HEADER IMMUNE SYSTEM 25-JUL-17 5WKG
TITLE CRYSTAL STRUCTURE OF HUMAN CD1B IN COMPLEX WITH PA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD1B;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD1B;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID
KEYWDS ANTIGEN PRESENTING MOLECULE, PA, PHOSPHOLIPID, MHC, CD1B, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SHAHINE,S.GRAS,J.ROSSJOHN
REVDAT 2 29-JUL-20 5WKG 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 01-NOV-17 5WKG 0
JRNL AUTH A.SHAHINE,I.VAN RHIJN,T.Y.CHENG,S.IWANY,S.GRAS,D.B.MOODY,
JRNL AUTH 2 J.ROSSJOHN
JRNL TITL A MOLECULAR BASIS OF HUMAN T CELL RECEPTOR AUTOREACTIVITY
JRNL TITL 2 TOWARD SELF-PHOSPHOLIPIDS.
JRNL REF SCI IMMUNOL V. 2 2017
JRNL REFN ESSN 2470-9468
JRNL PMID 29054999
JRNL DOI 10.1126/SCIIMMUNOL.AAO1384
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 24235
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1259
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2906
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2040
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2750
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.37
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2979
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 220
REMARK 3 SOLVENT ATOMS : 292
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.33
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.07040
REMARK 3 B22 (A**2) : -0.36360
REMARK 3 B33 (A**2) : -0.70680
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) : 0.230
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.231
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.181
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.209
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.176
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 : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3356 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4560 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1566 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 75 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 481 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3356 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 438 ; 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 : 3988 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.72
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.37
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|4 - 109}
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1617 13.3603 8.8704
REMARK 3 T TENSOR
REMARK 3 T11: -0.0271 T22: 0.0107
REMARK 3 T33: 0.0065 T12: 0.0079
REMARK 3 T13: -0.0031 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.1968
REMARK 3 L33: 0.2544 L12: 0.1191
REMARK 3 L13: 0.1021 L23: -0.0655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: -0.0087 S13: 0.0037
REMARK 3 S21: -0.0189 S22: -0.0015 S23: 0.0196
REMARK 3 S31: 0.0044 S32: -0.0044 S33: 0.0014
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|110 - 175}
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7379 24.4003 5.2011
REMARK 3 T TENSOR
REMARK 3 T11: 0.0140 T22: -0.0086
REMARK 3 T33: -0.0053 T12: 0.0045
REMARK 3 T13: -0.0192 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.0012 L22: 0.0000
REMARK 3 L33: 0.2242 L12: -0.1820
REMARK 3 L13: 0.0330 L23: 0.2012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.0030 S13: 0.0115
REMARK 3 S21: -0.0092 S22: -0.0003 S23: 0.0092
REMARK 3 S31: -0.0087 S32: 0.0009 S33: -0.0006
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|176 - 283}
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2009 -2.8343 14.5757
REMARK 3 T TENSOR
REMARK 3 T11: -0.0090 T22: -0.0027
REMARK 3 T33: 0.0049 T12: 0.0142
REMARK 3 T13: 0.0112 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.2531 L22: 0.0641
REMARK 3 L33: 0.1014 L12: -0.2721
REMARK 3 L13: 0.0563 L23: -0.0938
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: 0.0057 S13: 0.0041
REMARK 3 S21: -0.0036 S22: -0.0072 S23: -0.0037
REMARK 3 S31: 0.0009 S32: 0.0084 S33: 0.0082
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {B|3 - 98}
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7783 -8.0916 4.6669
REMARK 3 T TENSOR
REMARK 3 T11: 0.0128 T22: -0.0099
REMARK 3 T33: -0.0141 T12: 0.0244
REMARK 3 T13: -0.0215 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.1647 L22: 0.4780
REMARK 3 L33: 0.3348 L12: 0.0175
REMARK 3 L13: 0.2723 L23: -0.3162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: 0.0013 S13: -0.0203
REMARK 3 S21: -0.0142 S22: -0.0073 S23: 0.0015
REMARK 3 S31: 0.0055 S32: 0.0004 S33: 0.0051
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5WKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000229154.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95370
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24235
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 57.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PET 3350, 0.2M SODIUM MALONATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, 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 28.59500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.35500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.26500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.35500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.59500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.26500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HIS A 2
REMARK 465 ALA A 3
REMARK 465 ASP A 284
REMARK 465 ILE A 285
REMARK 465 PHE A 286
REMARK 465 GLU A 287
REMARK 465 ALA A 288
REMARK 465 GLN A 289
REMARK 465 LYS A 290
REMARK 465 ILE A 291
REMARK 465 GLU A 292
REMARK 465 TRP A 293
REMARK 465 HIS A 294
REMARK 465 GLU A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 ASP B 100
REMARK 465 MET B 101
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 TRP A 23 CD2 CE3 CZ2 CZ3 CH2
REMARK 470 GLN A 25 CG CD OE1 NE2
REMARK 470 GLN A 152 CG CD OE1 NE2
REMARK 470 LYS B 77 CG CD CE NZ
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 33 -113.63 56.86
REMARK 500 PHE A 123 -52.47 -120.01
REMARK 500 LEU A 282 34.60 -99.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CUY A 412
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 580 O
REMARK 620 2 HOH A 648 O 84.8
REMARK 620 3 ASN B 85 OD1 83.3 168.0
REMARK 620 4 HIS B 86 O 89.1 95.4 85.7
REMARK 620 5 LEU B 89 O 168.6 84.7 107.3 87.6
REMARK 620 6 HOH B 338 O 88.6 92.2 86.2 171.8 96.2
REMARK 620 N 1 2 3 4 5
DBREF 5WKG A 2 278 UNP P29016 CD1B_HUMAN 20 296
DBREF 5WKG B 3 101 UNP P61769 B2MG_HUMAN 21 119
SEQADV 5WKG GLY A 279 UNP P29016 EXPRESSION TAG
SEQADV 5WKG SER A 280 UNP P29016 EXPRESSION TAG
SEQADV 5WKG GLY A 281 UNP P29016 EXPRESSION TAG
SEQADV 5WKG LEU A 282 UNP P29016 EXPRESSION TAG
SEQADV 5WKG ASN A 283 UNP P29016 EXPRESSION TAG
SEQADV 5WKG ASP A 284 UNP P29016 EXPRESSION TAG
SEQADV 5WKG ILE A 285 UNP P29016 EXPRESSION TAG
SEQADV 5WKG PHE A 286 UNP P29016 EXPRESSION TAG
SEQADV 5WKG GLU A 287 UNP P29016 EXPRESSION TAG
SEQADV 5WKG ALA A 288 UNP P29016 EXPRESSION TAG
SEQADV 5WKG GLN A 289 UNP P29016 EXPRESSION TAG
SEQADV 5WKG LYS A 290 UNP P29016 EXPRESSION TAG
SEQADV 5WKG ILE A 291 UNP P29016 EXPRESSION TAG
SEQADV 5WKG GLU A 292 UNP P29016 EXPRESSION TAG
SEQADV 5WKG TRP A 293 UNP P29016 EXPRESSION TAG
SEQADV 5WKG HIS A 294 UNP P29016 EXPRESSION TAG
SEQADV 5WKG GLU A 295 UNP P29016 EXPRESSION TAG
SEQADV 5WKG HIS A 296 UNP P29016 EXPRESSION TAG
SEQADV 5WKG HIS A 297 UNP P29016 EXPRESSION TAG
SEQADV 5WKG HIS A 298 UNP P29016 EXPRESSION TAG
SEQADV 5WKG HIS A 299 UNP P29016 EXPRESSION TAG
SEQADV 5WKG HIS A 300 UNP P29016 EXPRESSION TAG
SEQADV 5WKG HIS A 301 UNP P29016 EXPRESSION TAG
SEQRES 1 A 300 HIS ALA PHE GLN GLY PRO THR SER PHE HIS VAL ILE GLN
SEQRES 2 A 300 THR SER SER PHE THR ASN SER THR TRP ALA GLN THR GLN
SEQRES 3 A 300 GLY SER GLY TRP LEU ASP ASP LEU GLN ILE HIS GLY TRP
SEQRES 4 A 300 ASP SER ASP SER GLY THR ALA ILE PHE LEU LYS PRO TRP
SEQRES 5 A 300 SER LYS GLY ASN PHE SER ASP LYS GLU VAL ALA GLU LEU
SEQRES 6 A 300 GLU GLU ILE PHE ARG VAL TYR ILE PHE GLY PHE ALA ARG
SEQRES 7 A 300 GLU VAL GLN ASP PHE ALA GLY ASP PHE GLN MET LYS TYR
SEQRES 8 A 300 PRO PHE GLU ILE GLN GLY ILE ALA GLY CYS GLU LEU HIS
SEQRES 9 A 300 SER GLY GLY ALA ILE VAL SER PHE LEU ARG GLY ALA LEU
SEQRES 10 A 300 GLY GLY LEU ASP PHE LEU SER VAL LYS ASN ALA SER CYS
SEQRES 11 A 300 VAL PRO SER PRO GLU GLY GLY SER ARG ALA GLN LYS PHE
SEQRES 12 A 300 CYS ALA LEU ILE ILE GLN TYR GLN GLY ILE MET GLU THR
SEQRES 13 A 300 VAL ARG ILE LEU LEU TYR GLU THR CYS PRO ARG TYR LEU
SEQRES 14 A 300 LEU GLY VAL LEU ASN ALA GLY LYS ALA ASP LEU GLN ARG
SEQRES 15 A 300 GLN VAL LYS PRO GLU ALA TRP LEU SER SER GLY PRO SER
SEQRES 16 A 300 PRO GLY PRO GLY ARG LEU GLN LEU VAL CYS HIS VAL SER
SEQRES 17 A 300 GLY PHE TYR PRO LYS PRO VAL TRP VAL MET TRP MET ARG
SEQRES 18 A 300 GLY GLU GLN GLU GLN GLN GLY THR GLN LEU GLY ASP ILE
SEQRES 19 A 300 LEU PRO ASN ALA ASN TRP THR TRP TYR LEU ARG ALA THR
SEQRES 20 A 300 LEU ASP VAL ALA ASP GLY GLU ALA ALA GLY LEU SER CYS
SEQRES 21 A 300 ARG VAL LYS HIS SER SER LEU GLU GLY GLN ASP ILE ILE
SEQRES 22 A 300 LEU TYR TRP ARG GLY SER GLY LEU ASN ASP ILE PHE GLU
SEQRES 23 A 300 ALA GLN LYS ILE GLU TRP HIS GLU HIS HIS HIS HIS HIS
SEQRES 24 A 300 HIS
SEQRES 1 B 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 B 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 B 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 B 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 B 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 B 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 B 99 ILE VAL LYS TRP ASP ARG ASP MET
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET FUC C 6 10
HET FUC C 7 10
HET NAG D 1 14
HET FUC D 2 10
HET NAG A 408 14
HET D21 A 411 46
HET CUY A 412 36
HET PEG A 413 7
HET CL A 414 1
HET CL A 415 1
HET CL A 416 1
HET EDO A 417 4
HET IOD A 418 1
HET IOD A 419 1
HET NA B 201 1
HET CL B 202 1
HET IOD B 203 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM D21 (2R)-1-(HEXADECANOYLOXY)-3-(PHOSPHONOOXY)PROPAN-2-YL
HETNAM 2 D21 (9Z)-OCTADEC-9-ENOATE
HETNAM CUY TETRACOSYL OCTADECANOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM IOD IODIDE ION
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 BMA C6 H12 O6
FORMUL 3 MAN 2(C6 H12 O6)
FORMUL 3 FUC 3(C6 H12 O5)
FORMUL 6 D21 C37 H71 O8 P
FORMUL 7 CUY C42 H84 O2
FORMUL 8 PEG C4 H10 O3
FORMUL 9 CL 4(CL 1-)
FORMUL 12 EDO C2 H6 O2
FORMUL 13 IOD 3(I 1-)
FORMUL 15 NA NA 1+
FORMUL 18 HOH *292(H2 O)
HELIX 1 AA1 SER A 59 ALA A 85 1 27
HELIX 2 AA2 GLY A 137 ILE A 149 1 13
HELIX 3 AA3 TYR A 151 GLU A 164 1 14
HELIX 4 AA4 GLU A 164 GLY A 177 1 14
HELIX 5 AA5 GLY A 177 GLN A 182 1 6
HELIX 6 AA6 HIS A 265 GLU A 269 5 5
SHEET 1 AA1 8 THR A 46 PHE A 49 0
SHEET 2 AA1 8 LEU A 35 ASP A 41 -1 N ASP A 41 O THR A 46
SHEET 3 AA1 8 TRP A 23 LEU A 32 -1 N LEU A 32 O LEU A 35
SHEET 4 AA1 8 SER A 9 ASN A 20 -1 N THR A 15 O GLN A 27
SHEET 5 AA1 8 PHE A 94 LEU A 104 -1 O ILE A 96 N SER A 16
SHEET 6 AA1 8 ILE A 110 LEU A 118 -1 O ARG A 115 N ILE A 99
SHEET 7 AA1 8 LEU A 121 LYS A 127 -1 O LEU A 124 N GLY A 116
SHEET 8 AA1 8 SER A 130 PRO A 133 -1 O VAL A 132 N SER A 125
SHEET 1 AA2 4 GLU A 188 GLY A 194 0
SHEET 2 AA2 4 ARG A 201 PHE A 211 -1 O HIS A 207 N TRP A 190
SHEET 3 AA2 4 THR A 242 ALA A 252 -1 O ALA A 247 N CYS A 206
SHEET 4 AA2 4 GLN A 231 LEU A 232 -1 N GLN A 231 O THR A 248
SHEET 1 AA3 4 GLU A 188 GLY A 194 0
SHEET 2 AA3 4 ARG A 201 PHE A 211 -1 O HIS A 207 N TRP A 190
SHEET 3 AA3 4 THR A 242 ALA A 252 -1 O ALA A 247 N CYS A 206
SHEET 4 AA3 4 LEU A 236 ASN A 238 -1 N LEU A 236 O TYR A 244
SHEET 1 AA4 4 GLN A 225 GLU A 226 0
SHEET 2 AA4 4 TRP A 217 ARG A 222 -1 N ARG A 222 O GLN A 225
SHEET 3 AA4 4 SER A 260 LYS A 264 -1 O SER A 260 N MET A 221
SHEET 4 AA4 4 ILE A 273 TYR A 276 -1 O LEU A 275 N CYS A 261
SHEET 1 AA5 4 LYS B 8 SER B 13 0
SHEET 2 AA5 4 ASN B 23 PHE B 32 -1 O SER B 30 N LYS B 8
SHEET 3 AA5 4 PHE B 64 PHE B 72 -1 O THR B 70 N LEU B 25
SHEET 4 AA5 4 GLU B 52 HIS B 53 -1 N GLU B 52 O TYR B 69
SHEET 1 AA6 4 LYS B 8 SER B 13 0
SHEET 2 AA6 4 ASN B 23 PHE B 32 -1 O SER B 30 N LYS B 8
SHEET 3 AA6 4 PHE B 64 PHE B 72 -1 O THR B 70 N LEU B 25
SHEET 4 AA6 4 SER B 57 PHE B 58 -1 N SER B 57 O TYR B 65
SHEET 1 AA7 4 GLU B 46 ARG B 47 0
SHEET 2 AA7 4 GLU B 38 LYS B 43 -1 N LYS B 43 O GLU B 46
SHEET 3 AA7 4 TYR B 80 ASN B 85 -1 O ARG B 83 N ASP B 40
SHEET 4 AA7 4 LYS B 93 LYS B 96 -1 O LYS B 93 N VAL B 84
SSBOND 1 CYS A 102 CYS A 166 1555 1555 2.08
SSBOND 2 CYS A 131 CYS A 145 1555 1555 2.03
SSBOND 3 CYS A 206 CYS A 261 1555 1555 2.02
SSBOND 4 CYS B 27 CYS B 82 1555 1555 2.02
LINK ND2 ASN A 20 C1 NAG A 408 1555 1555 1.44
LINK ND2 ASN A 57 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN A 128 C1 NAG D 1 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.38
LINK O3 NAG C 1 C1 FUC C 6 1555 1555 1.43
LINK O6 NAG C 1 C1 FUC C 7 1555 1555 1.41
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.43
LINK O6 BMA C 3 C1 MAN C 5 1555 1555 1.38
LINK O3 NAG D 1 C1 FUC D 2 1555 1555 1.43
LINK O HOH A 580 NA NA B 201 2554 1555 2.44
LINK O HOH A 648 NA NA B 201 2554 1555 2.75
LINK OD1 ASN B 85 NA NA B 201 1555 1555 2.38
LINK O HIS B 86 NA NA B 201 1555 1555 2.35
LINK O LEU B 89 NA NA B 201 1555 1555 2.26
LINK NA NA B 201 O HOH B 338 1555 1555 2.38
CISPEP 1 TYR A 92 PRO A 93 0 -2.02
CISPEP 2 TYR A 212 PRO A 213 0 2.95
CISPEP 3 HIS B 33 PRO B 34 0 -3.20
CRYST1 57.190 78.530 84.710 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 0.017486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012734 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011805 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
