HEADER IMMUNE SYSTEM 22-DEC-11 3V8C
TITLE CRYSTAL STRUCTURE OF MONOCLONAL HUMAN ANTI-RHESUS D FC IGG1
TITLE 2 T125(YB2/0) DOUBLE MUTANT (H310 AND H435 IN K)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IG GAMMA-1 CHAIN C REGION;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 119-330;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HUMAN, IGHG1;
SOURCE 6 EXPRESSION_SYSTEM: RATTUS NORVEGICUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: RAT;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10116;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EBV-TRANSFECTED B CELL CRL-1662;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: CMV PROMOTER;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCI-NEO
KEYWDS FC IGG1, FC-GAMMA RECEPTOR, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MENEZ,E.A.STURA,D.BOUREL,S.SIBERIL,S.JORIEUX,C.DE ROMEUF,
AUTHOR 2 F.DUCANCEL,W.H.FRIDMAN,J.L.TEILLAUD
REVDAT 6 13-SEP-23 3V8C 1 HETSYN
REVDAT 5 29-JUL-20 3V8C 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 08-OCT-14 3V8C 1 AUTHOR
REVDAT 3 28-AUG-13 3V8C 1 JRNL
REVDAT 2 22-AUG-12 3V8C 1 REMARK
REVDAT 1 22-FEB-12 3V8C 0
JRNL AUTH S.SIBERIL,R.MENEZ,S.JORIEUX,C.DE ROMEUF,D.BOUREL,
JRNL AUTH 2 W.H.FRIDMAN,F.DUCANCEL,E.A.STURA,J.L.TEILLAUD
JRNL TITL EFFECT OF ZINC ON HUMAN IGG1 AND ITS FC GAMMA R
JRNL TITL 2 INTERACTIONS.
JRNL REF IMMUNOL.LETT. V. 143 60 2012
JRNL REFN ISSN 0165-2478
JRNL PMID 22553781
REMARK 2
REMARK 2 RESOLUTION. 2.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13744
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) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.254
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 723
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) : 2.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 981
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3710
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.4450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3352
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 218
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.16000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : 3.09000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.460
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.398
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.921
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.850
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3661 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4981 ; 1.762 ; 2.028
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 419 ; 7.613 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;35.462 ;25.102
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 594 ;24.324 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.029 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 581 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2642 ; 0.008 ; 0.022
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): 2122 ; 0.823 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3487 ; 1.515 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1539 ; 1.373 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1494 ; 2.341 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 3V8C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9340
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14467
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.769
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : 0.13800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.34
REMARK 200 R MERGE FOR SHELL (I) : 1.11300
REMARK 200 R SYM FOR SHELL (I) : 0.85000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.220
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3V7M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% MPEG 5000; 21.5% ETHYLENE GLYCOL,
REMARK 280 0.1M SODIUM CACODYLATE, PH 5.1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.82500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.82500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.70000
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: 7490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 GLY B 236
REMARK 465 GLY B 446
REMARK 465 LYS B 447
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 GLN B 386 CG CD OE1 NE2
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 O4 NAG A 505 C2 GAL A 506 1.64
REMARK 500 O2 MAN C 1 O5 NAG C 2 1.65
REMARK 500 O4 NAG A 502 C1 MAN A 503 1.72
REMARK 500 NE2 GLN B 347 OH TYR B 349 1.98
REMARK 500 O4 NAG A 505 C1 GAL A 506 2.07
REMARK 500 O4 NAG A 502 C2 MAN A 503 2.17
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 A 257 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO B 346 C - N - CA ANGL. DEV. = 11.2 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 PRO A 244 157.07 -45.40
REMARK 500 ILE A 253 -19.64 -43.79
REMARK 500 SER A 267 144.15 -35.15
REMARK 500 ARG A 292 89.61 -40.68
REMARK 500 SER A 298 29.29 82.09
REMARK 500 ALA A 327 60.11 -108.41
REMARK 500 ASN A 384 75.07 33.68
REMARK 500 ASN A 390 58.19 -114.20
REMARK 500 ASP A 399 -169.71 -69.10
REMARK 500 ASP A 401 32.37 -76.53
REMARK 500 LEU A 406 149.10 179.20
REMARK 500 GLN A 419 1.51 -69.09
REMARK 500 TYR A 436 132.03 -177.79
REMARK 500 SER A 444 78.40 -110.60
REMARK 500 PRO B 238 -122.60 -90.44
REMARK 500 VAL B 262 122.24 -38.46
REMARK 500 ASP B 265 31.65 87.35
REMARK 500 PRO B 271 -101.93 -32.80
REMARK 500 VAL B 282 -156.75 -87.96
REMARK 500 HIS B 285 63.12 -150.07
REMARK 500 ASN B 286 35.25 -78.45
REMARK 500 ARG B 292 144.64 -37.06
REMARK 500 GLU B 293 -139.23 -117.09
REMARK 500 GLU B 294 -162.60 -117.03
REMARK 500 TYR B 296 -28.84 -158.79
REMARK 500 SER B 298 22.98 92.07
REMARK 500 LYS B 317 139.39 -33.61
REMARK 500 SER B 324 59.65 34.69
REMARK 500 LYS B 326 -83.01 -59.08
REMARK 500 ALA B 327 -80.98 50.21
REMARK 500 LEU B 328 -90.08 -114.82
REMARK 500 PRO B 329 -77.12 -91.01
REMARK 500 ARG B 355 -53.75 -28.93
REMARK 500 GLU B 357 0.65 -53.43
REMARK 500 THR B 359 31.44 -81.39
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 MAN C 1
REMARK 610 NAG A 501
REMARK 610 NAG A 502
REMARK 610 MAN A 503
REMARK 610 MAN A 504
REMARK 610 NAG A 505
REMARK 610 GAL A 506
REMARK 610 MAN A 507
REMARK 610 NAG A 508
REMARK 610 NAG B 501
REMARK 610 NAG B 502
REMARK 610 MAN B 503
REMARK 610 MAN B 504
REMARK 610 NAG B 505
REMARK 610 GAL B 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V7M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOCLONAL HUMAN ANTI-RHESUS D FC IGG1
REMARK 900 T125(YB2/0) IN THE PRESENCE OF ZN2+
REMARK 900 RELATED ID: 2J6E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN AUTOIMMUNE COMPLEX BETWEEN A HUMAN IGM
REMARK 900 RHEUMATOID FACTOR AND IGG1 FC REVEALS A NOVEL FC EPITOPE AND
REMARK 900 EVIDENCE FOR AFFINITY MATURATION
REMARK 900 RELATED ID: 3FJT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HUMAN FC FRAGMENT ENGINEERED FOR EXTENDED
REMARK 900 SERUM HALF-LIFE
DBREF 3V8C A 236 447 UNP P01857 IGHG1_HUMAN 119 330
DBREF 3V8C B 236 447 UNP P01857 IGHG1_HUMAN 119 330
SEQADV 3V8C LYS A 310 UNP P01857 HIS 193 ENGINEERED MUTATION
SEQADV 3V8C LYS A 435 UNP P01857 HIS 318 ENGINEERED MUTATION
SEQADV 3V8C LYS B 310 UNP P01857 HIS 193 ENGINEERED MUTATION
SEQADV 3V8C LYS B 435 UNP P01857 HIS 318 ENGINEERED MUTATION
SEQRES 1 A 212 GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS PRO LYS
SEQRES 2 A 212 ASP THR LEU MET ILE SER ARG THR PRO GLU VAL THR CYS
SEQRES 3 A 212 VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU VAL LYS
SEQRES 4 A 212 PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA
SEQRES 5 A 212 LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER THR TYR
SEQRES 6 A 212 ARG VAL VAL SER VAL LEU THR VAL LEU LYS GLN ASP TRP
SEQRES 7 A 212 LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN LYS
SEQRES 8 A 212 ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER LYS ALA
SEQRES 9 A 212 LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU PRO
SEQRES 10 A 212 PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL SER LEU
SEQRES 11 A 212 THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE ALA
SEQRES 12 A 212 VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN TYR
SEQRES 13 A 212 LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY SER PHE
SEQRES 14 A 212 PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER ARG TRP
SEQRES 15 A 212 GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS GLU
SEQRES 16 A 212 ALA LEU HIS ASN LYS TYR THR GLN LYS SER LEU SER LEU
SEQRES 17 A 212 SER PRO GLY LYS
SEQRES 1 B 212 GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS PRO LYS
SEQRES 2 B 212 ASP THR LEU MET ILE SER ARG THR PRO GLU VAL THR CYS
SEQRES 3 B 212 VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU VAL LYS
SEQRES 4 B 212 PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA
SEQRES 5 B 212 LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER THR TYR
SEQRES 6 B 212 ARG VAL VAL SER VAL LEU THR VAL LEU LYS GLN ASP TRP
SEQRES 7 B 212 LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN LYS
SEQRES 8 B 212 ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER LYS ALA
SEQRES 9 B 212 LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU PRO
SEQRES 10 B 212 PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL SER LEU
SEQRES 11 B 212 THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE ALA
SEQRES 12 B 212 VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN TYR
SEQRES 13 B 212 LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY SER PHE
SEQRES 14 B 212 PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER ARG TRP
SEQRES 15 B 212 GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS GLU
SEQRES 16 B 212 ALA LEU HIS ASN LYS TYR THR GLN LYS SER LEU SER LEU
SEQRES 17 B 212 SER PRO GLY LYS
HET MAN C 1 11
HET NAG C 2 14
HET NAG A 501 14
HET NAG A 502 14
HET GOL A 509 6
HET MAN A 503 11
HET GOL A 510 6
HET MAN A 504 11
HET NAG A 505 14
HET GAL A 506 11
HET MAN A 507 11
HET NAG A 508 14
HET NAG B 501 14
HET GOL B 509 6
HET NAG B 502 14
HET MAN B 503 11
HET MAN B 504 11
HET NAG B 505 14
HET GAL B 506 11
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
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 GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 3 MAN 6(C6 H12 O6)
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 11 GAL 2(C6 H12 O6)
FORMUL 21 HOH *98(H2 O)
HELIX 1 1 LYS A 246 MET A 252 1 7
HELIX 2 2 LEU A 309 ASN A 315 1 7
HELIX 3 3 ARG A 355 LYS A 360 5 6
HELIX 4 4 LYS A 414 GLN A 419 1 6
HELIX 5 5 PRO B 247 MET B 252 1 6
HELIX 6 6 GLN B 311 GLY B 316 1 6
HELIX 7 7 ARG B 355 THR B 359 5 5
HELIX 8 8 LYS B 414 GLY B 420 1 7
HELIX 9 9 LEU B 432 TYR B 436 5 5
SHEET 1 A 4 SER A 239 PHE A 243 0
SHEET 2 A 4 GLU A 258 VAL A 266 -1 O VAL A 262 N PHE A 241
SHEET 3 A 4 TYR A 300 THR A 307 -1 O VAL A 302 N VAL A 263
SHEET 4 A 4 LYS A 288 THR A 289 -1 N LYS A 288 O VAL A 305
SHEET 1 B 4 SER A 239 PHE A 243 0
SHEET 2 B 4 GLU A 258 VAL A 266 -1 O VAL A 262 N PHE A 241
SHEET 3 B 4 TYR A 300 THR A 307 -1 O VAL A 302 N VAL A 263
SHEET 4 B 4 GLU A 293 GLU A 294 -1 N GLU A 293 O ARG A 301
SHEET 1 C 4 VAL A 282 VAL A 284 0
SHEET 2 C 4 VAL A 273 VAL A 279 -1 N VAL A 279 O VAL A 282
SHEET 3 C 4 TYR A 319 ASN A 325 -1 O LYS A 322 N ASN A 276
SHEET 4 C 4 ILE A 332 ILE A 336 -1 O LYS A 334 N CYS A 321
SHEET 1 D 4 GLN A 347 LEU A 351 0
SHEET 2 D 4 GLN A 362 PHE A 372 -1 O LEU A 368 N TYR A 349
SHEET 3 D 4 PHE A 404 ASP A 413 -1 O LEU A 410 N LEU A 365
SHEET 4 D 4 TYR A 391 THR A 393 -1 N LYS A 392 O LYS A 409
SHEET 1 E 4 GLN A 347 LEU A 351 0
SHEET 2 E 4 GLN A 362 PHE A 372 -1 O LEU A 368 N TYR A 349
SHEET 3 E 4 PHE A 404 ASP A 413 -1 O LEU A 410 N LEU A 365
SHEET 4 E 4 VAL A 397 LEU A 398 -1 N VAL A 397 O PHE A 405
SHEET 1 F 4 GLN A 386 PRO A 387 0
SHEET 2 F 4 ALA A 378 SER A 383 -1 N SER A 383 O GLN A 386
SHEET 3 F 4 PHE A 423 MET A 428 -1 O SER A 426 N GLU A 380
SHEET 4 F 4 THR A 437 LEU A 441 -1 O LYS A 439 N CYS A 425
SHEET 1 G 3 GLU B 258 THR B 260 0
SHEET 2 G 3 VAL B 305 THR B 307 -1 O LEU B 306 N VAL B 259
SHEET 3 G 3 ALA B 287 LYS B 288 -1 N LYS B 288 O VAL B 305
SHEET 1 H 2 VAL B 263 VAL B 266 0
SHEET 2 H 2 TYR B 300 VAL B 302 -1 O VAL B 302 N VAL B 263
SHEET 1 I 3 ASN B 276 VAL B 279 0
SHEET 2 I 3 TYR B 319 LYS B 322 -1 O LYS B 322 N ASN B 276
SHEET 3 I 3 THR B 335 ILE B 336 -1 O ILE B 336 N TYR B 319
SHEET 1 J 4 GLN B 347 LEU B 351 0
SHEET 2 J 4 GLN B 362 PHE B 372 -1 O LYS B 370 N GLN B 347
SHEET 3 J 4 PHE B 404 ASP B 413 -1 O VAL B 412 N VAL B 363
SHEET 4 J 4 TYR B 391 THR B 393 -1 N LYS B 392 O LYS B 409
SHEET 1 K 4 GLN B 347 LEU B 351 0
SHEET 2 K 4 GLN B 362 PHE B 372 -1 O LYS B 370 N GLN B 347
SHEET 3 K 4 PHE B 404 ASP B 413 -1 O VAL B 412 N VAL B 363
SHEET 4 K 4 VAL B 397 LEU B 398 -1 N VAL B 397 O PHE B 405
SHEET 1 L 4 GLN B 386 PRO B 387 0
SHEET 2 L 4 ALA B 378 SER B 383 -1 N SER B 383 O GLN B 386
SHEET 3 L 4 PHE B 423 MET B 428 -1 O SER B 426 N GLU B 380
SHEET 4 L 4 THR B 437 LEU B 441 -1 O THR B 437 N VAL B 427
SSBOND 1 CYS A 261 CYS A 321 1555 1555 2.03
SSBOND 2 CYS A 367 CYS A 425 1555 1555 2.03
SSBOND 3 CYS B 261 CYS B 321 1555 1555 2.03
SSBOND 4 CYS B 367 CYS B 425 1555 1555 1.99
LINK O2 MAN C 1 C1 NAG C 2 1555 1555 1.53
CISPEP 1 TYR A 373 PRO A 374 0 -6.83
CISPEP 2 TYR B 373 PRO B 374 0 -8.46
CRYST1 49.540 79.400 139.650 90.00 90.00 90.00 P 21 21 21 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 0.020186 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
