HEADER IMMUNE SYSTEM 27-MAR-03 1OVZ
TITLE CRYSTAL STRUCTURE OF HUMAN FCARI
CAVEAT 1OVZ NAG C 1 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN ALPHA FC RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ECTODOMAIN;
COMPND 5 SYNONYM: IGA FC RECEPTOR, CD89 ANTIGEN;
COMPND 6 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: FCAR OR CD89;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HIGH 5 INSECT CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PACGP67
KEYWDS FCARI, CD89, IGA, FC RECEPTOR, IMMUNOGLOBULIN-LIKE DOMAIN, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.HERR,E.R.BALLISTER,P.J.BJORKMAN
REVDAT 5 29-JUL-20 1OVZ 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HET HETNAM HETSYN FORMUL
REVDAT 5 3 1 LINK SITE ATOM
REVDAT 4 13-JUL-11 1OVZ 1 VERSN
REVDAT 3 24-FEB-09 1OVZ 1 VERSN
REVDAT 2 24-JUN-03 1OVZ 1 JRNL
REVDAT 1 27-MAY-03 1OVZ 0
JRNL AUTH A.B.HERR,E.R.BALLISTER,P.J.BJORKMAN
JRNL TITL INSIGHTS INTO IGA-MEDIATED IMMUNE RESPONSES FROM THE CRYSTAL
JRNL TITL 2 STRUCTURES OF HUMAN FC-ALPHA-RI AND ITS COMPLEX WITH IGA1-FC
JRNL REF NATURE V. 423 614 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12768205
JRNL DOI 10.1038/NATURE01685
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.B.HERR,C.L.WHITE,C.MILBURN,C.WU,P.J.BJORKMAN
REMARK 1 TITL BIVALENT BINDING OF IGA1 TO FCARI SUGGESTS A MECHANISM FOR
REMARK 1 TITL 2 CYTOKINE ACTIVATION OF IGA PHAGOCYTOSIS
REMARK 1 REF J.MOL.BIOL. V. 327 645 2003
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1016/S0022-2836(03)00149-9
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 9590
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 SET) : 0.235
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 991
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.11
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 672
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 78
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.046
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2806
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.65000
REMARK 3 B22 (A**2) : -11.65000
REMARK 3 B33 (A**2) : 23.31000
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) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.52
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.69
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.080
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 38.52
REMARK 3
REMARK 3 NCS MODEL : CONSTR
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : TRIS.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : TRIS.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OVZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018720.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10204
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 15.10
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.4000
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) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MES, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 79.07500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 19.95500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 9.97750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.93250
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 79.07500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.95500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 79.07500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 29.93250
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 79.07500
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 9.97750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY STATE IS A MONOMER.
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 APPLY THE FOLLOWING TO CHAINS: A, C
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLN A 1
REMARK 465 GLU A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 PHE A 5
REMARK 465 GLY A 199
REMARK 465 ARG A 200
REMARK 465 ALA A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 HIS A 207
REMARK 465 GLN B 1
REMARK 465 GLY B 112
REMARK 465 LEU B 113
REMARK 465 VAL B 114
REMARK 465 LEU B 115
REMARK 465 MET B 116
REMARK 465 PRO B 117
REMARK 465 GLY B 118
REMARK 465 GLU B 119
REMARK 465 ASN B 120
REMARK 465 ILE B 121
REMARK 465 SER B 122
REMARK 465 VAL B 194
REMARK 465 THR B 195
REMARK 465 ALA B 196
REMARK 465 ILE B 197
REMARK 465 ASP B 198
REMARK 465 GLY B 199
REMARK 465 ARG B 200
REMARK 465 ALA B 201
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
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 PRO A 6 CG CD
REMARK 470 ARG A 32 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 44 CG OD1 ND2
REMARK 470 SER A 45 OG
REMARK 470 THR A 46 OG1 CG2
REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 52 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 PHE A 56 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 57 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 57 CZ3 CH2
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 SER A 126 OG
REMARK 470 HIS A 129 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 130 CG1 CG2 CD1
REMARK 470 ASN A 165 CG OD1 ND2
REMARK 470 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 198 CG OD1 OD2
REMARK 470 GLU B 2 CG CD OE1 OE2
REMARK 470 ASP B 4 CG OD1 OD2
REMARK 470 PHE B 5 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 32 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 43 CG CD CE NZ
REMARK 470 ARG B 48 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 PHE B 106 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 108 OG
REMARK 470 ARG B 111 CG CD NE CZ NH1 NH2
REMARK 470 THR B 124 OG1 CG2
REMARK 470 SER B 126 OG
REMARK 470 SER B 127 OG
REMARK 470 HIS B 129 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 130 CG1 CG2 CD1
REMARK 470 GLU B 140 CG CD OE1 OE2
REMARK 470 GLU B 142 CG CD OE1 OE2
REMARK 470 GLN B 147 CG CD OE1 NE2
REMARK 470 HIS B 148 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 150 OG
REMARK 470 GLU B 152 CG CD OE1 OE2
REMARK 470 HIS B 153 CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 156 CG OD1 ND2
REMARK 470 PHE B 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 158 OG
REMARK 470 LEU B 159 CG CD1 CD2
REMARK 470 VAL B 162 CG1 CG2
REMARK 470 ASP B 163 CG OD1 OD2
REMARK 470 LEU B 164 CG CD1 CD2
REMARK 470 ASN B 165 CG OD1 ND2
REMARK 470 VAL B 166 CG1 CG2
REMARK 470 ARG B 178 CG CD NE CZ NH1 NH2
REMARK 470 SER B 187 OG
REMARK 470 ASN B 188 CG OD1 ND2
REMARK 470 LEU B 192 CG CD1 CD2
REMARK 470 VAL B 193 CG1 CG2
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 A 180 C - N - CA ANGL. DEV. = 10.5 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 LEU A 20 -83.49 -19.54
REMARK 500 ARG A 32 -33.66 -38.78
REMARK 500 TRP A 57 138.40 -179.02
REMARK 500 ASN A 58 -1.03 63.75
REMARK 500 THR A 60 -62.62 -104.39
REMARK 500 ARG A 111 -148.25 -147.94
REMARK 500 SER A 127 76.40 -173.82
REMARK 500 ALA A 128 47.07 -61.95
REMARK 500 HIS A 129 -58.07 -175.80
REMARK 500 PRO A 131 63.52 -68.47
REMARK 500 GLU A 142 136.87 -34.98
REMARK 500 LEU A 143 77.11 -102.63
REMARK 500 SER A 144 -157.38 -178.95
REMARK 500 ALA A 155 82.29 64.44
REMARK 500 LEU A 164 -22.37 -36.63
REMARK 500 TRP A 175 113.14 89.45
REMARK 500 ASP B 4 -86.33 -62.77
REMARK 500 LEU B 20 -81.46 -21.52
REMARK 500 LYS B 43 -94.72 -103.70
REMARK 500 ASN B 44 58.05 -91.29
REMARK 500 GLU B 59 138.24 -24.11
REMARK 500 HIS B 68 81.67 60.07
REMARK 500 PRO B 105 -124.15 -89.12
REMARK 500 ALA B 109 -174.66 -179.26
REMARK 500 ALA B 128 41.24 -90.23
REMARK 500 HIS B 129 -57.89 -176.25
REMARK 500 HIS B 148 89.36 -164.35
REMARK 500 PHE B 157 77.21 -100.46
REMARK 500 SER B 158 109.16 -56.42
REMARK 500 VAL B 162 -165.15 -68.01
REMARK 500 ASP B 163 -3.36 62.06
REMARK 500 LEU B 164 -86.65 -67.76
REMARK 500 VAL B 166 38.11 -72.61
REMARK 500 TRP B 175 113.00 91.88
REMARK 500 SER B 179 70.20 -116.29
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OVZ A 1 195 UNP P24071 FCAR_HUMAN 22 216
DBREF 1OVZ B 1 195 UNP P24071 FCAR_HUMAN 22 216
SEQADV 1OVZ ALA A 196 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ILE A 197 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ASP A 198 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ GLY A 199 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ARG A 200 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ALA A 201 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS A 202 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS A 203 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS A 204 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS A 205 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS A 206 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS A 207 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ALA B 196 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ILE B 197 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ASP B 198 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ GLY B 199 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ARG B 200 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ ALA B 201 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS B 202 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS B 203 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS B 204 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS B 205 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS B 206 UNP P24071 EXPRESSION TAG
SEQADV 1OVZ HIS B 207 UNP P24071 EXPRESSION TAG
SEQRES 1 A 207 GLN GLU GLY ASP PHE PRO MET PRO PHE ILE SER ALA LYS
SEQRES 2 A 207 SER SER PRO VAL ILE PRO LEU ASP GLY SER VAL LYS ILE
SEQRES 3 A 207 GLN CYS GLN ALA ILE ARG GLU ALA TYR LEU THR GLN LEU
SEQRES 4 A 207 MET ILE ILE LYS ASN SER THR TYR ARG GLU ILE GLY ARG
SEQRES 5 A 207 ARG LEU LYS PHE TRP ASN GLU THR ASP PRO GLU PHE VAL
SEQRES 6 A 207 ILE ASP HIS MET ASP ALA ASN LYS ALA GLY ARG TYR GLN
SEQRES 7 A 207 CYS GLN TYR ARG ILE GLY HIS TYR ARG PHE ARG TYR SER
SEQRES 8 A 207 ASP THR LEU GLU LEU VAL VAL THR GLY LEU TYR GLY LYS
SEQRES 9 A 207 PRO PHE LEU SER ALA ASP ARG GLY LEU VAL LEU MET PRO
SEQRES 10 A 207 GLY GLU ASN ILE SER LEU THR CYS SER SER ALA HIS ILE
SEQRES 11 A 207 PRO PHE ASP ARG PHE SER LEU ALA LYS GLU GLY GLU LEU
SEQRES 12 A 207 SER LEU PRO GLN HIS GLN SER GLY GLU HIS PRO ALA ASN
SEQRES 13 A 207 PHE SER LEU GLY PRO VAL ASP LEU ASN VAL SER GLY ILE
SEQRES 14 A 207 TYR ARG CYS TYR GLY TRP TYR ASN ARG SER PRO TYR LEU
SEQRES 15 A 207 TRP SER PHE PRO SER ASN ALA LEU GLU LEU VAL VAL THR
SEQRES 16 A 207 ALA ILE ASP GLY ARG ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 207 GLN GLU GLY ASP PHE PRO MET PRO PHE ILE SER ALA LYS
SEQRES 2 B 207 SER SER PRO VAL ILE PRO LEU ASP GLY SER VAL LYS ILE
SEQRES 3 B 207 GLN CYS GLN ALA ILE ARG GLU ALA TYR LEU THR GLN LEU
SEQRES 4 B 207 MET ILE ILE LYS ASN SER THR TYR ARG GLU ILE GLY ARG
SEQRES 5 B 207 ARG LEU LYS PHE TRP ASN GLU THR ASP PRO GLU PHE VAL
SEQRES 6 B 207 ILE ASP HIS MET ASP ALA ASN LYS ALA GLY ARG TYR GLN
SEQRES 7 B 207 CYS GLN TYR ARG ILE GLY HIS TYR ARG PHE ARG TYR SER
SEQRES 8 B 207 ASP THR LEU GLU LEU VAL VAL THR GLY LEU TYR GLY LYS
SEQRES 9 B 207 PRO PHE LEU SER ALA ASP ARG GLY LEU VAL LEU MET PRO
SEQRES 10 B 207 GLY GLU ASN ILE SER LEU THR CYS SER SER ALA HIS ILE
SEQRES 11 B 207 PRO PHE ASP ARG PHE SER LEU ALA LYS GLU GLY GLU LEU
SEQRES 12 B 207 SER LEU PRO GLN HIS GLN SER GLY GLU HIS PRO ALA ASN
SEQRES 13 B 207 PHE SER LEU GLY PRO VAL ASP LEU ASN VAL SER GLY ILE
SEQRES 14 B 207 TYR ARG CYS TYR GLY TRP TYR ASN ARG SER PRO TYR LEU
SEQRES 15 B 207 TRP SER PHE PRO SER ASN ALA LEU GLU LEU VAL VAL THR
SEQRES 16 B 207 ALA ILE ASP GLY ARG ALA HIS HIS HIS HIS HIS HIS
MODRES 1OVZ ASN A 120 ASN GLYCOSYLATION SITE
MODRES 1OVZ ASN A 156 ASN GLYCOSYLATION SITE
MODRES 1OVZ ASN B 44 ASN GLYCOSYLATION SITE
MODRES 1OVZ ASN B 58 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG A 320 14
HET TRS A 401 8
HET NAG B 300 14
HET NAG B 310 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 5 TRS C4 H12 N O3 1+
HELIX 1 1 ASP A 70 ALA A 74 5 5
HELIX 2 2 ASP A 163 SER A 167 5 5
HELIX 3 3 ASP B 70 ALA B 74 5 5
SHEET 1 A 4 ILE A 10 ALA A 12 0
SHEET 2 A 4 VAL A 24 CYS A 28 -1 N GLN A 27 O SER A 11
SHEET 3 A 4 GLU A 63 ILE A 66 -1 N PHE A 64 O ILE A 26
SHEET 4 A 4 ARG A 52 ARG A 53 -1 N ARG A 52 O VAL A 65
SHEET 1 B 9 TYR A 47 GLU A 49 0
SHEET 2 B 9 LEU A 36 ILE A 42 -1 O ILE A 41 N ARG A 48
SHEET 3 B 9 GLY A 75 ARG A 82 -1 O ARG A 76 N ILE A 42
SHEET 4 B 9 PHE A 88 TYR A 90 -1 O ARG A 89 N TYR A 81
SHEET 5 B 9 GLY A 75 ARG A 82 -1 N TYR A 81 O ARG A 89
SHEET 6 B 9 LEU A 94 THR A 99 -1 O LEU A 94 N TYR A 77
SHEET 7 B 9 LEU A 182 TRP A 183 1 N TRP A 183 O VAL A 98
SHEET 8 B 9 LEU A 94 THR A 99 1 O VAL A 98 N TRP A 183
SHEET 9 B 9 VAL A 17 PRO A 19 1 N ILE A 18 O VAL A 97
SHEET 1 C 3 PHE A 106 ALA A 109 0
SHEET 2 C 3 SER A 122 SER A 126 -1 N THR A 124 O SER A 108
SHEET 3 C 3 ASN A 156 SER A 158 -1 N PHE A 157 O LEU A 123
SHEET 1 D 5 VAL A 114 LEU A 115 0
SHEET 2 D 5 LEU A 190 VAL A 194 1 O VAL A 193 N LEU A 115
SHEET 3 D 5 GLY A 168 TYR A 173 -1 N GLY A 168 O LEU A 192
SHEET 4 D 5 PHE A 135 LYS A 139 -1 O SER A 136 N TYR A 173
SHEET 5 D 5 GLN A 149 SER A 150 -1 O SER A 150 N PHE A 135
SHEET 1 E 4 ILE B 10 ALA B 12 0
SHEET 2 E 4 VAL B 24 CYS B 28 -1 N GLN B 27 O SER B 11
SHEET 3 E 4 GLU B 63 ILE B 66 -1 N PHE B 64 O ILE B 26
SHEET 4 E 4 ARG B 52 LEU B 54 -1 N ARG B 52 O VAL B 65
SHEET 1 F 7 TYR B 47 GLU B 49 0
SHEET 2 F 7 LEU B 36 ILE B 42 -1 O ILE B 41 N ARG B 48
SHEET 3 F 7 GLY B 75 ARG B 82 -1 O ARG B 76 N ILE B 42
SHEET 4 F 7 PHE B 88 TYR B 90 -1 O ARG B 89 N TYR B 81
SHEET 5 F 7 GLY B 75 ARG B 82 -1 N TYR B 81 O ARG B 89
SHEET 6 F 7 LEU B 94 THR B 99 -1 O LEU B 94 N TYR B 77
SHEET 7 F 7 VAL B 17 PRO B 19 1 O ILE B 18 N THR B 99
SHEET 1 G 2 LEU B 107 SER B 108 0
SHEET 2 G 2 THR B 124 CYS B 125 -1 N THR B 124 O SER B 108
SHEET 1 H 4 GLN B 149 SER B 150 0
SHEET 2 H 4 PHE B 135 LYS B 139 -1 O PHE B 135 N SER B 150
SHEET 3 H 4 GLY B 168 TYR B 173 -1 O ARG B 171 N ALA B 138
SHEET 4 H 4 LEU B 190 LEU B 192 -1 O LEU B 190 N TYR B 170
SSBOND 1 CYS A 28 CYS A 79 1555 1555 2.02
SSBOND 2 CYS A 125 CYS A 172 1555 1555 2.02
SSBOND 3 CYS B 28 CYS B 79 1555 1555 2.02
SSBOND 4 CYS B 125 CYS B 172 1555 1555 2.03
LINK ND2 ASN A 120 C1 NAG A 320 1555 1555 1.45
LINK ND2 ASN A 156 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 44 C1 NAG B 300 1555 1555 1.46
LINK ND2 ASN B 58 C1 NAG B 310 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
CRYST1 158.150 158.150 39.910 90.00 90.00 90.00 I 41 16
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 0.006323 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006323 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025056 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
