HEADER IMMUNE SYSTEM 18-OCT-18 6MSS
TITLE DIVERSITY IN THE TYPE II NATURAL KILLER T CELL RECEPTOR REPERTOIRE AND
TITLE 2 ANTIGEN SPECIFICITY LEADS TO DIFFERING CD1D DOCKING STRATEGIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: A11B8.2 NKT TCR ALPHA-CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: A11B8.2 NKT TCR BETA-CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ANTIGEN-PRESENTING GLYCOPROTEIN CD1D1;
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 15 CHAIN: D;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 9 ORGANISM_COMMON: MOUSE;
SOURCE 10 ORGANISM_TAXID: 10090;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 15 ORGANISM_COMMON: MOUSE;
SOURCE 16 ORGANISM_TAXID: 10090;
SOURCE 17 GENE: CD1D1, CD1.1;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 22 ORGANISM_COMMON: MOUSE;
SOURCE 23 ORGANISM_TAXID: 10090;
SOURCE 24 GENE: B2M;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NKT CELLS, CD1D MOLECULE, MICROBIAL LIPID ANTIGEN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SUNDARARAJ,J.LE NOURS,T.PRAVEENA,J.ROSSJOHN
REVDAT 3 29-JUL-20 6MSS 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 22-JAN-20 6MSS 1 JRNL
REVDAT 1 02-OCT-19 6MSS 0
JRNL AUTH C.F.ALMEIDA,S.SUNDARARAJ,J.LE NOURS,T.PRAVEENA,B.CAO,
JRNL AUTH 2 S.BURUGUPALLI,D.G.M.SMITH,O.PATEL,M.BRIGL,D.G.PELLICCI,
JRNL AUTH 3 S.J.WILLIAMS,A.P.ULDRICH,D.I.GODFREY,J.ROSSJOHN
JRNL TITL DISTINCT CD1D DOCKING STRATEGIES EXHIBITED BY DIVERSE TYPE
JRNL TITL 2 II NKT CELL RECEPTORS.
JRNL REF NAT COMMUN V. 10 5242 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31748533
JRNL DOI 10.1038/S41467-019-12941-9
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 21485
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1102
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 430
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2727
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 412
REMARK 3 BIN R VALUE (WORKING SET) : 0.2643
REMARK 3 BIN FREE R VALUE : 0.5397
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.19
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 6151
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 112
REMARK 3 SOLVENT ATOMS : 24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.97140
REMARK 3 B22 (A**2) : -7.15260
REMARK 3 B33 (A**2) : 9.12400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.340
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.388
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.855
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6464 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8809 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2897 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1093 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6464 ; 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 : 843 ; 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 : 6726 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.88
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.00
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): 3.9781 -23.7412 85.1546
REMARK 3 T TENSOR
REMARK 3 T11: -0.1021 T22: -0.1050
REMARK 3 T33: 0.0052 T12: 0.0167
REMARK 3 T13: 0.0762 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.7225 L22: 0.5544
REMARK 3 L33: 5.1655 L12: 0.3291
REMARK 3 L13: 0.4204 L23: 0.8312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: 0.0223 S13: 0.0463
REMARK 3 S21: 0.1191 S22: 0.0657 S23: 0.2675
REMARK 3 S31: -0.0466 S32: -0.2447 S33: -0.1136
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0952 -9.6329 81.4149
REMARK 3 T TENSOR
REMARK 3 T11: -0.0761 T22: -0.1400
REMARK 3 T33: -0.0601 T12: -0.0752
REMARK 3 T13: 0.0790 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 1.2903 L22: 1.1732
REMARK 3 L33: 1.7392 L12: 0.5197
REMARK 3 L13: 0.4656 L23: 0.5270
REMARK 3 S TENSOR
REMARK 3 S11: -0.1091 S12: 0.1847 S13: 0.0828
REMARK 3 S21: -0.0549 S22: 0.1995 S23: 0.0396
REMARK 3 S31: -0.5419 S32: 0.2374 S33: -0.0904
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1733 -32.3130 30.2214
REMARK 3 T TENSOR
REMARK 3 T11: -0.1741 T22: -0.0969
REMARK 3 T33: -0.0255 T12: -0.0075
REMARK 3 T13: 0.0446 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 1.8707 L22: 0.2704
REMARK 3 L33: 2.8534 L12: 0.1253
REMARK 3 L13: 1.4493 L23: 0.4387
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: -0.0061 S13: -0.0965
REMARK 3 S21: 0.0365 S22: 0.0150 S23: 0.0036
REMARK 3 S31: 0.1586 S32: 0.0724 S33: -0.0855
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9382 -17.9139 20.4336
REMARK 3 T TENSOR
REMARK 3 T11: -0.0539 T22: -0.0752
REMARK 3 T33: -0.0178 T12: -0.0315
REMARK 3 T13: 0.0283 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 3.5189 L22: 1.9133
REMARK 3 L33: 1.7140 L12: 0.4415
REMARK 3 L13: 0.5996 L23: 0.2632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: 0.1488 S13: 0.1334
REMARK 3 S21: -0.0438 S22: 0.0634 S23: 0.0259
REMARK 3 S31: -0.4903 S32: -0.0188 S33: -0.0162
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6MSS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
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) : 0.9537
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21533
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 73.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-25% PEG 1500 10% SUCCINATE
REMARK 280 PHOSPHATE GLYCINE PH 6.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.29000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.33500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.63000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.33500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.29000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.63000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -21.29000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -70.63000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 170.67000
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 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 127
REMARK 465 ASP A 128
REMARK 465 LYS A 147
REMARK 465 ASP A 148
REMARK 465 ASN A 188
REMARK 465 SER A 189
REMARK 465 ILE A 190
REMARK 465 ILE A 191
REMARK 465 PRO A 192
REMARK 465 GLU A 193
REMARK 465 ASP A 194
REMARK 465 THR A 195
REMARK 465 PHE A 196
REMARK 465 PHE A 197
REMARK 465 PRO A 198
REMARK 465 SER A 199
REMARK 465 PRO A 200
REMARK 465 GLU A 201
REMARK 465 SER A 202
REMARK 465 SER A 203
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 SER C 1
REMARK 465 GLU C 2
REMARK 465 ALA C 3
REMARK 465 GLN C 4
REMARK 465 GLN C 5
REMARK 465 LYS C 6
REMARK 465 SER C 198
REMARK 465 SER C 199
REMARK 465 ALA C 200
REMARK 465 HIS C 201
REMARK 465 SER C 281
REMARK 465 LEU C 282
REMARK 465 HIS C 283
REMARK 465 HIS C 284
REMARK 465 ILE C 285
REMARK 465 LEU C 286
REMARK 465 ASP C 287
REMARK 465 ALA C 288
REMARK 465 GLN C 289
REMARK 465 LYS C 290
REMARK 465 MET C 291
REMARK 465 VAL C 292
REMARK 465 TRP C 293
REMARK 465 ASN C 294
REMARK 465 HIS C 295
REMARK 465 ARG C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 HIS C 300
REMARK 465 HIS C 301
REMARK 465 HIS C 302
REMARK 465 ILE D 1
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 GLU A 6 CG CD OE1 OE2
REMARK 470 ARG A 41 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 ILE A 111 CG1 CG2 CD1
REMARK 470 GLN A 112 CG CD OE1 NE2
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 123 CG OD1 OD2
REMARK 470 GLN A 140 CG CD OE1 NE2
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 SER A 178 OG
REMARK 470 ASP A 179 CG OD1 OD2
REMARK 470 ASN A 184 CG OD1 ND2
REMARK 470 LYS B 19 CG CD CE NZ
REMARK 470 LYS B 66 CG CD CE NZ
REMARK 470 GLU B 73 CG CD OE1 OE2
REMARK 470 GLU B 80 CG CD OE1 OE2
REMARK 470 LEU B 81 CG CD1 CD2
REMARK 470 GLU B 116 CG CD OE1 OE2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 GLU B 133 CG CD OE1 OE2
REMARK 470 GLN B 140 CG CD OE1 NE2
REMARK 470 GLN B 181 CG CD OE1 NE2
REMARK 470 ASN B 185 CG OD1 ND2
REMARK 470 ARG B 206 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 221 CG OD1 ND2
REMARK 470 GLU B 223 CG CD OE1 OE2
REMARK 470 GLN C 61 CG CD OE1 NE2
REMARK 470 GLU C 64 CG CD OE1 OE2
REMARK 470 LYS C 65 CG CD CE NZ
REMARK 470 ARG C 79 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 93 CG OD1 OD2
REMARK 470 ASN C 110 CG OD1 ND2
REMARK 470 GLU C 113 CG CD OE1 OE2
REMARK 470 LYS C 123 CG CD CE NZ
REMARK 470 ASP C 226 CG OD1 OD2
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 LYS D 58 CG CD CE NZ
REMARK 470 GLU D 69 CG CD OE1 OE2
REMARK 470 GLU D 89 CG CD OE1 OE2
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 ASP A 77 75.98 54.09
REMARK 500 ILE A 111 99.58 -69.26
REMARK 500 GLN A 140 39.37 -82.65
REMARK 500 GLN A 145 -158.62 -133.78
REMARK 500 LYS A 167 40.95 -81.53
REMARK 500 ALA A 185 -38.96 -149.06
REMARK 500 HIS B 42 -17.97 -140.45
REMARK 500 ILE B 61 70.80 -119.48
REMARK 500 LEU B 79 77.61 -116.72
REMARK 500 ALA B 183 48.49 -80.05
REMARK 500 LYS D 48 59.95 -102.06
REMARK 500 TRP D 60 -1.00 76.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6MSS A 1 203 PDB 6MSS 6MSS 1 203
DBREF 6MSS B 1 245 PDB 6MSS 6MSS 1 245
DBREF 6MSS C 1 279 UNP P11609 CD1D1_MOUSE 19 297
DBREF 6MSS D 1 99 UNP P01887 B2MG_MOUSE 21 119
SEQADV 6MSS HIS C 201 UNP P11609 ASP 219 CONFLICT
SEQADV 6MSS GLY C 280 UNP P11609 EXPRESSION TAG
SEQADV 6MSS SER C 281 UNP P11609 EXPRESSION TAG
SEQADV 6MSS LEU C 282 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 283 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 284 UNP P11609 EXPRESSION TAG
SEQADV 6MSS ILE C 285 UNP P11609 EXPRESSION TAG
SEQADV 6MSS LEU C 286 UNP P11609 EXPRESSION TAG
SEQADV 6MSS ASP C 287 UNP P11609 EXPRESSION TAG
SEQADV 6MSS ALA C 288 UNP P11609 EXPRESSION TAG
SEQADV 6MSS GLN C 289 UNP P11609 EXPRESSION TAG
SEQADV 6MSS LYS C 290 UNP P11609 EXPRESSION TAG
SEQADV 6MSS MET C 291 UNP P11609 EXPRESSION TAG
SEQADV 6MSS VAL C 292 UNP P11609 EXPRESSION TAG
SEQADV 6MSS TRP C 293 UNP P11609 EXPRESSION TAG
SEQADV 6MSS ASN C 294 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 295 UNP P11609 EXPRESSION TAG
SEQADV 6MSS ARG C 296 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 297 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 298 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 299 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 300 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 301 UNP P11609 EXPRESSION TAG
SEQADV 6MSS HIS C 302 UNP P11609 EXPRESSION TAG
SEQRES 1 A 203 MET GLY MET PRO VAL GLU GLN ASN PRO PRO ALA LEU SER
SEQRES 2 A 203 LEU TYR GLU GLY ALA ASP SER GLY LEU ARG CYS ASN PHE
SEQRES 3 A 203 SER THR THR MET LYS SER VAL GLN TRP PHE GLN GLN ASN
SEQRES 4 A 203 HIS ARG GLY ARG LEU ILE THR LEU PHE TYR LEU ALA GLN
SEQRES 5 A 203 GLY THR LYS GLU ASN GLY ARG LEU LYS SER THR PHE ASN
SEQRES 6 A 203 SER LYS GLU ARG TYR SER THR LEU HIS ILE LYS ASP ALA
SEQRES 7 A 203 GLN LEU GLU ASP SER GLY THR TYR PHE CYS ALA ALA VAL
SEQRES 8 A 203 ASN MET GLY TYR LYS LEU THR PHE GLY THR GLY THR SER
SEQRES 9 A 203 LEU LEU VAL ASP PRO ASN ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 A 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 A 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 A 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 A 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 A 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 A 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 A 203 PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 B 245 MET GLU ALA ALA VAL THR GLN SER PRO ARG ASN LYS VAL
SEQRES 2 B 245 ALA VAL THR GLY GLY LYS VAL THR LEU SER CYS ASN GLN
SEQRES 3 B 245 THR ASN ASN HIS ASN ASN MET TYR TRP TYR ARG GLN ASP
SEQRES 4 B 245 THR GLY HIS GLY LEU ARG LEU ILE HIS TYR SER TYR GLY
SEQRES 5 B 245 ALA GLY SER THR GLU LYS GLY ASP ILE PRO ASP GLY TYR
SEQRES 6 B 245 LYS ALA SER ARG PRO SER GLN GLU ASN PHE SER LEU ILE
SEQRES 7 B 245 LEU GLU LEU ALA THR PRO SER GLN THR SER VAL TYR PHE
SEQRES 8 B 245 CYS ALA SER GLY ASP PRO GLN GLY VAL SER TYR GLU GLN
SEQRES 9 B 245 TYR PHE GLY PRO GLY THR ARG LEU THR VAL LEU GLU ASP
SEQRES 10 B 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 B 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 B 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 B 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 B 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 B 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 B 245 ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES 17 B 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 B 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 B 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 C 302 SER GLU ALA GLN GLN LYS ASN TYR THR PHE ARG CYS LEU
SEQRES 2 C 302 GLN MET SER SER PHE ALA ASN ARG SER TRP SER ARG THR
SEQRES 3 C 302 ASP SER VAL VAL TRP LEU GLY ASP LEU GLN THR HIS ARG
SEQRES 4 C 302 TRP SER ASN ASP SER ALA THR ILE SER PHE THR LYS PRO
SEQRES 5 C 302 TRP SER GLN GLY LYS LEU SER ASN GLN GLN TRP GLU LYS
SEQRES 6 C 302 LEU GLN HIS MET PHE GLN VAL TYR ARG VAL SER PHE THR
SEQRES 7 C 302 ARG ASP ILE GLN GLU LEU VAL LYS MET MET SER PRO LYS
SEQRES 8 C 302 GLU ASP TYR PRO ILE GLU ILE GLN LEU SER ALA GLY CYS
SEQRES 9 C 302 GLU MET TYR PRO GLY ASN ALA SER GLU SER PHE LEU HIS
SEQRES 10 C 302 VAL ALA PHE GLN GLY LYS TYR VAL VAL ARG PHE TRP GLY
SEQRES 11 C 302 THR SER TRP GLN THR VAL PRO GLY ALA PRO SER TRP LEU
SEQRES 12 C 302 ASP LEU PRO ILE LYS VAL LEU ASN ALA ASP GLN GLY THR
SEQRES 13 C 302 SER ALA THR VAL GLN MET LEU LEU ASN ASP THR CYS PRO
SEQRES 14 C 302 LEU PHE VAL ARG GLY LEU LEU GLU ALA GLY LYS SER ASP
SEQRES 15 C 302 LEU GLU LYS GLN GLU LYS PRO VAL ALA TRP LEU SER SER
SEQRES 16 C 302 VAL PRO SER SER ALA HIS GLY HIS ARG GLN LEU VAL CYS
SEQRES 17 C 302 HIS VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL MET
SEQRES 18 C 302 TRP MET ARG GLY ASP GLN GLU GLN GLN GLY THR HIS ARG
SEQRES 19 C 302 GLY ASP PHE LEU PRO ASN ALA ASP GLU THR TRP TYR LEU
SEQRES 20 C 302 GLN ALA THR LEU ASP VAL GLU ALA GLY GLU GLU ALA GLY
SEQRES 21 C 302 LEU ALA CYS ARG VAL LYS HIS SER SER LEU GLY GLY GLN
SEQRES 22 C 302 ASP ILE ILE LEU TYR TRP GLY SER LEU HIS HIS ILE LEU
SEQRES 23 C 302 ASP ALA GLN LYS MET VAL TRP ASN HIS ARG HIS HIS HIS
SEQRES 24 C 302 HIS HIS HIS
SEQRES 1 D 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 D 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 D 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 D 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 D 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 D 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 D 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS
SEQRES 8 D 99 THR VAL TYR TRP ASP ARG ASP MET
HET NAG E 1 14
HET NAG E 2 14
HET NAG C 401 14
HET NAG C 402 14
HET SRV C 405 56
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SRV (2S)-2-(HEPTADECANOYLOXY)-3-{[(10S)-10-
HETNAM 2 SRV METHYLOCTADECANOYL]OXY}PROPYL ALPHA-D-
HETNAM 3 SRV GLUCOPYRANOSIDURONIC ACID
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 8 SRV C45 H84 O11
FORMUL 9 HOH *24(H2 O)
HELIX 1 AA1 GLN A 79 SER A 83 5 5
HELIX 2 AA2 THR B 83 THR B 87 5 5
HELIX 3 AA3 PRO B 97 VAL B 100 5 4
HELIX 4 AA4 ASP B 117 VAL B 121 5 5
HELIX 5 AA5 SER B 132 THR B 139 1 8
HELIX 6 AA6 ALA B 199 ASN B 204 1 6
HELIX 7 AA7 SER C 59 SER C 89 1 31
HELIX 8 AA8 PRO C 140 TRP C 142 5 3
HELIX 9 AA9 LEU C 143 ALA C 152 1 10
HELIX 10 AB1 ASP C 153 ASP C 166 1 14
HELIX 11 AB2 ASP C 166 GLY C 179 1 14
HELIX 12 AB3 GLY C 179 GLU C 184 1 6
HELIX 13 AB4 HIS C 267 GLY C 271 5 5
SHEET 1 AA1 5 VAL A 5 ASN A 8 0
SHEET 2 AA1 5 SER A 20 PHE A 26 -1 O ASN A 25 N GLU A 6
SHEET 3 AA1 5 TYR A 70 ILE A 75 -1 O ILE A 75 N SER A 20
SHEET 4 AA1 5 LEU A 60 ASN A 65 -1 N LYS A 61 O HIS A 74
SHEET 5 AA1 5 THR A 54 ASN A 57 -1 N ASN A 57 O LEU A 60
SHEET 1 AA2 5 ALA A 11 TYR A 15 0
SHEET 2 AA2 5 THR A 103 ASP A 108 1 O SER A 104 N LEU A 12
SHEET 3 AA2 5 GLY A 84 ASN A 92 -1 N TYR A 86 O THR A 103
SHEET 4 AA2 5 VAL A 33 GLN A 38 -1 N GLN A 38 O THR A 85
SHEET 5 AA2 5 LEU A 44 LEU A 50 -1 O LEU A 47 N TRP A 35
SHEET 1 AA3 4 ALA A 11 TYR A 15 0
SHEET 2 AA3 4 THR A 103 ASP A 108 1 O SER A 104 N LEU A 12
SHEET 3 AA3 4 GLY A 84 ASN A 92 -1 N TYR A 86 O THR A 103
SHEET 4 AA3 4 LYS A 96 PHE A 99 -1 O THR A 98 N ALA A 90
SHEET 1 AA4 9 VAL A 151 ILE A 153 0
SHEET 2 AA4 9 SER A 170 SER A 175 -1 O TRP A 174 N TYR A 152
SHEET 3 AA4 9 SER A 130 THR A 135 -1 N CYS A 132 O ALA A 173
SHEET 4 AA4 9 ALA A 117 ASP A 123 -1 N LEU A 121 O VAL A 131
SHEET 5 AA4 9 VAL B 128 GLU B 130 -1 O GLU B 130 N ARG A 122
SHEET 6 AA4 9 LYS B 141 PHE B 151 -1 O VAL B 145 N PHE B 129
SHEET 7 AA4 9 TYR B 189 SER B 198 -1 O TYR B 189 N PHE B 151
SHEET 8 AA4 9 VAL B 171 THR B 173 -1 N CYS B 172 O ARG B 194
SHEET 9 AA4 9 VAL A 158 LEU A 159 -1 N VAL A 158 O THR B 173
SHEET 1 AA5 8 VAL A 151 ILE A 153 0
SHEET 2 AA5 8 SER A 170 SER A 175 -1 O TRP A 174 N TYR A 152
SHEET 3 AA5 8 SER A 130 THR A 135 -1 N CYS A 132 O ALA A 173
SHEET 4 AA5 8 ALA A 117 ASP A 123 -1 N LEU A 121 O VAL A 131
SHEET 5 AA5 8 VAL B 128 GLU B 130 -1 O GLU B 130 N ARG A 122
SHEET 6 AA5 8 LYS B 141 PHE B 151 -1 O VAL B 145 N PHE B 129
SHEET 7 AA5 8 TYR B 189 SER B 198 -1 O TYR B 189 N PHE B 151
SHEET 8 AA5 8 LEU B 178 LYS B 179 -1 N LEU B 178 O ALA B 190
SHEET 1 AA6 4 THR B 6 SER B 8 0
SHEET 2 AA6 4 VAL B 20 ASN B 25 -1 O ASN B 25 N THR B 6
SHEET 3 AA6 4 ASN B 74 LEU B 79 -1 O LEU B 77 N LEU B 22
SHEET 4 AA6 4 LYS B 66 SER B 68 -1 N SER B 68 O SER B 76
SHEET 1 AA7 6 ASN B 11 VAL B 15 0
SHEET 2 AA7 6 THR B 110 LEU B 115 1 O THR B 113 N ALA B 14
SHEET 3 AA7 6 SER B 88 GLY B 95 -1 N TYR B 90 O THR B 110
SHEET 4 AA7 6 ASN B 32 ASP B 39 -1 N TYR B 36 O PHE B 91
SHEET 5 AA7 6 GLY B 43 SER B 50 -1 O ILE B 47 N TRP B 35
SHEET 6 AA7 6 GLU B 57 LYS B 58 -1 O GLU B 57 N TYR B 49
SHEET 1 AA8 4 ASN B 11 VAL B 15 0
SHEET 2 AA8 4 THR B 110 LEU B 115 1 O THR B 113 N ALA B 14
SHEET 3 AA8 4 SER B 88 GLY B 95 -1 N TYR B 90 O THR B 110
SHEET 4 AA8 4 GLN B 104 PHE B 106 -1 O TYR B 105 N SER B 94
SHEET 1 AA9 4 LYS B 165 VAL B 167 0
SHEET 2 AA9 4 VAL B 156 VAL B 162 -1 N TRP B 160 O VAL B 167
SHEET 3 AA9 4 HIS B 208 PHE B 215 -1 O GLN B 212 N SER B 159
SHEET 4 AA9 4 GLN B 234 TRP B 241 -1 O ALA B 240 N PHE B 209
SHEET 1 AB1 8 SER C 48 PHE C 49 0
SHEET 2 AB1 8 LEU C 35 TRP C 40 -1 N ARG C 39 O SER C 48
SHEET 3 AB1 8 TRP C 23 LEU C 32 -1 N LEU C 32 O LEU C 35
SHEET 4 AB1 8 PHE C 10 ASN C 20 -1 N LEU C 13 O VAL C 29
SHEET 5 AB1 8 ILE C 96 MET C 106 -1 O ILE C 98 N SER C 16
SHEET 6 AB1 8 SER C 112 PHE C 120 -1 O GLU C 113 N GLU C 105
SHEET 7 AB1 8 LYS C 123 TRP C 129 -1 O VAL C 126 N VAL C 118
SHEET 8 AB1 8 SER C 132 THR C 135 -1 O SER C 132 N TRP C 129
SHEET 1 AB2 4 VAL C 190 VAL C 196 0
SHEET 2 AB2 4 HIS C 203 PHE C 213 -1 O HIS C 209 N TRP C 192
SHEET 3 AB2 4 TRP C 245 GLU C 254 -1 O LEU C 247 N VAL C 210
SHEET 4 AB2 4 HIS C 233 ARG C 234 -1 N HIS C 233 O THR C 250
SHEET 1 AB3 4 VAL C 190 VAL C 196 0
SHEET 2 AB3 4 HIS C 203 PHE C 213 -1 O HIS C 209 N TRP C 192
SHEET 3 AB3 4 TRP C 245 GLU C 254 -1 O LEU C 247 N VAL C 210
SHEET 4 AB3 4 LEU C 238 PRO C 239 -1 N LEU C 238 O TYR C 246
SHEET 1 AB4 4 GLN C 227 GLU C 228 0
SHEET 2 AB4 4 TRP C 219 ARG C 224 -1 N ARG C 224 O GLN C 227
SHEET 3 AB4 4 LEU C 261 LYS C 266 -1 O ALA C 262 N MET C 223
SHEET 4 AB4 4 ILE C 275 TYR C 278 -1 O ILE C 275 N VAL C 265
SHEET 1 AB5 4 GLN D 6 SER D 11 0
SHEET 2 AB5 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB5 4 PHE D 62 PHE D 70 -1 O ALA D 66 N CYS D 25
SHEET 4 AB5 4 GLU D 50 MET D 51 -1 N GLU D 50 O HIS D 67
SHEET 1 AB6 4 GLN D 6 SER D 11 0
SHEET 2 AB6 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB6 4 PHE D 62 PHE D 70 -1 O ALA D 66 N CYS D 25
SHEET 4 AB6 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 AB7 4 LYS D 44 LYS D 45 0
SHEET 2 AB7 4 ILE D 35 LYS D 41 -1 N LYS D 41 O LYS D 44
SHEET 3 AB7 4 TYR D 78 HIS D 84 -1 O ARG D 81 N GLN D 38
SHEET 4 AB7 4 LYS D 91 TYR D 94 -1 O LYS D 91 N VAL D 82
SSBOND 1 CYS A 24 CYS A 88 1555 1555 2.05
SSBOND 2 CYS A 157 CYS B 172 1555 1555 2.04
SSBOND 3 CYS B 24 CYS B 92 1555 1555 2.03
SSBOND 4 CYS B 146 CYS B 211 1555 1555 2.03
SSBOND 5 CYS C 104 CYS C 168 1555 1555 2.06
SSBOND 6 CYS C 208 CYS C 263 1555 1555 2.04
SSBOND 7 CYS D 25 CYS D 80 1555 1555 2.04
LINK ND2 ASN C 20 C1 NAG C 401 1555 1555 1.44
LINK ND2 ASN C 42 C1 NAG C 402 1555 1555 1.44
LINK ND2 ASN C 165 C1 NAG E 1 1555 1555 1.43
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
CISPEP 1 ASN A 8 PRO A 9 0 -4.30
CISPEP 2 SER A 178 ASP A 179 0 2.45
CISPEP 3 SER B 8 PRO B 9 0 -1.31
CISPEP 4 TYR B 152 PRO B 153 0 2.83
CISPEP 5 SER C 89 PRO C 90 0 4.42
CISPEP 6 TYR C 94 PRO C 95 0 -1.69
CISPEP 7 TYR C 214 PRO C 215 0 6.73
CISPEP 8 HIS D 31 PRO D 32 0 3.81
CRYST1 42.580 141.260 170.670 90.00 90.00 90.00 P 21 21 21 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 0.023485 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005859 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
