HEADER IMMUNE SYSTEM 19-MAR-13 4BFI
TITLE STRUCTURE OF THE COMPLEX OF THE EXTRACELLULAR PORTIONS OF MOUSE CD200R
TITLE 2 AND MOUSE CD200
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL SURFACE GLYCOPROTEIN CD200 RECEPTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 26-228;
COMPND 5 SYNONYM: CD200 CELL SURFACE GLYCOPROTEIN RECEPTOR, CELL SURFACE
COMPND 6 GLYCOPROTEIN OX2 RECEPTOR 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: OX-2 MEMBRANE GLYCOPROTEIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 31-232;
COMPND 12 SYNONYM: MRC OX-2 ANTIGEN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: LEC3.2.8.1;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PEE14;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 14 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 15 ORGANISM_TAXID: 10090;
SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 19 EXPRESSION_SYSTEM_VARIANT: LEC3.2.8.1;
SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PEE14
KEYWDS IMMUNE SYSTEM, PAIRED RECEPTOR, IG DOMAINS, VIRAL MIMICRY, LEUKAEMIA
KEYWDS 2 MIMICRY, LEUKAEMIA
EXPDTA X-RAY DIFFRACTION
AUTHOR D.HATHERLEY,S.M.LEA,S.JOHNSON,A.N.BARCLAY
REVDAT 5 20-DEC-23 4BFI 1 HETSYN
REVDAT 4 29-JUL-20 4BFI 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 29-MAY-13 4BFI 1 JRNL
REVDAT 2 08-MAY-13 4BFI 1 JRNL
REVDAT 1 01-MAY-13 4BFI 0
JRNL AUTH D.HATHERLEY,S.M.LEA,S.JOHNSON,A.N.BARCLAY
JRNL TITL STRUCTURES OF CD200/CD200 RECEPTOR FAMILY AND IMPLICATIONS
JRNL TITL 2 FOR TOPOLOGY, REGULATION, AND EVOLUTION
JRNL REF STRUCTURE V. 21 820 2013
JRNL REFN ISSN 0969-2126
JRNL PMID 23602662
JRNL DOI 10.1016/J.STR.2013.03.008
REMARK 2
REMARK 2 RESOLUTION. 3.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 3.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 15284
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 819
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) : 3.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 990
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3028
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 165
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 94.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.92000
REMARK 3 B22 (A**2) : 3.92000
REMARK 3 B33 (A**2) : -7.85000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.756
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.378
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.285
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.879
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3274 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4476 ; 1.404 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 391 ; 6.298 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 122 ;40.011 ;25.246
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 518 ;17.487 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;10.648 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 551 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2387 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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.
REMARK 4
REMARK 4 4BFI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.984
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS XIA2
REMARK 200 DATA SCALING SOFTWARE : XSCALE XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16034
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.220
REMARK 200 RESOLUTION RANGE LOW (A) : 86.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4BFG
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M IMIDAZOLE PH7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 58.04000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.08500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.06000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.08500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.08500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.02000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.08500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.08500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.06000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.08500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.08500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.02000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.04000
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: 4850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 29.4 KCAL/MOL
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 THR A 2
REMARK 465 ASP A 3
REMARK 465 LYS A 4
REMARK 465 ASN A 5
REMARK 465 GLN A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 GLN A 9
REMARK 465 ASN A 10
REMARK 465 ASN A 11
REMARK 465 SER A 12
REMARK 465 SER A 13
REMARK 465 SER A 14
REMARK 465 ARG A 206
REMARK 465 GLY A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 THR A 210
REMARK 465 ARG A 211
REMARK 465 HIS A 212
REMARK 465 HIS A 213
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 HIS A 216
REMARK 465 HIS A 217
REMARK 465 GLN B 1
REMARK 465 THR B 204
REMARK 465 ARG B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 HIS B 211
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 ND2 ASN A 20 C2 NAG A 2000 2.06
REMARK 500 ND2 ASN B 73 C2 NAG B 730 2.10
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 B 174 C - N - CA ANGL. DEV. = 9.7 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 ASP A 85 25.15 47.20
REMARK 500 ALA A 144 57.72 39.52
REMARK 500 ASN A 168 36.26 -80.64
REMARK 500 ASN A 182 -105.94 -150.21
REMARK 500 THR A 195 1.65 -68.06
REMARK 500 VAL B 40 -144.93 72.10
REMARK 500 ARG B 63 -31.04 -131.04
REMARK 500 SER B 98 85.07 -153.06
REMARK 500 GLN B 99 -129.13 38.08
REMARK 500 PHE B 122 -128.55 -129.23
REMARK 500 ASP B 124 -44.71 66.05
REMARK 500 THR B 147 -51.66 63.26
REMARK 500 ILE B 149 159.46 77.24
REMARK 500 PRO B 174 76.21 -65.60
REMARK 500 LYS B 175 -81.94 -136.92
REMARK 500 SER B 198 -166.87 -111.24
REMARK 500 LEU B 199 109.89 -167.97
REMARK 500 LYS B 201 -86.99 -100.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BFE RELATED DB: PDB
REMARK 900 STRUCTURE OF THE EXTRACELLULAR PORTION OF MOUSE CD200RLA
REMARK 900 RELATED ID: 4BFG RELATED DB: PDB
REMARK 900 STRUCTURE OF THE EXTRACELLULAR PORTION OF MOUSE CD200R
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NUMBERING IN THE PDB IS BASED ON THE MATURE SEQUENCE AS
REMARK 999 DETERMINED BY N-TERMINAL SEQUENCING.
DBREF 4BFI A 2 204 UNP Q9ES57 MO2R1_MOUSE 26 228
DBREF 4BFI B 1 202 UNP O54901 OX2G_MOUSE 31 232
SEQADV 4BFI GLY A 205 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI ARG A 206 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI GLY A 207 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI GLY A 208 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI SER A 209 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI THR A 210 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI ARG A 211 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI HIS A 212 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI HIS A 213 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI HIS A 214 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI HIS A 215 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI HIS A 216 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI HIS A 217 UNP Q9ES57 EXPRESSION TAG
SEQADV 4BFI SER B 203 UNP O54901 EXPRESSION TAG
SEQADV 4BFI THR B 204 UNP O54901 EXPRESSION TAG
SEQADV 4BFI ARG B 205 UNP O54901 EXPRESSION TAG
SEQADV 4BFI HIS B 206 UNP O54901 EXPRESSION TAG
SEQADV 4BFI HIS B 207 UNP O54901 EXPRESSION TAG
SEQADV 4BFI HIS B 208 UNP O54901 EXPRESSION TAG
SEQADV 4BFI HIS B 209 UNP O54901 EXPRESSION TAG
SEQADV 4BFI HIS B 210 UNP O54901 EXPRESSION TAG
SEQADV 4BFI HIS B 211 UNP O54901 EXPRESSION TAG
SEQRES 1 A 216 THR ASP LYS ASN GLN THR THR GLN ASN ASN SER SER SER
SEQRES 2 A 216 PRO LEU THR GLN VAL ASN THR THR VAL SER VAL GLN ILE
SEQRES 3 A 216 GLY THR LYS ALA LEU LEU CYS CYS PHE SER ILE PRO LEU
SEQRES 4 A 216 THR LYS ALA VAL LEU ILE THR TRP ILE ILE LYS LEU ARG
SEQRES 5 A 216 GLY LEU PRO SER CYS THR ILE ALA TYR LYS VAL ASP THR
SEQRES 6 A 216 LYS THR ASN GLU THR SER CYS LEU GLY ARG ASN ILE THR
SEQRES 7 A 216 TRP ALA SER THR PRO ASP HIS SER PRO GLU LEU GLN ILE
SEQRES 8 A 216 SER ALA VAL THR LEU GLN HIS GLU GLY THR TYR THR CYS
SEQRES 9 A 216 GLU THR VAL THR PRO GLU GLY ASN PHE GLU LYS ASN TYR
SEQRES 10 A 216 ASP LEU GLN VAL LEU VAL PRO PRO GLU VAL THR TYR PHE
SEQRES 11 A 216 PRO GLU LYS ASN ARG SER ALA VAL CYS GLU ALA MET ALA
SEQRES 12 A 216 GLY LYS PRO ALA ALA GLN ILE SER TRP SER PRO ASP GLY
SEQRES 13 A 216 ASP CYS VAL THR THR SER GLU SER HIS SER ASN GLY THR
SEQRES 14 A 216 VAL THR VAL ARG SER THR CYS HIS TRP GLU GLN ASN ASN
SEQRES 15 A 216 VAL SER ASP VAL SER CYS ILE VAL SER HIS LEU THR GLY
SEQRES 16 A 216 ASN GLN SER LEU SER ILE GLU LEU GLY ARG GLY GLY SER
SEQRES 17 A 216 THR ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 B 211 GLN VAL GLU VAL VAL THR GLN ASP GLU ARG LYS ALA LEU
SEQRES 2 B 211 HIS THR THR ALA SER LEU ARG CYS SER LEU LYS THR SER
SEQRES 3 B 211 GLN GLU PRO LEU ILE VAL THR TRP GLN LYS LYS LYS ALA
SEQRES 4 B 211 VAL SER PRO GLU ASN MET VAL THR TYR SER LYS THR HIS
SEQRES 5 B 211 GLY VAL VAL ILE GLN PRO ALA TYR LYS ASP ARG ILE ASN
SEQRES 6 B 211 VAL THR GLU LEU GLY LEU TRP ASN SER SER ILE THR PHE
SEQRES 7 B 211 TRP ASN THR THR LEU GLU ASP GLU GLY CYS TYR MET CYS
SEQRES 8 B 211 LEU PHE ASN THR PHE GLY SER GLN LYS VAL SER GLY THR
SEQRES 9 B 211 ALA CYS LEU THR LEU TYR VAL GLN PRO ILE VAL HIS LEU
SEQRES 10 B 211 HIS TYR ASN TYR PHE GLU ASP HIS LEU ASN ILE THR CYS
SEQRES 11 B 211 SER ALA THR ALA ARG PRO ALA PRO ALA ILE SER TRP LYS
SEQRES 12 B 211 GLY THR GLY THR GLY ILE GLU ASN SER THR GLU SER HIS
SEQRES 13 B 211 PHE HIS SER ASN GLY THR THR SER VAL THR SER ILE LEU
SEQRES 14 B 211 ARG VAL LYS ASP PRO LYS THR GLN VAL GLY LYS GLU VAL
SEQRES 15 B 211 ILE CYS GLN VAL LEU TYR LEU GLY ASN VAL ILE ASP TYR
SEQRES 16 B 211 LYS GLN SER LEU ASP LYS GLY SER THR ARG HIS HIS HIS
SEQRES 17 B 211 HIS HIS HIS
MODRES 4BFI ASN A 20 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN A 69 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN A 77 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN A 168 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN A 197 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN B 65 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN B 73 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN B 80 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN B 127 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN B 151 ASN GLYCOSYLATION SITE
MODRES 4BFI ASN B 160 ASN GLYCOSYLATION SITE
HET NAG A 690 14
HET NAG A 770 14
HET EDO A1206 4
HET CYS A1207 7
HET NAG A1680 14
HET NAG A1970 14
HET NAG A2000 14
HET NAG B 650 14
HET NAG B 730 14
HET NAG B 800 14
HET NAG B1270 14
HET NAG B1510 14
HET NAG B1600 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CYS CYSTEINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 11(C8 H15 N O6)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 CYS C3 H7 N O2 S
FORMUL 16 HOH *27(H2 O)
HELIX 1 1 THR A 96 HIS A 99 5 4
HELIX 2 2 PRO B 58 LYS B 61 5 4
HELIX 3 3 THR B 82 GLU B 86 5 5
SHEET 1 AA 6 GLN A 18 GLN A 26 0
SHEET 2 AA 6 GLY A 112 LEU A 123 1 O GLU A 115 N VAL A 19
SHEET 3 AA 6 GLY A 101 THR A 109 -1 O GLY A 101 N LEU A 120
SHEET 4 AA 6 LEU A 45 LEU A 52 -1 O LEU A 45 N VAL A 108
SHEET 5 AA 6 THR A 59 LYS A 63 -1 O ILE A 60 N TRP A 48
SHEET 6 AA 6 THR A 68 THR A 71 -1 O THR A 68 N LYS A 63
SHEET 1 AB 3 ALA A 31 LEU A 33 0
SHEET 2 AB 3 HIS A 86 ILE A 92 -1 O LEU A 90 N LEU A 33
SHEET 3 AB 3 THR A 79 THR A 83 -1 O THR A 79 N GLN A 91
SHEET 1 AC 4 GLU A 127 GLU A 133 0
SHEET 2 AC 4 SER A 137 GLY A 145 -1 O SER A 137 N GLU A 133
SHEET 3 AC 4 VAL A 171 HIS A 178 -1 O VAL A 171 N GLY A 145
SHEET 4 AC 4 ASP A 158 SER A 165 -1 O ASP A 158 N HIS A 178
SHEET 1 AD 3 GLN A 150 SER A 154 0
SHEET 2 AD 3 ASP A 186 SER A 192 -1 O SER A 188 N SER A 154
SHEET 3 AD 3 GLN A 198 GLU A 203 -1 O GLN A 198 N VAL A 191
SHEET 1 BA 4 VAL B 4 THR B 6 0
SHEET 2 BA 4 ALA B 17 LEU B 23 -1 O SER B 22 N VAL B 5
SHEET 3 BA 4 ASN B 73 PHE B 78 -1 O SER B 74 N CYS B 21
SHEET 4 BA 4 ILE B 64 GLU B 68 -1 O ASN B 65 N THR B 77
SHEET 1 BB 2 GLU B 9 ALA B 12 0
SHEET 2 BB 2 THR B 104 TYR B 121 -1 O CYS B 106 N GLU B 9
SHEET 1 BC 5 GLY B 53 ILE B 56 0
SHEET 2 BC 5 GLU B 43 SER B 49 -1 O THR B 47 N VAL B 55
SHEET 3 BC 5 ILE B 31 LYS B 36 -1 O VAL B 32 N TYR B 48
SHEET 4 BC 5 GLY B 87 ASN B 94 -1 O MET B 90 N GLN B 35
SHEET 5 BC 5 LYS B 100 VAL B 101 -1 O VAL B 101 N PHE B 93
SHEET 1 BD 8 GLY B 53 ILE B 56 0
SHEET 2 BD 8 GLU B 43 SER B 49 -1 O THR B 47 N VAL B 55
SHEET 3 BD 8 ILE B 31 LYS B 36 -1 O VAL B 32 N TYR B 48
SHEET 4 BD 8 GLY B 87 ASN B 94 -1 O MET B 90 N GLN B 35
SHEET 5 BD 8 THR B 104 TYR B 121 -1 O ALA B 105 N TYR B 89
SHEET 6 BD 8 LEU B 126 ARG B 135 -1 O ASN B 127 N ASN B 120
SHEET 7 BD 8 THR B 163 ARG B 170 -1 O THR B 163 N ALA B 134
SHEET 8 BD 8 GLU B 150 PHE B 157 -1 O GLU B 150 N ARG B 170
SHEET 1 BE 6 GLY B 53 ILE B 56 0
SHEET 2 BE 6 GLU B 43 SER B 49 -1 O THR B 47 N VAL B 55
SHEET 3 BE 6 ILE B 31 LYS B 36 -1 O VAL B 32 N TYR B 48
SHEET 4 BE 6 GLY B 87 ASN B 94 -1 O MET B 90 N GLN B 35
SHEET 5 BE 6 THR B 104 TYR B 121 -1 O ALA B 105 N TYR B 89
SHEET 6 BE 6 GLU B 9 ALA B 12 -1 O GLU B 9 N THR B 108
SHEET 1 BF 2 LYS B 100 VAL B 101 0
SHEET 2 BF 2 GLY B 87 ASN B 94 -1 O PHE B 93 N VAL B 101
SHEET 1 BG 3 ALA B 139 TRP B 142 0
SHEET 2 BG 3 VAL B 182 TYR B 188 -1 O GLN B 185 N SER B 141
SHEET 3 BG 3 ASN B 191 GLN B 197 -1 O ASN B 191 N TYR B 188
SSBOND 1 CYS A 34 CYS A 1207 1555 1555 2.04
SSBOND 2 CYS A 35 CYS A 105 1555 1555 2.05
SSBOND 3 CYS A 58 CYS A 73 1555 1555 2.04
SSBOND 4 CYS A 140 CYS A 189 1555 1555 2.03
SSBOND 5 CYS A 159 CYS A 177 1555 1555 2.03
SSBOND 6 CYS B 21 CYS B 91 1555 1555 2.03
SSBOND 7 CYS B 88 CYS B 106 1555 1555 2.05
SSBOND 8 CYS B 130 CYS B 184 1555 1555 2.04
LINK ND2 ASN A 20 C1 NAG A2000 1555 1555 1.43
LINK ND2 ASN A 69 C1 NAG A 690 1555 1555 1.44
LINK ND2 ASN A 77 C1 NAG A 770 1555 1555 1.44
LINK ND2 ASN A 168 C1 NAG A1680 1555 1555 1.44
LINK ND2 ASN A 197 C1 NAG A1970 1555 1555 1.44
LINK ND2 ASN B 65 C1 NAG B 650 1555 1555 1.44
LINK ND2 ASN B 73 C1 NAG B 730 1555 1555 1.44
LINK ND2 ASN B 80 C1 NAG B 800 1555 1555 1.44
LINK ND2 ASN B 127 C1 NAG B1270 1555 1555 1.46
LINK ND2 ASN B 151 C1 NAG B1510 1555 1555 1.45
LINK ND2 ASN B 160 C1 NAG B1600 1555 1555 1.43
CISPEP 1 LYS A 146 PRO A 147 0 -6.95
CISPEP 2 SER A 154 PRO A 155 0 -0.34
CISPEP 3 ARG B 135 PRO B 136 0 2.12
CRYST1 128.170 128.170 116.080 90.00 90.00 90.00 P 43 21 2 8
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 0.007802 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007802 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008615 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
