HEADER REPLICATION CHAPERONE 17-AUG-06 2I32
TITLE STRUCTURE OF A HUMAN ASF1A-HIRA COMPLEX AND INSIGHTS INTO SPECIFICITY
TITLE 2 OF HISTONE CHAPERONE COMPLEX ASSEMBLY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTI-SILENCING FACTOR 1 PARALOG A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-157;
COMPND 5 SYNONYM: ASF1A PROTEIN, ASF1 ANTI-SILENCING FUNCTION 1 HOMOLOG A,
COMPND 6 HYPOTHETICAL PROTEIN FLJ22085, ANTI-SILENCING FUNCTION 1A, CGI-98
COMPND 7 PROTEIN, CIA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: HISTONE REGULATORY HOMOLOG A;
COMPND 11 CHAIN: E, F;
COMPND 12 FRAGMENT: RESIDUES 425-472;
COMPND 13 SYNONYM: HIRA PROTEIN, TUP1-LIKE ENHANCER OF SPLIT PROTEIN 1;
COMPND 14 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: ASF1A, DKFZP564E2182;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21_GOLD (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET_DUET (NOVAGEN);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HIRA, DGCR1, HIR, TUPLE1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21_GOLD(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: MODIFIED PCDF_DUET VECTOR (NOVAGEN)
KEYWDS HISTONE DEPOSITION, CHROMATIN REGULATION, HISTONE CHAPERONES, ASF1,
KEYWDS 2 HIRA, CAF-1, REPLICATION CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MARMORSTEIN,Y.TANG
REVDAT 5 30-AUG-23 2I32 1 SEQADV
REVDAT 4 18-OCT-17 2I32 1 REMARK
REVDAT 3 24-FEB-09 2I32 1 VERSN
REVDAT 2 07-NOV-06 2I32 1 JRNL
REVDAT 1 19-SEP-06 2I32 0
JRNL AUTH Y.TANG,M.V.POUSTOVOITOV,K.ZHAO,M.GARFINKEL,A.CANUTESCU,
JRNL AUTH 2 R.DUNBRACK,P.D.ADAMS,R.MARMORSTEIN
JRNL TITL STRUCTURE OF A HUMAN ASF1A-HIRA COMPLEX AND INSIGHTS INTO
JRNL TITL 2 SPECIFICITY OF HISTONE CHAPERONE COMPLEX ASSEMBLY.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 921 2006
JRNL REFN ISSN 1545-9993
JRNL PMID 16980972
JRNL DOI 10.1038/NSMB1147
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 43841
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) : 0.229
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1813
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 : 2780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.45100
REMARK 3 B22 (A**2) : -8.45100
REMARK 3 B33 (A**2) : 16.90100
REMARK 3 B12 (A**2) : -8.55600
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.421
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.464 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.561 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.133 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.275 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 41.49
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2I32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000039074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 5.6
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) : 0.980
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43841
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.64100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 1ROC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE HUMAN ASF1AN-HIRA(425
REMARK 280 -472) COMPLEX WERE GROWN BY HANGING DROP VAPOR DIFFUSION AT ROOM
REMARK 280 TEMPERATURE AND WERE OBTAINED BY MIXING 2 UL OF A 0.5 MM PROTEIN
REMARK 280 COMPLEX SOLUTION (IN 20 MM HEPES PH 7.0, 150 MM NACL AND 5 MM
REMARK 280 BETA-ME) WITH 2 UL OF RESERVOIR SOLUTION CONTAINING 1.44 M
REMARK 280 NAH2PO4 AND 0.16 M K2HPO4 AT PH 5.6, AND EQUILIBRATING OVER 1.0
REMARK 280 ML OF RESERVOIR SOLUTION. CRYSTALS WERE FULLY GROWN WITHIN TWO
REMARK 280 WEEKS TO A TYPICAL SIZE OF 0.3MMX0.3MMX0.2MM, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 111.73267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.86633
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 83.79950
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.93317
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 139.66583
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 111.73267
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 55.86633
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 27.93317
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 83.79950
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 139.66583
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 1460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 APPLY THE FOLLOWING TO CHAINS: B, 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 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 MET A -24
REMARK 465 GLY A -23
REMARK 465 SER A -22
REMARK 465 SER A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 ASP A -14
REMARK 465 TYR A -13
REMARK 465 ASP A -12
REMARK 465 ILE A -11
REMARK 465 PRO A -10
REMARK 465 THR A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 ASP A 155
REMARK 465 ASN A 156
REMARK 465 THR A 157
REMARK 465 MET B -24
REMARK 465 GLY B -23
REMARK 465 SER B -22
REMARK 465 SER B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 ASP B -14
REMARK 465 TYR B -13
REMARK 465 ASP B -12
REMARK 465 ILE B -11
REMARK 465 PRO B -10
REMARK 465 THR B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 ASP B 155
REMARK 465 ASN B 156
REMARK 465 THR B 157
REMARK 465 SER E 416
REMARK 465 GLU E 417
REMARK 465 ASN E 418
REMARK 465 LEU E 419
REMARK 465 TYR E 420
REMARK 465 PHE E 421
REMARK 465 GLN E 422
REMARK 465 GLY E 423
REMARK 465 SER E 424
REMARK 465 SER E 425
REMARK 465 ALA E 426
REMARK 465 THR E 427
REMARK 465 SER E 428
REMARK 465 VAL E 429
REMARK 465 ALA E 430
REMARK 465 GLY E 431
REMARK 465 VAL E 432
REMARK 465 VAL E 433
REMARK 465 ASN E 434
REMARK 465 GLY E 435
REMARK 465 GLU E 436
REMARK 465 SER E 437
REMARK 465 LEU E 438
REMARK 465 GLU E 439
REMARK 465 ASP E 440
REMARK 465 ILE E 441
REMARK 465 ARG E 442
REMARK 465 LYS E 443
REMARK 465 ASN E 444
REMARK 465 LEU E 445
REMARK 465 ALA E 467
REMARK 465 GLN E 468
REMARK 465 LEU E 469
REMARK 465 ASP E 470
REMARK 465 THR E 471
REMARK 465 GLY E 472
REMARK 465 SER F 416
REMARK 465 GLU F 417
REMARK 465 ASN F 418
REMARK 465 LEU F 419
REMARK 465 TYR F 420
REMARK 465 PHE F 421
REMARK 465 GLN F 422
REMARK 465 GLY F 423
REMARK 465 SER F 424
REMARK 465 SER F 425
REMARK 465 ALA F 426
REMARK 465 THR F 427
REMARK 465 SER F 428
REMARK 465 VAL F 429
REMARK 465 ALA F 430
REMARK 465 GLY F 431
REMARK 465 VAL F 432
REMARK 465 VAL F 433
REMARK 465 ASN F 434
REMARK 465 GLY F 435
REMARK 465 GLU F 436
REMARK 465 SER F 437
REMARK 465 LEU F 438
REMARK 465 GLU F 439
REMARK 465 ASP F 440
REMARK 465 ILE F 441
REMARK 465 ARG F 442
REMARK 465 LYS F 443
REMARK 465 ASN F 444
REMARK 465 LEU F 445
REMARK 465 LEU F 446
REMARK 465 LYS F 447
REMARK 465 LYS F 448
REMARK 465 CYS F 465
REMARK 465 ILE F 466
REMARK 465 ALA F 467
REMARK 465 GLN F 468
REMARK 465 LEU F 469
REMARK 465 ASP F 470
REMARK 465 THR F 471
REMARK 465 GLY F 472
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 LYS E 448 N - CA - C ANGL. DEV. = -19.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 33 120.69 -31.19
REMARK 500 GLU A 52 -8.84 -57.66
REMARK 500 ASN A 125 78.61 -115.96
REMARK 500 ASP B 13 67.85 37.44
REMARK 500 PRO B 15 -175.68 -64.43
REMARK 500 GLU B 32 141.13 -176.05
REMARK 500 ASP B 33 128.83 -26.69
REMARK 500 GLU B 49 -43.96 -148.92
REMARK 500 ARG B 102 54.31 39.48
REMARK 500 SER B 142 45.14 -86.31
REMARK 500 ASN B 143 58.08 -174.81
REMARK 500 TRP B 153 -73.27 -71.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2I32 A 1 157 UNP Q9Y294 Q9Y294_HUMAN 1 157
DBREF 2I32 B 1 157 UNP Q9Y294 Q9Y294_HUMAN 1 157
DBREF 2I32 E 425 472 UNP P54198 HIRA_HUMAN 425 472
DBREF 2I32 F 425 472 UNP P54198 HIRA_HUMAN 425 472
SEQADV 2I32 MET A -24 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLY A -23 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 SER A -22 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 SER A -21 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 HIS A -20 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS A -19 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS A -18 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS A -17 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS A -16 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS A -15 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 ASP A -14 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 TYR A -13 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 ASP A -12 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 ILE A -11 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 PRO A -10 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 THR A -9 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 THR A -8 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLU A -7 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 ASN A -6 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 LEU A -5 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 TYR A -4 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 PHE A -3 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLN A -2 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLY A -1 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 SER A 0 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 MET B -24 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLY B -23 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 SER B -22 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 SER B -21 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 HIS B -20 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS B -19 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS B -18 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS B -17 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS B -16 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 HIS B -15 UNP Q9Y294 EXPRESSION TAG
SEQADV 2I32 ASP B -14 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 TYR B -13 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 ASP B -12 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 ILE B -11 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 PRO B -10 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 THR B -9 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 THR B -8 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLU B -7 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 ASN B -6 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 LEU B -5 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 TYR B -4 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 PHE B -3 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLN B -2 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 GLY B -1 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 SER B 0 UNP Q9Y294 CLONING ARTIFACT
SEQADV 2I32 SER E 416 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 GLU E 417 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 ASN E 418 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 LEU E 419 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 TYR E 420 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 PHE E 421 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 GLN E 422 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 GLY E 423 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 SER E 424 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 SER F 416 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 GLU F 417 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 ASN F 418 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 LEU F 419 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 TYR F 420 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 PHE F 421 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 GLN F 422 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 GLY F 423 UNP P54198 CLONING ARTIFACT
SEQADV 2I32 SER F 424 UNP P54198 CLONING ARTIFACT
SEQRES 1 A 182 MET GLY SER SER HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 182 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY SER MET
SEQRES 3 A 182 ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP ASN
SEQRES 4 A 182 PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE THR
SEQRES 5 A 182 PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU TRP
SEQRES 6 A 182 LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU TYR
SEQRES 7 A 182 ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL PRO
SEQRES 8 A 182 ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA PRO
SEQRES 9 A 182 ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY VAL
SEQRES 10 A 182 THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN GLU
SEQRES 11 A 182 PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR THR
SEQRES 12 A 182 GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO ASP
SEQRES 13 A 182 PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN PRO
SEQRES 14 A 182 ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN THR
SEQRES 1 B 182 MET GLY SER SER HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 182 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY SER MET
SEQRES 3 B 182 ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL LEU ASP ASN
SEQRES 4 B 182 PRO SER PRO PHE TYR ASN PRO PHE GLN PHE GLU ILE THR
SEQRES 5 B 182 PHE GLU CYS ILE GLU ASP LEU SER GLU ASP LEU GLU TRP
SEQRES 6 B 182 LYS ILE ILE TYR VAL GLY SER ALA GLU SER GLU GLU TYR
SEQRES 7 B 182 ASP GLN VAL LEU ASP SER VAL LEU VAL GLY PRO VAL PRO
SEQRES 8 B 182 ALA GLY ARG HIS MET PHE VAL PHE GLN ALA ASP ALA PRO
SEQRES 9 B 182 ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA VAL GLY VAL
SEQRES 10 B 182 THR VAL VAL LEU ILE THR CYS THR TYR ARG GLY GLN GLU
SEQRES 11 B 182 PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR THR
SEQRES 12 B 182 GLU THR GLU LEU ARG GLU ASN PRO PRO VAL LYS PRO ASP
SEQRES 13 B 182 PHE SER LYS LEU GLN ARG ASN ILE LEU ALA SER ASN PRO
SEQRES 14 B 182 ARG VAL THR ARG PHE HIS ILE ASN TRP GLU ASP ASN THR
SEQRES 1 E 57 SER GLU ASN LEU TYR PHE GLN GLY SER SER ALA THR SER
SEQRES 2 E 57 VAL ALA GLY VAL VAL ASN GLY GLU SER LEU GLU ASP ILE
SEQRES 3 E 57 ARG LYS ASN LEU LEU LYS LYS GLN VAL GLU THR ARG THR
SEQRES 4 E 57 ALA ASP GLY ARG ARG ARG ILE THR PRO LEU CYS ILE ALA
SEQRES 5 E 57 GLN LEU ASP THR GLY
SEQRES 1 F 57 SER GLU ASN LEU TYR PHE GLN GLY SER SER ALA THR SER
SEQRES 2 F 57 VAL ALA GLY VAL VAL ASN GLY GLU SER LEU GLU ASP ILE
SEQRES 3 F 57 ARG LYS ASN LEU LEU LYS LYS GLN VAL GLU THR ARG THR
SEQRES 4 F 57 ALA ASP GLY ARG ARG ARG ILE THR PRO LEU CYS ILE ALA
SEQRES 5 F 57 GLN LEU ASP THR GLY
FORMUL 5 HOH *130(H2 O)
HELIX 1 1 SER A 50 GLU A 52 5 3
HELIX 2 2 ASN A 80 ILE A 84 5 5
HELIX 3 3 PRO A 85 VAL A 90 1 6
HELIX 4 4 GLU A 119 ASN A 125 1 7
HELIX 5 5 ASP A 131 SER A 133 5 3
HELIX 6 6 SER B 50 GLU B 52 5 3
HELIX 7 7 ASN B 80 ILE B 84 5 5
HELIX 8 8 PRO B 85 VAL B 90 1 6
HELIX 9 9 GLU B 119 ASN B 125 1 7
HELIX 10 10 ASP B 131 SER B 133 5 3
SHEET 1 A 4 VAL A 4 VAL A 11 0
SHEET 2 A 4 PHE A 22 CYS A 30 -1 O GLU A 29 N GLN A 5
SHEET 3 A 4 GLY A 68 ALA A 76 -1 O GLY A 68 N CYS A 30
SHEET 4 A 4 LEU E 464 CYS E 465 -1 O LEU E 464 N MET A 71
SHEET 1 B 4 SER A 16 PRO A 17 0
SHEET 2 B 4 LEU A 135 ILE A 139 -1 O ARG A 137 N SER A 16
SHEET 3 B 4 GLN A 104 TYR A 117 -1 N GLU A 116 O GLN A 136
SHEET 4 B 4 ARG A 145 ARG A 148 -1 O THR A 147 N ARG A 108
SHEET 1 C 8 SER A 16 PRO A 17 0
SHEET 2 C 8 LEU A 135 ILE A 139 -1 O ARG A 137 N SER A 16
SHEET 3 C 8 GLN A 104 TYR A 117 -1 N GLU A 116 O GLN A 136
SHEET 4 C 8 GLY A 91 TYR A 101 -1 N GLY A 91 O ASN A 115
SHEET 5 C 8 LEU A 38 VAL A 45 -1 N ILE A 43 O LEU A 96
SHEET 6 C 8 ASP A 54 VAL A 62 -1 O VAL A 60 N TRP A 40
SHEET 7 C 8 ARG E 459 THR E 462 1 O ILE E 461 N LEU A 61
SHEET 8 C 8 VAL E 450 ARG E 453 -1 N VAL E 450 O THR E 462
SHEET 1 D 3 VAL B 4 VAL B 11 0
SHEET 2 D 3 PHE B 22 CYS B 30 -1 O GLU B 25 N VAL B 10
SHEET 3 D 3 GLY B 68 ALA B 76 -1 O HIS B 70 N PHE B 28
SHEET 1 E 8 SER B 16 PRO B 17 0
SHEET 2 E 8 LEU B 135 ARG B 148 -1 O ARG B 137 N SER B 16
SHEET 3 E 8 GLN B 104 TYR B 117 -1 N GLU B 116 O GLN B 136
SHEET 4 E 8 GLY B 91 TYR B 101 -1 N THR B 93 O VAL B 113
SHEET 5 E 8 LEU B 38 VAL B 45 -1 N ILE B 43 O LEU B 96
SHEET 6 E 8 ASP B 54 VAL B 62 -1 O VAL B 62 N LEU B 38
SHEET 7 E 8 ARG F 459 THR F 462 1 O ILE F 461 N LEU B 61
SHEET 8 E 8 VAL F 450 ARG F 453 -1 N VAL F 450 O THR F 462
CISPEP 1 ASN A 14 PRO A 15 0 0.05
CISPEP 2 GLY A 63 PRO A 64 0 -0.37
CISPEP 3 ASN B 14 PRO B 15 0 -0.36
CISPEP 4 GLY B 63 PRO B 64 0 -0.23
CRYST1 116.226 116.226 167.599 90.00 90.00 120.00 P 65 2 2 24
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 0.008604 0.004967 0.000000 0.00000
SCALE2 0.000000 0.009935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005967 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
