HEADER IMMUNE SYSTEM/INHIBITOR 04-MAR-10 3M1B
TITLE CRYSTAL STRUCTURE OF HUMAN FCRN WITH A DIMERIC PEPTIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGG RECEPTOR FCRN LARGE SUBUNIT P51;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: UNP RESIDUES 24-290;
COMPND 5 SYNONYM: FCRN, NEONATAL FC RECEPTOR, IGG FC FRAGMENT RECEPTOR
COMPND 6 TRANSPORTER ALPHA CHAIN;
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 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: DIMERIC PEPTIDE INHIBITOR;
COMPND 16 CHAIN: I, J;
COMPND 17 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: CRICETINAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HAMSTERS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10026;
SOURCE 9 EXPRESSION_SYSTEM_CELL: CHOK1SV CELLS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 15 EXPRESSION_SYSTEM: CRICETINAE;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HAMSTERS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10026;
SOURCE 18 EXPRESSION_SYSTEM_CELL: CHOK1SV CELLS;
SOURCE 19 MOL_ID: 3;
SOURCE 20 SYNTHETIC: YES
KEYWDS IMMUNOGLOBULIN BINDING PROTEIN, CELL MEMBRANE, DISULFIDE BOND,
KEYWDS 2 GLYCOPROTEIN, IGG-BINDING PROTEIN, IMMUNOGLOBULIN DOMAIN, MEMBRANE,
KEYWDS 3 RECEPTOR, TRANSMEMBRANE, AMYLOID, AMYLOIDOSIS, DISEASE MUTATION,
KEYWDS 4 GLYCATION, IMMUNE RESPONSE, MHC I, PYRROLIDONE CARBOXYLIC ACID,
KEYWDS 5 SECRETED, IMMUNE SYSTEM-IMMUNE SYSTEM INHIBITOR, IMMUNE SYSTEM-
KEYWDS 6 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.MEZO,V.SRIDHAR,J.BADGER,P.SAKORAFAS,V.NIENABER
REVDAT 6 22-NOV-23 3M1B 1 REMARK
REVDAT 5 06-SEP-23 3M1B 1 REMARK
REVDAT 4 04-MAY-22 3M1B 1 HETSYN LINK
REVDAT 3 24-AUG-11 3M1B 1 HEADER LINK VERSN
REVDAT 2 15-SEP-10 3M1B 1 JRNL
REVDAT 1 16-JUN-10 3M1B 0
JRNL AUTH A.R.MEZO,V.SRIDHAR,J.BADGER,P.SAKORAFAS,V.NIENABER
JRNL TITL X-RAY CRYSTAL STRUCTURES OF MONOMERIC AND DIMERIC PEPTIDE
JRNL TITL 2 INHIBITORS IN COMPLEX WITH THE HUMAN NEONATAL FC RECEPTOR,
JRNL TITL 3 FCRN.
JRNL REF J.BIOL.CHEM. V. 285 27694 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20592032
JRNL DOI 10.1074/JBC.M110.120667
REMARK 2
REMARK 2 RESOLUTION. 3.10 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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27550
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) : 0.318
REMARK 3 R VALUE (WORKING SET) : 0.314
REMARK 3 FREE R VALUE : 0.397
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1475
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11241
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) : 106.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.44000
REMARK 3 B22 (A**2) : 1.06000
REMARK 3 B33 (A**2) : 0.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
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): 0.793
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.901
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.517
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3M1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000057982.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29051
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
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 (%) : 90.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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
REMARK 200 STARTING MODEL: PDB ENTRY 3M17
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2UL PROTEIN:PEPTIDE WITH 2UL BUFFER
REMARK 280 CONTAINING 100 MM PHOSPHATE/CITRIC ACID, 22% PEG 1000 AND 8%
REMARK 280 ETHANOL , PH 4.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 79.21550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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 APPLY THE FOLLOWING TO CHAINS: 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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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 APPLY THE FOLLOWING TO CHAINS: J
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE DIMERIC PEPTIDE INHIBITOR IS POLYPEPTIDE, A MEMBER OF INHIBITOR
REMARK 400 CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: DIMERIC PEPTIDE INHIBITOR
REMARK 400 CHAIN: I, J
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 I 0
REMARK 465 ARG I 1
REMARK 465 PHE I 2
REMARK 465 LYS I 14
REMARK 465 NH2 I 15
REMARK 465 ACE J 100
REMARK 465 ARG J 101
REMARK 465 LYS J 114
REMARK 465 NH2 J 115
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 LEU A 5 CG CD1 CD2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 VAL A 57 CG1 CG2
REMARK 470 SER A 58 OG
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 143 CG CD OE1 NE2
REMARK 470 LYS A 146 CD CE NZ
REMARK 470 LEU A 152 CG CD1 CD2
REMARK 470 PHE A 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 164 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 177 CE NZ
REMARK 470 LYS A 185 CG CD CE NZ
REMARK 470 ARG A 187 CG CD NE CZ NH1 NH2
REMARK 470 SER A 189 OG
REMARK 470 SER A 190 OG
REMARK 470 PHE A 193 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 194 OG
REMARK 470 GLN A 209 CD OE1 NE2
REMARK 470 ARG A 211 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 214 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 215 CG OD1 ND2
REMARK 470 LEU A 217 CG CD1 CD2
REMARK 470 GLN A 223 CG CD OE1 NE2
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 HIS A 249 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 255 CG CD OE1 NE2
REMARK 470 LEU A 267 CG CD1 CD2
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 LYS B 58 CD CE NZ
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 LYS B 91 CD CE NZ
REMARK 470 LYS B 94 CD CE NZ
REMARK 470 LEU C 5 CG CD1 CD2
REMARK 470 GLU C 46 CG CD OE1 OE2
REMARK 470 VAL C 57 CG1 CG2
REMARK 470 SER C 58 OG
REMARK 470 LYS C 63 CD CE NZ
REMARK 470 LYS C 73 CD CE NZ
REMARK 470 LYS C 85 CG CD CE NZ
REMARK 470 ASN C 102 CG OD1 ND2
REMARK 470 LYS C 123 CG CD CE NZ
REMARK 470 GLN C 143 CG CD OE1 NE2
REMARK 470 LYS C 146 CD CE NZ
REMARK 470 LEU C 152 CG CD1 CD2
REMARK 470 PHE C 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 164 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 177 CE NZ
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 PHE C 193 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER C 194 OG
REMARK 470 GLN C 209 CD OE1 NE2
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 HIS C 249 CG ND1 CD2 CE1 NE2
REMARK 470 GLN C 255 CG CD OE1 NE2
REMARK 470 LEU C 267 CG CD1 CD2
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 LYS D 58 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 CD CE NZ
REMARK 470 LEU E 5 CG CD1 CD2
REMARK 470 GLU E 46 CG CD OE1 OE2
REMARK 470 VAL E 57 CG1 CG2
REMARK 470 SER E 58 OG
REMARK 470 LYS E 63 CD CE NZ
REMARK 470 LYS E 73 CD CE NZ
REMARK 470 LYS E 85 CG CD CE NZ
REMARK 470 ASN E 102 CG OD1 ND2
REMARK 470 LYS E 123 CG CD CE NZ
REMARK 470 GLN E 143 CG CD OE1 NE2
REMARK 470 LYS E 146 CD CE NZ
REMARK 470 LEU E 152 CG CD1 CD2
REMARK 470 PHE E 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG E 164 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 177 CE NZ
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 PHE E 193 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER E 194 OG
REMARK 470 GLN E 209 CD OE1 NE2
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 CG CD CE NZ
REMARK 470 HIS E 249 CG ND1 CD2 CE1 NE2
REMARK 470 GLN E 255 CG CD OE1 NE2
REMARK 470 LEU E 267 CG CD1 CD2
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 LYS F 58 CD CE NZ
REMARK 470 LYS F 75 CG CD CE NZ
REMARK 470 GLU F 77 CG CD OE1 OE2
REMARK 470 LYS F 91 CD CE NZ
REMARK 470 LYS F 94 CD CE NZ
REMARK 470 LEU G 5 CG CD1 CD2
REMARK 470 GLU G 46 CG CD OE1 OE2
REMARK 470 VAL G 57 CG1 CG2
REMARK 470 SER G 58 OG
REMARK 470 LYS G 63 CD CE NZ
REMARK 470 LYS G 73 CD CE NZ
REMARK 470 LYS G 85 CG CD CE NZ
REMARK 470 ASN G 102 CG OD1 ND2
REMARK 470 LYS G 123 CG CD CE NZ
REMARK 470 GLN G 143 CG CD OE1 NE2
REMARK 470 LYS G 146 CD CE NZ
REMARK 470 LEU G 152 CG CD1 CD2
REMARK 470 PHE G 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG G 164 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 177 CE NZ
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 GLN G 209 CD OE1 NE2
REMARK 470 ARG G 211 CG CD NE CZ NH1 NH2
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 GLN G 223 CG CD OE1 NE2
REMARK 470 LYS G 243 CG CD CE NZ
REMARK 470 HIS G 249 CG ND1 CD2 CE1 NE2
REMARK 470 GLN G 255 CG CD OE1 NE2
REMARK 470 LEU G 267 CG CD1 CD2
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 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 PHE J 102 N LE1 J 103 1.39
REMARK 500 ND2 ASN H 17 OE1 GLU H 74 2.05
REMARK 500 OD2 ASP A 67 NH2 ARG A 162 2.15
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 H 5 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 LE1 I 3 CA - C - N ANGL. DEV. = 19.9 DEGREES
REMARK 500 LE1 I 3 O - C - N ANGL. DEV. = -25.2 DEGREES
REMARK 500 THR I 4 C - N - CA ANGL. DEV. = 28.4 DEGREES
REMARK 500 PHE J 102 CA - C - N ANGL. DEV. = 43.2 DEGREES
REMARK 500 PHE J 102 O - C - N ANGL. DEV. = -57.7 DEGREES
REMARK 500 LE1 J 103 C - N - CA ANGL. DEV. = 34.8 DEGREES
REMARK 500 LE1 J 103 O - C - N ANGL. DEV. = -25.9 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 PRO A 19 102.06 -57.06
REMARK 500 TYR A 35 -5.76 -152.86
REMARK 500 TYR A 38 132.56 177.41
REMARK 500 ALA A 50 1.00 -62.20
REMARK 500 ASN A 55 84.83 -53.93
REMARK 500 SER A 58 -92.36 54.02
REMARK 500 PRO A 100 -71.46 -86.65
REMARK 500 ASN A 102 -14.88 64.25
REMARK 500 PHE A 117 -5.81 -146.60
REMARK 500 ALA A 134 25.41 -74.30
REMARK 500 LYS A 146 6.94 56.92
REMARK 500 LYS A 150 29.38 -76.00
REMARK 500 GLU A 151 -65.31 -123.97
REMARK 500 CYS A 159 -73.64 -61.27
REMARK 500 GLU A 165 -78.72 -90.50
REMARK 500 HIS A 166 -33.65 -39.39
REMARK 500 SER A 189 -157.61 -108.80
REMARK 500 PRO A 191 96.21 -43.99
REMARK 500 PHE A 193 154.98 171.01
REMARK 500 PRO A 205 -179.02 -65.93
REMARK 500 GLU A 207 85.71 -55.50
REMARK 500 ASN A 215 58.78 22.34
REMARK 500 ALA A 219 -48.90 -156.39
REMARK 500 ASN A 229 -165.79 -102.11
REMARK 500 HIS A 249 50.35 -90.53
REMARK 500 ASN B 21 -144.11 -153.79
REMARK 500 PRO B 32 -133.37 -71.06
REMARK 500 ASN B 42 77.01 58.10
REMARK 500 ASP B 59 10.03 -64.22
REMARK 500 TRP B 60 -21.73 77.85
REMARK 500 TYR C 38 124.91 177.01
REMARK 500 VAL C 57 56.59 -69.94
REMARK 500 SER C 58 -52.13 45.74
REMARK 500 THR C 65 -79.30 -52.73
REMARK 500 GLU C 97 125.59 -173.26
REMARK 500 ASP C 101 32.90 -144.16
REMARK 500 ASN C 102 -6.52 75.57
REMARK 500 ASN C 113 59.15 21.61
REMARK 500 PHE C 117 -28.62 -152.62
REMARK 500 ASP C 130 -36.92 -140.74
REMARK 500 LYS C 150 -7.21 -56.90
REMARK 500 PHE C 157 -87.32 -98.02
REMARK 500 CYS C 159 -70.57 -61.77
REMARK 500 LEU C 167 1.87 -65.36
REMARK 500 GLU C 168 -73.19 -118.27
REMARK 500 GLU C 175 6.22 -63.73
REMARK 500 LEU C 184 39.18 -155.71
REMARK 500 SER C 189 -136.86 -86.08
REMARK 500 CYS C 198 78.18 -107.87
REMARK 500 SER C 202 109.44 55.56
REMARK 500
REMARK 500 THIS ENTRY HAS 132 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 LE1 I 3 THR I 4 -124.83
REMARK 500 GLY I 8 SAR I 9 -145.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LE1 I 3 19.28
REMARK 500 PHE J 102 -65.75
REMARK 500 LE1 J 103 33.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M17 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN FCRN WITH A MONOMERIC PEPTIDE INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACE AT THE N-TERMINUS OF CHAIN I IS COVALENTLY BONDED WITH ACE AT
REMARK 999 THE N-TERMINUS OF CHAIN J
DBREF 3M1B A 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 3M1B B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3M1B C 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 3M1B D 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3M1B E 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 3M1B F 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3M1B G 1 267 UNP P55899 FCGRN_HUMAN 24 290
DBREF 3M1B H 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3M1B I 2 14 PDB 3M1B 3M1B 2 14
DBREF 3M1B J 102 114 PDB 3M1B 3M1B 102 114
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 I 16 ACE ARG PHE LE1 THR GLY HIS PHE GLY SAR MLE TYR PRO
SEQRES 2 I 16 CYS LYS NH2
SEQRES 1 J 16 ACE ARG PHE LE1 THR GLY HIS PHE GLY SAR MLE TYR PRO
SEQRES 2 J 16 CYS LYS NH2
MODRES 3M1B LE1 I 3 VAL 3-SULFANYL-L-VALINE
MODRES 3M1B SAR I 9 GLY SARCOSINE
MODRES 3M1B MLE I 10 LEU N-METHYLLEUCINE
MODRES 3M1B LE1 J 103 VAL 3-SULFANYL-L-VALINE
MODRES 3M1B SAR J 109 GLY SARCOSINE
MODRES 3M1B MLE J 110 LEU N-METHYLLEUCINE
HET LE1 I 3 8
HET SAR I 9 5
HET MLE I 10 9
HET LE1 J 103 8
HET SAR J 109 5
HET MLE J 110 9
HETNAM LE1 3-SULFANYL-L-VALINE
HETNAM SAR SARCOSINE
HETNAM MLE N-METHYLLEUCINE
HETSYN LE1 L-LE1ICILLAMINE; L-PENICILLAMINE
FORMUL 9 LE1 2(C5 H11 N O2 S)
FORMUL 9 SAR 2(C3 H7 N O2)
FORMUL 9 MLE 2(C7 H15 N O2)
HELIX 1 1 GLY A 49 VAL A 52 5 4
HELIX 2 2 TRP A 59 LEU A 82 1 24
HELIX 3 3 PRO A 132 LEU A 135 5 4
HELIX 4 4 ALA A 136 GLN A 144 1 9
HELIX 5 5 ALA A 148 PHE A 157 1 10
HELIX 6 6 PHE A 157 TRP A 176 1 20
HELIX 7 7 GLY A 245 HIS A 248 5 4
HELIX 8 8 CYS C 48 TRP C 53 5 6
HELIX 9 9 TRP C 59 ALA C 81 1 23
HELIX 10 10 TRP C 131 GLN C 139 1 9
HELIX 11 11 ALA C 148 PHE C 157 1 10
HELIX 12 12 PHE C 157 GLY C 170 1 14
HELIX 13 13 GLY C 170 GLU C 175 1 6
HELIX 14 14 ASP C 246 TYR C 250 5 5
HELIX 15 15 CYS E 48 VAL E 52 5 5
HELIX 16 16 TRP E 59 PHE E 79 1 21
HELIX 17 17 LEU E 122 GLY E 125 5 4
HELIX 18 18 TRP E 131 GLN E 144 1 14
HELIX 19 19 ALA E 148 PHE E 157 1 10
HELIX 20 20 SER E 158 GLY E 170 1 13
HELIX 21 21 GLY E 170 TRP E 176 1 7
HELIX 22 22 ASP E 246 HIS E 248 5 3
HELIX 23 23 TRP G 59 ALA G 81 1 23
HELIX 24 24 ASP G 121 GLY G 125 5 5
HELIX 25 25 PRO G 132 GLN G 144 1 13
HELIX 26 26 LYS G 146 PHE G 157 1 12
HELIX 27 27 PHE G 157 ARG G 169 1 13
HELIX 28 28 GLY G 170 TRP G 176 1 7
SHEET 1 A 6 GLU A 46 PRO A 47 0
SHEET 2 A 6 GLN A 33 TYR A 38 -1 N SER A 37 O GLU A 46
SHEET 3 A 6 PHE A 24 LEU A 30 -1 N LEU A 30 O GLN A 33
SHEET 4 A 6 LEU A 7 VAL A 14 -1 N LEU A 8 O TRP A 29
SHEET 5 A 6 THR A 89 LEU A 98 -1 O LEU A 94 N TYR A 9
SHEET 6 A 6 SER A 104 PRO A 106 -1 O VAL A 105 N GLU A 97
SHEET 1 B 8 GLU A 46 PRO A 47 0
SHEET 2 B 8 GLN A 33 TYR A 38 -1 N SER A 37 O GLU A 46
SHEET 3 B 8 PHE A 24 LEU A 30 -1 N LEU A 30 O GLN A 33
SHEET 4 B 8 LEU A 7 VAL A 14 -1 N LEU A 8 O TRP A 29
SHEET 5 B 8 THR A 89 LEU A 98 -1 O LEU A 94 N TYR A 9
SHEET 6 B 8 LYS A 109 LEU A 112 -1 O LYS A 109 N LEU A 93
SHEET 7 B 8 GLU A 116 ASP A 121 -1 O PHE A 117 N PHE A 110
SHEET 8 B 8 THR A 126 GLY A 128 -1 O GLY A 128 N ASN A 119
SHEET 1 C 4 SER A 181 LYS A 185 0
SHEET 2 C 4 THR A 197 PHE A 203 -1 O PHE A 201 N SER A 181
SHEET 3 C 4 PHE A 234 SER A 239 -1 O SER A 238 N CYS A 198
SHEET 4 C 4 GLN A 223 PRO A 228 -1 N GLN A 223 O SER A 239
SHEET 1 D 2 SER A 194 VAL A 195 0
SHEET 2 D 2 THR A 241 VAL A 242 -1 O VAL A 242 N SER A 194
SHEET 1 E 4 LEU A 217 ALA A 218 0
SHEET 2 E 4 GLN A 209 ARG A 214 -1 N ARG A 214 O LEU A 217
SHEET 3 E 4 TYR A 250 GLN A 255 -1 O CYS A 251 N LEU A 213
SHEET 4 E 4 LEU A 263 VAL A 265 -1 O VAL A 265 N CYS A 252
SHEET 1 F 4 VAL B 9 TYR B 10 0
SHEET 2 F 4 LEU B 23 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 F 4 PHE B 62 THR B 68 -1 O PHE B 62 N GLY B 29
SHEET 4 F 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 G 4 VAL B 9 TYR B 10 0
SHEET 2 G 4 LEU B 23 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 G 4 PHE B 62 THR B 68 -1 O PHE B 62 N GLY B 29
SHEET 4 G 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 H 4 GLU B 44 ARG B 45 0
SHEET 2 H 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 H 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38
SHEET 4 H 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 I 7 GLN C 33 ASN C 39 0
SHEET 2 I 7 PHE C 24 LEU C 30 -1 N GLY C 28 O TYR C 35
SHEET 3 I 7 LEU C 7 VAL C 14 -1 N THR C 12 O TRP C 25
SHEET 4 I 7 THR C 89 CYS C 96 -1 O LEU C 94 N TYR C 9
SHEET 5 I 7 PHE C 110 LEU C 112 -1 O ALA C 111 N GLN C 91
SHEET 6 I 7 GLU C 115 ASP C 121 -1 O MET C 118 N PHE C 110
SHEET 7 I 7 THR C 126 GLY C 128 -1 O THR C 126 N ASP C 121
SHEET 1 J 4 SER C 181 MET C 182 0
SHEET 2 J 4 ALA C 200 PHE C 203 -1 O PHE C 201 N SER C 181
SHEET 3 J 4 PHE C 234 ALA C 236 -1 O PHE C 234 N PHE C 203
SHEET 4 J 4 PHE C 226 PRO C 228 -1 N GLY C 227 O HIS C 235
SHEET 1 K 2 PHE C 193 SER C 194 0
SHEET 2 K 2 VAL C 242 LYS C 243 -1 O VAL C 242 N SER C 194
SHEET 1 L 3 LEU C 208 PHE C 212 0
SHEET 2 L 3 CYS C 252 HIS C 256 -1 O ILE C 253 N ARG C 211
SHEET 3 L 3 LEU C 263 VAL C 265 -1 O VAL C 265 N CYS C 252
SHEET 1 M 4 LYS D 6 SER D 11 0
SHEET 2 M 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 M 4 PHE D 62 PHE D 70 -1 O TYR D 66 N CYS D 25
SHEET 4 M 4 GLU D 50 SER D 55 -1 N SER D 52 O LEU D 65
SHEET 1 N 3 ILE D 35 LYS D 41 0
SHEET 2 N 3 TYR D 78 HIS D 84 -1 O ALA D 79 N LEU D 40
SHEET 3 N 3 LYS D 91 LYS D 94 -1 O VAL D 93 N CYS D 80
SHEET 1 O 7 GLN E 33 ASN E 39 0
SHEET 2 O 7 PHE E 24 LEU E 30 -1 N GLY E 28 O TYR E 35
SHEET 3 O 7 SER E 6 VAL E 14 -1 N LEU E 8 O TRP E 29
SHEET 4 O 7 THR E 89 GLU E 97 -1 O LEU E 90 N ALA E 13
SHEET 5 O 7 THR E 107 LEU E 112 -1 O LYS E 109 N LEU E 93
SHEET 6 O 7 GLU E 115 ASP E 121 -1 O PHE E 117 N PHE E 110
SHEET 7 O 7 THR E 126 GLY E 128 -1 O THR E 126 N ASP E 121
SHEET 1 P 4 SER E 181 PRO E 188 0
SHEET 2 P 4 SER E 194 PHE E 201 -1 O SER E 199 N ARG E 183
SHEET 3 P 4 PHE E 234 VAL E 242 -1 O ALA E 236 N ALA E 200
SHEET 4 P 4 GLN E 223 GLY E 224 -1 N GLN E 223 O SER E 239
SHEET 1 Q 4 SER E 181 PRO E 188 0
SHEET 2 Q 4 SER E 194 PHE E 201 -1 O SER E 199 N ARG E 183
SHEET 3 Q 4 PHE E 234 VAL E 242 -1 O ALA E 236 N ALA E 200
SHEET 4 Q 4 GLY E 227 PRO E 228 -1 N GLY E 227 O HIS E 235
SHEET 1 R 4 GLN E 209 LEU E 210 0
SHEET 2 R 4 TYR E 250 GLN E 255 -1 O GLN E 255 N GLN E 209
SHEET 3 R 4 LEU E 213 ARG E 214 -1 N LEU E 213 O CYS E 251
SHEET 4 R 4 LEU E 217 ALA E 218 -1 O LEU E 217 N ARG E 214
SHEET 1 S 3 GLN E 209 LEU E 210 0
SHEET 2 S 3 TYR E 250 GLN E 255 -1 O GLN E 255 N GLN E 209
SHEET 3 S 3 LEU E 263 VAL E 265 -1 O VAL E 265 N CYS E 252
SHEET 1 T 4 VAL F 9 SER F 11 0
SHEET 2 T 4 ASN F 21 SER F 28 -1 O ASN F 24 N TYR F 10
SHEET 3 T 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 T 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 U 4 VAL F 9 SER F 11 0
SHEET 2 U 4 ASN F 21 SER F 28 -1 O ASN F 24 N TYR F 10
SHEET 3 U 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 U 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 V 2 GLU F 36 LYS F 41 0
SHEET 2 V 2 TYR F 78 ASN F 83 -1 O ARG F 81 N ASP F 38
SHEET 1 W 5 GLN G 33 ASN G 39 0
SHEET 2 W 5 PHE G 24 LEU G 30 -1 N GLY G 28 O LEU G 36
SHEET 3 W 5 LEU G 7 ALA G 13 -1 N LEU G 8 O TRP G 29
SHEET 4 W 5 LEU G 90 GLU G 97 -1 O GLY G 92 N LEU G 11
SHEET 5 W 5 VAL G 105 PRO G 106 -1 O VAL G 105 N GLU G 97
SHEET 1 X 6 GLN G 33 ASN G 39 0
SHEET 2 X 6 PHE G 24 LEU G 30 -1 N GLY G 28 O LEU G 36
SHEET 3 X 6 LEU G 7 ALA G 13 -1 N LEU G 8 O TRP G 29
SHEET 4 X 6 LEU G 90 GLU G 97 -1 O GLY G 92 N LEU G 11
SHEET 5 X 6 PHE G 110 LEU G 112 -1 O ALA G 111 N GLN G 91
SHEET 6 X 6 GLU G 115 MET G 118 -1 O PHE G 117 N PHE G 110
SHEET 1 Y 4 SER G 181 PRO G 188 0
SHEET 2 Y 4 PHE G 193 PHE G 203 -1 O PHE G 201 N SER G 181
SHEET 3 Y 4 PHE G 234 LYS G 243 -1 O PHE G 234 N PHE G 203
SHEET 4 Y 4 GLN G 223 PRO G 228 -1 N GLN G 223 O SER G 239
SHEET 1 Z 3 LEU G 208 ARG G 211 0
SHEET 2 Z 3 CYS G 252 HIS G 256 -1 O ILE G 253 N ARG G 211
SHEET 3 Z 3 LEU G 263 VAL G 265 -1 O VAL G 265 N CYS G 252
SHEET 1 AA 2 LEU G 213 ARG G 214 0
SHEET 2 AA 2 LEU G 217 ALA G 218 -1 O LEU G 217 N ARG G 214
SHEET 1 AB 4 LYS H 6 SER H 11 0
SHEET 2 AB 4 ASN H 21 PHE H 30 -1 O TYR H 26 N GLN H 8
SHEET 3 AB 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 AB 4 GLU H 50 PHE H 56 -1 N GLU H 50 O TYR H 67
SHEET 1 AC 4 GLU H 44 ARG H 45 0
SHEET 2 AC 4 ILE H 35 LYS H 41 -1 N LYS H 41 O GLU H 44
SHEET 3 AC 4 TYR H 78 HIS H 84 -1 O ASN H 83 N GLU H 36
SHEET 4 AC 4 LYS H 91 LYS H 94 -1 O LYS H 91 N VAL H 82
SHEET 1 AD 2 LE1 J 103 THR J 104 0
SHEET 2 AD 2 MLE J 110 TYR J 111 -1 O TYR J 111 N LE1 J 103
SSBOND 1 CYS A 96 CYS A 159 1555 1555 2.06
SSBOND 2 CYS A 198 CYS A 252 1555 1555 2.06
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04
SSBOND 4 CYS C 96 CYS C 159 1555 1555 2.04
SSBOND 5 CYS C 198 CYS C 252 1555 1555 2.04
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.04
SSBOND 7 CYS E 96 CYS E 159 1555 1555 2.06
SSBOND 8 CYS E 198 CYS E 252 1555 1555 2.05
SSBOND 9 CYS F 25 CYS F 80 1555 1555 2.03
SSBOND 10 CYS G 96 CYS G 159 1555 1555 2.04
SSBOND 11 CYS G 198 CYS G 252 1555 1555 2.05
SSBOND 12 CYS H 25 CYS H 80 1555 1555 2.05
SSBOND 13 LE1 I 3 CYS I 13 1555 1555 2.05
SSBOND 14 LE1 J 103 CYS J 113 1555 1555 2.04
LINK C LE1 I 3 N THR I 4 1555 1555 1.34
LINK C GLY I 8 N SAR I 9 1555 1555 1.33
LINK C SAR I 9 N MLE I 10 1555 1555 1.33
LINK C MLE I 10 N TYR I 11 1555 1555 1.33
LINK C PHE J 102 N LE1 J 103 1555 1555 1.34
LINK C LE1 J 103 N THR J 104 1555 1555 1.33
LINK C GLY J 108 N SAR J 109 1555 1555 1.34
LINK C SAR J 109 N MLE J 110 1555 1555 1.33
LINK C MLE J 110 N TYR J 111 1555 1555 1.33
CISPEP 1 GLY A 86 PRO A 87 0 -14.18
CISPEP 2 TYR A 204 PRO A 205 0 -0.37
CISPEP 3 HIS B 31 PRO B 32 0 2.96
CISPEP 4 GLY C 86 PRO C 87 0 -1.95
CISPEP 5 TYR C 204 PRO C 205 0 -4.13
CISPEP 6 HIS D 31 PRO D 32 0 5.19
CISPEP 7 GLY E 86 PRO E 87 0 -1.75
CISPEP 8 TYR E 204 PRO E 205 0 -1.70
CISPEP 9 HIS F 31 PRO F 32 0 -2.96
CISPEP 10 GLY G 86 PRO G 87 0 -5.56
CISPEP 11 TYR G 204 PRO G 205 0 -6.50
CISPEP 12 HIS H 31 PRO H 32 0 -1.97
CRYST1 68.050 158.431 82.539 90.00 90.11 90.00 P 1 21 1 8
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 0.014695 0.000000 0.000029 0.00000
SCALE2 0.000000 0.006312 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012116 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
