HEADER IMMUNE SYSTEM 19-DEC-00 1HQR
TITLE CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-
TITLE 2 AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA-DR ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DRA*0101;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HLA-DR BETA CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: DRB5*0101;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: MYELIN BASIC PROTEIN;
COMPND 13 CHAIN: C;
COMPND 14 SYNONYM: MBP;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: STREPTOCOCCAL PYROGENIC EXOTOXIN C;
COMPND 18 CHAIN: D;
COMPND 19 SYNONYM: SPE-C;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;
SOURCE 22 ORGANISM_TAXID: 1314;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SUPERANTIGEN-MHC CLASS II COMPLEX, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LI,H.LI,N.DIMASI,P.SCHLIEVERT,R.MARIUZZA
REVDAT 4 24-FEB-09 1HQR 1 VERSN
REVDAT 3 01-APR-03 1HQR 1 JRNL
REVDAT 2 04-APR-01 1HQR 1 JRNL
REVDAT 1 03-JAN-01 1HQR 0
JRNL AUTH Y.LI,H.LI,N.DIMASI,J.K.MCCORMICK,R.MARTIN,P.SCHUCK,
JRNL AUTH 2 P.M.SCHLIEVERT,R.A.MARIUZZA
JRNL TITL CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE
JRNL TITL 2 HIGH-AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II.
JRNL REF IMMUNITY V. 14 93 2001
JRNL REFN ISSN 1074-7613
JRNL PMID 11163233
JRNL DOI 10.1016/S1074-7613(01)00092-9
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.4
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1943820.410
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 11585
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) : 0.224
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1187
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1715
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 12.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 234
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4538
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.45000
REMARK 3 B22 (A**2) : -14.05000
REMARK 3 B33 (A**2) : 1.59000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.38
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) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.87
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 10.110; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 15.290; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 10.900; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 15.390; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 69.48
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HQR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-00.
REMARK 100 THE RCSB ID CODE IS RCSB012528.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
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 : 11585
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
REMARK 200 R SYM FOR SHELL (I) : 0.36000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 400, SODIUM
REMARK 280 CACODYLATE, ZNCL, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.91350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.97500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 108.30850
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.91350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.97500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 108.30850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.91350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.97500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 108.30850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.91350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.97500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 108.30850
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ILE A 1
REMARK 465 LYS A 2
REMARK 465 THR A 130
REMARK 465 GLY B 201
REMARK 465 ARG B 305
REMARK 465 THR B 306
REMARK 465 GLN B 307
REMARK 465 THR B 308
REMARK 465 LEU B 309
REMARK 465 GLN B 310
REMARK 465 HIS B 311
REMARK 465 SER B 367
REMARK 465 GLY B 368
REMARK 465 ARG C 416
REMARK 465 THR C 417
REMARK 465 PRO C 418
REMARK 465 ASP D 501
REMARK 465 SER D 502
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 GLU A 3 CG CD OE1 OE2
REMARK 470 LYS A 39 CD CE NZ
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 LYS A 67 CD CE NZ
REMARK 470 LYS A 75 CE NZ
REMARK 470 LEU A 92 CG CD1 CD2
REMARK 470 GLU A 98 CD OE1 OE2
REMARK 470 THR A 120 OG1 CG2
REMARK 470 ARG A 123 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 THR A 129 O
REMARK 470 VAL A 132 CG1 CG2
REMARK 470 SER A 133 OG
REMARK 470 ARG A 164 CZ NH1 NH2
REMARK 470 GLU A 172 CG CD OE1 OE2
REMARK 470 LYS A 176 CD CE NZ
REMARK 470 ASP A 181 O CG OD1 OD2
REMARK 470 THR B 203 OG1 CG2
REMARK 470 ASN B 219 OD1 ND2
REMARK 470 GLU B 259 CG CD OE1 OE2
REMARK 470 GLN B 264 CG CD OE1 NE2
REMARK 470 GLU B 269 CG CD OE1 OE2
REMARK 470 GLU B 296 CG CD OE1 OE2
REMARK 470 LYS B 298 CD CE NZ
REMARK 470 HIS B 312 CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 313 CG OD1 ND2
REMARK 470 LEU B 315 CG CD1 CD2
REMARK 470 VAL B 316 CG1 CG2
REMARK 470 SER B 326 OG
REMARK 470 GLU B 328 CG CD OE1 OE2
REMARK 470 ARG B 330 CG CD NE CZ NH1 NH2
REMARK 470 SER B 335 OG
REMARK 470 GLN B 336 CG CD OE1 NE2
REMARK 470 GLU B 337 CG CD OE1 OE2
REMARK 470 LYS B 339 CG CD CE NZ
REMARK 470 GLN B 349 CD OE1 NE2
REMARK 470 GLU B 362 CG CD OE1 OE2
REMARK 470 PRO B 365 CG CD
REMARK 470 ARG B 366 O CG CD NE CZ NH1 NH2
REMARK 470 GLN B 374 CG CD OE1 NE2
REMARK 470 GLU B 376 CG CD OE1 OE2
REMARK 470 VAL B 380 CG1 CG2
REMARK 470 VAL B 386 CG1 CG2
REMARK 470 GLU B 387 CG CD OE1 OE2
REMARK 470 ARG B 389 NE CZ NH1 NH2
REMARK 470 LYS D 503 N CA CB CG CD CE NZ
REMARK 470 LYS D 510 CG CD CE NZ
REMARK 470 SER D 532 OG
REMARK 470 HIS D 535 CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 540 CG OD1 OD2
REMARK 470 LYS D 547 CD CE NZ
REMARK 470 SER D 552 OG
REMARK 470 SER D 560 OG
REMARK 470 GLN D 561 CG CD OE1 NE2
REMARK 470 LYS D 562 CE NZ
REMARK 470 ASP D 566 CG OD1 OD2
REMARK 470 LYS D 597 CD CE NZ
REMARK 470 SER D 609 OG
REMARK 470 LYS D 619 CG CD CE NZ
REMARK 470 LYS D 666 CG CD CE NZ
REMARK 470 GLN D 669 CG CD OE1 NE2
REMARK 470 GLU D 678 CG CD OE1 OE2
REMARK 470 LYS D 689 CG CD CE NZ
REMARK 470 LYS D 708 CG CD CE NZ
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 NH2 ARG A 44 O GLY B 351 2.15
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 27 15.33 38.32
REMARK 500 GLU A 46 -30.45 -37.64
REMARK 500 GLU A 55 96.27 -59.58
REMARK 500 ARG A 76 -31.56 -38.65
REMARK 500 TYR A 79 68.08 31.16
REMARK 500 PRO A 81 -167.15 -59.09
REMARK 500 THR A 90 137.28 168.86
REMARK 500 LEU A 99 126.04 -20.92
REMARK 500 ARG A 100 -36.40 66.60
REMARK 500 PRO A 102 141.86 -31.42
REMARK 500 PRO A 115 64.92 -61.09
REMARK 500 ASN A 124 -36.64 67.27
REMARK 500 VAL A 132 -176.78 -66.76
REMARK 500 SER A 133 107.45 149.59
REMARK 500 PHE A 137 106.80 -53.44
REMARK 500 GLU A 141 -14.94 -44.46
REMARK 500 LEU A 151 111.32 -160.69
REMARK 500 PRO A 155 150.41 -38.03
REMARK 500 SER A 156 -142.97 -154.80
REMARK 500 THR A 157 -20.38 -152.05
REMARK 500 TRP A 168 47.18 -74.94
REMARK 500 PRO A 173 153.31 -49.47
REMARK 500 TRP A 178 138.13 -174.43
REMARK 500 ASN B 219 71.46 51.30
REMARK 500 ASN B 233 -61.35 67.15
REMARK 500 GLN B 234 -17.51 -166.93
REMARK 500 PHE B 240 123.80 -171.57
REMARK 500 ASP B 243 -16.89 -41.98
REMARK 500 TYR B 260 -70.28 -62.01
REMARK 500 GLN B 264 72.14 -109.09
REMARK 500 LYS B 265 -46.13 -26.80
REMARK 500 ASP B 266 -89.43 -43.11
REMARK 500 PHE B 267 -22.80 -36.72
REMARK 500 ASP B 276 -70.64 -102.14
REMARK 500 TYR B 278 -60.21 -123.29
REMARK 500 GLU B 287 -62.66 -19.06
REMARK 500 THR B 290 -71.65 -129.10
REMARK 500 PRO B 297 -134.22 -63.22
REMARK 500 LYS B 298 107.96 165.40
REMARK 500 TYR B 323 138.01 -171.22
REMARK 500 PRO B 324 -175.84 -69.82
REMARK 500 ASN B 334 -45.65 59.62
REMARK 500 SER B 335 25.57 -169.04
REMARK 500 GLU B 338 91.72 -62.15
REMARK 500 ALA B 340 135.26 -174.94
REMARK 500 VAL B 370 102.84 -161.11
REMARK 500 PRO B 378 0.05 -47.23
REMARK 500 VAL B 380 106.71 -160.67
REMARK 500 LYS D 504 65.96 60.16
REMARK 500 ASP D 505 125.58 -36.64
REMARK 500 ASP D 526 79.37 60.78
REMARK 500 THR D 533 -141.78 -120.94
REMARK 500 THR D 534 -84.33 -103.88
REMARK 500 THR D 536 -166.36 -101.15
REMARK 500 LEU D 537 108.20 175.02
REMARK 500 THR D 541 36.54 -74.44
REMARK 500 TYR D 544 -65.21 -124.83
REMARK 500 ASP D 548 9.03 83.19
REMARK 500 TYR D 550 -170.87 -175.07
REMARK 500 SER D 560 -8.06 -58.14
REMARK 500 ARG D 565 154.36 -25.99
REMARK 500 ASP D 566 -11.14 67.33
REMARK 500 PHE D 572 85.13 -160.23
REMARK 500 ASN D 579 39.84 36.39
REMARK 500 SER D 580 55.41 -104.93
REMARK 500 HIS D 581 -115.62 71.49
REMARK 500 SER D 609 98.19 -52.57
REMARK 500 LEU D 616 47.59 -104.33
REMARK 500 ASN D 618 42.29 35.53
REMARK 500 ILE D 646 -9.94 -56.05
REMARK 500 TYR D 653 120.42 -20.18
REMARK 500 ASP D 671 129.29 -37.12
REMARK 500 ASN D 677 -148.72 57.38
REMARK 500 ASP D 690 -4.50 -51.51
REMARK 500 ASN D 691 24.00 41.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 709 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 281 ND1
REMARK 620 2 HIS D 667 NE2 114.8
REMARK 620 3 ASP D 703 OD2 114.2 102.4
REMARK 620 4 HIS D 701 NE2 98.3 132.1 93.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 709
DBREF 1HQR A 1 181 UNP P01903 2DRA_HUMAN 26 206
DBREF 1HQR B 201 390 UNP Q29703 Q29703_HUMAN 30 219
DBREF 1HQR C 406 418 UNP P02686 MBP_HUMAN 114 126
DBREF 1HQR D 501 708 UNP P13380 SPEC_STRPY 28 235
SEQRES 1 A 181 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 181 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 181 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 181 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 181 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 181 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 181 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 181 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 181 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 181 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 181 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 181 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 181 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 181 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES 1 B 190 GLY ASP THR ARG PRO ARG PHE LEU GLN GLN ASP LYS TYR
SEQRES 2 B 190 GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE
SEQRES 3 B 190 LEU HIS ARG ASP ILE TYR ASN GLN GLU GLU ASP LEU ARG
SEQRES 4 B 190 PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES 5 B 190 LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES 6 B 190 ASP PHE LEU GLU ASP ARG ARG ALA ALA VAL ASP THR TYR
SEQRES 7 B 190 CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES 8 B 190 GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO ALA
SEQRES 9 B 190 ARG THR GLN THR LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES 10 B 190 SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES 11 B 190 TRP PHE ARG ASN SER GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES 12 B 190 SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES 13 B 190 THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES 14 B 190 VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES 15 B 190 PRO LEU THR VAL GLU TRP ARG ALA
SEQRES 1 C 13 VAL HIS PHE PHE LYS ASN ILE VAL THR PRO ARG THR PRO
SEQRES 1 D 208 ASP SER LYS LYS ASP ILE SER ASN VAL LYS SER ASP LEU
SEQRES 2 D 208 LEU TYR ALA TYR THR ILE THR PRO TYR ASP TYR LYS ASP
SEQRES 3 D 208 CYS ARG VAL ASN PHE SER THR THR HIS THR LEU ASN ILE
SEQRES 4 D 208 ASP THR GLN LYS TYR ARG GLY LYS ASP TYR TYR ILE SER
SEQRES 5 D 208 SER GLU MET SER TYR GLU ALA SER GLN LYS PHE LYS ARG
SEQRES 6 D 208 ASP ASP HIS VAL ASP VAL PHE GLY LEU PHE TYR ILE LEU
SEQRES 7 D 208 ASN SER HIS THR GLY GLU TYR ILE TYR GLY GLY ILE THR
SEQRES 8 D 208 PRO ALA GLN ASN ASN LYS VAL ASN HIS LYS LEU LEU GLY
SEQRES 9 D 208 ASN LEU PHE ILE SER GLY GLU SER GLN GLN ASN LEU ASN
SEQRES 10 D 208 ASN LYS ILE ILE LEU GLU LYS ASP ILE VAL THR PHE GLN
SEQRES 11 D 208 GLU ILE ASP PHE LYS ILE ARG LYS TYR LEU MET ASP ASN
SEQRES 12 D 208 TYR LYS ILE TYR ASP ALA THR SER PRO TYR VAL SER GLY
SEQRES 13 D 208 ARG ILE GLU ILE GLY THR LYS ASP GLY LYS HIS GLU GLN
SEQRES 14 D 208 ILE ASP LEU PHE ASP SER PRO ASN GLU GLY THR ARG SER
SEQRES 15 D 208 ASP ILE PHE ALA LYS TYR LYS ASP ASN ARG ILE ILE ASN
SEQRES 16 D 208 MET LYS ASN PHE SER HIS PHE ASP ILE TYR LEU GLU LYS
HET ZN D 709 1
HETNAM ZN ZINC ION
FORMUL 5 ZN ZN 2+
HELIX 1 1 GLU A 47 PHE A 51 5 5
HELIX 2 2 GLU A 55 SER A 77 1 23
HELIX 3 3 THR B 251 LEU B 253 5 3
HELIX 4 4 GLY B 254 ASN B 262 1 9
HELIX 5 5 GLN B 264 ALA B 273 1 10
HELIX 6 6 ALA B 273 TYR B 278 1 6
HELIX 7 7 TYR B 278 GLU B 287 1 10
HELIX 8 8 SER B 288 THR B 290 5 3
HELIX 9 9 ASP D 505 THR D 518 1 14
HELIX 10 10 SER D 556 GLN D 561 1 6
HELIX 11 11 PHE D 629 LYS D 645 1 17
HELIX 12 12 THR D 680 PHE D 685 1 6
HELIX 13 13 ALA D 686 ASN D 691 5 6
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 O HIS A 33 N VAL A 42
SHEET 3 A 8 SER A 19 PHE A 26 -1 O PHE A 22 N VAL A 34
SHEET 4 A 8 HIS A 5 ASN A 15 -1 O ILE A 8 N ASP A 25
SHEET 5 A 8 PHE B 207 PHE B 218 -1 N PHE B 207 O ASN A 15
SHEET 6 A 8 ARG B 223 TYR B 232 -1 N ARG B 223 O PHE B 218
SHEET 7 A 8 GLU B 235 ASP B 241 -1 N GLU B 235 O TYR B 232
SHEET 8 A 8 TYR B 247 ALA B 249 -1 O ARG B 248 N ARG B 239
SHEET 1 B 4 VAL A 91 THR A 93 0
SHEET 2 B 4 ASN A 103 PHE A 112 -1 N ILE A 106 O LEU A 92
SHEET 3 B 4 PHE A 145 PHE A 153 -1 N PHE A 145 O PHE A 112
SHEET 4 B 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 C 4 LYS A 126 VAL A 128 0
SHEET 2 C 4 ASN A 118 ARG A 123 -1 O TRP A 121 N VAL A 128
SHEET 3 C 4 TYR A 161 GLU A 166 -1 O ASP A 162 N LEU A 122
SHEET 4 C 4 HIS A 177 TRP A 178 -1 O TRP A 178 N TYR A 161
SHEET 1 D 4 VAL B 299 TYR B 302 0
SHEET 2 D 4 ASN B 313 PHE B 322 -1 N VAL B 316 O TYR B 302
SHEET 3 D 4 PHE B 355 THR B 363 -1 N PHE B 355 O PHE B 322
SHEET 4 D 4 VAL B 342 SER B 344 -1 O VAL B 343 N MET B 360
SHEET 1 E 4 VAL B 299 TYR B 302 0
SHEET 2 E 4 ASN B 313 PHE B 322 -1 N VAL B 316 O TYR B 302
SHEET 3 E 4 PHE B 355 THR B 363 -1 N PHE B 355 O PHE B 322
SHEET 4 E 4 ILE B 348 GLN B 349 -1 N ILE B 348 O GLN B 356
SHEET 1 F 4 GLN B 336 GLU B 337 0
SHEET 2 F 4 GLU B 328 ARG B 333 -1 N ARG B 333 O GLN B 336
SHEET 3 F 4 VAL B 370 HIS B 377 -1 O THR B 372 N PHE B 332
SHEET 4 F 4 VAL B 380 ARG B 389 -1 N VAL B 380 O HIS B 377
SHEET 1 G 6 TYR D 585 TYR D 587 0
SHEET 2 G 6 ILE D 551 GLU D 554 1 O SER D 552 N ILE D 586
SHEET 3 G 6 ASN D 538 ASP D 540 -1 N ILE D 539 O ILE D 551
SHEET 4 G 6 CYS D 527 VAL D 529 -1 O ARG D 528 N ASP D 540
SHEET 5 G 6 HIS D 568 VAL D 571 -1 O VAL D 569 N CYS D 527
SHEET 6 G 6 ILE D 590 PRO D 592 -1 O THR D 591 N ASP D 570
SHEET 1 H 2 HIS D 600 LYS D 601 0
SHEET 2 H 2 ILE D 621 LEU D 622 -1 O LEU D 622 N HIS D 600
SHEET 1 I 3 GLY D 604 SER D 609 0
SHEET 2 I 3 PHE D 699 GLU D 707 1 O PHE D 702 N ASN D 605
SHEET 3 I 3 SER D 655 THR D 662 -1 O SER D 655 N GLU D 707
SHEET 1 J 2 ILE D 626 THR D 628 0
SHEET 2 J 2 ILE D 693 ASN D 695 -1 O ILE D 694 N VAL D 627
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 215 CYS B 279 1555 1555 2.03
SSBOND 3 CYS B 317 CYS B 373 1555 1555 2.03
LINK ZN ZN D 709 ND1 HIS B 281 1555 1555 1.93
LINK ZN ZN D 709 NE2 HIS D 667 1555 1555 2.12
LINK ZN ZN D 709 OD2 ASP D 703 1555 1555 1.92
LINK ZN ZN D 709 NE2 HIS D 701 1555 1555 2.14
CISPEP 1 ASN A 15 PRO A 16 0 -0.10
CISPEP 2 TYR B 323 PRO B 324 0 0.56
SITE 1 AC1 4 HIS B 281 HIS D 667 HIS D 701 ASP D 703
CRYST1 61.827 111.950 216.617 90.00 90.00 90.00 I 2 2 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 0.016174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008933 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004616 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
