HEADER IMMUNE SYSTEM, LIPID BINDING PROTEIN 25-MAY-11 3S6C
TITLE STRUCTURE OF HUMAN CD1E
CAVEAT 3S6C FUC B 2 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-2-MICROGLOBULIN, T-CELL SURFACE GLYCOPROTEIN CD1E,
COMPND 3 MEMBRANE-ASSOCIATED;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: P61769 RESIDUES 21-119, P15812 RESIDUES 32-303;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: FUSION OF BETA-2 MICROGLOBULIN AND CD1E HEAVY CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: B2M, CD1E;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: M10;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFUSE-MIGG1
KEYWDS MHC, IMMUNOGLOBULIN DOMAIN, IMMUNE SYSTEM, ANTIGEN PRESENTATION, N-
KEYWDS 2 GLYCOSYLATION, INTRACELLULAR, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.F.GARCIA-ALLES,L.MAVEYRAUD,S.TRANIER,L.MOUREY
REVDAT 5 29-JUL-20 3S6C 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM SSBOND LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 08-NOV-17 3S6C 1 REMARK
REVDAT 3 23-AUG-17 3S6C 1 SOURCE REMARK
REVDAT 2 31-AUG-11 3S6C 1 JRNL HETATM
REVDAT 1 20-JUL-11 3S6C 0
JRNL AUTH L.F.GARCIA-ALLES,G.GIACOMETTI,C.VERSLUIS,L.MAVEYRAUD,
JRNL AUTH 2 D.DE PAEPE,J.GUIARD,S.TRANIER,M.GILLERON,J.PRANDI,D.HANAU,
JRNL AUTH 3 A.J.HECK,L.MORI,G.DE LIBERO,G.PUZO,L.MOUREY,H.DE LA SALLE
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CD1E REVEALS A GROOVE SUITED FOR
JRNL TITL 2 LIPID-EXCHANGE PROCESSES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 13230 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21788486
JRNL DOI 10.1073/PNAS.1105627108
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 12460
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) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 664
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 904
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2861
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.10000
REMARK 3 B22 (A**2) : 1.79000
REMARK 3 B33 (A**2) : -0.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.429
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.400
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.092
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2986 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1966 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4065 ; 1.832 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4747 ; 0.995 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 371 ; 8.155 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;39.063 ;23.688
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 427 ;21.749 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.875 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 424 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3404 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 644 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1849 ; 0.637 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 755 ; 0.098 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2935 ; 1.192 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1137 ; 1.666 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1129 ; 2.910 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 277
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1600 14.0880 -18.9590
REMARK 3 T TENSOR
REMARK 3 T11: 0.6546 T22: 0.5777
REMARK 3 T33: 0.4919 T12: 0.0245
REMARK 3 T13: 0.0193 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 10.0986 L22: 0.7863
REMARK 3 L33: 1.1776 L12: -1.4774
REMARK 3 L13: 2.5439 L23: -0.1633
REMARK 3 S TENSOR
REMARK 3 S11: -0.1871 S12: -1.2030 S13: 0.0025
REMARK 3 S21: 0.2572 S22: 0.2219 S23: 0.2094
REMARK 3 S31: 0.1215 S32: 0.1438 S33: -0.0348
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1001 A 1100
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5250 26.9770 -31.8750
REMARK 3 T TENSOR
REMARK 3 T11: 0.6316 T22: 0.5483
REMARK 3 T33: 0.9849 T12: -0.1245
REMARK 3 T13: -0.2444 T23: 0.1363
REMARK 3 L TENSOR
REMARK 3 L11: 10.4824 L22: 4.9921
REMARK 3 L33: 0.9617 L12: -2.4105
REMARK 3 L13: -2.9900 L23: 0.7625
REMARK 3 S TENSOR
REMARK 3 S11: 0.4176 S12: 0.5197 S13: 1.6816
REMARK 3 S21: -0.4095 S22: -0.0793 S23: 0.2490
REMARK 3 S31: -0.2474 S32: 0.0652 S33: -0.3383
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. B-FACTORS WERE REFINED ISOTROPICALLY, BUT ARE
REMARK 3 REPORTED AS ANISOTROPIC BECAUSE OF THE TLS CONTRIBUTION THAT IS
REMARK 3 ADDED TO THE REFINED ISOTROPIC VALUE
REMARK 4
REMARK 4 3S6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000065816.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9395
REMARK 200 MONOCHROMATOR : KHOZU MONOCHROMATOR WITH DUAL
REMARK 200 PARALLEL SI(111) CRYSTALS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12460
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 103.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37200
REMARK 200 R SYM FOR SHELL (I) : 0.37200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 6000, 0.2 M SODIUM MALONATE,
REMARK 280 0.1 M MAGNESIUM VALERATE, 0.1 M SODIUM BORATE , PH 3.6, VAPOR
REMARK 280 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 103.14450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.96500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 103.14450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.96500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ASP A 1101
REMARK 465 ASP A 1102
REMARK 465 ASP A 1103
REMARK 465 LYS A 1104
REMARK 465 GLY A 1105
REMARK 465 SER A 1106
REMARK 465 SER A 1107
REMARK 465 SER A 1108
REMARK 465 SER A 1109
REMARK 465 ASP A 1110
REMARK 465 ASP A 1111
REMARK 465 ASP A 1112
REMARK 465 ASP A 1113
REMARK 465 LYS A 1114
REMARK 465 GLU A 1
REMARK 465 GLU A 2
REMARK 465 GLN A 120
REMARK 465 GLY A 121
REMARK 465 ILE A 122
REMARK 465 GLN A 278
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 LYS A1006 CD CE NZ
REMARK 470 ILE A1007 CD1
REMARK 470 LYS A1041 CG CD CE NZ
REMARK 470 GLU A1044 CG CD OE1 OE2
REMARK 470 ARG A1045 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1048 CG CD CE NZ
REMARK 470 LYS A1058 CG CD CE NZ
REMARK 470 GLU A1069 CG CD OE1 OE2
REMARK 470 LYS A1075 CG CD CE NZ
REMARK 470 SER A 18 OG
REMARK 470 TRP A 19 CE3 CZ2 CZ3 CH2
REMARK 470 GLU A 23 CD OE1 OE2
REMARK 470 LEU A 31 CG CD1 CD2
REMARK 470 VAL A 39 CG1 CG2
REMARK 470 LEU A 40 CD1 CD2
REMARK 470 LEU A 46 CD1 CD2
REMARK 470 LYS A 47 CD CE NZ
REMARK 470 PHE A 54 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 LEU A 59 CD1
REMARK 470 LYS A 60 CE NZ
REMARK 470 LEU A 68 CD1 CD2
REMARK 470 ILE A 74 CG1 CD1
REMARK 470 ILE A 76 CD1
REMARK 470 LEU A 95 CD1 CD2
REMARK 470 ARG A 99 CG CD NE CZ NH1 NH2
REMARK 470 MET A 100 CG SD CE
REMARK 470 ASN A 101 CG OD1 ND2
REMARK 470 GLN A 104 CG CD OE1 NE2
REMARK 470 ILE A 105 CG1 CG2 CD1
REMARK 470 GLU A 125 CD OE1 OE2
REMARK 470 ILE A 132 CG1 CG2 CD1
REMARK 470 ILE A 137 CD1
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 LEU A 155 CD1
REMARK 470 ARG A 161 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 163 CD1
REMARK 470 LEU A 166 CG CD1 CD2
REMARK 470 SER A 172 OG
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 SER A 189 OG
REMARK 470 LEU A 195 CG CD1 CD2
REMARK 470 LEU A 197 CG CD1 CD2
REMARK 470 ILE A 268 CD1
REMARK 470 ASN A 274 CG OD1 ND2
REMARK 470 PHE A 277 CG CD1 CD2 CE1 CE2 CZ
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 O THR A 33 O PHE A 45 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A1014 C - N - CA ANGL. DEV. = -13.0 DEGREES
REMARK 500 LEU A 117 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 VAL A 201 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A1010 149.55 -170.67
REMARK 500 ASN A1017 63.32 63.35
REMARK 500 ASP A1034 96.73 -63.90
REMARK 500 ILE A1046 -162.02 -104.13
REMARK 500 GLU A1047 -62.60 -134.07
REMARK 500 TRP A1060 -21.02 79.57
REMARK 500 SER A1061 150.99 -49.48
REMARK 500 PHE A1070 157.90 165.77
REMARK 500 LYS A1075 -142.69 -74.39
REMARK 500 ASP A1076 85.74 64.33
REMARK 500 HIS A1084 118.71 -170.80
REMARK 500 VAL A1085 -58.45 -6.56
REMARK 500 GLN A1089 147.84 -175.77
REMARK 500 ASP A1098 34.14 -87.07
REMARK 500 MET A1099 -53.38 77.19
REMARK 500 LEU A 4 59.71 23.94
REMARK 500 VAL A 39 -75.64 -53.86
REMARK 500 LEU A 46 -102.09 77.86
REMARK 500 TRP A 49 3.75 -59.13
REMARK 500 ALA A 79 -82.38 -53.57
REMARK 500 SER A 80 -36.62 -35.05
REMARK 500 ALA A 81 -65.67 -14.09
REMARK 500 ARG A 99 127.36 160.25
REMARK 500 MET A 100 169.17 75.84
REMARK 500 ASN A 101 56.32 72.43
REMARK 500 ALA A 102 115.71 55.73
REMARK 500 GLN A 104 -55.17 146.25
REMARK 500 LEU A 107 108.09 177.03
REMARK 500 ASP A 115 115.43 -37.07
REMARK 500 LEU A 117 144.99 -172.97
REMARK 500 LYS A 139 -71.06 -55.57
REMARK 500 GLU A 171 -80.30 41.47
REMARK 500 LYS A 175 39.18 -70.55
REMARK 500 PRO A 180 -149.23 -70.14
REMARK 500 GLU A 181 137.87 -178.85
REMARK 500 TRP A 183 -157.18 -147.14
REMARK 500 PRO A 192 -155.74 -67.86
REMARK 500 GLN A 196 62.72 -179.56
REMARK 500 HIS A 200 54.10 -162.72
REMARK 500 MET A 214 -166.12 -110.60
REMARK 500 ARG A 215 98.39 176.54
REMARK 500 GLN A 218 94.15 -60.17
REMARK 500 ASP A 233 34.40 -79.71
REMARK 500 SER A 253 -164.09 -107.96
REMARK 500 HIS A 258 143.10 -174.58
REMARK 500 GLU A 273 51.22 -95.53
REMARK 500 LEU A 275 118.65 -161.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 274 LEU A 275 -140.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS POSITION IS SUBJET TO POLYMORPHISM IN UNP ENTRY P15812, GLN OR
REMARK 999 ARG BEING POSSIBLE
DBREF 3S6C A 1001 1099 UNP P61769 B2MG_HUMAN 21 119
DBREF 3S6C A 1 272 UNP P15812 CD1E_HUMAN 32 303
SEQADV 3S6C ASP A 1100 UNP P61769 LINKER
SEQADV 3S6C ASP A 1101 UNP P61769 LINKER
SEQADV 3S6C ASP A 1102 UNP P61769 LINKER
SEQADV 3S6C ASP A 1103 UNP P61769 LINKER
SEQADV 3S6C LYS A 1104 UNP P61769 LINKER
SEQADV 3S6C GLY A 1105 UNP P61769 LINKER
SEQADV 3S6C SER A 1106 UNP P61769 LINKER
SEQADV 3S6C SER A 1107 UNP P61769 LINKER
SEQADV 3S6C SER A 1108 UNP P61769 LINKER
SEQADV 3S6C SER A 1109 UNP P61769 LINKER
SEQADV 3S6C ASP A 1110 UNP P61769 LINKER
SEQADV 3S6C ASP A 1111 UNP P61769 LINKER
SEQADV 3S6C ASP A 1112 UNP P61769 LINKER
SEQADV 3S6C ASP A 1113 UNP P61769 LINKER
SEQADV 3S6C LYS A 1114 UNP P61769 LINKER
SEQADV 3S6C ARG A 75 UNP P15812 GLN 106 SEE REMARK 999
SEQADV 3S6C GLU A 273 UNP P15812 EXPRESSION TAG
SEQADV 3S6C ASN A 274 UNP P15812 EXPRESSION TAG
SEQADV 3S6C LEU A 275 UNP P15812 EXPRESSION TAG
SEQADV 3S6C TYR A 276 UNP P15812 EXPRESSION TAG
SEQADV 3S6C PHE A 277 UNP P15812 EXPRESSION TAG
SEQADV 3S6C GLN A 278 UNP P15812 EXPRESSION TAG
SEQRES 1 A 392 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 A 392 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 A 392 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 A 392 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 A 392 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 A 392 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 A 392 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 A 392 ILE VAL LYS TRP ASP ARG ASP MET ASP ASP ASP ASP LYS
SEQRES 9 A 392 GLY SER SER SER SER ASP ASP ASP ASP LYS GLU GLU GLN
SEQRES 10 A 392 LEU SER PHE ARG MET LEU GLN THR SER SER PHE ALA ASN
SEQRES 11 A 392 HIS SER TRP ALA HIS SER GLU GLY SER GLY TRP LEU GLY
SEQRES 12 A 392 ASP LEU GLN THR HIS GLY TRP ASP THR VAL LEU GLY THR
SEQRES 13 A 392 ILE ARG PHE LEU LYS PRO TRP SER HIS GLY ASN PHE SER
SEQRES 14 A 392 LYS GLN GLU LEU LYS ASN LEU GLN SER LEU PHE GLN LEU
SEQRES 15 A 392 TYR PHE HIS SER PHE ILE ARG ILE VAL GLN ALA SER ALA
SEQRES 16 A 392 GLY GLN PHE GLN LEU GLU TYR PRO PHE GLU ILE GLN ILE
SEQRES 17 A 392 LEU ALA GLY CYS ARG MET ASN ALA PRO GLN ILE PHE LEU
SEQRES 18 A 392 ASN MET ALA TYR GLN GLY SER ASP PHE LEU SER PHE GLN
SEQRES 19 A 392 GLY ILE SER TRP GLU PRO SER PRO GLY ALA GLY ILE ARG
SEQRES 20 A 392 ALA GLN ASN ILE CYS LYS VAL LEU ASN ARG TYR LEU ASP
SEQRES 21 A 392 ILE LYS GLU ILE LEU GLN SER LEU LEU GLY HIS THR CYS
SEQRES 22 A 392 PRO ARG PHE LEU ALA GLY LEU MET GLU ALA GLY GLU SER
SEQRES 23 A 392 GLU LEU LYS ARG LYS VAL LYS PRO GLU ALA TRP LEU SER
SEQRES 24 A 392 CYS GLY PRO SER PRO GLY PRO GLY ARG LEU GLN LEU VAL
SEQRES 25 A 392 CYS HIS VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL
SEQRES 26 A 392 MET TRP MET ARG GLY GLU GLN GLU GLN ARG GLY THR GLN
SEQRES 27 A 392 ARG GLY ASP VAL LEU PRO ASN ALA ASP GLU THR TRP TYR
SEQRES 28 A 392 LEU ARG ALA THR LEU ASP VAL ALA ALA GLY GLU ALA ALA
SEQRES 29 A 392 GLY LEU SER CYS ARG VAL LYS HIS SER SER LEU GLY GLY
SEQRES 30 A 392 HIS ASP LEU ILE ILE HIS TRP GLY GLY GLU ASN LEU TYR
SEQRES 31 A 392 PHE GLN
MODRES 3S6C ASN A 16 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET FUC B 2 10
HET GOL A2003 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG C8 H15 N O6
FORMUL 2 FUC C6 H12 O5
FORMUL 3 GOL C3 H8 O3
HELIX 1 1 LYS A 47 GLY A 52 5 6
HELIX 2 2 SER A 55 ALA A 81 1 27
HELIX 3 3 GLY A 131 TYR A 144 1 14
HELIX 4 4 TYR A 144 GLU A 171 1 28
HELIX 5 5 ALA A 245 ALA A 250 1 6
SHEET 1 A 4 GLN A1008 SER A1011 0
SHEET 2 A 4 ASN A1021 PHE A1030 -1 O ASN A1024 N TYR A1010
SHEET 3 A 4 PHE A1062 PHE A1070 -1 O LEU A1064 N VAL A1027
SHEET 4 A 4 GLU A1050 HIS A1051 -1 N GLU A1050 O TYR A1067
SHEET 1 B 4 GLN A1008 SER A1011 0
SHEET 2 B 4 ASN A1021 PHE A1030 -1 O ASN A1024 N TYR A1010
SHEET 3 B 4 PHE A1062 PHE A1070 -1 O LEU A1064 N VAL A1027
SHEET 4 B 4 SER A1055 PHE A1056 -1 N SER A1055 O TYR A1063
SHEET 1 C 4 GLU A1044 ARG A1045 0
SHEET 2 C 4 GLU A1036 LYS A1041 -1 N LYS A1041 O GLU A1044
SHEET 3 C 4 TYR A1078 ASN A1083 -1 O ARG A1081 N ASP A1038
SHEET 4 C 4 LYS A1091 LYS A1094 -1 O VAL A1093 N CYS A1080
SHEET 1 D 6 THR A 42 ARG A 44 0
SHEET 2 D 6 LEU A 31 ASP A 37 -1 N ASP A 37 O THR A 42
SHEET 3 D 6 HIS A 21 LEU A 28 -1 N GLY A 26 O HIS A 34
SHEET 4 D 6 PHE A 6 PHE A 14 -1 N LEU A 9 O SER A 25
SHEET 5 D 6 PHE A 90 CYS A 98 -1 O ILE A 94 N GLN A 10
SHEET 6 D 6 ILE A 105 ASN A 108 -1 O PHE A 106 N GLY A 97
SHEET 1 E 2 LEU A 117 SER A 118 0
SHEET 2 E 2 GLU A 125 PRO A 126 -1 O GLU A 125 N SER A 118
SHEET 1 F 3 LEU A 197 VAL A 198 0
SHEET 2 F 3 ALA A 240 LEU A 242 -1 O LEU A 242 N LEU A 197
SHEET 3 F 3 GLN A 224 ARG A 225 -1 N GLN A 224 O THR A 241
SHEET 1 G 3 VAL A 201 SER A 202 0
SHEET 2 G 3 THR A 235 LEU A 238 -1 O LEU A 238 N VAL A 201
SHEET 3 G 3 LEU A 229 ASN A 231 -1 N ASN A 231 O THR A 235
SHEET 1 H 3 TRP A 210 TRP A 213 0
SHEET 2 H 3 CYS A 254 LYS A 257 -1 O ARG A 255 N MET A 212
SHEET 3 H 3 LEU A 266 ILE A 267 -1 O LEU A 266 N VAL A 256
SHEET 1 I 2 HIS A 269 GLY A 271 0
SHEET 2 I 2 ASN A 274 TYR A 276 -1 O ASN A 274 N GLY A 271
SSBOND 1 CYS A 98 CYS A 159 1555 1555 2.05
SSBOND 2 CYS A 199 CYS A 254 1555 1555 2.10
SSBOND 3 CYS A 1025 CYS A 1080 1555 1555 2.02
LINK ND2 ASN A 16 C1 NAG B 1 1555 1555 1.44
LINK O6 NAG B 1 C1 FUC B 2 1555 1555 1.45
CISPEP 1 HIS A 1031 PRO A 1032 0 -15.92
CISPEP 2 TYR A 88 PRO A 89 0 -2.42
CISPEP 3 MET A 100 ASN A 101 0 14.45
CISPEP 4 ALA A 102 PRO A 103 0 -13.28
CISPEP 5 TYR A 205 PRO A 206 0 8.44
CISPEP 6 GLY A 272 GLU A 273 0 2.36
CISPEP 7 TYR A 276 PHE A 277 0 3.23
CRYST1 206.289 45.930 65.628 90.00 91.48 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 0.004848 0.000000 0.000125 0.00000
SCALE2 0.000000 0.021772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015242 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
