HEADER IMMUNE SYSTEM 29-JUL-10 3O6F
TITLE CRYSTAL STRUCTURE OF A HUMAN AUTOIMMUNE TCR MS2-3C8 BOUND TO MHC CLASS
TITLE 2 II SELF-LIGAND MBP/HLA-DR4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 3 CHAIN: A, E;
COMPND 4 FRAGMENT: UNP RESIDUES 26-207;
COMPND 5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-4 BETA CHAIN;
COMPND 9 CHAIN: B, F;
COMPND 10 FRAGMENT: UNP RESIDUES 30-220;
COMPND 11 SYNONYM: MHC CLASS II ANTIGEN DRB1*4, DR-4, DR4;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: T-CELL RECEPTOR ALPHA CHAIN C REGION;
COMPND 15 CHAIN: C, G;
COMPND 16 FRAGMENT: UNP RESIDUES 1-92;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: T-CELL RECEPTOR BETA-1 CHAIN C REGION;
COMPND 20 CHAIN: D, H;
COMPND 21 FRAGMENT: UNP RESIDUES 1-130;
COMPND 22 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: HLA-DRA, HLA-DRA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HLA-DRB1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-26B(+);
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: TRAC, TCRA;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET-26B(+);
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 GENE: TRBC1;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PET-26B(+)
KEYWDS AUTOIMMUNITY, MULTIPLE SCLEROSIS, T CELL RECEPTOR, HLA CLASS II,
KEYWDS 2 PROTEIN-PROTEIN COMPLEX, IMMUNOGLOBULIN FOLD, MEMBRANE, IMMUNE
KEYWDS 3 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YIN,Y.LI,R.MARTIN,R.A.MARIUZZA
REVDAT 4 06-SEP-23 3O6F 1 REMARK SEQADV
REVDAT 3 09-AUG-17 3O6F 1 SOURCE REMARK
REVDAT 2 07-SEP-11 3O6F 1 JRNL VERSN
REVDAT 1 02-MAR-11 3O6F 0
JRNL AUTH Y.YIN,Y.LI,M.C.KERZIC,R.MARTIN,R.A.MARIUZZA
JRNL TITL STRUCTURE OF A TCR WITH HIGH AFFINITY FOR SELF-ANTIGEN
JRNL TITL 2 REVEALS BASIS FOR ESCAPE FROM NEGATIVE SELECTION.
JRNL REF EMBO J. V. 30 1137 2011
JRNL REFN ISSN 0261-4189
JRNL PMID 21297580
JRNL DOI 10.1038/EMBOJ.2011.21
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.2_432)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 55100
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2782
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.2136 - 6.0291 1.00 5501 301 0.2345 0.2418
REMARK 3 2 6.0291 - 4.7868 1.00 5305 290 0.2077 0.2375
REMARK 3 3 4.7868 - 4.1821 1.00 5283 266 0.1960 0.2336
REMARK 3 4 4.1821 - 3.7998 1.00 5174 302 0.2290 0.2892
REMARK 3 5 3.7998 - 3.5276 1.00 5233 252 0.2503 0.2872
REMARK 3 6 3.5276 - 3.3196 1.00 5209 262 0.2613 0.3036
REMARK 3 7 3.3196 - 3.1534 1.00 5162 304 0.2789 0.3574
REMARK 3 8 3.1534 - 3.0162 1.00 5197 247 0.2784 0.3444
REMARK 3 9 3.0162 - 2.9001 1.00 5160 291 0.3109 0.3841
REMARK 3 10 2.9001 - 2.8000 0.99 5094 267 0.3202 0.3669
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 35.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.59030
REMARK 3 B22 (A**2) : 9.55020
REMARK 3 B33 (A**2) : -5.95990
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 13230
REMARK 3 ANGLE : 1.339 18009
REMARK 3 CHIRALITY : 0.084 1963
REMARK 3 PLANARITY : 0.007 2358
REMARK 3 DIHEDRAL : 14.891 4686
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3O6F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060723.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING MONOCHROMETER
REMARK 200 AND VERTICAL FOCUSING MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55156
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 49.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.70
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.90
REMARK 200 R MERGE FOR SHELL (I) : 0.35500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
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: PDBG ENTRIES 1J8H, 1YMM, 3DX9, 1KGC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (W/V) POLYETHYLENE GLYCOL 8000,
REMARK 280 0.2 M CALCIUM ACETATE, AND 0.1 M IMIDAZOLE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 51.24000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 109.20150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.24000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 109.20150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ILE A 1
REMARK 465 LYS A 2
REMARK 465 GLU A 3
REMARK 465 ALA A 182
REMARK 465 GLY B 17
REMARK 465 SER B 18
REMARK 465 LEU B 19
REMARK 465 VAL B 20
REMARK 465 PRO B 21
REMARK 465 ARG B 22
REMARK 465 GLY B 23
REMARK 465 SER B 24
REMARK 465 GLY B 25
REMARK 465 GLY B 26
REMARK 465 GLY B 27
REMARK 465 GLY B 28
REMARK 465 SER B 29
REMARK 465 GLY B 30
REMARK 465 LYS B 134
REMARK 465 THR B 135
REMARK 465 GLN B 136
REMARK 465 PRO B 137
REMARK 465 LEU B 138
REMARK 465 GLN B 139
REMARK 465 HIS B 140
REMARK 465 HIS B 141
REMARK 465 ASN B 142
REMARK 465 ALA B 219
REMARK 465 ARG B 220
REMARK 465 SER B 221
REMARK 465 GLY C -1
REMARK 465 ASP C 0
REMARK 465 SER C 130
REMARK 465 GLN C 145
REMARK 465 ALA C 185
REMARK 465 PHE C 186
REMARK 465 ASN C 187
REMARK 465 PHE C 197
REMARK 465 PRO C 198
REMARK 465 SER C 199
REMARK 465 PRO C 200
REMARK 465 GLU C 201
REMARK 465 SER C 202
REMARK 465 SER C 203
REMARK 465 CYS C 204
REMARK 465 ILE E 1
REMARK 465 ASP E 181
REMARK 465 ALA E 182
REMARK 465 LYS F 134
REMARK 465 THR F 135
REMARK 465 GLN F 136
REMARK 465 PRO F 137
REMARK 465 LEU F 138
REMARK 465 GLN F 139
REMARK 465 HIS F 140
REMARK 465 HIS F 141
REMARK 465 ALA F 219
REMARK 465 ARG F 220
REMARK 465 SER F 221
REMARK 465 GLY G -1
REMARK 465 ASP G 0
REMARK 465 SER G 130
REMARK 465 SER G 146
REMARK 465 LYS G 147
REMARK 465 ASP G 148
REMARK 465 SER G 149
REMARK 465 ALA G 185
REMARK 465 PHE G 186
REMARK 465 ASN G 187
REMARK 465 PHE G 197
REMARK 465 PRO G 198
REMARK 465 SER G 199
REMARK 465 PRO G 200
REMARK 465 GLU G 201
REMARK 465 SER G 202
REMARK 465 SER G 203
REMARK 465 CYS G 204
REMARK 465 ASP H 244
REMARK 465 CYS H 245
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 100 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 123 CG CD NE CZ NH1 NH2
REMARK 470 THR A 130 OG1 CG2
REMARK 470 GLU A 158 CG CD OE1 OE2
REMARK 470 ARG B 52 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 ARG B 195 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 218 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 2 CG CD CE NZ
REMARK 470 ARG C 57 CG CD NE CZ NH1 NH2
REMARK 470 MET C 58 CG SD CE
REMARK 470 ARG C 76 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 122 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 125 CG CD CE NZ
REMARK 470 ASP C 138 CG OD1 OD2
REMARK 470 GLN C 140 CG CD OE1 NE2
REMARK 470 SER C 146 OG
REMARK 470 ASP C 155 CG OD1 OD2
REMARK 470 LYS C 177 CG CD CE NZ
REMARK 470 LYS D 18 CG CD CE NZ
REMARK 470 ARG D 22 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 39 CG CD CE NZ
REMARK 470 ARG D 205 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 71 CG CD OE1 OE2
REMARK 470 GLU E 98 CG CD OE1 OE2
REMARK 470 ARG E 100 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 158 CG CD OE1 OE2
REMARK 470 ARG F 52 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 81 CG CD OE1 OE2
REMARK 470 ARG F 195 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 14 CG CD OE1 OE2
REMARK 470 ARG G 122 CG CD NE CZ NH1 NH2
REMARK 470 ASP G 138 CG OD1 OD2
REMARK 470 GLN G 145 CG CD OE1 NE2
REMARK 470 LYS H 18 CG CD CE NZ
REMARK 470 ARG H 22 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 39 CG CD CE NZ
REMARK 470 ARG H 205 CG CD NE CZ NH1 NH2
REMARK 470 GLN H 225 CG CD OE1 NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU C 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 SD MET H 31 CB SER H 75 1.95
REMARK 500 O HOH F 224 O HOH F 225 2.07
REMARK 500 CD2 LEU C 121 N SER D 131 2.08
REMARK 500 O ARG F 101 O HOH F 225 2.13
REMARK 500 O PRO D 6 OG1 THR D 109 2.15
REMARK 500 O SER F 29 N ASP F 31 2.19
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 E 127 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO F 194 C - N - CA ANGL. DEV. = 12.0 DEGREES
REMARK 500 ARG F 218 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 84 151.34 -45.28
REMARK 500 ARG A 100 -3.56 83.23
REMARK 500 THR A 113 151.79 173.83
REMARK 500 ASN A 124 31.82 85.28
REMARK 500 THR A 129 19.16 -154.12
REMARK 500 VAL A 132 170.04 -56.00
REMARK 500 LYS A 147 140.80 179.42
REMARK 500 SER B 2 90.55 84.28
REMARK 500 ASN B 48 63.46 60.16
REMARK 500 HIS B 62 -120.07 63.33
REMARK 500 TYR B 107 -67.57 -120.39
REMARK 500 THR B 119 -72.42 -118.27
REMARK 500 ASN B 163 64.35 37.86
REMARK 500 TRP B 182 31.04 70.71
REMARK 500 PRO B 194 60.48 -66.23
REMARK 500 PRO B 212 134.35 -35.09
REMARK 500 GLU C 14 -2.25 65.95
REMARK 500 HIS C 23 73.72 -156.73
REMARK 500 ILE C 47 161.07 177.91
REMARK 500 SER C 52 -135.42 66.36
REMARK 500 MET C 58 -18.81 81.31
REMARK 500 ALA C 117 140.59 175.78
REMARK 500 LYS C 147 6.81 81.27
REMARK 500 SER C 163 -5.18 72.16
REMARK 500 ASP C 165 14.64 49.72
REMARK 500 ALA C 183 -0.70 80.62
REMARK 500 PRO C 192 -169.44 -70.83
REMARK 500 SER D 13 150.87 -44.76
REMARK 500 LYS D 39 -11.24 76.66
REMARK 500 LEU D 72 9.48 81.01
REMARK 500 THR D 73 -25.47 -143.76
REMARK 500 SER D 98 -129.87 -114.68
REMARK 500 TYR D 99 117.81 -36.93
REMARK 500 PRO D 152 -167.73 -77.81
REMARK 500 HIS D 154 78.22 -104.87
REMARK 500 ASP D 185 47.26 -100.88
REMARK 500 GLU E 4 -54.45 -125.16
REMARK 500 ARG E 100 -14.10 64.36
REMARK 500 THR E 113 145.78 175.97
REMARK 500 THR E 129 12.93 -141.42
REMARK 500 LYS E 147 138.50 -175.27
REMARK 500 SER F 2 88.13 95.88
REMARK 500 PRO F 21 140.83 -33.58
REMARK 500 HIS F 62 -116.70 57.59
REMARK 500 TYR F 107 -67.71 -131.03
REMARK 500 THR F 119 -74.21 -123.52
REMARK 500 SER F 155 108.42 -45.59
REMARK 500 ASP F 181 27.80 -140.16
REMARK 500 TRP F 182 34.75 70.18
REMARK 500 PRO F 194 -19.91 -44.77
REMARK 500
REMARK 500 THIS ENTRY HAS 88 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG F 68 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3O6F A 1 182 UNP P01903 DRA_HUMAN 26 207
DBREF 3O6F B 1 30 PDB 3O6F 3O6F 1 30
DBREF 3O6F B 31 221 UNP P13760 2B14_HUMAN 30 220
DBREF 3O6F C -1 108 PDB 3O6F 3O6F -1 108
DBREF 3O6F C 109 200 UNP P01848 TCA_HUMAN 1 92
DBREF 3O6F D 1 115 PDB 3O6F 3O6F 1 115
DBREF 3O6F D 116 245 UNP A0A5B9 TRBC2_HUMAN 1 130
DBREF 3O6F E 1 182 UNP P01903 DRA_HUMAN 26 207
DBREF 3O6F F 1 30 PDB 3O6F 3O6F 1 30
DBREF 3O6F F 31 221 UNP P13760 2B14_HUMAN 30 220
DBREF 3O6F G -1 108 PDB 3O6F 3O6F -1 108
DBREF 3O6F G 109 200 UNP P01848 TCA_HUMAN 1 92
DBREF 3O6F H 1 115 PDB 3O6F 3O6F 1 115
DBREF 3O6F H 116 245 UNP A0A5B9 TRBC2_HUMAN 1 130
SEQADV 3O6F SER D 189 UNP A0A5B9 CYS 74 ENGINEERED MUTATION
SEQADV 3O6F SER H 189 UNP A0A5B9 CYS 74 ENGINEERED MUTATION
SEQRES 1 A 182 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 182 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 182 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 182 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 182 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 182 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 182 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 182 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 182 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 182 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 182 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 182 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 182 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 182 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES 1 B 221 PHE SER TRP GLY ALA GLU GLY GLN ARG PRO GLY PHE GLY
SEQRES 2 B 221 SER GLY GLY GLY SER LEU VAL PRO ARG GLY SER GLY GLY
SEQRES 3 B 221 GLY GLY SER GLY ASP THR ARG PRO ARG PHE LEU GLU GLN
SEQRES 4 B 221 VAL LYS HIS GLU CYS HIS PHE PHE ASN GLY THR GLU ARG
SEQRES 5 B 221 VAL ARG PHE LEU ASP ARG TYR PHE TYR HIS GLN GLU GLU
SEQRES 6 B 221 TYR VAL ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA
SEQRES 7 B 221 VAL THR GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN
SEQRES 8 B 221 SER GLN LYS ASP LEU LEU GLU GLN LYS ARG ALA ALA VAL
SEQRES 9 B 221 ASP THR TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER
SEQRES 10 B 221 PHE THR VAL GLN ARG ARG VAL TYR PRO GLU VAL THR VAL
SEQRES 11 B 221 TYR PRO ALA LYS THR GLN PRO LEU GLN HIS HIS ASN LEU
SEQRES 12 B 221 LEU VAL CYS SER VAL ASN GLY PHE TYR PRO GLY SER ILE
SEQRES 13 B 221 GLU VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS THR
SEQRES 14 B 221 GLY VAL VAL SER THR GLY LEU ILE GLN ASN GLY ASP TRP
SEQRES 15 B 221 THR PHE GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG
SEQRES 16 B 221 SER GLY GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER
SEQRES 17 B 221 LEU THR SER PRO LEU THR VAL GLU TRP ARG ALA ARG SER
SEQRES 1 C 206 GLY ASP ALA LYS THR THR GLN PRO ASN SER MET GLU SER
SEQRES 2 C 206 ASN GLU GLU GLU PRO VAL HIS LEU PRO CYS ASN HIS SER
SEQRES 3 C 206 THR ILE SER GLY THR ASP TYR ILE HIS TRP TYR ARG GLN
SEQRES 4 C 206 LEU PRO SER GLN GLY PRO GLU TYR VAL ILE HIS GLY LEU
SEQRES 5 C 206 THR SER ASN VAL ASN ASN ARG MET ALA SER LEU ALA ILE
SEQRES 6 C 206 ALA GLU ASP ARG LYS SER SER THR LEU ILE LEU HIS ARG
SEQRES 7 C 206 ALA THR LEU ARG ASP ALA ALA VAL TYR TYR CYS THR VAL
SEQRES 8 C 206 TYR GLY GLY ALA THR ASN LYS LEU ILE PHE GLY THR GLY
SEQRES 9 C 206 THR LEU LEU ALA VAL GLN PRO ASN ILE GLN ASN PRO ASP
SEQRES 10 C 206 PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP
SEQRES 11 C 206 LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR
SEQRES 12 C 206 ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR
SEQRES 13 C 206 ASP LYS THR VAL LEU ASP MET ARG SER MET ASP PHE LYS
SEQRES 14 C 206 SER ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE
SEQRES 15 C 206 ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU
SEQRES 16 C 206 ASP THR PHE PHE PRO SER PRO GLU SER SER CYS
SEQRES 1 D 245 VAL VAL SER GLN HIS PRO SER TRP VAL ILE ALA LYS SER
SEQRES 2 D 245 GLY THR SER VAL LYS ILE GLU CYS ARG SER LEU ASP PHE
SEQRES 3 D 245 GLN ALA THR THR MET PHE TRP TYR ARG GLN PHE PRO LYS
SEQRES 4 D 245 GLN SER LEU MET LEU MET ALA THR SER ASN GLU GLY SER
SEQRES 5 D 245 LYS ALA THR TYR GLU GLN GLY VAL GLU LYS ASP LYS PHE
SEQRES 6 D 245 LEU ILE ASN HIS ALA SER LEU THR LEU SER THR LEU THR
SEQRES 7 D 245 VAL THR SER ALA HIS PRO GLU ASP SER SER PHE TYR ILE
SEQRES 8 D 245 CYS SER ALA ARG GLY GLY SER TYR ASN SER PRO LEU HIS
SEQRES 9 D 245 PHE GLY ASN GLY THR ARG LEU THR VAL THR GLU ASP LEU
SEQRES 10 D 245 LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO
SEQRES 11 D 245 SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU
SEQRES 12 D 245 VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU
SEQRES 13 D 245 LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY
SEQRES 14 D 245 VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA
SEQRES 15 D 245 LEU ASN ASP SER ARG TYR SER LEU SER SER ARG LEU ARG
SEQRES 16 D 245 VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE
SEQRES 17 D 245 ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP
SEQRES 18 D 245 GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE
SEQRES 19 D 245 VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS
SEQRES 1 E 182 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 E 182 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 E 182 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 E 182 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 E 182 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 E 182 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 E 182 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 E 182 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 E 182 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 E 182 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 E 182 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 E 182 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 E 182 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 E 182 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES 1 F 221 PHE SER TRP GLY ALA GLU GLY GLN ARG PRO GLY PHE GLY
SEQRES 2 F 221 SER GLY GLY GLY SER LEU VAL PRO ARG GLY SER GLY GLY
SEQRES 3 F 221 GLY GLY SER GLY ASP THR ARG PRO ARG PHE LEU GLU GLN
SEQRES 4 F 221 VAL LYS HIS GLU CYS HIS PHE PHE ASN GLY THR GLU ARG
SEQRES 5 F 221 VAL ARG PHE LEU ASP ARG TYR PHE TYR HIS GLN GLU GLU
SEQRES 6 F 221 TYR VAL ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA
SEQRES 7 F 221 VAL THR GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN
SEQRES 8 F 221 SER GLN LYS ASP LEU LEU GLU GLN LYS ARG ALA ALA VAL
SEQRES 9 F 221 ASP THR TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER
SEQRES 10 F 221 PHE THR VAL GLN ARG ARG VAL TYR PRO GLU VAL THR VAL
SEQRES 11 F 221 TYR PRO ALA LYS THR GLN PRO LEU GLN HIS HIS ASN LEU
SEQRES 12 F 221 LEU VAL CYS SER VAL ASN GLY PHE TYR PRO GLY SER ILE
SEQRES 13 F 221 GLU VAL ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS THR
SEQRES 14 F 221 GLY VAL VAL SER THR GLY LEU ILE GLN ASN GLY ASP TRP
SEQRES 15 F 221 THR PHE GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG
SEQRES 16 F 221 SER GLY GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER
SEQRES 17 F 221 LEU THR SER PRO LEU THR VAL GLU TRP ARG ALA ARG SER
SEQRES 1 G 206 GLY ASP ALA LYS THR THR GLN PRO ASN SER MET GLU SER
SEQRES 2 G 206 ASN GLU GLU GLU PRO VAL HIS LEU PRO CYS ASN HIS SER
SEQRES 3 G 206 THR ILE SER GLY THR ASP TYR ILE HIS TRP TYR ARG GLN
SEQRES 4 G 206 LEU PRO SER GLN GLY PRO GLU TYR VAL ILE HIS GLY LEU
SEQRES 5 G 206 THR SER ASN VAL ASN ASN ARG MET ALA SER LEU ALA ILE
SEQRES 6 G 206 ALA GLU ASP ARG LYS SER SER THR LEU ILE LEU HIS ARG
SEQRES 7 G 206 ALA THR LEU ARG ASP ALA ALA VAL TYR TYR CYS THR VAL
SEQRES 8 G 206 TYR GLY GLY ALA THR ASN LYS LEU ILE PHE GLY THR GLY
SEQRES 9 G 206 THR LEU LEU ALA VAL GLN PRO ASN ILE GLN ASN PRO ASP
SEQRES 10 G 206 PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP
SEQRES 11 G 206 LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR
SEQRES 12 G 206 ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR
SEQRES 13 G 206 ASP LYS THR VAL LEU ASP MET ARG SER MET ASP PHE LYS
SEQRES 14 G 206 SER ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE
SEQRES 15 G 206 ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU
SEQRES 16 G 206 ASP THR PHE PHE PRO SER PRO GLU SER SER CYS
SEQRES 1 H 245 VAL VAL SER GLN HIS PRO SER TRP VAL ILE ALA LYS SER
SEQRES 2 H 245 GLY THR SER VAL LYS ILE GLU CYS ARG SER LEU ASP PHE
SEQRES 3 H 245 GLN ALA THR THR MET PHE TRP TYR ARG GLN PHE PRO LYS
SEQRES 4 H 245 GLN SER LEU MET LEU MET ALA THR SER ASN GLU GLY SER
SEQRES 5 H 245 LYS ALA THR TYR GLU GLN GLY VAL GLU LYS ASP LYS PHE
SEQRES 6 H 245 LEU ILE ASN HIS ALA SER LEU THR LEU SER THR LEU THR
SEQRES 7 H 245 VAL THR SER ALA HIS PRO GLU ASP SER SER PHE TYR ILE
SEQRES 8 H 245 CYS SER ALA ARG GLY GLY SER TYR ASN SER PRO LEU HIS
SEQRES 9 H 245 PHE GLY ASN GLY THR ARG LEU THR VAL THR GLU ASP LEU
SEQRES 10 H 245 LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO
SEQRES 11 H 245 SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU
SEQRES 12 H 245 VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU
SEQRES 13 H 245 LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY
SEQRES 14 H 245 VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA
SEQRES 15 H 245 LEU ASN ASP SER ARG TYR SER LEU SER SER ARG LEU ARG
SEQRES 16 H 245 VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE
SEQRES 17 H 245 ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP
SEQRES 18 H 245 GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE
SEQRES 19 H 245 VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS
FORMUL 9 HOH *27(H2 O)
HELIX 1 1 GLU A 47 ALA A 52 1 6
HELIX 2 2 ALA A 56 SER A 77 1 22
HELIX 3 3 THR B 80 LEU B 82 5 3
HELIX 4 4 GLY B 83 ASN B 91 1 9
HELIX 5 5 GLN B 93 ARG B 101 1 9
HELIX 6 6 ALA B 102 TYR B 107 1 6
HELIX 7 7 TYR B 107 GLU B 116 1 10
HELIX 8 8 SER B 117 THR B 119 5 3
HELIX 9 9 THR C 78 ALA C 82 5 5
HELIX 10 10 HIS D 83 SER D 87 5 5
HELIX 11 11 ASP D 116 VAL D 120 5 5
HELIX 12 12 GLU D 132 GLN D 139 1 8
HELIX 13 13 ALA D 198 GLN D 202 1 5
HELIX 14 14 GLU E 47 ALA E 52 1 6
HELIX 15 15 ALA E 56 SER E 77 1 22
HELIX 16 16 THR F 80 LEU F 82 5 3
HELIX 17 17 GLY F 83 ASN F 91 1 9
HELIX 18 18 GLN F 93 TYR F 107 1 15
HELIX 19 19 TYR F 107 GLU F 116 1 10
HELIX 20 20 THR G 78 ALA G 82 5 5
HELIX 21 21 HIS H 83 SER H 87 5 5
HELIX 22 22 ASP H 116 VAL H 120 5 5
HELIX 23 23 SER H 131 SER H 136 1 6
HELIX 24 24 THR H 199 TRP H 201 5 3
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 N ASP A 35 O GLU A 40
SHEET 3 A 8 SER A 19 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 4 A 8 HIS A 5 ASN A 15 -1 N ILE A 8 O ASP A 25
SHEET 5 A 8 PHE B 36 PHE B 47 -1 O PHE B 36 N ASN A 15
SHEET 6 A 8 ARG B 52 TYR B 61 -1 O PHE B 60 N GLN B 39
SHEET 7 A 8 GLU B 64 ASP B 70 -1 O PHE B 69 N ASP B 57
SHEET 8 A 8 TYR B 76 ALA B 78 -1 O ARG B 77 N ARG B 68
SHEET 1 B 4 VAL A 91 THR A 93 0
SHEET 2 B 4 ASN A 103 PHE A 108 -1 O ILE A 106 N LEU A 92
SHEET 3 B 4 PHE A 148 PHE A 153 -1 O PHE A 153 N ASN A 103
SHEET 4 B 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 C 4 PRO A 127 VAL A 128 0
SHEET 2 C 4 ASN A 118 ARG A 123 -1 N TRP A 121 O VAL A 128
SHEET 3 C 4 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 C 4 HIS A 177 TRP A 178 -1 O TRP A 178 N TYR A 161
SHEET 1 D 2 LEU A 138 PRO A 139 0
SHEET 2 D 2 PHE A 145 ARG A 146 -1 O ARG A 146 N LEU A 138
SHEET 1 E 4 GLU B 127 TYR B 131 0
SHEET 2 E 4 LEU B 144 PHE B 151 -1 O VAL B 145 N TYR B 131
SHEET 3 E 4 PHE B 184 LEU B 190 -1 O THR B 186 N VAL B 148
SHEET 4 E 4 VAL B 171 SER B 173 -1 N VAL B 172 O MET B 189
SHEET 1 F 4 GLU B 127 TYR B 131 0
SHEET 2 F 4 LEU B 144 PHE B 151 -1 O VAL B 145 N TYR B 131
SHEET 3 F 4 PHE B 184 LEU B 190 -1 O THR B 186 N VAL B 148
SHEET 4 F 4 ILE B 177 GLN B 178 -1 N ILE B 177 O GLN B 185
SHEET 1 G 4 GLN B 165 GLU B 166 0
SHEET 2 G 4 GLU B 157 ARG B 162 -1 N ARG B 162 O GLN B 165
SHEET 3 G 4 TYR B 200 GLU B 205 -1 O GLN B 203 N ARG B 159
SHEET 4 G 4 LEU B 213 VAL B 215 -1 O LEU B 213 N VAL B 204
SHEET 1 H 5 SER C 8 ASN C 12 0
SHEET 2 H 5 THR C 103 GLN C 108 1 O GLN C 108 N SER C 11
SHEET 3 H 5 VAL C 84 GLY C 91 -1 N TYR C 85 O THR C 103
SHEET 4 H 5 ASP C 30 GLN C 37 -1 N HIS C 33 O THR C 88
SHEET 5 H 5 GLU C 44 GLY C 49 -1 O VAL C 46 N TRP C 34
SHEET 1 I 4 VAL C 17 ASN C 22 0
SHEET 2 I 4 SER C 69 LEU C 74 -1 O LEU C 72 N LEU C 19
SHEET 3 I 4 ALA C 59 ILE C 63 -1 N SER C 60 O ILE C 73
SHEET 4 I 4 ASN C 53 ASN C 56 -1 N VAL C 54 O LEU C 61
SHEET 1 J 4 ALA C 117 GLN C 120 0
SHEET 2 J 4 VAL C 131 THR C 135 -1 O LEU C 133 N TYR C 119
SHEET 3 J 4 ALA C 171 TRP C 174 -1 O ALA C 173 N CYS C 132
SHEET 4 J 4 TYR C 152 ILE C 153 -1 N TYR C 152 O TRP C 174
SHEET 1 K 2 LEU C 159 MET C 161 0
SHEET 2 K 2 PHE C 166 SER C 168 -1 O SER C 168 N LEU C 159
SHEET 1 L 4 VAL D 2 HIS D 5 0
SHEET 2 L 4 VAL D 17 SER D 23 -1 O GLU D 20 N HIS D 5
SHEET 3 L 4 LEU D 74 VAL D 79 -1 O VAL D 79 N VAL D 17
SHEET 4 L 4 PHE D 65 ASN D 68 -1 N LEU D 66 O THR D 78
SHEET 1 M 6 TRP D 8 LYS D 12 0
SHEET 2 M 6 THR D 109 THR D 114 1 O THR D 112 N VAL D 9
SHEET 3 M 6 SER D 88 ARG D 95 -1 N SER D 88 O LEU D 111
SHEET 4 M 6 THR D 30 GLN D 36 -1 N TYR D 34 O ILE D 91
SHEET 5 M 6 MET D 43 ASN D 49 -1 O MET D 45 N TRP D 33
SHEET 6 M 6 THR D 55 TYR D 56 -1 O THR D 55 N THR D 47
SHEET 1 N 4 TRP D 8 LYS D 12 0
SHEET 2 N 4 THR D 109 THR D 114 1 O THR D 112 N VAL D 9
SHEET 3 N 4 SER D 88 ARG D 95 -1 N SER D 88 O LEU D 111
SHEET 4 N 4 LEU D 103 PHE D 105 -1 O HIS D 104 N ALA D 94
SHEET 1 O 4 GLU D 124 PHE D 128 0
SHEET 2 O 4 LYS D 140 PHE D 150 -1 O VAL D 144 N PHE D 128
SHEET 3 O 4 TYR D 188 SER D 197 -1 O VAL D 196 N ALA D 141
SHEET 4 O 4 SER D 171 THR D 172 -1 N SER D 171 O ARG D 193
SHEET 1 P 4 GLU D 124 PHE D 128 0
SHEET 2 P 4 LYS D 140 PHE D 150 -1 O VAL D 144 N PHE D 128
SHEET 3 P 4 TYR D 188 SER D 197 -1 O VAL D 196 N ALA D 141
SHEET 4 P 4 LEU D 177 LYS D 178 -1 N LEU D 177 O SER D 189
SHEET 1 Q 4 LYS D 164 VAL D 166 0
SHEET 2 Q 4 VAL D 155 VAL D 161 -1 N TRP D 159 O VAL D 166
SHEET 3 Q 4 HIS D 207 PHE D 214 -1 O GLN D 211 N SER D 158
SHEET 4 Q 4 GLN D 233 TRP D 240 -1 O GLN D 233 N PHE D 214
SHEET 1 R 8 GLU E 40 TRP E 43 0
SHEET 2 R 8 ASP E 29 ASP E 35 -1 N HIS E 33 O VAL E 42
SHEET 3 R 8 SER E 19 PHE E 26 -1 N PHE E 26 O ASP E 29
SHEET 4 R 8 GLU E 3 ASN E 15 -1 N LEU E 14 O SER E 19
SHEET 5 R 8 PHE F 36 PHE F 47 -1 O CYS F 44 N ILE E 7
SHEET 6 R 8 ARG F 52 TYR F 61 -1 O LEU F 56 N GLU F 43
SHEET 7 R 8 GLU F 64 ASP F 70 -1 O PHE F 69 N ASP F 57
SHEET 8 R 8 TYR F 76 ALA F 78 -1 O ARG F 77 N ARG F 68
SHEET 1 S 4 GLU E 88 THR E 93 0
SHEET 2 S 4 ASN E 103 ASP E 110 -1 O ILE E 106 N LEU E 92
SHEET 3 S 4 PHE E 148 TYR E 150 -1 O HIS E 149 N CYS E 107
SHEET 4 S 4 SER E 133 GLU E 134 -1 N SER E 133 O TYR E 150
SHEET 1 T 3 GLU E 88 THR E 93 0
SHEET 2 T 3 ASN E 103 ASP E 110 -1 O ILE E 106 N LEU E 92
SHEET 3 T 3 PRO E 152 PHE E 153 -1 O PHE E 153 N ASN E 103
SHEET 1 U 4 LYS E 126 PRO E 127 0
SHEET 2 U 4 ASN E 118 ARG E 123 -1 N ARG E 123 O LYS E 126
SHEET 3 U 4 VAL E 160 GLU E 166 -1 O ARG E 164 N THR E 120
SHEET 4 U 4 LEU E 174 GLU E 179 -1 O TRP E 178 N TYR E 161
SHEET 1 V 2 LEU E 138 PRO E 139 0
SHEET 2 V 2 PHE E 145 ARG E 146 -1 O ARG E 146 N LEU E 138
SHEET 1 W 4 GLU F 127 PRO F 132 0
SHEET 2 W 4 LEU F 143 PHE F 151 -1 O SER F 147 N THR F 129
SHEET 3 W 4 PHE F 184 GLU F 191 -1 O LEU F 190 N LEU F 144
SHEET 4 W 4 VAL F 171 SER F 173 -1 N VAL F 172 O MET F 189
SHEET 1 X 4 GLU F 127 PRO F 132 0
SHEET 2 X 4 LEU F 143 PHE F 151 -1 O SER F 147 N THR F 129
SHEET 3 X 4 PHE F 184 GLU F 191 -1 O LEU F 190 N LEU F 144
SHEET 4 X 4 ILE F 177 GLN F 178 -1 N ILE F 177 O GLN F 185
SHEET 1 Y 4 GLN F 165 GLU F 166 0
SHEET 2 Y 4 GLU F 157 ARG F 162 -1 N ARG F 162 O GLN F 165
SHEET 3 Y 4 TYR F 200 GLU F 205 -1 O GLN F 203 N ARG F 159
SHEET 4 Y 4 LEU F 213 VAL F 215 -1 O LEU F 213 N VAL F 204
SHEET 1 Z 5 SER G 8 ASN G 12 0
SHEET 2 Z 5 THR G 103 GLN G 108 1 O GLN G 108 N SER G 11
SHEET 3 Z 5 VAL G 84 GLY G 91 -1 N TYR G 85 O THR G 103
SHEET 4 Z 5 ASP G 30 GLN G 37 -1 N TYR G 35 O TYR G 86
SHEET 5 Z 5 GLU G 44 GLY G 49 -1 O ILE G 47 N TRP G 34
SHEET 1 AA 4 VAL G 17 ASN G 22 0
SHEET 2 AA 4 SER G 69 LEU G 74 -1 O LEU G 72 N LEU G 19
SHEET 3 AA 4 ALA G 59 ILE G 63 -1 N SER G 60 O ILE G 73
SHEET 4 AA 4 ASN G 53 ASN G 55 -1 N VAL G 54 O LEU G 61
SHEET 1 AB 4 ALA G 117 TYR G 119 0
SHEET 2 AB 4 CYS G 132 THR G 135 -1 O LEU G 133 N TYR G 119
SHEET 3 AB 4 ALA G 171 TRP G 174 -1 O ALA G 173 N CYS G 132
SHEET 4 AB 4 TYR G 152 ILE G 153 -1 N TYR G 152 O TRP G 174
SHEET 1 AC 2 ARG G 122 ASP G 123 0
SHEET 2 AC 2 PHE H 128 GLU H 129 -1 O GLU H 129 N ARG G 122
SHEET 1 AD 2 LEU G 159 MET G 161 0
SHEET 2 AD 2 PHE G 166 SER G 168 -1 O PHE G 166 N MET G 161
SHEET 1 AE 4 VAL H 2 HIS H 5 0
SHEET 2 AE 4 VAL H 17 SER H 23 -1 O GLU H 20 N HIS H 5
SHEET 3 AE 4 LEU H 74 VAL H 79 -1 O SER H 75 N CYS H 21
SHEET 4 AE 4 PHE H 65 ASN H 68 -1 N LEU H 66 O THR H 78
SHEET 1 AF 6 TRP H 8 LYS H 12 0
SHEET 2 AF 6 THR H 109 THR H 114 1 O THR H 112 N VAL H 9
SHEET 3 AF 6 SER H 88 ARG H 95 -1 N TYR H 90 O THR H 109
SHEET 4 AF 6 THR H 30 GLN H 36 -1 N TYR H 34 O ILE H 91
SHEET 5 AF 6 MET H 43 ASN H 49 -1 O MET H 45 N TRP H 33
SHEET 6 AF 6 THR H 55 TYR H 56 -1 O THR H 55 N THR H 47
SHEET 1 AG 4 TRP H 8 LYS H 12 0
SHEET 2 AG 4 THR H 109 THR H 114 1 O THR H 112 N VAL H 9
SHEET 3 AG 4 SER H 88 ARG H 95 -1 N TYR H 90 O THR H 109
SHEET 4 AG 4 LEU H 103 PHE H 105 -1 O HIS H 104 N ALA H 94
SHEET 1 AH 3 LYS H 140 PHE H 150 0
SHEET 2 AH 3 TYR H 188 SER H 197 -1 O VAL H 196 N ALA H 141
SHEET 3 AH 3 LEU H 177 LYS H 178 -1 N LEU H 177 O SER H 189
SHEET 1 AI 4 LYS H 164 VAL H 166 0
SHEET 2 AI 4 VAL H 155 VAL H 161 -1 N TRP H 159 O VAL H 166
SHEET 3 AI 4 HIS H 207 PHE H 214 -1 O ARG H 209 N TRP H 160
SHEET 4 AI 4 ALA H 237 TRP H 240 -1 O ALA H 239 N PHE H 208
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.04
SSBOND 2 CYS B 44 CYS B 108 1555 1555 2.07
SSBOND 3 CYS B 146 CYS B 202 1555 1555 2.04
SSBOND 4 CYS C 21 CYS C 87 1555 1555 2.05
SSBOND 5 CYS C 132 CYS C 182 1555 1555 1.99
SSBOND 6 CYS D 21 CYS D 92 1555 1555 2.03
SSBOND 7 CYS D 145 CYS D 210 1555 1555 2.02
SSBOND 8 CYS E 107 CYS E 163 1555 1555 2.03
SSBOND 9 CYS F 44 CYS F 108 1555 1555 2.08
SSBOND 10 CYS F 146 CYS F 202 1555 1555 2.03
SSBOND 11 CYS G 21 CYS G 87 1555 1555 2.05
SSBOND 12 CYS G 132 CYS G 182 1555 1555 2.05
SSBOND 13 CYS H 21 CYS H 92 1555 1555 2.04
SSBOND 14 CYS H 145 CYS H 210 1555 1555 2.01
CISPEP 1 ASN A 15 PRO A 16 0 -5.23
CISPEP 2 THR A 113 PRO A 114 0 -6.71
CISPEP 3 GLY B 15 GLY B 16 0 3.79
CISPEP 4 TYR B 152 PRO B 153 0 3.70
CISPEP 5 HIS D 5 PRO D 6 0 3.51
CISPEP 6 TYR D 151 PRO D 152 0 -2.66
CISPEP 7 ASN E 15 PRO E 16 0 -1.04
CISPEP 8 THR E 113 PRO E 114 0 -3.20
CISPEP 9 TYR F 152 PRO F 153 0 5.46
CISPEP 10 HIS H 5 PRO H 6 0 -1.66
CISPEP 11 TYR H 151 PRO H 152 0 -1.17
CRYST1 102.480 218.403 98.412 90.00 90.00 90.00 P 21 21 2 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 0.009758 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004579 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END