LYS H 12 0
SHEET 2 C 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12
SHEET 3 C 4 ALA H 88 PHE H 96 -1 N ALA H 88 O VAL H 109
SHEET 4 C 4 TYR H 100D TRP H 103 -1 O PHE H 100E N ARG H 95
SHEET 1 D 4 SER H 120 LEU H 124 0
SHEET 2 D 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 D 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 D 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 E 4 SER H 120 LEU H 124 0
SHEET 2 E 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 E 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 E 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 F 3 THR H 151 TRP H 154 0
SHEET 2 F 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 F 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198
SHEET 1 G 4 MET L 4 THR L 7 0
SHEET 2 G 4 ALA L 19 SER L 25 -1 O THR L 24 N THR L 5
SHEET 3 G 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23
SHEET 4 G 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74
SHEET 1 H 6 SER L 10 VAL L 13 0
SHEET 2 H 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11
SHEET 3 H 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104
SHEET 4 H 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85
SHEET 5 H 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 H 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49
SHEET 1 I 4 SER L 10 VAL L 13 0
SHEET 2 I 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11
SHEET 3 I 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104
SHEET 4 I 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 J 4 SER L 114 PHE L 118 0
SHEET 2 J 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116
SHEET 3 J 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130
SHEET 4 J 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178
SHEET 1 K 4 ALA L 153 LEU L 154 0
SHEET 2 K 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 K 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147
SHEET 4 K 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SHEET 1 L 4 GLN I 3 GLN I 6 0
SHEET 2 L 4 LEU I 18 PHE I 25 -1 O GLN I 23 N VAL I 5
SHEET 3 L 4 THR I 77 TRP I 82 -1 O ALA I 78 N CYS I 22
SHEET 4 L 4 ALA I 67 ASP I 72 -1 N ASP I 72 O THR I 77
SHEET 1 M 6 GLU I 10 LYS I 12 0
SHEET 2 M 6 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12
SHEET 3 M 6 ALA I 88 PHE I 96 -1 N TYR I 90 O THR I 107
SHEET 4 M 6 ILE I 34 GLN I 39 -1 N ILE I 37 O PHE I 91
SHEET 5 M 6 LEU I 45 ASN I 52 -1 O GLU I 46 N ARG I 38
SHEET 6 M 6 TYR I 56 TYR I 59 -1 O ASN I 58 N LEU I 50
SHEET 1 N 4 GLU I 10 LYS I 12 0
SHEET 2 N 4 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12
SHEET 3 N 4 ALA I 88 PHE I 96 -1 N TYR I 90 O THR I 107
SHEET 4 N 4 TYR I 100D TRP I 103 -1 O PHE I 100E N ARG I 95
SHEET 1 O 4 SER I 120 LEU I 124 0
SHEET 2 O 4 THR I 135 TYR I 145 -1 O LYS I 143 N SER I 120
SHEET 3 O 4 TYR I 176 PRO I 185 -1 O LEU I 178 N VAL I 142
SHEET 4 O 4 VAL I 163 THR I 165 -1 N HIS I 164 O VAL I 181
SHEET 1 P 4 SER I 120 LEU I 124 0
SHEET 2 P 4 THR I 135 TYR I 145 -1 O LYS I 143 N SER I 120
SHEET 3 P 4 TYR I 176 PRO I 185 -1 O LEU I 178 N VAL I 142
SHEET 4 P 4 VAL I 169 LEU I 170 -1 N VAL I 169 O SER I 177
SHEET 1 Q 3 THR I 151 TRP I 154 0
SHEET 2 Q 3 ILE I 195 HIS I 200 -1 O ASN I 197 N SER I 153
SHEET 3 Q 3 THR I 205 ARG I 210 -1 O VAL I 207 N VAL I 198
SHEET 1 R 4 MET M 4 THR M 7 0
SHEET 2 R 4 ALA M 19 SER M 25 -1 O THR M 24 N THR M 5
SHEET 3 R 4 ASP M 70 ILE M 75 -1 O LEU M 73 N ILE M 21
SHEET 4 R 4 PHE M 62 SER M 67 -1 N SER M 63 O LYS M 74
SHEET 1 S 6 SER M 10 VAL M 13 0
SHEET 2 S 6 THR M 102 ILE M 106 1 O LYS M 103 N LEU M 11
SHEET 3 S 6 GLY M 84 GLN M 90 -1 N GLY M 84 O LEU M 104
SHEET 4 S 6 LEU M 33 GLN M 38 -1 N HIS M 34 O SER M 89
SHEET 5 S 6 PRO M 44 TYR M 49 -1 O LEU M 47 N TRP M 35
SHEET 6 S 6 ASN M 53 LEU M 54 -1 O ASN M 53 N TYR M 49
SHEET 1 T 4 SER M 10 VAL M 13 0
SHEET 2 T 4 THR M 102 ILE M 106 1 O LYS M 103 N LEU M 11
SHEET 3 T 4 GLY M 84 GLN M 90 -1 N GLY M 84 O LEU M 104
SHEET 4 T 4 THR M 97 PHE M 98 -1 O THR M 97 N GLN M 90
SHEET 1 U 4 SER M 114 PHE M 118 0
SHEET 2 U 4 THR M 129 PHE M 139 -1 O ASN M 137 N SER M 114
SHEET 3 U 4 TYR M 173 SER M 182 -1 O TYR M 173 N PHE M 139
SHEET 4 U 4 SER M 159 VAL M 163 -1 N GLN M 160 O THR M 178
SHEET 1 V 4 ALA M 153 LEU M 154 0
SHEET 2 V 4 LYS M 145 VAL M 150 -1 N VAL M 150 O ALA M 153
SHEET 3 V 4 VAL M 191 THR M 197 -1 O THR M 197 N LYS M 145
SHEET 4 V 4 VAL M 205 ASN M 210 -1 O VAL M 205 N VAL M 196
SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.06
SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05
SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.12
SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03
SSBOND 5 CYS I 22 CYS I 92 1555 1555 2.06
SSBOND 6 CYS I 140 CYS I 196 1555 1555 2.03
SSBOND 7 CYS M 23 CYS M 88 1555 1555 2.08
SSBOND 8 CYS M 134 CYS M 194 1555 1555 2.01
CISPEP 1 PHE H 146 PRO H 147 0 -6.06
CISPEP 2 GLU H 148 PRO H 149 0 -0.17
CISPEP 3 THR L 7 PRO L 8 0 -6.78
CISPEP 4 PHE L 94 PRO L 95 0 -5.92
CISPEP 5 TYR L 140 PRO L 141 0 4.02
CISPEP 6 PHE I 146 PRO I 147 0 -4.93
CISPEP 7 GLU I 148 PRO I 149 0 -3.11
CISPEP 8 THR M 7 PRO M 8 0 -7.03
CISPEP 9 PHE M 94 PRO M 95 0 -6.10
CISPEP 10 TYR M 140 PRO M 141 0 0.01
SITE 1 AC1 17 TYR H 56 PHE H 96 GLY H 97 TYR H 98
SITE 2 AC1 17 TYR H 99 GLY H 100 SER H 100A GLY H 100B
SITE 3 AC1 17 ASN H 100C TYR H 100D HOH H 263 HOH H 264
SITE 4 AC1 17 NKN I 215 ASN L 30 TYR L 32 LYS L 50
SITE 5 AC1 17 SER L 91
SITE 1 AC2 17 NKN H 215 TYR I 56 PHE I 96 GLY I 97
SITE 2 AC2 17 TYR I 98 TYR I 99 GLY I 100 SER I 100A
SITE 3 AC2 17 GLY I 100B ASN I 100C TYR I 100D HOH I 282
SITE 4 AC2 17 HOH I 283 ASN M 30 TYR M 32 LYS M 50
SITE 5 AC2 17 SER M 91
CRYST1 86.526 184.351 130.000 90.00 90.00 90.00 C 2 2 21 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 0.011557 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005424 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007692 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
