HEADER IMMUNE SYSTEM 18-OCT-05 2BC4
TITLE CRYSTAL STRUCTURE OF HLA-DM
CAVEAT 2BC4 NAG E 1 HAS WRONG CHIRALITY AT ATOM C1 NAG F 1 HAS WRONG
CAVEAT 2 2BC4 CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: MHC CLASS II ANTIGEN DMA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;
COMPND 8 CHAIN: B, D;
COMPND 9 SYNONYM: MHC CLASS II ANTIGEN DMB;
COMPND 10 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: HLA-DMA, DMA, RING6;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE TRANSFECTION PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRMHA-3;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HLA-DMB, DMB, RING7;
SOURCE 16 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE TRANSFECTION PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PRMHA-3
KEYWDS MHC CLASS II, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.NICHOLSON,B.MORADI,N.P.SETH,X.XING,G.D.CUNY,R.L.STEIN,
AUTHOR 2 K.W.WUCHERPFENNIG
REVDAT 4 29-JUL-20 2BC4 1 CAVEAT COMPND REMARK HET
REVDAT 4 2 1 HETNAM FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 18-OCT-17 2BC4 1 REMARK
REVDAT 2 24-FEB-09 2BC4 1 VERSN
REVDAT 1 23-MAY-06 2BC4 0
JRNL AUTH M.J.NICHOLSON,B.MORADI,N.P.SETH,X.XING,G.D.CUNY,R.L.STEIN,
JRNL AUTH 2 K.W.WUCHERPFENNIG
JRNL TITL SMALL MOLECULES THAT ENHANCE THE CATALYTIC EFFICIENCY OF
JRNL TITL 2 HLA-DM.
JRNL REF J.IMMUNOL. V. 176 4208 2006
JRNL REFN ISSN 0022-1767
JRNL PMID 16547258
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 54814
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1477
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6143
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.13700
REMARK 3 B22 (A**2) : 4.40400
REMARK 3 B33 (A**2) : -2.26700
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.413
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 41.12
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CNS_TOPPAR:CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9195
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59797
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30900
REMARK 200 R SYM FOR SHELL (I) : 0.31000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.020
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: PDB ENTRY 1HDM (ALANINE SUBSTITUTION)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LITHIUM SULFATE, 0.3M AMMONIUM
REMARK 280 SULFATE, 0.1M SODIUM CITRATE BUFFER, PH 5.4, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
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 49.03400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.10350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.21000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.10350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.03400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.21000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 UNIT IS A HETERODIMER. THERE ARE 2
REMARK 300 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT (CHAINS A & B AND CHAINS C &
REMARK 300 D).
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: 6510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
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 APPLY THE FOLLOWING TO CHAINS: C, D, F
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 98.06800
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -54.21000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 55.10350
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 VAL A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 3
REMARK 465 ALA A 4
REMARK 465 PRO A 5
REMARK 465 THR A 6
REMARK 465 PRO A 7
REMARK 465 MET A 8
REMARK 465 TRP A 9
REMARK 465 PRO A 10
REMARK 465 ASP A 11
REMARK 465 ASP A 12
REMARK 465 LEU A 201
REMARK 465 LEU A 202
REMARK 465 GLU A 203
REMARK 465 ASP A 204
REMARK 465 TYR A 205
REMARK 465 LYS A 206
REMARK 465 ASP A 207
REMARK 465 ASP A 208
REMARK 465 ASP A 209
REMARK 465 ASP A 210
REMARK 465 LYS A 211
REMARK 465 GLY B 1
REMARK 465 GLY B 2
REMARK 465 SER B 194
REMARK 465 PRO B 195
REMARK 465 MET B 196
REMARK 465 GLN B 197
REMARK 465 THR B 198
REMARK 465 LEU B 199
REMARK 465 LYS B 200
REMARK 465 LYS B 201
REMARK 465 PRO B 202
REMARK 465 PRO B 203
REMARK 465 THR B 204
REMARK 465 PRO B 205
REMARK 465 PRO B 206
REMARK 465 PRO B 207
REMARK 465 GLU B 208
REMARK 465 PRO B 209
REMARK 465 GLU B 210
REMARK 465 THR B 211
REMARK 465 VAL C 1
REMARK 465 PRO C 2
REMARK 465 GLU C 3
REMARK 465 ALA C 4
REMARK 465 PRO C 5
REMARK 465 THR C 6
REMARK 465 PRO C 7
REMARK 465 MET C 8
REMARK 465 TRP C 9
REMARK 465 PRO C 10
REMARK 465 ASP C 11
REMARK 465 ASP C 207
REMARK 465 ASP C 208
REMARK 465 ASP C 209
REMARK 465 ASP C 210
REMARK 465 LYS C 211
REMARK 465 GLY D 1
REMARK 465 GLY D 2
REMARK 465 LYS D 200
REMARK 465 LYS D 201
REMARK 465 PRO D 202
REMARK 465 PRO D 203
REMARK 465 THR D 204
REMARK 465 PRO D 205
REMARK 465 PRO D 206
REMARK 465 PRO D 207
REMARK 465 GLU D 208
REMARK 465 PRO D 209
REMARK 465 GLU D 210
REMARK 465 THR D 211
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 ARG A 98 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG A 98 NE - CZ - NH1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 98 NE - CZ - NH2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG C 98 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG C 98 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG C 98 NE - CZ - NH2 ANGL. DEV. = -7.2 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 ASP A 38 -123.78 53.07
REMARK 500 ASP A 91 107.44 -58.28
REMARK 500 GLU A 181 128.71 -25.58
REMARK 500 ILE A 182 47.02 80.08
REMARK 500 GLU B 39 31.91 -76.98
REMARK 500 GLU B 40 -18.93 -160.54
REMARK 500 PRO B 124 -173.02 -66.18
REMARK 500 SER B 167 18.58 -143.14
REMARK 500 TYR B 168 -26.81 61.12
REMARK 500 LEU C 13 109.83 64.99
REMARK 500 ASP C 38 -124.31 54.84
REMARK 500 GLU C 65 128.17 -32.56
REMARK 500 ALA C 69 -62.61 -23.62
REMARK 500 GLU C 181 128.69 -24.78
REMARK 500 ILE C 182 47.15 79.89
REMARK 500 GLU D 39 21.67 -72.83
REMARK 500 GLU D 40 -13.67 -145.10
REMARK 500 PRO D 124 -174.50 -66.08
REMARK 500 HIS D 141 35.18 -83.30
REMARK 500 SER D 167 31.89 -143.37
REMARK 500 TYR D 168 -14.20 45.44
REMARK 500 ILE D 179 -9.57 -58.20
REMARK 500 PRO D 184 154.77 -47.08
REMARK 500 SER D 194 -45.19 -29.09
REMARK 500 THR D 198 -157.38 -146.10
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2BC4 A 1 203 GB 18765715 NP_006111 27 229
DBREF 2BC4 C 1 203 GB 18765715 NP_006111 27 229
DBREF 2BC4 B 1 200 GB 4504399 NP_002109 19 218
DBREF 2BC4 D 1 200 GB 4504399 NP_002109 19 218
SEQADV 2BC4 ASP A 204 GB 18765715 FLAG TAG
SEQADV 2BC4 TYR A 205 GB 18765715 FLAG TAG
SEQADV 2BC4 LYS A 206 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP A 207 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP A 208 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP A 209 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP A 210 GB 18765715 FLAG TAG
SEQADV 2BC4 LYS A 211 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP C 204 GB 18765715 FLAG TAG
SEQADV 2BC4 TYR C 205 GB 18765715 FLAG TAG
SEQADV 2BC4 LYS C 206 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP C 207 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP C 208 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP C 209 GB 18765715 FLAG TAG
SEQADV 2BC4 ASP C 210 GB 18765715 FLAG TAG
SEQADV 2BC4 LYS C 211 GB 18765715 FLAG TAG
SEQADV 2BC4 LYS B 201 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO B 202 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO B 203 GB 4504399 KT3 TAG
SEQADV 2BC4 THR B 204 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO B 205 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO B 206 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO B 207 GB 4504399 KT3 TAG
SEQADV 2BC4 GLU B 208 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO B 209 GB 4504399 KT3 TAG
SEQADV 2BC4 GLU B 210 GB 4504399 KT3 TAG
SEQADV 2BC4 THR B 211 GB 4504399 KT3 TAG
SEQADV 2BC4 LYS D 201 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO D 202 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO D 203 GB 4504399 KT3 TAG
SEQADV 2BC4 THR D 204 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO D 205 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO D 206 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO D 207 GB 4504399 KT3 TAG
SEQADV 2BC4 GLU D 208 GB 4504399 KT3 TAG
SEQADV 2BC4 PRO D 209 GB 4504399 KT3 TAG
SEQADV 2BC4 GLU D 210 GB 4504399 KT3 TAG
SEQADV 2BC4 THR D 211 GB 4504399 KT3 TAG
SEQRES 1 A 211 VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU
SEQRES 2 A 211 GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP
SEQRES 3 A 211 GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU
SEQRES 4 A 211 ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG
SEQRES 5 A 211 VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU
SEQRES 6 A 211 GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE
SEQRES 7 A 211 CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP
SEQRES 8 A 211 GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU
SEQRES 9 A 211 VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN
SEQRES 10 A 211 THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET
SEQRES 11 A 211 LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU
SEQRES 12 A 211 GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU
SEQRES 13 A 211 SER PHE GLN ALA PHE SER TYR LEU ASN PHE THR PRO GLU
SEQRES 14 A 211 PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE
SEQRES 15 A 211 ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN
SEQRES 16 A 211 ALA LEU PRO SER ASP LEU LEU GLU ASP TYR LYS ASP ASP
SEQRES 17 A 211 ASP ASP LYS
SEQRES 1 B 211 GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU
SEQRES 2 B 211 ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE
SEQRES 3 B 211 SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU
SEQRES 4 B 211 GLU ASN LYS MET ALA PRO CYS GLU PHE GLY VAL LEU ASN
SEQRES 5 B 211 SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS
SEQRES 6 B 211 ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN
SEQRES 7 B 211 CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR
SEQRES 8 B 211 ASN ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR
SEQRES 9 B 211 THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS
SEQRES 10 B 211 TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR
SEQRES 11 B 211 TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER
SEQRES 12 B 211 ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR
SEQRES 13 B 211 GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY
SEQRES 14 B 211 ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO
SEQRES 15 B 211 GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU SER PRO
SEQRES 16 B 211 MET GLN THR LEU LYS LYS PRO PRO THR PRO PRO PRO GLU
SEQRES 17 B 211 PRO GLU THR
SEQRES 1 C 211 VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU
SEQRES 2 C 211 GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP
SEQRES 3 C 211 GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU
SEQRES 4 C 211 ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG
SEQRES 5 C 211 VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU
SEQRES 6 C 211 GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE
SEQRES 7 C 211 CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP
SEQRES 8 C 211 GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU
SEQRES 9 C 211 VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN
SEQRES 10 C 211 THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET
SEQRES 11 C 211 LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU
SEQRES 12 C 211 GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU
SEQRES 13 C 211 SER PHE GLN ALA PHE SER TYR LEU ASN PHE THR PRO GLU
SEQRES 14 C 211 PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE
SEQRES 15 C 211 ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN
SEQRES 16 C 211 ALA LEU PRO SER ASP LEU LEU GLU ASP TYR LYS ASP ASP
SEQRES 17 C 211 ASP ASP LYS
SEQRES 1 D 211 GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU
SEQRES 2 D 211 ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE
SEQRES 3 D 211 SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU
SEQRES 4 D 211 GLU ASN LYS MET ALA PRO CYS GLU PHE GLY VAL LEU ASN
SEQRES 5 D 211 SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS
SEQRES 6 D 211 ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN
SEQRES 7 D 211 CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR
SEQRES 8 D 211 ASN ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR
SEQRES 9 D 211 THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS
SEQRES 10 D 211 TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR
SEQRES 11 D 211 TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER
SEQRES 12 D 211 ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR
SEQRES 13 D 211 GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY
SEQRES 14 D 211 ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO
SEQRES 15 D 211 GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU SER PRO
SEQRES 16 D 211 MET GLN THR LEU LYS LYS PRO PRO THR PRO PRO PRO GLU
SEQRES 17 D 211 PRO GLU THR
MODRES 2BC4 ASN A 15 ASN GLYCOSYLATION SITE
MODRES 2BC4 ASN C 15 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NDG E 2 14
HET BMA E 3 11
HET BMA E 4 11
HET NAG F 1 14
HET NDG F 2 14
HET BMA F 3 11
HET BMA F 4 11
HET CL A 503 1
HET CL B 501 1
HET CL C 504 1
HET CL D 502 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM CL CHLORIDE ION
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 5 NDG 2(C8 H15 N O6)
FORMUL 5 BMA 4(C6 H12 O6)
FORMUL 7 CL 4(CL 1-)
FORMUL 11 HOH *420(H2 O)
HELIX 1 1 LEU A 56 GLN A 64 5 9
HELIX 2 2 ASP A 68 GLN A 85 1 18
HELIX 3 3 LEU B 51 GLN B 64 1 14
HELIX 4 4 LYS B 65 ASN B 74 1 10
HELIX 5 5 ASN B 74 ASN B 92 1 19
HELIX 6 6 LEU C 56 GLU C 58 5 3
HELIX 7 7 PHE C 59 GLN C 64 1 6
HELIX 8 8 ASP C 68 ILE C 86 1 19
HELIX 9 9 LEU C 202 LYS C 206 5 5
HELIX 10 10 PRO D 38 ASN D 41 5 4
HELIX 11 11 LEU D 51 GLN D 64 1 14
HELIX 12 12 LYS D 65 ASN D 74 1 10
HELIX 13 13 ASN D 74 ASN D 92 1 19
HELIX 14 14 LEU D 193 PRO D 195 5 3
SHEET 1 A 8 THR A 51 PRO A 54 0
SHEET 2 A 8 ASP A 40 ASP A 46 -1 N ASP A 46 O THR A 51
SHEET 3 A 8 VAL A 31 TYR A 37 -1 N GLU A 35 O LEU A 42
SHEET 4 A 8 ASN A 15 GLN A 25 -1 N THR A 21 O SER A 34
SHEET 5 A 8 VAL B 4 ASP B 14 -1 O SER B 9 N HIS A 20
SHEET 6 A 8 PRO B 19 PHE B 28 -1 O LYS B 20 N LEU B 12
SHEET 7 A 8 ASP B 31 ASP B 37 -1 O THR B 34 N ILE B 26
SHEET 8 A 8 LYS B 42 PRO B 45 -1 O ALA B 44 N CYS B 35
SHEET 1 B 4 ILE A 102 THR A 107 0
SHEET 2 B 4 ASN A 117 LEU A 126 -1 O VAL A 120 N PHE A 106
SHEET 3 B 4 SER A 157 PHE A 166 -1 O LEU A 164 N LEU A 119
SHEET 4 B 4 PHE A 149 VAL A 153 -1 N PHE A 149 O PHE A 161
SHEET 1 C 4 VAL A 140 VAL A 142 0
SHEET 2 C 4 LEU A 131 HIS A 137 -1 N HIS A 137 O VAL A 140
SHEET 3 C 4 PHE A 174 HIS A 180 -1 O ILE A 177 N ASN A 134
SHEET 4 C 4 TYR A 185 TRP A 191 -1 O ALA A 187 N VAL A 178
SHEET 1 D 4 SER B 98 LYS B 103 0
SHEET 2 D 4 VAL B 113 PHE B 122 -1 O TYR B 118 N GLN B 100
SHEET 3 D 4 TYR B 156 LEU B 164 -1 O LEU B 164 N VAL B 113
SHEET 4 D 4 GLN B 149 PRO B 150 -1 N GLN B 149 O GLN B 157
SHEET 1 E 4 LYS B 136 VAL B 138 0
SHEET 2 E 4 THR B 128 LYS B 133 -1 N LYS B 133 O LYS B 136
SHEET 3 E 4 TYR B 172 GLU B 177 -1 O THR B 173 N ARG B 132
SHEET 4 E 4 ILE B 185 TRP B 189 -1 O ILE B 185 N VAL B 176
SHEET 1 F 8 THR C 51 PRO C 54 0
SHEET 2 F 8 ASP C 40 ASP C 46 -1 N ASP C 46 O THR C 51
SHEET 3 F 8 VAL C 31 TYR C 37 -1 N GLU C 35 O LEU C 42
SHEET 4 F 8 ASN C 15 GLN C 25 -1 N THR C 21 O SER C 34
SHEET 5 F 8 VAL D 4 ASP D 14 -1 O SER D 9 N HIS C 20
SHEET 6 F 8 PRO D 19 PHE D 28 -1 O LYS D 20 N LEU D 12
SHEET 7 F 8 ASP D 31 TRP D 36 -1 O THR D 34 N ILE D 26
SHEET 8 F 8 MET D 43 PRO D 45 -1 O ALA D 44 N CYS D 35
SHEET 1 G 4 ILE C 102 THR C 107 0
SHEET 2 G 4 ASN C 117 LEU C 126 -1 O VAL C 120 N PHE C 106
SHEET 3 G 4 SER C 157 PHE C 166 -1 O LEU C 164 N LEU C 119
SHEET 4 G 4 PHE C 145 VAL C 153 -1 N PHE C 145 O TYR C 163
SHEET 1 H 4 VAL C 140 VAL C 142 0
SHEET 2 H 4 LEU C 131 HIS C 137 -1 N HIS C 137 O VAL C 140
SHEET 3 H 4 PHE C 174 HIS C 180 -1 O ILE C 177 N ASN C 134
SHEET 4 H 4 TYR C 185 TRP C 191 -1 O ALA C 187 N VAL C 178
SHEET 1 I 2 SER C 199 ASP C 200 0
SHEET 2 I 2 GLN D 197 THR D 198 -1 O THR D 198 N SER C 199
SHEET 1 J 4 SER D 98 LYS D 103 0
SHEET 2 J 4 VAL D 113 PHE D 122 -1 O TYR D 118 N GLN D 100
SHEET 3 J 4 TYR D 156 LEU D 164 -1 O SER D 160 N CYS D 117
SHEET 4 J 4 GLN D 149 PRO D 150 -1 N GLN D 149 O GLN D 157
SHEET 1 K 4 LEU D 137 VAL D 138 0
SHEET 2 K 4 THR D 128 LYS D 133 -1 N TRP D 131 O VAL D 138
SHEET 3 K 4 TYR D 172 GLU D 177 -1 O VAL D 175 N THR D 130
SHEET 4 K 4 ILE D 185 TRP D 189 -1 O ARG D 187 N CYS D 174
SSBOND 1 CYS A 24 CYS A 79 1555 1555 2.04
SSBOND 2 CYS A 121 CYS A 176 1555 1555 2.03
SSBOND 3 CYS B 11 CYS B 79 1555 1555 2.04
SSBOND 4 CYS B 25 CYS B 35 1555 1555 2.04
SSBOND 5 CYS B 117 CYS B 174 1555 1555 2.03
SSBOND 6 CYS C 24 CYS C 79 1555 1555 2.03
SSBOND 7 CYS C 121 CYS C 176 1555 1555 2.03
SSBOND 8 CYS D 11 CYS D 79 1555 1555 2.04
SSBOND 9 CYS D 25 CYS D 35 1555 1555 2.04
SSBOND 10 CYS D 117 CYS D 174 1555 1555 2.03
LINK ND2 ASN A 15 C1 NAG E 1 1555 1555 1.46
LINK ND2 ASN C 15 C1 NAG F 1 1555 1555 1.46
LINK O4 NAG E 1 C1 NDG E 2 1555 1555 1.40
LINK O4 NDG E 2 C1 BMA E 3 1555 1555 1.39
LINK O3 BMA E 3 C1 BMA E 4 1555 1555 1.40
LINK O4 NAG F 1 C1 NDG F 2 1555 1555 1.40
LINK O4 NDG F 2 C1 BMA F 3 1555 1555 1.39
LINK O3 BMA F 3 C1 BMA F 4 1555 1555 1.40
CISPEP 1 SER A 28 PRO A 29 0 -0.33
CISPEP 2 PHE A 127 PRO A 128 0 -0.65
CISPEP 3 TYR B 123 PRO B 124 0 0.35
CISPEP 4 SER C 28 PRO C 29 0 -0.15
CISPEP 5 PHE C 127 PRO C 128 0 0.45
CISPEP 6 TYR D 123 PRO D 124 0 -0.84
CRYST1 98.068 108.420 110.207 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 0.010197 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009223 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009074 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
