HEADER IMMUNE SYSTEM 10-NOV-14 4WW2
TITLE CRYSTAL STRUCTURE OF HUMAN TCR ALPHA CHAIN-TRAV21-TRAJ8, BETA CHAIN-
TITLE 2 TRBV7-8, ANTIGEN-PRESENTING GLYCOPROTEIN CD1D, AND BETA-2-
TITLE 3 MICROGLOBULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TCR ALPHA CHAIN-TRAV21-TRAJ8;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TCR BETA CHAIN-TRBV7-8;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ANTIGEN-PRESENTING GLYCOPROTEIN CD1D;
COMPND 11 CHAIN: C;
COMPND 12 SYNONYM: R3G1;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 16 CHAIN: F;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PET30;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 GENE: CD1D;
SOURCE 19 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL;
SOURCE 23 MOL_ID: 4;
SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 25 ORGANISM_COMMON: HUMAN;
SOURCE 26 ORGANISM_TAXID: 9606;
SOURCE 27 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 28 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 31 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL
KEYWDS NATURAL KILLER T CELLS, IMMUNITY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LE NOURS,T.PRAVEENA,D.PELLICCI,N.A.GHERARDIN,R.T.LIM,G.BESRA,
AUTHOR 2 S.KESHIPEDDY,S.K.RICHARDSON,A.R.HOWELL,S.GRAS,D.I.GODFREY,
AUTHOR 3 J.ROSSJOHN,A.P.ULDRICH
REVDAT 4 27-SEP-23 4WW2 1 REMARK HETSYN
REVDAT 3 29-JUL-20 4WW2 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 04-APR-18 4WW2 1 JRNL REMARK
REVDAT 1 03-FEB-16 4WW2 0
JRNL AUTH J.LE NOURS,T.PRAVEENA,D.G.PELLICCI,N.A.GHERARDIN,F.J.ROSS,
JRNL AUTH 2 R.T.LIM,G.S.BESRA,S.KESHIPEDDY,S.K.RICHARDSON,A.R.HOWELL,
JRNL AUTH 3 S.GRAS,D.I.GODFREY,J.ROSSJOHN,A.P.ULDRICH
JRNL TITL ATYPICAL NATURAL KILLER T-CELL RECEPTOR RECOGNITION OF
JRNL TITL 2 CD1D-LIPID ANTIGENS.
JRNL REF NAT COMMUN V. 7 10570 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 26875526
JRNL DOI 10.1038/NCOMMS10570
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 36324
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1815
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 18
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.26
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2818
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2502
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2640
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE : 0.2957
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.32
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 178
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6262
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.78
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.78900
REMARK 3 B22 (A**2) : -1.68180
REMARK 3 B33 (A**2) : 0.89290
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.27640
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.394
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.382
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.252
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.390
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.257
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6550 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8938 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2935 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 149 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 967 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6550 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 856 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 7043 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.02
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.79
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4937 -12.4426 -21.8917
REMARK 3 T TENSOR
REMARK 3 T11: -0.0058 T22: -0.2332
REMARK 3 T33: -0.0472 T12: -0.1200
REMARK 3 T13: -0.0195 T23: 0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 3.7317 L22: 0.3933
REMARK 3 L33: 3.4043 L12: -1.0246
REMARK 3 L13: -0.8893 L23: 0.3662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: 0.4005 S13: 0.1274
REMARK 3 S21: -0.1331 S22: -0.1257 S23: 0.1467
REMARK 3 S31: -0.0869 S32: -0.1963 S33: 0.0896
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 45.1080 -23.2759 -10.1966
REMARK 3 T TENSOR
REMARK 3 T11: -0.0627 T22: -0.2445
REMARK 3 T33: -0.0668 T12: -0.0002
REMARK 3 T13: -0.0273 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 2.8926 L22: 0.3815
REMARK 3 L33: 1.2869 L12: -0.6514
REMARK 3 L13: 0.0930 L23: 0.6486
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: -0.1155 S13: -0.0482
REMARK 3 S21: -0.0139 S22: 0.0142 S23: 0.1315
REMARK 3 S31: -0.0617 S32: 0.1153 S33: -0.0076
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2486 -8.4163 28.3926
REMARK 3 T TENSOR
REMARK 3 T11: -0.1995 T22: 0.3327
REMARK 3 T33: -0.2529 T12: 0.0640
REMARK 3 T13: -0.0030 T23: -0.1033
REMARK 3 L TENSOR
REMARK 3 L11: 2.3500 L22: 0.5059
REMARK 3 L33: 1.0243 L12: 0.3331
REMARK 3 L13: -1.6509 L23: -0.0860
REMARK 3 S TENSOR
REMARK 3 S11: 0.1244 S12: -0.7251 S13: -0.0354
REMARK 3 S21: 0.1489 S22: 0.0011 S23: -0.0952
REMARK 3 S31: 0.0263 S32: 0.4356 S33: -0.1254
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { F|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1366 -17.7016 45.2713
REMARK 3 T TENSOR
REMARK 3 T11: -0.4008 T22: 0.5687
REMARK 3 T33: -0.3020 T12: 0.0763
REMARK 3 T13: -0.1929 T23: 0.2278
REMARK 3 L TENSOR
REMARK 3 L11: -0.1552 L22: 3.7144
REMARK 3 L33: 5.3132 L12: 0.5759
REMARK 3 L13: -1.1966 L23: -2.1809
REMARK 3 S TENSOR
REMARK 3 S11: 0.2735 S12: -0.4411 S13: -0.7165
REMARK 3 S21: 0.4686 S22: 0.2382 S23: -0.3048
REMARK 3 S31: 0.5380 S32: 0.2459 S33: -0.5116
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.7108
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36324
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 44.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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 2PO6, 4WW1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9-10% PEG 6K 0.1M MES 6.0 4% ETHYLENE
REMARK 280 GLYCOL, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 104.99500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 104.99500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.15000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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, 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 PRO A 217
REMARK 465 GLU A 218
REMARK 465 SER A 219
REMARK 465 SER A 220
REMARK 465 SER C 0
REMARK 465 PRO C 1
REMARK 465 GLY C 2
REMARK 465 HIS C 278
REMARK 465 HIS C 279
REMARK 465 HIS C 280
REMARK 465 HIS C 281
REMARK 465 HIS C 282
REMARK 465 HIS C 283
REMARK 465 ILE F 1
REMARK 465 ASP F 98
REMARK 465 MET F 99
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 61 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 130 CG OD1 ND2
REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2
REMARK 470 SER A 144 OG
REMARK 470 ASP A 145 CG OD1 OD2
REMARK 470 LYS A 146 CG CD CE NZ
REMARK 470 GLN A 157 CG CD OE1 NE2
REMARK 470 GLN A 162 CG CD OE1 NE2
REMARK 470 LYS A 164 CG CD CE NZ
REMARK 470 ASP A 165 CG OD1 OD2
REMARK 470 SER A 166 OG
REMARK 470 ASP A 167 CG OD1 OD2
REMARK 470 ASP A 172 CG OD1 OD2
REMARK 470 SER A 195 OG
REMARK 470 ASN A 201 CG OD1 ND2
REMARK 470 ASN A 205 CG OD1 ND2
REMARK 470 GLU A 210 CG CD OE1 OE2
REMARK 470 GLN B 17 CG CD OE1 NE2
REMARK 470 ASN B 194 CG OD1 ND2
REMARK 470 ASP B 195 CG OD1 OD2
REMARK 470 GLU B 229 CG CD OE1 OE2
REMARK 470 SER C 22 OG
REMARK 470 LYS C 86 CG CD CE NZ
REMARK 470 LYS C 121 CG CD CE NZ
REMARK 470 GLN C 135 CG CD OE1 NE2
REMARK 470 GLU C 136 CG CD OE1 OE2
REMARK 470 LEU C 139 CG CD1 CD2
REMARK 470 GLN C 146 CG CD OE1 NE2
REMARK 470 LYS C 152 CG CD CE NZ
REMARK 470 GLN C 225 CG CD OE1 NE2
REMARK 470 GLN C 228 CG CD OE1 NE2
REMARK 470 GLN C 231 CG CD OE1 NE2
REMARK 470 VAL C 252 CG1 CG2
REMARK 470 GLU C 255 CG CD OE1 OE2
REMARK 470 ARG F 3 CG CD NE CZ NH1 NH2
REMARK 470 VAL F 9 CG1 CG2
REMARK 470 GLU F 16 CG CD OE1 OE2
REMARK 470 ASN F 17 CG OD1 ND2
REMARK 470 LYS F 19 CG CD CE NZ
REMARK 470 SER F 20 OG
REMARK 470 LEU F 23 CG CD1 CD2
REMARK 470 SER F 33 OG
REMARK 470 ASP F 34 CG OD1 OD2
REMARK 470 GLU F 36 CG CD OE1 OE2
REMARK 470 VAL F 37 CG1 CG2
REMARK 470 ASP F 38 CG OD1 OD2
REMARK 470 LEU F 39 CG CD1 CD2
REMARK 470 LEU F 40 CG CD1 CD2
REMARK 470 LYS F 41 CG CD CE NZ
REMARK 470 ASN F 42 CG OD1 ND2
REMARK 470 GLU F 44 CG CD OE1 OE2
REMARK 470 ARG F 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE F 46 CG1 CG2 CD1
REMARK 470 GLU F 47 CG CD OE1 OE2
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 VAL F 49 CG1 CG2
REMARK 470 THR F 73 OG1 CG2
REMARK 470 GLU F 74 CG CD OE1 OE2
REMARK 470 LYS F 75 CG CD CE NZ
REMARK 470 ASP F 76 CG OD1 OD2
REMARK 470 GLU F 77 CG CD OE1 OE2
REMARK 470 ARG F 81 CG CD NE CZ NH1 NH2
REMARK 470 VAL F 82 CG1 CG2
REMARK 470 ASN F 83 CG OD1 ND2
REMARK 470 VAL F 85 CG1 CG2
REMARK 470 GLN F 89 CG CD OE1 NE2
REMARK 470 ILE F 92 CG1 CG2 CD1
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 ARG F 97 CG CD NE CZ NH1 NH2
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 ARG B 252 NE CZ NH1 NH2
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 LEU A 53 -62.16 -104.07
REMARK 500 SER A 68 104.82 -172.96
REMARK 500 ALA A 93 59.54 32.45
REMARK 500 SER A 99 106.95 -49.23
REMARK 500 ALA A 100 -175.21 -170.64
REMARK 500 ASP A 132 58.71 -142.85
REMARK 500 ASP A 182 -18.78 77.82
REMARK 500 ASP A 211 30.14 -96.73
REMARK 500 ALA B 2 62.05 -115.09
REMARK 500 LEU B 53 -64.78 -104.78
REMARK 500 ASN B 58 -127.34 63.32
REMARK 500 ARG B 80 74.53 -160.85
REMARK 500 SER B 85 -97.44 -125.64
REMARK 500 SER B 85 -99.18 -125.64
REMARK 500 SER B 108 -155.39 -89.09
REMARK 500 HIS B 164 70.44 -119.73
REMARK 500 ALA B 192 45.55 -91.91
REMARK 500 TRP F 60 -0.71 78.91
REMARK 500 PRO F 72 94.06 -66.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WW1 RELATED DB: PDB
REMARK 900 CONTAINS THE SAME T CELL RECEPTOR
DBREF 4WW2 A 0 220 PDB 4WW2 4WW2 0 220
DBREF 4WW2 B 0 254 PDB 4WW2 4WW2 0 254
DBREF 4WW2 C 3 277 UNP P15813 CD1D_HUMAN 21 295
DBREF 4WW2 F 1 99 UNP P61769 B2MG_HUMAN 21 119
SEQADV 4WW2 SER C 0 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 PRO C 1 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 GLY C 2 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 HIS C 278 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 HIS C 279 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 HIS C 280 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 HIS C 281 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 HIS C 282 UNP P15813 EXPRESSION TAG
SEQADV 4WW2 HIS C 283 UNP P15813 EXPRESSION TAG
SEQRES 1 A 207 MET LYS GLN GLU VAL THR GLN ILE PRO ALA ALA LEU SER
SEQRES 2 A 207 VAL PRO GLU GLY GLU ASN LEU VAL LEU ASN CYS SER PHE
SEQRES 3 A 207 THR ASP SER ALA ILE TYR ASN LEU GLN TRP PHE ARG GLN
SEQRES 4 A 207 ASP PRO GLY LYS GLY LEU THR SER LEU LEU LEU ILE GLN
SEQRES 5 A 207 SER SER GLN ARG GLU GLN THR SER GLY ARG LEU ASN ALA
SEQRES 6 A 207 SER LEU ASP LYS SER SER GLY ARG SER THR LEU TYR ILE
SEQRES 7 A 207 ALA ALA SER GLN PRO GLY ASP SER ALA THR TYR LEU CYS
SEQRES 8 A 207 ALA GLY VAL ASN THR GLY PHE GLN LYS LEU VAL PHE GLY
SEQRES 9 A 207 THR GLY THR ARG LEU LEU VAL SER PRO ASN ILE GLN ASN
SEQRES 10 A 207 PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER
SEQRES 11 A 207 SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER
SEQRES 12 A 207 GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR
SEQRES 13 A 207 ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER MET ASP
SEQRES 14 A 207 PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS SER
SEQRES 15 A 207 ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE
SEQRES 16 A 207 PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 B 243 MET GLY ALA GLY VAL SER GLN SER PRO ARG TYR LYS VAL
SEQRES 2 B 243 ALA LYS ARG GLY GLN ASP VAL ALA LEU ARG CYS ASP PRO
SEQRES 3 B 243 ILE SER GLY HIS VAL SER LEU PHE TRP TYR GLN GLN ALA
SEQRES 4 B 243 LEU GLY GLN GLY PRO GLU PHE LEU THR TYR PHE GLN ASN
SEQRES 5 B 243 GLU ALA GLN LEU ASP LYS SER GLY LEU PRO SER ASP ARG
SEQRES 6 B 243 PHE PHE ALA GLU ARG PRO GLU GLY SER VAL SER THR LEU
SEQRES 7 B 243 LYS ILE GLN ARG THR GLN GLN GLU ASP SER ALA VAL TYR
SEQRES 8 B 243 LEU CYS ALA SER SER SER ARG ASP LEU GLU GLN TYR PHE
SEQRES 9 B 243 GLY PRO GLY THR ARG LEU THR VAL THR GLU ASP LEU LYS
SEQRES 10 B 243 ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER
SEQRES 11 B 243 GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL
SEQRES 12 B 243 CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU
SEQRES 13 B 243 SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL
SEQRES 14 B 243 CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU
SEQRES 15 B 243 ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL
SEQRES 16 B 243 SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG
SEQRES 17 B 243 CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU
SEQRES 18 B 243 TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL
SEQRES 19 B 243 SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 C 284 SER PRO GLY VAL PRO GLN ARG LEU PHE PRO LEU ARG CYS
SEQRES 2 C 284 LEU GLN ILE SER SER PHE ALA ASN SER SER TRP THR ARG
SEQRES 3 C 284 THR ASP GLY LEU ALA TRP LEU GLY GLU LEU GLN THR HIS
SEQRES 4 C 284 SER TRP SER ASN ASP SER ASP THR VAL ARG SER LEU LYS
SEQRES 5 C 284 PRO TRP SER GLN GLY THR PHE SER ASP GLN GLN TRP GLU
SEQRES 6 C 284 THR LEU GLN HIS ILE PHE ARG VAL TYR ARG SER SER PHE
SEQRES 7 C 284 THR ARG ASP VAL LYS GLU PHE ALA LYS MET LEU ARG LEU
SEQRES 8 C 284 SER TYR PRO LEU GLU LEU GLN VAL SER ALA GLY CYS GLU
SEQRES 9 C 284 VAL HIS PRO GLY ASN ALA SER ASN ASN PHE PHE HIS VAL
SEQRES 10 C 284 ALA PHE GLN GLY LYS ASP ILE LEU SER PHE GLN GLY THR
SEQRES 11 C 284 SER TRP GLU PRO THR GLN GLU ALA PRO LEU TRP VAL ASN
SEQRES 12 C 284 LEU ALA ILE GLN VAL LEU ASN GLN ASP LYS TRP THR ARG
SEQRES 13 C 284 GLU THR VAL GLN TRP LEU LEU ASN GLY THR CYS PRO GLN
SEQRES 14 C 284 PHE VAL SER GLY LEU LEU GLU SER GLY LYS SER GLU LEU
SEQRES 15 C 284 LYS LYS GLN VAL LYS PRO LYS ALA TRP LEU SER ARG GLY
SEQRES 16 C 284 PRO SER PRO GLY PRO GLY ARG LEU LEU LEU VAL CYS HIS
SEQRES 17 C 284 VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL LYS TRP
SEQRES 18 C 284 MET ARG GLY GLU GLN GLU GLN GLN GLY THR GLN PRO GLY
SEQRES 19 C 284 ASP ILE LEU PRO ASN ALA ASP GLU THR TRP TYR LEU ARG
SEQRES 20 C 284 ALA THR LEU ASP VAL VAL ALA GLY GLU ALA ALA GLY LEU
SEQRES 21 C 284 SER CYS ARG VAL LYS HIS SER SER LEU GLU GLY GLN ASP
SEQRES 22 C 284 ILE VAL LEU TYR TRP HIS HIS HIS HIS HIS HIS
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
HET NAG C 301 14
HET NAG C 302 14
HET JLS C 303 58
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM JLS (15Z)-N-[(2S,3S,4R)-1-(ALPHA-D-GALACTOPYRANOSYLOXY)-3,
HETNAM 2 JLS 4-DIHYDROXYOCTADECAN-2-YL]TETRACOS-15-ENAMIDE
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
HETSYN JLS PBS-44
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 7 JLS C48 H93 N O9
FORMUL 8 HOH *170(H2 O)
HELIX 1 AA1 GLN A 95 SER A 99 5 5
HELIX 2 AA2 GLN B 95 SER B 99 5 5
HELIX 3 AA3 ASP B 126 VAL B 130 5 5
HELIX 4 AA4 SER B 141 GLN B 149 1 9
HELIX 5 AA5 ALA B 208 ASN B 213 1 6
HELIX 6 AA6 SER C 59 LEU C 88 1 30
HELIX 7 AA7 PRO C 138 ASN C 149 1 12
HELIX 8 AA8 ASP C 151 GLY C 164 1 14
HELIX 9 AA9 GLY C 164 GLY C 177 1 14
HELIX 10 AB1 GLY C 177 LYS C 182 1 6
HELIX 11 AB2 HIS C 265 GLU C 269 5 5
SHEET 1 AA1 5 VAL A 4 ILE A 7 0
SHEET 2 AA1 5 LEU A 19 PHE A 25 -1 O SER A 24 N THR A 5
SHEET 3 AA1 5 ARG A 86 ILE A 91 -1 O LEU A 89 N LEU A 21
SHEET 4 AA1 5 LEU A 76 ASP A 81 -1 N ASN A 77 O TYR A 90
SHEET 5 AA1 5 GLU A 62 SER A 68 -1 N GLN A 66 O ALA A 78
SHEET 1 AA2 5 ALA A 10 PRO A 14 0
SHEET 2 AA2 5 THR A 120 SER A 125 1 O LEU A 123 N LEU A 11
SHEET 3 AA2 5 ALA A 100 ASN A 108 -1 N ALA A 100 O LEU A 122
SHEET 4 AA2 5 ILE A 30 GLN A 44 -1 N TYR A 31 O VAL A 107
SHEET 5 AA2 5 LEU A 50 GLN A 57 -1 O THR A 51 N ARG A 43
SHEET 1 AA3 4 ALA A 10 PRO A 14 0
SHEET 2 AA3 4 THR A 120 SER A 125 1 O LEU A 123 N LEU A 11
SHEET 3 AA3 4 ALA A 100 ASN A 108 -1 N ALA A 100 O LEU A 122
SHEET 4 AA3 4 VAL A 115 PHE A 116 -1 O VAL A 115 N GLY A 106
SHEET 1 AA4 4 ALA A 134 ARG A 139 0
SHEET 2 AA4 4 SER A 147 THR A 152 -1 O LEU A 150 N TYR A 136
SHEET 3 AA4 4 LYS A 184 SER A 192 -1 O ALA A 190 N CYS A 149
SHEET 4 AA4 4 VAL A 168 ILE A 170 -1 N TYR A 169 O TRP A 191
SHEET 1 AA5 4 ALA A 134 ARG A 139 0
SHEET 2 AA5 4 SER A 147 THR A 152 -1 O LEU A 150 N TYR A 136
SHEET 3 AA5 4 LYS A 184 SER A 192 -1 O ALA A 190 N CYS A 149
SHEET 4 AA5 4 CYS A 174 ASP A 177 -1 N LEU A 176 O SER A 185
SHEET 1 AA6 4 SER B 5 SER B 7 0
SHEET 2 AA6 4 VAL B 19 ASP B 24 -1 O ARG B 22 N SER B 7
SHEET 3 AA6 4 SER B 87 ILE B 91 -1 O LEU B 89 N LEU B 21
SHEET 4 AA6 4 PHE B 76 GLU B 79 -1 N PHE B 77 O LYS B 90
SHEET 1 AA7 6 TYR B 10 LYS B 14 0
SHEET 2 AA7 6 THR B 119 THR B 124 1 O THR B 124 N ALA B 13
SHEET 3 AA7 6 ALA B 100 SER B 107 -1 N ALA B 100 O LEU B 121
SHEET 4 AA7 6 SER B 31 GLN B 44 -1 N TYR B 42 O LEU B 103
SHEET 5 AA7 6 GLU B 51 GLN B 57 -1 O LEU B 53 N TRP B 41
SHEET 6 AA7 6 ALA B 60 ASP B 67 -1 O ASP B 67 N TYR B 55
SHEET 1 AA8 4 TYR B 10 LYS B 14 0
SHEET 2 AA8 4 THR B 119 THR B 124 1 O THR B 124 N ALA B 13
SHEET 3 AA8 4 ALA B 100 SER B 107 -1 N ALA B 100 O LEU B 121
SHEET 4 AA8 4 TYR B 114 PHE B 115 -1 O TYR B 114 N SER B 106
SHEET 1 AA9 4 GLU B 134 PHE B 138 0
SHEET 2 AA9 4 LYS B 150 PHE B 160 -1 O VAL B 154 N PHE B 138
SHEET 3 AA9 4 TYR B 198 SER B 207 -1 O VAL B 206 N ALA B 151
SHEET 4 AA9 4 VAL B 180 THR B 182 -1 N CYS B 181 O ARG B 203
SHEET 1 AB1 4 GLU B 134 PHE B 138 0
SHEET 2 AB1 4 LYS B 150 PHE B 160 -1 O VAL B 154 N PHE B 138
SHEET 3 AB1 4 TYR B 198 SER B 207 -1 O VAL B 206 N ALA B 151
SHEET 4 AB1 4 LEU B 187 LYS B 188 -1 N LEU B 187 O ALA B 199
SHEET 1 AB2 4 LYS B 174 VAL B 176 0
SHEET 2 AB2 4 VAL B 165 VAL B 171 -1 N VAL B 171 O LYS B 174
SHEET 3 AB2 4 HIS B 217 PHE B 224 -1 O ARG B 219 N TRP B 170
SHEET 4 AB2 4 GLN B 243 TRP B 250 -1 O GLN B 243 N PHE B 224
SHEET 1 AB3 8 ARG C 48 SER C 49 0
SHEET 2 AB3 8 LEU C 35 TRP C 40 -1 N SER C 39 O ARG C 48
SHEET 3 AB3 8 THR C 24 LEU C 32 -1 N GLY C 28 O TRP C 40
SHEET 4 AB3 8 LEU C 10 PHE C 18 -1 N ILE C 15 O ASP C 27
SHEET 5 AB3 8 LEU C 94 GLU C 103 -1 O ALA C 100 N CYS C 12
SHEET 6 AB3 8 ASN C 111 PHE C 118 -1 O HIS C 115 N SER C 99
SHEET 7 AB3 8 LYS C 121 GLN C 127 -1 O LYS C 121 N PHE C 118
SHEET 8 AB3 8 SER C 130 PRO C 133 -1 O SER C 130 N GLN C 127
SHEET 1 AB4 4 LYS C 188 GLY C 194 0
SHEET 2 AB4 4 ARG C 201 PHE C 211 -1 O SER C 209 N LYS C 188
SHEET 3 AB4 4 TRP C 243 VAL C 252 -1 O VAL C 251 N LEU C 202
SHEET 4 AB4 4 THR C 230 GLN C 231 -1 N GLN C 231 O THR C 248
SHEET 1 AB5 4 LYS C 188 GLY C 194 0
SHEET 2 AB5 4 ARG C 201 PHE C 211 -1 O SER C 209 N LYS C 188
SHEET 3 AB5 4 TRP C 243 VAL C 252 -1 O VAL C 251 N LEU C 202
SHEET 4 AB5 4 LEU C 236 PRO C 237 -1 N LEU C 236 O TYR C 244
SHEET 1 AB6 4 GLN C 225 GLU C 226 0
SHEET 2 AB6 4 TRP C 217 ARG C 222 -1 N ARG C 222 O GLN C 225
SHEET 3 AB6 4 SER C 260 LYS C 264 -1 O SER C 260 N MET C 221
SHEET 4 AB6 4 ILE C 273 TYR C 276 -1 O ILE C 273 N VAL C 263
SHEET 1 AB7 4 LYS F 6 SER F 11 0
SHEET 2 AB7 4 ASN F 21 PHE F 30 -1 O SER F 28 N LYS F 6
SHEET 3 AB7 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AB7 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 AB8 4 LYS F 6 SER F 11 0
SHEET 2 AB8 4 ASN F 21 PHE F 30 -1 O SER F 28 N LYS F 6
SHEET 3 AB8 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AB8 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 AB9 4 GLU F 44 ARG F 45 0
SHEET 2 AB9 4 GLU F 36 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 AB9 4 TYR F 78 ASN F 83 -1 O ASN F 83 N GLU F 36
SHEET 4 AB9 4 LYS F 91 LYS F 94 -1 O LYS F 91 N VAL F 82
SSBOND 1 CYS A 23 CYS A 104 1555 1555 2.04
SSBOND 2 CYS A 149 CYS A 199 1555 1555 2.04
SSBOND 3 CYS A 174 CYS B 181 1555 1555 2.04
SSBOND 4 CYS B 23 CYS B 104 1555 1555 2.01
SSBOND 5 CYS B 155 CYS B 220 1555 1555 2.02
SSBOND 6 CYS C 206 CYS C 261 1555 1555 2.61
LINK ND2 ASN C 20 C1 NAG C 301 1555 1555 1.44
LINK ND2 ASN C 42 C1 NAG C 302 1555 1555 1.43
CISPEP 1 ILE A 7 PRO A 8 0 -1.95
CISPEP 2 PRO A 46 GLY A 47 0 2.55
CISPEP 3 SER B 7 PRO B 8 0 -4.07
CISPEP 4 TYR B 161 PRO B 162 0 -1.48
CISPEP 5 TYR C 92 PRO C 93 0 0.96
CISPEP 6 TYR C 212 PRO C 213 0 -2.21
CISPEP 7 HIS F 31 PRO F 32 0 5.25
CRYST1 209.990 46.300 124.650 90.00 122.28 90.00 C 1 2 1 4
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 0.004762 0.000000 0.003008 0.00000
SCALE2 0.000000 0.021598 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009489 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
