HEADER IMMUNE SYSTEM/INHIBITOR 23-OCT-16 5BJT
TITLE CRYSTAL STRUCTURE OF HUMAN FCRN WITH A PEPTIDE INHIBITOR AT MULTIPLE
TITLE 2 SITES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGG RECEPTOR FCRN LARGE SUBUNIT P51;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN (UNP RESIDUES 24-290);
COMPND 5 SYNONYM: FCRN, IGG FC FRAGMENT RECEPTOR TRANSPORTER ALPHA CHAIN,
COMPND 6 NEONATAL FC RECEPTOR;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 10 CHAIN: B, D, F, H;
COMPND 11 FRAGMENT: UNP RESIDUES 21-119;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PEPTIDE INHIBITOR;
COMPND 15 CHAIN: P, Q, R, S, T, U, V;
COMPND 16 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: FCGRT, FCRN;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 20 ORGANISM_TAXID: 32630
KEYWDS IMMUNOGLOBULIN BINDING PROTEIN, CELL MEMBRANE, DISULFIDE BOND,
KEYWDS 2 GLYCOPROTEIN, IGG-BINDING PROTEIN, IMMUNOGLOBULIN DOMAIN, RECEPTOR,
KEYWDS 3 TRANSMEMBRANE, AMYLOID, AMYLOIDOSIS, DISEASE MUTATION, GLYCATION,
KEYWDS 4 IMMUNE RESPONSE, MHC I, PYRROLIDONE CARBOXYLIC ACID, SECRETED,
KEYWDS 5 IMMUNE SYSTEM-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.NIENABER,J.BADGER
REVDAT 4 27-SEP-23 5BJT 1 REMARK
REVDAT 3 19-APR-17 5BJT 1 JRNL
REVDAT 2 05-APR-17 5BJT 1 JRNL
REVDAT 1 22-MAR-17 5BJT 0
JRNL AUTH M.PYZIK,T.RATH,T.T.KUO,S.WIN,K.BAKER,J.J.HUBBARD,R.GRENHA,
JRNL AUTH 2 A.GANDHI,T.D.KRAMER,A.R.MEZO,Z.S.TAYLOR,K.MCDONNELL,
JRNL AUTH 3 V.NIENABER,J.T.ANDERSEN,A.MIZOGUCHI,L.BLUMBERG,S.PUROHIT,
JRNL AUTH 4 S.D.JONES,G.CHRISTIANSON,W.I.LENCER,I.SANDLIE,N.KAPLOWITZ,
JRNL AUTH 5 D.C.ROOPENIAN,R.S.BLUMBERG
JRNL TITL HEPATIC FCRN REGULATES ALBUMIN HOMEOSTASIS AND
JRNL TITL 2 SUSCEPTIBILITY TO LIVER INJURY.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E2862 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28330995
JRNL DOI 10.1073/PNAS.1618291114
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 35848
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) : 0.257
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.339
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1885
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2540
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.5040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11486
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.13000
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): 0.624
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.520
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.352
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.879
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.790
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11859 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16261 ; 1.965 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1545 ; 8.613 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 496 ;37.436 ;23.609
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1440 ;24.685 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;22.932 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1730 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9444 ; 0.008 ; 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): 7751 ; 0.973 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12125 ; 1.830 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4108 ; 1.847 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4136 ; 3.095 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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: NULL
REMARK 4
REMARK 4 5BJT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1001310036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37736
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.71800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 3M17
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 20% GLYCEROL,
REMARK 280 0.8 M SODIUM ACETATE, PH 4.7, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+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 0.00000
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 0.00000
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 52.45850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 88.07600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 122.75750
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 52.45850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 88.07600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 122.75750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 52.45850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 88.07600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 122.75750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 52.45850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 88.07600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 122.75750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11
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: 2570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
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: 2570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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
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: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
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: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 1600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 1720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 1710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 1530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 1450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 1540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 1450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: V
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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 SER A 3
REMARK 465 HIS A 4
REMARK 465 ALA C 1
REMARK 465 GLU C 2
REMARK 465 SER C 3
REMARK 465 HIS C 4
REMARK 465 ALA E 1
REMARK 465 GLU E 2
REMARK 465 SER E 3
REMARK 465 HIS E 4
REMARK 465 ALA G 1
REMARK 465 GLU G 2
REMARK 465 SER G 3
REMARK 465 HIS G 4
REMARK 465 ACE P 0
REMARK 465 THR P 17
REMARK 465 NH2 P 18
REMARK 465 ACE Q 0
REMARK 465 THR Q 17
REMARK 465 NH2 Q 18
REMARK 465 ACE R 0
REMARK 465 THR R 17
REMARK 465 NH2 R 18
REMARK 465 ACE S 0
REMARK 465 THR S 17
REMARK 465 NH2 S 18
REMARK 465 ACE T 0
REMARK 465 THR T 17
REMARK 465 NH2 T 18
REMARK 465 ACE U 0
REMARK 465 THR U 17
REMARK 465 NH2 U 18
REMARK 465 ACE V 0
REMARK 465 THR V 17
REMARK 465 NH2 V 18
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 ARG A 42 CG CD NE CZ NH1 NH2
REMARK 470 SER A 58 OG
REMARK 470 TRP A 59 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 59 CZ3 CH2
REMARK 470 GLU A 62 CG CD OE1 OE2
REMARK 470 LYS A 63 CD CE NZ
REMARK 470 LYS A 73 CD CE NZ
REMARK 470 LYS A 85 CG CD CE NZ
REMARK 470 ASN A 102 CG OD1 ND2
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 GLN A 124 CG CD OE1 NE2
REMARK 470 ASP A 130 CG OD1 OD2
REMARK 470 TRP A 131 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 131 CZ3 CH2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 143 CG CD OE1 NE2
REMARK 470 ASP A 145 CG OD1 OD2
REMARK 470 LYS A 146 CG CD CE NZ
REMARK 470 LYS A 150 CD CE NZ
REMARK 470 LYS A 177 CD CE NZ
REMARK 470 LYS A 185 CG CD CE NZ
REMARK 470 SER A 189 OG
REMARK 470 SER A 190 OG
REMARK 470 LEU A 217 CG CD1 CD2
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 ARG A 264 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 266 CG CD OE1 OE2
REMARK 470 LYS B 6 CG CD CE NZ
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 ASP B 53 CG OD1 OD2
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 91 CG CD CE NZ
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 LEU C 5 CG CD1 CD2
REMARK 470 ARG C 42 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 57 CG1 CG2
REMARK 470 TRP C 59 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 59 CZ3 CH2
REMARK 470 LYS C 63 CG CD CE NZ
REMARK 470 LYS C 73 CG CD CE NZ
REMARK 470 LYS C 80 CG CD CE NZ
REMARK 470 LYS C 85 CG CD CE NZ
REMARK 470 LEU C 98 CG CD1 CD2
REMARK 470 ASN C 102 CG OD1 ND2
REMARK 470 THR C 103 OG1 CG2
REMARK 470 LYS C 123 CG CD CE NZ
REMARK 470 LYS C 146 CG CD CE NZ
REMARK 470 GLU C 168 CG CD OE1 OE2
REMARK 470 GLU C 175 CG CD OE1 OE2
REMARK 470 LYS C 185 CG CD CE NZ
REMARK 470 ARG C 187 CG CD NE CZ NH1 NH2
REMARK 470 SER C 189 OG
REMARK 470 SER C 190 OG
REMARK 470 ARG C 211 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 214 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 215 CG OD1 ND2
REMARK 470 LEU C 217 CG CD1 CD2
REMARK 470 GLN C 223 CG CD OE1 NE2
REMARK 470 LYS C 243 CG CD CE NZ
REMARK 470 GLU C 247 CG CD OE1 OE2
REMARK 470 LEU C 263 CG CD1 CD2
REMARK 470 ARG C 264 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 19 CG CD CE NZ
REMARK 470 SER D 20 OG
REMARK 470 GLU D 36 CG CD OE1 OE2
REMARK 470 LYS D 41 CG CD CE NZ
REMARK 470 GLU D 44 CG CD OE1 OE2
REMARK 470 ARG D 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 LYS D 58 CG CD CE NZ
REMARK 470 LYS D 75 CG CD CE NZ
REMARK 470 GLU D 77 CG CD OE1 OE2
REMARK 470 LYS D 91 CD CE NZ
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 ARG D 97 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 98 CG OD1 OD2
REMARK 470 LEU E 5 CG CD1 CD2
REMARK 470 ARG E 42 CG CD NE CZ NH1 NH2
REMARK 470 VAL E 57 CG1 CG2
REMARK 470 SER E 58 OG
REMARK 470 TRP E 59 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP E 59 CZ3 CH2
REMARK 470 GLU E 62 CG CD OE1 OE2
REMARK 470 LYS E 63 CD CE NZ
REMARK 470 LYS E 73 CD CE NZ
REMARK 470 GLU E 77 CG CD OE1 OE2
REMARK 470 LYS E 80 CG CD CE NZ
REMARK 470 LYS E 85 CG CD CE NZ
REMARK 470 ASN E 102 CG OD1 ND2
REMARK 470 THR E 103 OG1 CG2
REMARK 470 LYS E 109 CD CE NZ
REMARK 470 LYS E 123 CG CD CE NZ
REMARK 470 LYS E 146 CG CD CE NZ
REMARK 470 GLU E 168 CG CD OE1 OE2
REMARK 470 LYS E 185 CG CD CE NZ
REMARK 470 ARG E 187 CG CD NE CZ NH1 NH2
REMARK 470 SER E 189 OG
REMARK 470 SER E 190 OG
REMARK 470 SER E 194 OG
REMARK 470 ARG E 211 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 214 CG CD NE CZ NH1 NH2
REMARK 470 ASN E 215 CG OD1 ND2
REMARK 470 LEU E 217 CG CD1 CD2
REMARK 470 GLN E 223 CG CD OE1 NE2
REMARK 470 LYS E 243 CE NZ
REMARK 470 SER E 244 OG
REMARK 470 GLU E 266 CG CD OE1 OE2
REMARK 470 GLU F 16 CG CD OE1 OE2
REMARK 470 LYS F 19 CG CD CE NZ
REMARK 470 SER F 20 OG
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 GLU F 50 CG CD OE1 OE2
REMARK 470 SER F 57 OG
REMARK 470 LYS F 58 CG CD CE NZ
REMARK 470 GLU F 69 CG CD OE1 OE2
REMARK 470 GLU F 74 CG CD OE1 OE2
REMARK 470 LYS F 75 CG CD CE NZ
REMARK 470 GLU F 77 CG CD OE1 OE2
REMARK 470 ARG F 81 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 91 CD CE NZ
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 ASP F 98 CG OD1 OD2
REMARK 470 LEU G 5 CG CD1 CD2
REMARK 470 LEU G 8 CG CD1 CD2
REMARK 470 SER G 15 OG
REMARK 470 SER G 16 OG
REMARK 470 SER G 27 OG
REMARK 470 GLN G 33 CG CD OE1 NE2
REMARK 470 TYR G 35 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU G 41 CG CD1 CD2
REMARK 470 ARG G 42 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 44 CG CD OE1 OE2
REMARK 470 GLU G 46 CG CD OE1 OE2
REMARK 470 GLU G 54 CG CD OE1 OE2
REMARK 470 VAL G 57 CG1 CG2
REMARK 470 SER G 58 OG
REMARK 470 GLU G 62 CG CD OE1 OE2
REMARK 470 LYS G 63 CG CD CE NZ
REMARK 470 LYS G 71 CG CD CE NZ
REMARK 470 LYS G 73 CG CD CE NZ
REMARK 470 GLU G 77 CG CD OE1 OE2
REMARK 470 LYS G 80 CG CD CE NZ
REMARK 470 LYS G 85 CG CD CE NZ
REMARK 470 GLU G 97 CG CD OE1 OE2
REMARK 470 LEU G 98 CG CD1 CD2
REMARK 470 ASP G 101 CG OD1 OD2
REMARK 470 ASN G 102 CG OD1 ND2
REMARK 470 THR G 103 OG1 CG2
REMARK 470 SER G 104 OG
REMARK 470 VAL G 105 CG1 CG2
REMARK 470 THR G 107 OG1 CG2
REMARK 470 LYS G 109 CG CD CE NZ
REMARK 470 ASN G 119 CG OD1 ND2
REMARK 470 LEU G 122 CG CD1 CD2
REMARK 470 LYS G 123 CG CD CE NZ
REMARK 470 GLN G 124 CG CD OE1 NE2
REMARK 470 THR G 126 OG1 CG2
REMARK 470 GLN G 142 CG CD OE1 NE2
REMARK 470 GLN G 143 CG CD OE1 NE2
REMARK 470 LYS G 146 CG CD CE NZ
REMARK 470 LYS G 150 CG CD CE NZ
REMARK 470 LEU G 152 CG CD1 CD2
REMARK 470 PHE G 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER G 158 OG
REMARK 470 HIS G 161 CG ND1 CD2 CE1 NE2
REMARK 470 ARG G 162 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 164 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 165 CG CD OE1 OE2
REMARK 470 GLU G 168 CG CD OE1 OE2
REMARK 470 ARG G 169 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 171 CG CD NE CZ NH1 NH2
REMARK 470 ASN G 173 CG OD1 ND2
REMARK 470 LEU G 174 CG CD1 CD2
REMARK 470 GLU G 175 CG CD OE1 OE2
REMARK 470 TRP G 176 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 176 CZ3 CH2
REMARK 470 LYS G 177 CG CD CE NZ
REMARK 470 GLU G 178 CG CD OE1 OE2
REMARK 470 SER G 181 OG
REMARK 470 ARG G 183 CG CD NE CZ NH1 NH2
REMARK 470 LEU G 184 CG CD1 CD2
REMARK 470 LYS G 185 CG CD CE NZ
REMARK 470 ARG G 187 CG CD NE CZ NH1 NH2
REMARK 470 SER G 189 OG
REMARK 470 SER G 190 OG
REMARK 470 PHE G 193 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER G 194 OG
REMARK 470 VAL G 195 CG1 CG2
REMARK 470 LEU G 196 CG CD1 CD2
REMARK 470 THR G 197 OG1 CG2
REMARK 470 CYS G 198 SG
REMARK 470 SER G 199 OG
REMARK 470 PHE G 201 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER G 202 OG
REMARK 470 PHE G 203 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR G 204 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU G 207 CG CD OE1 OE2
REMARK 470 LEU G 208 CG CD1 CD2
REMARK 470 GLN G 209 CG CD OE1 NE2
REMARK 470 LEU G 210 CG CD1 CD2
REMARK 470 ARG G 211 CG CD NE CZ NH1 NH2
REMARK 470 PHE G 212 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU G 213 CG CD1 CD2
REMARK 470 ARG G 214 CG CD NE CZ NH1 NH2
REMARK 470 ASN G 215 CG OD1 ND2
REMARK 470 LEU G 217 CG CD1 CD2
REMARK 470 THR G 221 OG1 CG2
REMARK 470 GLN G 223 CG CD OE1 NE2
REMARK 470 ASP G 225 CG OD1 OD2
REMARK 470 PHE G 226 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN G 229 CG OD1 ND2
REMARK 470 SER G 230 OG
REMARK 470 ASP G 231 CG OD1 OD2
REMARK 470 SER G 233 OG
REMARK 470 PHE G 234 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER G 237 OG
REMARK 470 SER G 238 OG
REMARK 470 SER G 239 OG
REMARK 470 LEU G 240 CG CD1 CD2
REMARK 470 THR G 241 OG1 CG2
REMARK 470 VAL G 242 CG1 CG2
REMARK 470 LYS G 243 CG CD CE NZ
REMARK 470 SER G 244 OG
REMARK 470 ASP G 246 CG OD1 OD2
REMARK 470 GLU G 247 CG CD OE1 OE2
REMARK 470 HIS G 248 CG ND1 CD2 CE1 NE2
REMARK 470 HIS G 249 CG ND1 CD2 CE1 NE2
REMARK 470 TYR G 250 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 CYS G 251 SG
REMARK 470 CYS G 252 SG
REMARK 470 ILE G 253 CG1 CG2 CD1
REMARK 470 VAL G 254 CG1 CG2
REMARK 470 GLN G 255 CG CD OE1 NE2
REMARK 470 HIS G 256 CG ND1 CD2 CE1 NE2
REMARK 470 LEU G 259 CG CD1 CD2
REMARK 470 GLN G 261 CG CD OE1 NE2
REMARK 470 LEU G 263 CG CD1 CD2
REMARK 470 ARG G 264 CG CD NE CZ NH1 NH2
REMARK 470 VAL G 265 CG1 CG2
REMARK 470 GLU G 266 CG CD OE1 OE2
REMARK 470 LEU G 267 CG CD1 CD2
REMARK 470 ILE H 1 CG1 CG2 CD1
REMARK 470 LYS H 6 CG CD CE NZ
REMARK 470 LYS H 48 CG CD CE NZ
REMARK 470 LYS H 58 CD CE NZ
REMARK 470 LYS H 75 CG CD CE NZ
REMARK 470 GLU H 77 CG CD OE1 OE2
REMARK 470 LYS H 91 CD CE NZ
REMARK 470 LYS H 94 CD CE NZ
REMARK 470 ARG P 1 CG CD NE CZ NH1 NH2
REMARK 470 LYS P 6 CG CD CE NZ
REMARK 470 LYS P 8 CG CD CE NZ
REMARK 470 HIS P 9 CG ND1 CD2 CE1 NE2
REMARK 470 GLU P 13 CG CD OE1 OE2
REMARK 470 GLU P 14 CG CD OE1 OE2
REMARK 470 LYS Q 6 CG CD CE NZ
REMARK 470 LYS Q 8 CG CD CE NZ
REMARK 470 HIS Q 9 CG ND1 CD2 CE1 NE2
REMARK 470 GLU Q 13 CG CD OE1 OE2
REMARK 470 GLU Q 14 CG CD OE1 OE2
REMARK 470 LYS R 6 CG CD CE NZ
REMARK 470 LYS R 8 CG CD CE NZ
REMARK 470 HIS R 9 CG ND1 CD2 CE1 NE2
REMARK 470 GLU R 13 CG CD OE1 OE2
REMARK 470 GLU R 14 CG CD OE1 OE2
REMARK 470 LYS S 6 CG CD CE NZ
REMARK 470 LYS S 8 CG CD CE NZ
REMARK 470 HIS S 9 CG ND1 CD2 CE1 NE2
REMARK 470 TRP S 11 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP S 11 CZ3 CH2
REMARK 470 GLU S 13 CG CD OE1 OE2
REMARK 470 GLU S 14 CG CD OE1 OE2
REMARK 470 ARG T 1 CG CD NE CZ NH1 NH2
REMARK 470 LYS T 6 CG CD CE NZ
REMARK 470 LYS T 8 CG CD CE NZ
REMARK 470 HIS T 9 CG ND1 CD2 CE1 NE2
REMARK 470 TRP T 11 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP T 11 CZ3 CH2
REMARK 470 GLU T 13 CG CD OE1 OE2
REMARK 470 GLU T 14 CG CD OE1 OE2
REMARK 470 LYS U 6 CG CD CE NZ
REMARK 470 LYS U 8 CG CD CE NZ
REMARK 470 HIS U 9 CG ND1 CD2 CE1 NE2
REMARK 470 TRP U 11 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP U 11 CZ3 CH2
REMARK 470 GLU U 13 CG CD OE1 OE2
REMARK 470 GLU U 14 CG CD OE1 OE2
REMARK 470 ARG V 1 CG CD NE CZ NH1 NH2
REMARK 470 LYS V 6 CG CD CE NZ
REMARK 470 LYS V 8 CG CD CE NZ
REMARK 470 HIS V 9 CG ND1 CD2 CE1 NE2
REMARK 470 TRP V 11 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP V 11 CZ3 CH2
REMARK 470 GLU V 13 CG CD OE1 OE2
REMARK 470 GLU V 14 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER A 202 O PHE A 234 2.02
REMARK 500 O ASN D 17 N LYS D 19 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 O LEU E 259 O LEU E 259 3555 2.13
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 TRP C 53 CB TRP C 53 CG -0.125
REMARK 500 HIS H 31 CG HIS H 31 CD2 0.057
REMARK 500 CYS T 12 CB CYS T 12 SG -0.096
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 PRO A 100 C - N - CA ANGL. DEV. = 11.6 DEGREES
REMARK 500 PRO A 132 C - N - CA ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG A 164 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 PRO A 228 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO C 32 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 LEU C 41 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 PRO C 100 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO C 206 C - N - CA ANGL. DEV. = 10.6 DEGREES
REMARK 500 PRO G 47 C - N - CA ANGL. DEV. = 10.6 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 ARG A 42 -21.15 -146.43
REMARK 500 VAL A 57 18.80 -64.05
REMARK 500 SER A 58 -58.35 40.72
REMARK 500 TRP A 59 29.69 -61.42
REMARK 500 THR A 65 -71.72 -52.61
REMARK 500 ALA A 81 12.63 -69.95
REMARK 500 PRO A 100 -41.16 4.99
REMARK 500 ASP A 101 50.99 -101.05
REMARK 500 ASN A 102 73.35 36.88
REMARK 500 ASN A 113 82.45 42.17
REMARK 500 PHE A 117 -26.32 -147.96
REMARK 500 THR A 126 -167.51 -165.88
REMARK 500 PRO A 132 -78.22 -8.65
REMARK 500 ALA A 134 -70.69 -64.78
REMARK 500 LEU A 135 -54.93 -29.35
REMARK 500 GLN A 142 -76.60 -42.18
REMARK 500 GLN A 143 59.29 -64.23
REMARK 500 PHE A 157 -76.00 -106.59
REMARK 500 SER A 202 -113.28 68.86
REMARK 500 PHE A 203 124.51 56.05
REMARK 500 PRO A 205 173.57 -59.76
REMARK 500 ASN A 215 41.48 21.62
REMARK 500 GLU A 247 -89.61 2.88
REMARK 500 HIS A 248 -4.59 -59.48
REMARK 500 GLN A 261 -159.10 -89.18
REMARK 500 ALA B 15 116.45 -26.62
REMARK 500 ASN B 17 87.99 -46.21
REMARK 500 ASN B 21 -145.75 -140.19
REMARK 500 PHE B 22 121.17 -171.54
REMARK 500 SER B 28 107.44 -164.83
REMARK 500 HIS B 31 126.18 -175.78
REMARK 500 ASN B 42 -32.18 65.13
REMARK 500 GLU B 47 -75.16 -77.08
REMARK 500 SER B 52 176.67 -55.86
REMARK 500 SER B 55 -169.96 -128.66
REMARK 500 ASP B 59 31.25 -147.10
REMARK 500 PHE B 70 -173.82 -171.74
REMARK 500 GLU B 74 14.85 -65.71
REMARK 500 LYS B 75 -82.18 -69.06
REMARK 500 VAL B 85 3.95 -39.68
REMARK 500 THR B 86 -45.30 -137.06
REMARK 500 LEU B 87 150.52 -48.84
REMARK 500 PRO B 90 153.17 -28.39
REMARK 500 ARG B 97 -177.51 -64.16
REMARK 500 ASP B 98 61.85 -3.29
REMARK 500 THR C 21 121.60 12.36
REMARK 500 TYR C 35 -27.74 -146.00
REMARK 500 ARG C 42 -70.11 -79.68
REMARK 500 GLU C 54 140.77 -32.21
REMARK 500 VAL C 57 67.74 -51.15
REMARK 500
REMARK 500 THIS ENTRY HAS 225 RAMACHANDRAN OUTLIERS.
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 GLY C 20 THR C 21 145.49
REMARK 500 ALA E 219 GLY E 220 146.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M17 RELATED DB: PDB
REMARK 900 RELATED ID: 3M1B RELATED DB: PDB
DBREF 5BJT A 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 5BJT B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5BJT C 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 5BJT D 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5BJT E 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 5BJT F 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5BJT G 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 5BJT H 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5BJT P 0 18 PDB 5BJT 5BJT 0 18
DBREF 5BJT Q 0 18 PDB 5BJT 5BJT 0 18
DBREF 5BJT R 0 18 PDB 5BJT 5BJT 0 18
DBREF 5BJT S 0 18 PDB 5BJT 5BJT 0 18
DBREF 5BJT T 0 18 PDB 5BJT 5BJT 0 18
DBREF 5BJT U 0 18 PDB 5BJT 5BJT 0 18
DBREF 5BJT V 0 18 PDB 5BJT 5BJT 0 18
SEQRES 1 A 267 ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA
SEQRES 2 A 267 VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL
SEQRES 3 A 267 SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN
SEQRES 4 A 267 SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL
SEQRES 5 A 267 TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR
SEQRES 6 A 267 THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA
SEQRES 7 A 267 PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN
SEQRES 8 A 267 GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER
SEQRES 9 A 267 VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE
SEQRES 10 A 267 MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP
SEQRES 11 A 267 TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN
SEQRES 12 A 267 GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU
SEQRES 13 A 267 PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG
SEQRES 14 A 267 GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET
SEQRES 15 A 267 ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL
SEQRES 16 A 267 LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU
SEQRES 17 A 267 GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR
SEQRES 18 A 267 GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE
SEQRES 19 A 267 HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU
SEQRES 20 A 267 HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA
SEQRES 21 A 267 GLN PRO LEU ARG VAL GLU LEU
SEQRES 1 B 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 B 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 B 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 B 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 B 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 B 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 B 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 267 ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA
SEQRES 2 C 267 VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL
SEQRES 3 C 267 SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN
SEQRES 4 C 267 SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL
SEQRES 5 C 267 TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR
SEQRES 6 C 267 THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA
SEQRES 7 C 267 PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN
SEQRES 8 C 267 GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER
SEQRES 9 C 267 VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE
SEQRES 10 C 267 MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP
SEQRES 11 C 267 TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN
SEQRES 12 C 267 GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU
SEQRES 13 C 267 PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG
SEQRES 14 C 267 GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET
SEQRES 15 C 267 ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL
SEQRES 16 C 267 LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU
SEQRES 17 C 267 GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR
SEQRES 18 C 267 GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE
SEQRES 19 C 267 HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU
SEQRES 20 C 267 HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA
SEQRES 21 C 267 GLN PRO LEU ARG VAL GLU LEU
SEQRES 1 D 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 D 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 D 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 D 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 D 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 D 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 D 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 D 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 E 267 ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA
SEQRES 2 E 267 VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL
SEQRES 3 E 267 SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN
SEQRES 4 E 267 SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL
SEQRES 5 E 267 TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR
SEQRES 6 E 267 THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA
SEQRES 7 E 267 PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN
SEQRES 8 E 267 GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER
SEQRES 9 E 267 VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE
SEQRES 10 E 267 MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP
SEQRES 11 E 267 TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN
SEQRES 12 E 267 GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU
SEQRES 13 E 267 PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG
SEQRES 14 E 267 GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET
SEQRES 15 E 267 ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL
SEQRES 16 E 267 LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU
SEQRES 17 E 267 GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR
SEQRES 18 E 267 GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE
SEQRES 19 E 267 HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU
SEQRES 20 E 267 HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA
SEQRES 21 E 267 GLN PRO LEU ARG VAL GLU LEU
SEQRES 1 F 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 F 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 F 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 F 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 F 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 F 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 F 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 F 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 G 267 ALA GLU SER HIS LEU SER LEU LEU TYR HIS LEU THR ALA
SEQRES 2 G 267 VAL SER SER PRO ALA PRO GLY THR PRO ALA PHE TRP VAL
SEQRES 3 G 267 SER GLY TRP LEU GLY PRO GLN GLN TYR LEU SER TYR ASN
SEQRES 4 G 267 SER LEU ARG GLY GLU ALA GLU PRO CYS GLY ALA TRP VAL
SEQRES 5 G 267 TRP GLU ASN GLN VAL SER TRP TYR TRP GLU LYS GLU THR
SEQRES 6 G 267 THR ASP LEU ARG ILE LYS GLU LYS LEU PHE LEU GLU ALA
SEQRES 7 G 267 PHE LYS ALA LEU GLY GLY LYS GLY PRO TYR THR LEU GLN
SEQRES 8 G 267 GLY LEU LEU GLY CYS GLU LEU GLY PRO ASP ASN THR SER
SEQRES 9 G 267 VAL PRO THR ALA LYS PHE ALA LEU ASN GLY GLU GLU PHE
SEQRES 10 G 267 MET ASN PHE ASP LEU LYS GLN GLY THR TRP GLY GLY ASP
SEQRES 11 G 267 TRP PRO GLU ALA LEU ALA ILE SER GLN ARG TRP GLN GLN
SEQRES 12 G 267 GLN ASP LYS ALA ALA ASN LYS GLU LEU THR PHE LEU LEU
SEQRES 13 G 267 PHE SER CYS PRO HIS ARG LEU ARG GLU HIS LEU GLU ARG
SEQRES 14 G 267 GLY ARG GLY ASN LEU GLU TRP LYS GLU PRO PRO SER MET
SEQRES 15 G 267 ARG LEU LYS ALA ARG PRO SER SER PRO GLY PHE SER VAL
SEQRES 16 G 267 LEU THR CYS SER ALA PHE SER PHE TYR PRO PRO GLU LEU
SEQRES 17 G 267 GLN LEU ARG PHE LEU ARG ASN GLY LEU ALA ALA GLY THR
SEQRES 18 G 267 GLY GLN GLY ASP PHE GLY PRO ASN SER ASP GLY SER PHE
SEQRES 19 G 267 HIS ALA SER SER SER LEU THR VAL LYS SER GLY ASP GLU
SEQRES 20 G 267 HIS HIS TYR CYS CYS ILE VAL GLN HIS ALA GLY LEU ALA
SEQRES 21 G 267 GLN PRO LEU ARG VAL GLU LEU
SEQRES 1 H 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 H 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 H 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 H 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 H 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 H 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 H 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 H 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 P 19 ACE ARG TYR PHE CYS THR LYS TRP LYS HIS GLY TRP CYS
SEQRES 2 P 19 GLU GLU VAL GLY THR NH2
SEQRES 1 Q 19 ACE ARG TYR PHE CYS THR LYS TRP LYS HIS GLY TRP CYS
SEQRES 2 Q 19 GLU GLU VAL GLY THR NH2
SEQRES 1 R 19 ACE ARG TYR PHE CYS THR LYS TRP LYS HIS GLY TRP CYS
SEQRES 2 R 19 GLU GLU VAL GLY THR NH2
SEQRES 1 S 19 ACE ARG TYR PHE CYS THR LYS TRP LYS HIS GLY TRP CYS
SEQRES 2 S 19 GLU GLU VAL GLY THR NH2
SEQRES 1 T 19 ACE ARG TYR PHE CYS THR LYS TRP LYS HIS GLY TRP CYS
SEQRES 2 T 19 GLU GLU VAL GLY THR NH2
SEQRES 1 U 19 ACE ARG TYR PHE CYS THR LYS TRP LYS HIS GLY TRP CYS
SEQRES 2 U 19 GLU GLU VAL GLY THR NH2
SEQRES 1 V 19 ACE ARG TYR PHE CYS THR LYS TRP LYS HIS GLY TRP CYS
SEQRES 2 V 19 GLU GLU VAL GLY THR NH2
HELIX 1 AA1 GLY A 49 TRP A 53 5 5
HELIX 2 AA2 TYR A 60 ALA A 81 1 22
HELIX 3 AA3 PRO A 132 GLN A 143 1 12
HELIX 4 AA4 LYS A 146 PHE A 157 1 12
HELIX 5 AA5 PHE A 157 GLY A 170 1 14
HELIX 6 AA6 GLY A 170 GLU A 175 1 6
HELIX 7 AA7 ASP A 246 HIS A 248 5 3
HELIX 8 AA8 GLY C 49 VAL C 52 5 4
HELIX 9 AA9 TYR C 60 ALA C 81 1 22
HELIX 10 AB1 TRP C 131 GLN C 144 1 14
HELIX 11 AB2 LYS C 146 PHE C 157 1 12
HELIX 12 AB3 PHE C 157 GLY C 170 1 14
HELIX 13 AB4 GLY C 170 GLU C 175 1 6
HELIX 14 AB5 GLY E 49 GLU E 54 5 6
HELIX 15 AB6 TRP E 59 ALA E 81 1 23
HELIX 16 AB7 TRP E 131 GLN E 143 1 13
HELIX 17 AB8 LYS E 146 PHE E 157 1 12
HELIX 18 AB9 PHE E 157 GLY E 170 1 14
HELIX 19 AC1 GLY E 170 TRP E 176 1 7
HELIX 20 AC2 ASP E 246 HIS E 248 5 3
HELIX 21 AC3 TRP G 59 TRP G 61 5 3
HELIX 22 AC4 GLU G 62 ALA G 78 1 17
HELIX 23 AC5 PHE G 79 LEU G 82 5 4
HELIX 24 AC6 PRO G 132 GLN G 143 1 12
HELIX 25 AC7 LYS G 146 LEU G 156 1 11
HELIX 26 AC8 PRO G 160 GLU G 165 1 6
HELIX 27 AC9 LEU G 167 LEU G 174 5 8
SHEET 1 AA1 7 GLU A 46 PRO A 47 0
SHEET 2 AA1 7 GLN A 33 ASN A 39 -1 N SER A 37 O GLU A 46
SHEET 3 AA1 7 PHE A 24 LEU A 30 -1 N VAL A 26 O TYR A 38
SHEET 4 AA1 7 SER A 6 VAL A 14 -1 N LEU A 8 O TRP A 29
SHEET 5 AA1 7 THR A 89 LEU A 98 -1 O GLY A 92 N LEU A 11
SHEET 6 AA1 7 THR A 103 LEU A 112 -1 O THR A 107 N GLY A 95
SHEET 7 AA1 7 GLU A 116 ASN A 119 -1 O MET A 118 N PHE A 110
SHEET 1 AA2 7 GLU A 46 PRO A 47 0
SHEET 2 AA2 7 GLN A 33 ASN A 39 -1 N SER A 37 O GLU A 46
SHEET 3 AA2 7 PHE A 24 LEU A 30 -1 N VAL A 26 O TYR A 38
SHEET 4 AA2 7 SER A 6 VAL A 14 -1 N LEU A 8 O TRP A 29
SHEET 5 AA2 7 THR A 89 LEU A 98 -1 O GLY A 92 N LEU A 11
SHEET 6 AA2 7 THR A 103 LEU A 112 -1 O THR A 107 N GLY A 95
SHEET 7 AA2 7 TYR S 2 PHE S 3 -1 O TYR S 2 N SER A 104
SHEET 1 AA3 4 GLU A 178 PRO A 188 0
SHEET 2 AA3 4 PHE A 193 TYR A 204 -1 O TYR A 204 N GLU A 178
SHEET 3 AA3 4 PHE A 234 LYS A 243 -1 O VAL A 242 N SER A 194
SHEET 4 AA3 4 GLN A 223 PRO A 228 -1 N GLY A 227 O HIS A 235
SHEET 1 AA4 4 LEU A 217 ALA A 218 0
SHEET 2 AA4 4 LEU A 208 ARG A 214 -1 N ARG A 214 O LEU A 217
SHEET 3 AA4 4 TYR A 250 HIS A 256 -1 O ILE A 253 N ARG A 211
SHEET 4 AA4 4 LEU A 263 VAL A 265 -1 O VAL A 265 N CYS A 252
SHEET 1 AA5 4 LYS B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 AA6 4 LYS B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 GLU B 44 ARG B 45 0
SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 AA7 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O VAL B 93 N CYS B 80
SHEET 1 AA8 8 ALA C 45 PRO C 47 0
SHEET 2 AA8 8 GLN C 33 ASN C 39 -1 N SER C 37 O GLU C 46
SHEET 3 AA8 8 PHE C 24 LEU C 30 -1 N VAL C 26 O TYR C 38
SHEET 4 AA8 8 SER C 6 VAL C 14 -1 N HIS C 10 O SER C 27
SHEET 5 AA8 8 THR C 89 LEU C 98 -1 O GLY C 92 N LEU C 11
SHEET 6 AA8 8 SER C 104 LEU C 112 -1 O THR C 107 N GLY C 95
SHEET 7 AA8 8 GLU C 115 ASP C 121 -1 O MET C 118 N PHE C 110
SHEET 8 AA8 8 THR C 126 GLY C 128 -1 O THR C 126 N ASP C 121
SHEET 1 AA9 4 SER C 181 PRO C 188 0
SHEET 2 AA9 4 PHE C 193 PHE C 203 -1 O THR C 197 N LYS C 185
SHEET 3 AA9 4 PHE C 234 LYS C 243 -1 O VAL C 242 N SER C 194
SHEET 4 AA9 4 GLN C 223 PRO C 228 -1 N ASP C 225 O SER C 237
SHEET 1 AB1 4 LEU C 217 GLY C 220 0
SHEET 2 AB1 4 GLN C 209 ARG C 214 -1 N ARG C 214 O LEU C 217
SHEET 3 AB1 4 TYR C 250 GLN C 255 -1 O GLN C 255 N GLN C 209
SHEET 4 AB1 4 LEU C 263 VAL C 265 -1 O VAL C 265 N CYS C 252
SHEET 1 AB2 4 LYS D 6 SER D 11 0
SHEET 2 AB2 4 ASN D 21 PHE D 30 -1 O SER D 28 N LYS D 6
SHEET 3 AB2 4 PHE D 62 PHE D 70 -1 O TYR D 66 N CYS D 25
SHEET 4 AB2 4 GLU D 50 HIS D 51 -1 N GLU D 50 O TYR D 67
SHEET 1 AB3 4 LYS D 6 SER D 11 0
SHEET 2 AB3 4 ASN D 21 PHE D 30 -1 O SER D 28 N LYS D 6
SHEET 3 AB3 4 PHE D 62 PHE D 70 -1 O TYR D 66 N CYS D 25
SHEET 4 AB3 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 AB4 4 GLU D 44 ARG D 45 0
SHEET 2 AB4 4 GLU D 36 LYS D 41 -1 N LYS D 41 O GLU D 44
SHEET 3 AB4 4 TYR D 78 ASN D 83 -1 O ARG D 81 N ASP D 38
SHEET 4 AB4 4 LYS D 91 LYS D 94 -1 O VAL D 93 N CYS D 80
SHEET 1 AB5 7 ALA E 45 PRO E 47 0
SHEET 2 AB5 7 GLN E 33 ASN E 39 -1 N SER E 37 O GLU E 46
SHEET 3 AB5 7 PHE E 24 LEU E 30 -1 N VAL E 26 O TYR E 38
SHEET 4 AB5 7 SER E 6 VAL E 14 -1 N HIS E 10 O SER E 27
SHEET 5 AB5 7 THR E 89 LEU E 98 -1 O GLY E 92 N LEU E 11
SHEET 6 AB5 7 SER E 104 LEU E 112 -1 O LYS E 109 N LEU E 93
SHEET 7 AB5 7 GLU E 115 ASN E 119 -1 O GLU E 115 N LEU E 112
SHEET 1 AB6 3 LEU E 184 ARG E 187 0
SHEET 2 AB6 3 PHE E 193 CYS E 198 -1 O THR E 197 N LYS E 185
SHEET 3 AB6 3 SER E 239 LYS E 243 -1 O LEU E 240 N LEU E 196
SHEET 1 AB7 3 ALA E 200 PHE E 203 0
SHEET 2 AB7 3 PHE E 234 ALA E 236 -1 O PHE E 234 N PHE E 203
SHEET 3 AB7 3 PHE E 226 PRO E 228 -1 N GLY E 227 O HIS E 235
SHEET 1 AB8 4 LEU E 217 ALA E 218 0
SHEET 2 AB8 4 GLN E 209 ARG E 214 -1 N ARG E 214 O LEU E 217
SHEET 3 AB8 4 TYR E 250 GLN E 255 -1 O ILE E 253 N ARG E 211
SHEET 4 AB8 4 LEU E 263 VAL E 265 -1 O VAL E 265 N CYS E 252
SHEET 1 AB9 4 LYS F 6 SER F 11 0
SHEET 2 AB9 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 AB9 4 PHE F 62 PHE F 70 -1 O PHE F 62 N PHE F 30
SHEET 4 AB9 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 AC1 4 LYS F 6 SER F 11 0
SHEET 2 AC1 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 AC1 4 PHE F 62 PHE F 70 -1 O PHE F 62 N PHE F 30
SHEET 4 AC1 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 AC2 4 GLU F 44 ARG F 45 0
SHEET 2 AC2 4 GLU F 36 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 AC2 4 ALA F 79 ASN F 83 -1 O ARG F 81 N ASP F 38
SHEET 4 AC2 4 LYS F 91 LYS F 94 -1 O LYS F 91 N VAL F 82
SHEET 1 AC3 4 GLN G 33 GLN G 34 0
SHEET 2 AC3 4 TRP G 29 LEU G 30 -1 N LEU G 30 O GLN G 33
SHEET 3 AC3 4 SER G 6 LEU G 8 -1 N LEU G 8 O TRP G 29
SHEET 4 AC3 4 GLY G 95 GLU G 97 -1 O CYS G 96 N LEU G 7
SHEET 1 AC4 7 TYR G 38 ASN G 39 0
SHEET 2 AC4 7 PHE G 24 VAL G 26 -1 N VAL G 26 O TYR G 38
SHEET 3 AC4 7 LEU G 11 ALA G 13 -1 N THR G 12 O TRP G 25
SHEET 4 AC4 7 LEU G 90 GLY G 92 -1 O GLY G 92 N LEU G 11
SHEET 5 AC4 7 LYS G 109 LEU G 112 -1 O ALA G 111 N GLN G 91
SHEET 6 AC4 7 GLU G 115 PHE G 120 -1 O PHE G 117 N PHE G 110
SHEET 7 AC4 7 TRP G 127 GLY G 129 -1 O GLY G 128 N ASN G 119
SHEET 1 AC5 3 SER G 181 ARG G 183 0
SHEET 2 AC5 3 CYS G 198 PHE G 201 -1 O PHE G 201 N SER G 181
SHEET 3 AC5 3 HIS G 235 SER G 238 -1 O SER G 238 N CYS G 198
SHEET 1 AC6 2 SER G 194 VAL G 195 0
SHEET 2 AC6 2 THR G 241 VAL G 242 -1 O VAL G 242 N SER G 194
SHEET 1 AC7 4 VAL H 9 SER H 11 0
SHEET 2 AC7 4 ASN H 21 CYS H 25 -1 O ASN H 24 N TYR H 10
SHEET 3 AC7 4 TYR H 66 PHE H 70 -1 O TYR H 66 N CYS H 25
SHEET 4 AC7 4 GLU H 50 HIS H 51 -1 N GLU H 50 O TYR H 67
SHEET 1 AC8 3 SER H 28 PHE H 30 0
SHEET 2 AC8 3 PHE H 62 TYR H 63 -1 O PHE H 62 N PHE H 30
SHEET 3 AC8 3 SER H 55 PHE H 56 -1 N SER H 55 O TYR H 63
SHEET 1 AC9 4 GLU H 44 ARG H 45 0
SHEET 2 AC9 4 ILE H 35 LYS H 41 -1 N LYS H 41 O GLU H 44
SHEET 3 AC9 4 TYR H 78 HIS H 84 -1 O ASN H 83 N GLU H 36
SHEET 4 AC9 4 VAL H 93 TRP H 95 -1 O VAL H 93 N CYS H 80
SHEET 1 AD1 2 TRP T 7 LYS T 8 0
SHEET 2 AD1 2 TRP T 11 CYS T 12 -1 O TRP T 11 N LYS T 8
SHEET 1 AD2 2 CYS U 4 THR U 5 0
SHEET 2 AD2 2 GLU U 14 VAL U 15 -1 O GLU U 14 N THR U 5
SSBOND 1 CYS A 96 CYS A 159 1555 1555 2.12
SSBOND 2 CYS A 198 CYS A 252 1555 1555 2.03
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.05
SSBOND 4 CYS C 96 CYS C 159 1555 1555 2.16
SSBOND 5 CYS C 198 CYS C 252 1555 1555 2.06
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.03
SSBOND 7 CYS E 96 CYS E 159 1555 1555 2.10
SSBOND 8 CYS E 198 CYS E 252 1555 1555 2.05
SSBOND 9 CYS F 25 CYS F 80 1555 1555 2.06
SSBOND 10 CYS G 96 CYS G 159 1555 1555 2.06
SSBOND 11 CYS H 25 CYS H 80 1555 1555 2.05
SSBOND 12 CYS P 4 CYS P 12 1555 1555 2.03
SSBOND 13 CYS Q 4 CYS Q 12 1555 1555 2.06
SSBOND 14 CYS R 4 CYS R 12 1555 1555 2.06
SSBOND 15 CYS S 4 CYS S 12 1555 1555 2.08
SSBOND 16 CYS T 4 CYS T 12 1555 1555 2.07
SSBOND 17 CYS U 4 CYS U 12 1555 1555 2.06
SSBOND 18 CYS V 4 CYS V 12 1555 1555 2.11
CISPEP 1 GLY A 86 PRO A 87 0 -6.25
CISPEP 2 TYR A 204 PRO A 205 0 -6.46
CISPEP 3 HIS B 31 PRO B 32 0 1.39
CISPEP 4 GLY C 86 PRO C 87 0 -0.70
CISPEP 5 TYR C 204 PRO C 205 0 -8.71
CISPEP 6 HIS D 31 PRO D 32 0 4.42
CISPEP 7 GLY E 86 PRO E 87 0 15.88
CISPEP 8 TYR E 204 PRO E 205 0 -1.24
CISPEP 9 HIS F 31 PRO F 32 0 -6.16
CISPEP 10 GLY G 86 PRO G 87 0 2.23
CISPEP 11 TYR G 204 PRO G 205 0 -2.09
CISPEP 12 HIS H 31 PRO H 32 0 1.28
CRYST1 104.917 176.152 245.515 90.00 90.00 90.00 I 2 2 2 56
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 0.009531 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
