HEADER IMMUNE SYSTEM 13-AUG-10 3OF6
TITLE HUMAN PRE-T CELL RECEPTOR CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T CELL RECEPTOR BETA CHAIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: ECTODOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PRE T-CELL ANTIGEN RECEPTOR ALPHA;
COMPND 9 CHAIN: D, E, F;
COMPND 10 FRAGMENT: ECTODOMAIN, UNP RESIDUES 17-135;
COMPND 11 SYNONYM: PRE-T ALPHA CHAIN, PT-ALPHA, PTA, PT-ALPHA-TCR;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIFIVE INSECT CELLS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PFASTBAC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HIFIVE INSECT CELLS;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: PFASTBAC
KEYWDS IG FOLD, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.S.PANG
REVDAT 4 01-NOV-23 3OF6 1 HETSYN
REVDAT 3 29-JUL-20 3OF6 1 COMPND REMARK DBREF SEQADV
REVDAT 3 2 1 HETNAM LINK SITE
REVDAT 2 27-OCT-10 3OF6 1 JRNL
REVDAT 1 20-OCT-10 3OF6 0
JRNL AUTH S.S.PANG,R.BERRY,Z.CHEN,L.KJER-NIELSEN,M.A.PERUGINI,
JRNL AUTH 2 G.F.KING,C.WANG,S.H.CHEW,N.L.LA GRUTA,N.K.WILLIAMS,T.BEDDOE,
JRNL AUTH 3 T.TIGANIS,N.P.COWIESON,D.I.GODFREY,A.W.PURCELL,M.C.J.WILCE,
JRNL AUTH 4 J.MCCLUSKEY,J.ROSSJOHN
JRNL TITL THE STRUCTURAL BASIS FOR AUTONOMOUS DIMERIZATION OF THE
JRNL TITL 2 PRE-T-CELL ANTIGEN RECEPTOR
JRNL REF NATURE V. 467 844 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20944746
JRNL DOI 10.1038/NATURE09448
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_4)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35090
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 1809
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 48.6701 - 6.5807 0.95 2722 152 0.1723 0.2282
REMARK 3 2 6.5807 - 5.2253 0.95 2601 140 0.1747 0.2739
REMARK 3 3 5.2253 - 4.5653 0.95 2593 140 0.1233 0.1994
REMARK 3 4 4.5653 - 4.1482 0.95 2561 141 0.1374 0.2028
REMARK 3 5 4.1482 - 3.8510 0.95 2551 141 0.1578 0.2545
REMARK 3 6 3.8510 - 3.6240 0.95 2536 138 0.1776 0.2145
REMARK 3 7 3.6240 - 3.4426 0.95 2537 140 0.1905 0.2002
REMARK 3 8 3.4426 - 3.2927 0.95 2536 137 0.2054 0.3377
REMARK 3 9 3.2927 - 3.1660 0.95 2529 138 0.2219 0.2906
REMARK 3 10 3.1660 - 3.0568 0.95 2544 134 0.2255 0.2644
REMARK 3 11 3.0568 - 2.9612 0.95 2489 132 0.2407 0.2521
REMARK 3 12 2.9612 - 2.8766 0.95 2515 136 0.2528 0.3001
REMARK 3 13 2.8766 - 2.8009 0.95 2531 140 0.2604 0.2847
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 80.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.92590
REMARK 3 B22 (A**2) : 4.92590
REMARK 3 B33 (A**2) : -18.49470
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: 0.5150
REMARK 3 OPERATOR: -K,H+K,L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 8196
REMARK 3 ANGLE : 0.378 11205
REMARK 3 CHIRALITY : 0.021 1226
REMARK 3 PLANARITY : 0.003 1472
REMARK 3 DIHEDRAL : 10.375 2870
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 3OF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000061038.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979461
REMARK 200 MONOCHROMATOR : SI VORTEX-ES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35135
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 67.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 1KGC; E CHAIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE, PH 7.0, 0.1M
REMARK 280 CALCIUM ACETATE, 13-16% PEG 1500, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 122.06733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.03367
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.03367
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 122.06733
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -199.01610
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 61.03367
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 HIS A 1
REMARK 465 ALA A 246
REMARK 465 ASP A 247
REMARK 465 CYS A 248
REMARK 465 THR A 249
REMARK 465 SER A 250
REMARK 465 GLY A 251
REMARK 465 ASP A 252
REMARK 465 ASP A 253
REMARK 465 ASP A 254
REMARK 465 ASP A 255
REMARK 465 LYS A 256
REMARK 465 ALA B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 HIS B 1
REMARK 465 CYS B 248
REMARK 465 THR B 249
REMARK 465 SER B 250
REMARK 465 GLY B 251
REMARK 465 ASP B 252
REMARK 465 ASP B 253
REMARK 465 ASP B 254
REMARK 465 ASP B 255
REMARK 465 LYS B 256
REMARK 465 ALA C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 CYS C 248
REMARK 465 THR C 249
REMARK 465 SER C 250
REMARK 465 GLY C 251
REMARK 465 ASP C 252
REMARK 465 ASP C 253
REMARK 465 ASP C 254
REMARK 465 ASP C 255
REMARK 465 LYS C 256
REMARK 465 GLY D -3
REMARK 465 ALA D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 LEU D 1
REMARK 465 PRO D 2
REMARK 465 THR D 3
REMARK 465 GLY D 4
REMARK 465 VAL D 5
REMARK 465 GLY D 6
REMARK 465 GLY D 96
REMARK 465 ALA D 97
REMARK 465 GLU D 98
REMARK 465 GLY D 99
REMARK 465 GLY D 111
REMARK 465 GLU D 112
REMARK 465 ALA D 113
REMARK 465 SER D 114
REMARK 465 THR D 115
REMARK 465 ALA D 116
REMARK 465 ARG D 117
REMARK 465 THR D 118
REMARK 465 CYS D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 ASP D 122
REMARK 465 ASP D 123
REMARK 465 ASP D 124
REMARK 465 ASP D 125
REMARK 465 LYS D 126
REMARK 465 GLY E -3
REMARK 465 ALA E -2
REMARK 465 HIS E -1
REMARK 465 MET E 0
REMARK 465 LEU E 1
REMARK 465 PRO E 2
REMARK 465 THR E 3
REMARK 465 GLY E 4
REMARK 465 VAL E 5
REMARK 465 GLY E 6
REMARK 465 GLY E 111
REMARK 465 GLU E 112
REMARK 465 ALA E 113
REMARK 465 SER E 114
REMARK 465 THR E 115
REMARK 465 ALA E 116
REMARK 465 ARG E 117
REMARK 465 THR E 118
REMARK 465 CYS E 119
REMARK 465 SER E 120
REMARK 465 GLY E 121
REMARK 465 ASP E 122
REMARK 465 ASP E 123
REMARK 465 ASP E 124
REMARK 465 ASP E 125
REMARK 465 LYS E 126
REMARK 465 GLY F -3
REMARK 465 ALA F -2
REMARK 465 HIS F -1
REMARK 465 MET F 0
REMARK 465 LEU F 1
REMARK 465 PRO F 2
REMARK 465 THR F 3
REMARK 465 GLY F 4
REMARK 465 VAL F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 GLY F 111
REMARK 465 GLU F 112
REMARK 465 ALA F 113
REMARK 465 SER F 114
REMARK 465 THR F 115
REMARK 465 ALA F 116
REMARK 465 ARG F 117
REMARK 465 THR F 118
REMARK 465 CYS F 119
REMARK 465 SER F 120
REMARK 465 GLY F 121
REMARK 465 ASP F 122
REMARK 465 ASP F 123
REMARK 465 ASP F 124
REMARK 465 ASP F 125
REMARK 465 LYS F 126
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 MET A 2 CG SD CE
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 63 CG OD1 OD2
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 GLN A 83 CG CD OE1 NE2
REMARK 470 GLN A 98 CG CD OE1 NE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 GLN A 178 CG CD OE1 NE2
REMARK 470 ASN A 187 CG OD1 ND2
REMARK 470 CYS A 192 SG
REMARK 470 GLU A 225 CG CD OE1 OE2
REMARK 470 ARG B 15 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 83 CG CD OE1 NE2
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 GLU B 135 CG CD OE1 OE2
REMARK 470 LYS B 167 CG CD CE NZ
REMARK 470 CYS B 192 SG
REMARK 470 GLN B 228 CG CD OE1 NE2
REMARK 470 ASP B 229 CG OD1 OD2
REMARK 470 ASP B 247 CG OD1 OD2
REMARK 470 HIS C 1 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 52 CG CD OE1 OE2
REMARK 470 LEU C 55 CG CD1 CD2
REMARK 470 ARG C 81 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 121 CG CD CE NZ
REMARK 470 GLU C 127 CG CD OE1 OE2
REMARK 470 CYS C 192 SG
REMARK 470 ASP C 229 CG OD1 OD2
REMARK 470 LEU D 41 CG CD1 CD2
REMARK 470 ARG D 102 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 108 CG ND1 CD2 CE1 NE2
REMARK 470 SER D 110 OG
REMARK 470 ARG E 102 CG CD NE CZ NH1 NH2
REMARK 470 SER E 110 OG
REMARK 470 GLU F 98 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 ND2 ASN D 51 C2 NAG D 1000 1.91
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 25 170.51 -58.47
REMARK 500 PRO A 43 109.96 -54.73
REMARK 500 LEU A 46 -73.13 -126.76
REMARK 500 ASN A 51 70.00 49.48
REMARK 500 GLU A 52 18.13 56.57
REMARK 500 PHE A 66 116.35 -164.96
REMARK 500 GLU A 85 1.53 -69.64
REMARK 500 SER A 87 91.10 -67.30
REMARK 500 PRO A 155 -161.28 -79.47
REMARK 500 ASP A 156 47.13 -82.96
REMARK 500 ALA A 231 -166.59 48.49
REMARK 500 LYS A 232 114.87 -160.84
REMARK 500 PRO A 233 76.76 -66.67
REMARK 500 THR A 235 105.00 -59.05
REMARK 500 PRO B 25 -173.27 -60.19
REMARK 500 LEU B 46 -75.18 -128.34
REMARK 500 ASN B 51 88.69 54.80
REMARK 500 PRO B 61 -71.19 -73.70
REMARK 500 PRO B 70 -91.22 -50.80
REMARK 500 ALA B 88 -173.85 -172.27
REMARK 500 PRO B 155 -156.10 -82.71
REMARK 500 HIS B 157 77.45 -112.97
REMARK 500 GLN B 228 16.13 -143.48
REMARK 500 THR B 235 90.16 -68.05
REMARK 500 ALA B 242 106.69 -168.07
REMARK 500 ALA B 246 -161.09 -75.97
REMARK 500 PRO C 25 -177.96 -65.21
REMARK 500 PRO C 43 106.22 -59.95
REMARK 500 PRO C 61 -103.39 -59.57
REMARK 500 ARG C 69 66.05 -169.52
REMARK 500 PRO C 70 -70.75 -49.44
REMARK 500 SER C 73 -81.49 -122.33
REMARK 500 ARG C 81 76.67 50.52
REMARK 500 HIS C 140 -72.28 -114.23
REMARK 500 ASP C 156 46.54 -82.01
REMARK 500 ALA C 231 -172.09 -64.72
REMARK 500 PRO C 233 85.00 -62.73
REMARK 500 THR C 235 99.75 -59.20
REMARK 500 VAL D 21 -74.29 -116.46
REMARK 500 ALA D 37 170.14 -59.22
REMARK 500 LEU D 41 -131.35 -87.33
REMARK 500 ASP D 42 -177.24 -175.99
REMARK 500 ALA D 49 -158.83 -100.65
REMARK 500 SER D 85 -31.62 -133.06
REMARK 500 VAL E 21 -82.42 -123.49
REMARK 500 ASP E 22 62.03 -119.17
REMARK 500 PRO E 39 -179.53 -46.87
REMARK 500 PRO E 44 152.58 -46.69
REMARK 500 THR E 69 -164.56 -78.29
REMARK 500 VAL F 21 -93.21 -96.32
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KGC RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE NUMBERING OF THE PROTEIN IS BASED THAT OF A T CELL RECEPTOR AND
REMARK 999 THERE IS A GAP IN THE NUMBERING IN THE CDR3 LOOP REGION (101-104).
REMARK 999 FOR CHAINS A,B,C, THE UNICODE IS DEFINE AS P01850. THE N-TERMINAL
REMARK 999 HALF OF THE PROTEIN (RESIDUE 3-117) IS A VARIABLE REGION OF A T
REMARK 999 CELL RECEPTOR. THE FIRST FOUR RESIDUES AGSH AND LAST 9 RESIDUES
REMARK 999 CTSGDDDDK ARE EXPRESSION TAG REGIONS.
DBREF 3OF6 A -2 256 PDB 3OF6 3OF6 -2 256
DBREF 3OF6 B -2 256 PDB 3OF6 3OF6 -2 256
DBREF 3OF6 C -2 256 PDB 3OF6 3OF6 -2 256
DBREF 3OF6 D 1 119 UNP Q6ISU1 PTCRA_HUMAN 17 135
DBREF 3OF6 E 1 119 UNP Q6ISU1 PTCRA_HUMAN 17 135
DBREF 3OF6 F 1 119 UNP Q6ISU1 PTCRA_HUMAN 17 135
SEQADV 3OF6 GLY D -3 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ALA D -2 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 HIS D -1 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 MET D 0 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 SER D 120 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 GLY D 121 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP D 122 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP D 123 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP D 124 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP D 125 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 LYS D 126 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 GLY E -3 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ALA E -2 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 HIS E -1 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 MET E 0 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 SER E 120 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 GLY E 121 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP E 122 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP E 123 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP E 124 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP E 125 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 LYS E 126 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 GLY F -3 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ALA F -2 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 HIS F -1 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 MET F 0 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 SER F 120 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 GLY F 121 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP F 122 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP F 123 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP F 124 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 ASP F 125 UNP Q6ISU1 EXPRESSION TAG
SEQADV 3OF6 LYS F 126 UNP Q6ISU1 EXPRESSION TAG
SEQRES 1 A 255 ALA GLY SER HIS MET GLY VAL SER GLN SER PRO ARG TYR
SEQRES 2 A 255 LYS VAL ALA LYS ARG GLY GLN ASP VAL ALA LEU ARG CYS
SEQRES 3 A 255 ASP PRO ILE SER GLY HIS VAL SER LEU PHE TRP TYR GLN
SEQRES 4 A 255 GLN ALA LEU GLY GLN GLY PRO GLU PHE LEU THR TYR PHE
SEQRES 5 A 255 GLN ASN GLU ALA GLN LEU ASP LYS SER GLY LEU PRO SER
SEQRES 6 A 255 ASP ARG PHE PHE ALA GLU ARG PRO GLU GLY SER VAL SER
SEQRES 7 A 255 THR LEU LYS ILE GLN ARG THR GLN GLN GLU ASP SER ALA
SEQRES 8 A 255 VAL TYR LEU CYS ALA SER SER LEU GLY GLN ALA TYR GLU
SEQRES 9 A 255 GLN TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU
SEQRES 10 A 255 ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE
SEQRES 11 A 255 GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA
SEQRES 12 A 255 THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS
SEQRES 13 A 255 VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS
SEQRES 14 A 255 SER GLY VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN
SEQRES 15 A 255 PRO ALA LEU ASN ASP SER ARG TYR CYS LEU SER SER ARG
SEQRES 16 A 255 LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN
SEQRES 17 A 255 HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU
SEQRES 18 A 255 ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR
SEQRES 19 A 255 GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS
SEQRES 20 A 255 THR SER GLY ASP ASP ASP ASP LYS
SEQRES 1 B 255 ALA GLY SER HIS MET GLY VAL SER GLN SER PRO ARG TYR
SEQRES 2 B 255 LYS VAL ALA LYS ARG GLY GLN ASP VAL ALA LEU ARG CYS
SEQRES 3 B 255 ASP PRO ILE SER GLY HIS VAL SER LEU PHE TRP TYR GLN
SEQRES 4 B 255 GLN ALA LEU GLY GLN GLY PRO GLU PHE LEU THR TYR PHE
SEQRES 5 B 255 GLN ASN GLU ALA GLN LEU ASP LYS SER GLY LEU PRO SER
SEQRES 6 B 255 ASP ARG PHE PHE ALA GLU ARG PRO GLU GLY SER VAL SER
SEQRES 7 B 255 THR LEU LYS ILE GLN ARG THR GLN GLN GLU ASP SER ALA
SEQRES 8 B 255 VAL TYR LEU CYS ALA SER SER LEU GLY GLN ALA TYR GLU
SEQRES 9 B 255 GLN TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU
SEQRES 10 B 255 ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE
SEQRES 11 B 255 GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA
SEQRES 12 B 255 THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS
SEQRES 13 B 255 VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS
SEQRES 14 B 255 SER GLY VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN
SEQRES 15 B 255 PRO ALA LEU ASN ASP SER ARG TYR CYS LEU SER SER ARG
SEQRES 16 B 255 LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN
SEQRES 17 B 255 HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU
SEQRES 18 B 255 ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR
SEQRES 19 B 255 GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS
SEQRES 20 B 255 THR SER GLY ASP ASP ASP ASP LYS
SEQRES 1 C 255 ALA GLY SER HIS MET GLY VAL SER GLN SER PRO ARG TYR
SEQRES 2 C 255 LYS VAL ALA LYS ARG GLY GLN ASP VAL ALA LEU ARG CYS
SEQRES 3 C 255 ASP PRO ILE SER GLY HIS VAL SER LEU PHE TRP TYR GLN
SEQRES 4 C 255 GLN ALA LEU GLY GLN GLY PRO GLU PHE LEU THR TYR PHE
SEQRES 5 C 255 GLN ASN GLU ALA GLN LEU ASP LYS SER GLY LEU PRO SER
SEQRES 6 C 255 ASP ARG PHE PHE ALA GLU ARG PRO GLU GLY SER VAL SER
SEQRES 7 C 255 THR LEU LYS ILE GLN ARG THR GLN GLN GLU ASP SER ALA
SEQRES 8 C 255 VAL TYR LEU CYS ALA SER SER LEU GLY GLN ALA TYR GLU
SEQRES 9 C 255 GLN TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU
SEQRES 10 C 255 ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE
SEQRES 11 C 255 GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA
SEQRES 12 C 255 THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS
SEQRES 13 C 255 VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS
SEQRES 14 C 255 SER GLY VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN
SEQRES 15 C 255 PRO ALA LEU ASN ASP SER ARG TYR CYS LEU SER SER ARG
SEQRES 16 C 255 LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN
SEQRES 17 C 255 HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU
SEQRES 18 C 255 ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR
SEQRES 19 C 255 GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS
SEQRES 20 C 255 THR SER GLY ASP ASP ASP ASP LYS
SEQRES 1 D 130 GLY ALA HIS MET LEU PRO THR GLY VAL GLY GLY THR PRO
SEQRES 2 D 130 PHE PRO SER LEU ALA PRO PRO ILE MET LEU LEU VAL ASP
SEQRES 3 D 130 GLY LYS GLN GLN MET VAL VAL VAL CYS LEU VAL LEU ASP
SEQRES 4 D 130 VAL ALA PRO PRO GLY LEU ASP SER PRO ILE TRP PHE SER
SEQRES 5 D 130 ALA GLY ASN GLY SER ALA LEU ASP ALA PHE THR TYR GLY
SEQRES 6 D 130 PRO SER PRO ALA THR ASP GLY THR TRP THR ASN LEU ALA
SEQRES 7 D 130 HIS LEU SER LEU PRO SER GLU GLU LEU ALA SER TRP GLU
SEQRES 8 D 130 PRO LEU VAL CYS HIS THR GLY PRO GLY ALA GLU GLY HIS
SEQRES 9 D 130 SER ARG SER THR GLN PRO MET HIS LEU SER GLY GLU ALA
SEQRES 10 D 130 SER THR ALA ARG THR CYS SER GLY ASP ASP ASP ASP LYS
SEQRES 1 E 130 GLY ALA HIS MET LEU PRO THR GLY VAL GLY GLY THR PRO
SEQRES 2 E 130 PHE PRO SER LEU ALA PRO PRO ILE MET LEU LEU VAL ASP
SEQRES 3 E 130 GLY LYS GLN GLN MET VAL VAL VAL CYS LEU VAL LEU ASP
SEQRES 4 E 130 VAL ALA PRO PRO GLY LEU ASP SER PRO ILE TRP PHE SER
SEQRES 5 E 130 ALA GLY ASN GLY SER ALA LEU ASP ALA PHE THR TYR GLY
SEQRES 6 E 130 PRO SER PRO ALA THR ASP GLY THR TRP THR ASN LEU ALA
SEQRES 7 E 130 HIS LEU SER LEU PRO SER GLU GLU LEU ALA SER TRP GLU
SEQRES 8 E 130 PRO LEU VAL CYS HIS THR GLY PRO GLY ALA GLU GLY HIS
SEQRES 9 E 130 SER ARG SER THR GLN PRO MET HIS LEU SER GLY GLU ALA
SEQRES 10 E 130 SER THR ALA ARG THR CYS SER GLY ASP ASP ASP ASP LYS
SEQRES 1 F 130 GLY ALA HIS MET LEU PRO THR GLY VAL GLY GLY THR PRO
SEQRES 2 F 130 PHE PRO SER LEU ALA PRO PRO ILE MET LEU LEU VAL ASP
SEQRES 3 F 130 GLY LYS GLN GLN MET VAL VAL VAL CYS LEU VAL LEU ASP
SEQRES 4 F 130 VAL ALA PRO PRO GLY LEU ASP SER PRO ILE TRP PHE SER
SEQRES 5 F 130 ALA GLY ASN GLY SER ALA LEU ASP ALA PHE THR TYR GLY
SEQRES 6 F 130 PRO SER PRO ALA THR ASP GLY THR TRP THR ASN LEU ALA
SEQRES 7 F 130 HIS LEU SER LEU PRO SER GLU GLU LEU ALA SER TRP GLU
SEQRES 8 F 130 PRO LEU VAL CYS HIS THR GLY PRO GLY ALA GLU GLY HIS
SEQRES 9 F 130 SER ARG SER THR GLN PRO MET HIS LEU SER GLY GLU ALA
SEQRES 10 F 130 SER THR ALA ARG THR CYS SER GLY ASP ASP ASP ASP LYS
MODRES 3OF6 ASN F 51 ASN GLYCOSYLATION SITE
MODRES 3OF6 ASN E 51 ASN GLYCOSYLATION SITE
MODRES 3OF6 ASN C 187 ASN GLYCOSYLATION SITE
MODRES 3OF6 ASN D 51 ASN GLYCOSYLATION SITE
HET NAG C1000 14
HET NAG D1000 14
HET NAG E1000 14
HET NAG F1000 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 7 NAG 4(C8 H15 N O6)
FORMUL 11 HOH *109(H2 O)
HELIX 1 1 GLN A 83 SER A 87 5 5
HELIX 2 2 ASP A 119 VAL A 123 5 5
HELIX 3 3 SER A 134 GLN A 142 1 9
HELIX 4 4 ALA A 201 GLN A 205 1 5
HELIX 5 5 GLN B 83 SER B 87 5 5
HELIX 6 6 ASP B 119 VAL B 123 5 5
HELIX 7 7 SER B 134 GLN B 142 1 9
HELIX 8 8 ALA B 201 GLN B 205 1 5
HELIX 9 9 GLN C 83 SER C 87 5 5
HELIX 10 10 ASP C 119 VAL C 123 5 5
HELIX 11 11 SER C 134 SER C 139 1 6
HELIX 12 12 ALA C 201 GLN C 205 1 5
HELIX 13 13 GLU D 81 SER D 85 5 5
HELIX 14 14 LEU E 83 GLU E 87 5 5
HELIX 15 15 GLU F 82 TRP F 86 5 5
SHEET 1 A 4 SER A 5 SER A 7 0
SHEET 2 A 4 VAL A 19 ASP A 24 -1 O ASP A 24 N SER A 5
SHEET 3 A 4 SER A 75 ILE A 79 -1 O LEU A 77 N LEU A 21
SHEET 4 A 4 PHE A 65 GLU A 68 -1 N PHE A 66 O LYS A 78
SHEET 1 B 6 TYR A 10 LYS A 14 0
SHEET 2 B 6 THR A 112 THR A 117 1 O ARG A 113 N LYS A 11
SHEET 3 B 6 VAL A 89 SER A 95 -1 N TYR A 90 O THR A 112
SHEET 4 B 6 SER A 31 GLN A 37 -1 N PHE A 33 O ALA A 93
SHEET 5 B 6 GLU A 44 GLN A 50 -1 O PHE A 49 N LEU A 32
SHEET 6 B 6 GLN A 54 ASP A 56 -1 O ASP A 56 N TYR A 48
SHEET 1 C 4 TYR A 10 LYS A 14 0
SHEET 2 C 4 THR A 112 THR A 117 1 O ARG A 113 N LYS A 11
SHEET 3 C 4 VAL A 89 SER A 95 -1 N TYR A 90 O THR A 112
SHEET 4 C 4 TYR A 107 PHE A 108 -1 O TYR A 107 N SER A 94
SHEET 1 D 4 GLU A 127 PHE A 131 0
SHEET 2 D 4 LYS A 143 PHE A 153 -1 O VAL A 147 N PHE A 131
SHEET 3 D 4 TYR A 191 SER A 200 -1 O VAL A 199 N ALA A 144
SHEET 4 D 4 VAL A 173 THR A 175 -1 N SER A 174 O ARG A 196
SHEET 1 E 4 GLU A 127 PHE A 131 0
SHEET 2 E 4 LYS A 143 PHE A 153 -1 O VAL A 147 N PHE A 131
SHEET 3 E 4 TYR A 191 SER A 200 -1 O VAL A 199 N ALA A 144
SHEET 4 E 4 LEU A 180 LYS A 181 -1 N LEU A 180 O CYS A 192
SHEET 1 F 4 LYS A 167 VAL A 169 0
SHEET 2 F 4 VAL A 158 VAL A 164 -1 N TRP A 162 O VAL A 169
SHEET 3 F 4 HIS A 210 PHE A 217 -1 O GLN A 214 N SER A 161
SHEET 4 F 4 GLN A 236 TRP A 243 -1 O ALA A 240 N CYS A 213
SHEET 1 G 4 SER B 5 SER B 7 0
SHEET 2 G 4 VAL B 19 ASP B 24 -1 O ASP B 24 N SER B 5
SHEET 3 G 4 SER B 75 ILE B 79 -1 O LEU B 77 N LEU B 21
SHEET 4 G 4 PHE B 65 GLU B 68 -1 N PHE B 66 O LYS B 78
SHEET 1 H 6 TYR B 10 LYS B 11 0
SHEET 2 H 6 THR B 112 LEU B 114 1 O ARG B 113 N LYS B 11
SHEET 3 H 6 ALA B 88 LEU B 91 -1 N ALA B 88 O LEU B 114
SHEET 4 H 6 SER B 31 GLN B 37 -1 N TYR B 35 O LEU B 91
SHEET 5 H 6 GLU B 44 GLN B 50 -1 O PHE B 49 N LEU B 32
SHEET 6 H 6 GLN B 54 ASP B 56 -1 O LEU B 55 N TYR B 48
SHEET 1 I 4 GLU B 127 PHE B 131 0
SHEET 2 I 4 LYS B 143 PHE B 153 -1 O THR B 151 N GLU B 127
SHEET 3 I 4 TYR B 191 SER B 200 -1 O VAL B 199 N ALA B 144
SHEET 4 I 4 VAL B 173 THR B 175 -1 N SER B 174 O ARG B 196
SHEET 1 J 4 GLU B 127 PHE B 131 0
SHEET 2 J 4 LYS B 143 PHE B 153 -1 O THR B 151 N GLU B 127
SHEET 3 J 4 TYR B 191 SER B 200 -1 O VAL B 199 N ALA B 144
SHEET 4 J 4 LEU B 180 LYS B 181 -1 N LEU B 180 O CYS B 192
SHEET 1 K 4 LYS B 167 VAL B 169 0
SHEET 2 K 4 VAL B 158 VAL B 164 -1 N VAL B 164 O LYS B 167
SHEET 3 K 4 PHE B 211 PHE B 217 -1 O GLN B 214 N SER B 161
SHEET 4 K 4 ILE B 237 GLU B 241 -1 O ALA B 240 N CYS B 213
SHEET 1 L 4 SER C 5 SER C 7 0
SHEET 2 L 4 VAL C 19 ASP C 24 -1 O ASP C 24 N SER C 5
SHEET 3 L 4 SER C 75 ILE C 79 -1 O LEU C 77 N LEU C 21
SHEET 4 L 4 PHE C 65 GLU C 68 -1 N GLU C 68 O THR C 76
SHEET 1 M 5 TYR C 10 LYS C 14 0
SHEET 2 M 5 THR C 112 THR C 117 1 O ARG C 113 N LYS C 11
SHEET 3 M 5 VAL C 89 SER C 95 -1 N TYR C 90 O THR C 112
SHEET 4 M 5 SER C 31 GLN C 37 -1 N GLN C 37 O VAL C 89
SHEET 5 M 5 GLU C 44 GLN C 50 -1 O GLU C 44 N GLN C 36
SHEET 1 N 4 TYR C 10 LYS C 14 0
SHEET 2 N 4 THR C 112 THR C 117 1 O ARG C 113 N LYS C 11
SHEET 3 N 4 VAL C 89 SER C 95 -1 N TYR C 90 O THR C 112
SHEET 4 N 4 TYR C 107 PHE C 108 -1 O TYR C 107 N SER C 94
SHEET 1 O 4 GLU C 127 PHE C 131 0
SHEET 2 O 4 LYS C 143 PHE C 153 -1 O VAL C 147 N PHE C 131
SHEET 3 O 4 TYR C 191 SER C 200 -1 O VAL C 199 N ALA C 144
SHEET 4 O 4 VAL C 173 THR C 175 -1 N SER C 174 O ARG C 196
SHEET 1 P 4 GLU C 127 PHE C 131 0
SHEET 2 P 4 LYS C 143 PHE C 153 -1 O VAL C 147 N PHE C 131
SHEET 3 P 4 TYR C 191 SER C 200 -1 O VAL C 199 N ALA C 144
SHEET 4 P 4 LEU C 180 LYS C 181 -1 N LEU C 180 O CYS C 192
SHEET 1 Q 4 LYS C 167 GLU C 168 0
SHEET 2 Q 4 VAL C 158 VAL C 164 -1 N VAL C 164 O LYS C 167
SHEET 3 Q 4 HIS C 210 PHE C 217 -1 O GLN C 214 N SER C 161
SHEET 4 Q 4 ILE C 237 TRP C 243 -1 O ALA C 240 N CYS C 213
SHEET 1 R 4 ILE D 17 LEU D 20 0
SHEET 2 R 4 GLN D 25 VAL D 36 -1 O GLN D 26 N LEU D 19
SHEET 3 R 4 THR D 69 PRO D 79 -1 O LEU D 76 N VAL D 29
SHEET 4 R 4 PHE D 58 THR D 59 -1 N PHE D 58 O HIS D 75
SHEET 1 S 4 ILE D 17 LEU D 20 0
SHEET 2 S 4 GLN D 25 VAL D 36 -1 O GLN D 26 N LEU D 19
SHEET 3 S 4 THR D 69 PRO D 79 -1 O LEU D 76 N VAL D 29
SHEET 4 S 4 SER D 63 ALA D 65 -1 N ALA D 65 O THR D 69
SHEET 1 T 4 ALA D 54 LEU D 55 0
SHEET 2 T 4 TRP D 46 SER D 48 -1 N PHE D 47 O LEU D 55
SHEET 3 T 4 VAL D 90 THR D 93 -1 O VAL D 90 N SER D 48
SHEET 4 T 4 ARG D 102 SER D 103 -1 O ARG D 102 N THR D 93
SHEET 1 U 4 ILE E 17 LEU E 20 0
SHEET 2 U 4 GLN E 25 VAL E 36 -1 O GLN E 26 N LEU E 19
SHEET 3 U 4 TRP E 70 PRO E 79 -1 O LEU E 78 N MET E 27
SHEET 4 U 4 PHE E 58 THR E 59 -1 N PHE E 58 O HIS E 75
SHEET 1 V 4 ILE E 17 LEU E 20 0
SHEET 2 V 4 GLN E 25 VAL E 36 -1 O GLN E 26 N LEU E 19
SHEET 3 V 4 TRP E 70 PRO E 79 -1 O LEU E 78 N MET E 27
SHEET 4 V 4 SER E 63 PRO E 64 -1 N SER E 63 O THR E 71
SHEET 1 W 4 ALA E 54 LEU E 55 0
SHEET 2 W 4 TRP E 46 ALA E 49 -1 N PHE E 47 O LEU E 55
SHEET 3 W 4 LEU E 89 THR E 93 -1 O VAL E 90 N SER E 48
SHEET 4 W 4 ARG E 102 SER E 103 -1 O ARG E 102 N THR E 93
SHEET 1 X 4 LEU F 13 LEU F 20 0
SHEET 2 X 4 GLN F 25 VAL F 36 -1 O GLN F 26 N LEU F 19
SHEET 3 X 4 TRP F 70 PRO F 79 -1 O LEU F 78 N MET F 27
SHEET 4 X 4 PHE F 58 THR F 59 -1 N PHE F 58 O HIS F 75
SHEET 1 Y 4 LEU F 13 LEU F 20 0
SHEET 2 Y 4 GLN F 25 VAL F 36 -1 O GLN F 26 N LEU F 19
SHEET 3 Y 4 TRP F 70 PRO F 79 -1 O LEU F 78 N MET F 27
SHEET 4 Y 4 SER F 63 PRO F 64 -1 N SER F 63 O THR F 71
SHEET 1 Z 4 ALA F 54 LEU F 55 0
SHEET 2 Z 4 TRP F 46 SER F 48 -1 N PHE F 47 O LEU F 55
SHEET 3 Z 4 VAL F 90 THR F 93 -1 O VAL F 90 N SER F 48
SHEET 4 Z 4 ARG F 102 SER F 103 -1 O ARG F 102 N THR F 93
SSBOND 1 CYS A 23 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 148 CYS A 213 1555 1555 2.03
SSBOND 3 CYS B 23 CYS B 92 1555 1555 2.03
SSBOND 4 CYS B 148 CYS B 213 1555 1555 2.03
SSBOND 5 CYS C 23 CYS C 92 1555 1555 2.03
SSBOND 6 CYS C 148 CYS C 213 1555 1555 2.03
SSBOND 7 CYS D 31 CYS D 91 1555 1555 2.03
SSBOND 8 CYS E 31 CYS E 91 1555 1555 2.03
SSBOND 9 CYS F 31 CYS F 91 1555 1555 2.03
LINK ND2 ASN C 187 C1 NAG C1000 1555 1555 1.44
LINK ND2 ASN D 51 C1 NAG D1000 1555 1555 1.44
LINK ND2 ASN E 51 C1 NAG E1000 1555 1555 1.44
LINK ND2 ASN F 51 C1 NAG F1000 1555 1555 1.44
CISPEP 1 MET A 2 GLY A 3 0 0.05
CISPEP 2 SER A 7 PRO A 8 0 -2.10
CISPEP 3 TYR A 154 PRO A 155 0 -1.67
CISPEP 4 GLY B 3 VAL B 4 0 0.44
CISPEP 5 SER B 7 PRO B 8 0 -2.59
CISPEP 6 TYR B 154 PRO B 155 0 -2.35
CISPEP 7 SER C 7 PRO C 8 0 -2.65
CISPEP 8 TYR C 154 PRO C 155 0 -2.73
CISPEP 9 GLU D 87 PRO D 88 0 -3.78
CISPEP 10 GLY D 94 PRO D 95 0 -0.05
CISPEP 11 PRO E 39 GLY E 40 0 5.66
CISPEP 12 GLU E 87 PRO E 88 0 -2.98
CISPEP 13 GLY E 94 PRO E 95 0 -0.45
CISPEP 14 LEU E 109 SER E 110 0 0.03
CISPEP 15 PRO F 39 GLY F 40 0 -2.21
CISPEP 16 GLU F 87 PRO F 88 0 -3.39
CISPEP 17 GLY F 94 PRO F 95 0 -1.84
CRYST1 114.902 114.902 183.101 90.00 90.00 120.00 P 32 2 1 18
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 0.008703 0.005025 0.000000 0.00000
SCALE2 0.000000 0.010049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005461 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
