HEADER DNA REPAIR 19-JUN-98 1BIX
TITLE THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1
TITLE 2 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC
TITLE 3 SITES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AP ENDONUCLEASE 1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.99.18;
COMPND 5 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: BL21 (DE3)
KEYWDS DNA REPAIR, ENDONUCLEASE, HAP1, REF-1, ABASIC SITE RECOGNITION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.GORMAN,S.MORERA,D.G.ROTHWELL,E.DE LA FORTELLE,C.D.MOL,J.A.TAINER,
AUTHOR 2 I.D.HICKSON,P.S.FREEMONT
REVDAT 4 07-FEB-24 1BIX 1 REMARK LINK
REVDAT 3 24-FEB-09 1BIX 1 VERSN
REVDAT 2 01-APR-03 1BIX 1 JRNL
REVDAT 1 22-JUN-99 1BIX 0
JRNL AUTH M.A.GORMAN,S.MORERA,D.G.ROTHWELL,E.DE LA FORTELLE,C.D.MOL,
JRNL AUTH 2 J.A.TAINER,I.D.HICKSON,P.S.FREEMONT
JRNL TITL THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE
JRNL TITL 2 HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE
JRNL TITL 3 AT DNA ABASIC SITES.
JRNL REF EMBO J. V. 16 6548 1997
JRNL REFN ISSN 0261-4189
JRNL PMID 9351835
JRNL DOI 10.1093/EMBOJ/16.21.6548
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.A.GORMAN
REMARK 1 TITL CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENZYME AP
REMARK 1 TITL 2 ENDONUCLEASE 1
REMARK 1 REF THESIS, THE OPEN UNIVERSITY 1998
REMARK 1 PUBL MILTON KEYES, ENG. : THE OPEN UNIVERSITY (THESIS)
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 15001
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) : 0.184
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1454
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1539
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 193
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2190
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 20.0
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) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.920
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.34
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.780
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : UNRESTRAINED
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 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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171811.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-96
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15089
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.11400
REMARK 200 R SYM FOR SHELL (I) : 0.11400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200 REPLACEMENT AND ANOMALOUS SCATTERING
REMARK 200 SOFTWARE USED: SHARP, X-PLOR 3.84
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 43.63000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.35050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 43.63000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.35050
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 400
REMARK 400 COMPOUND
REMARK 400 THE STRUCTURE IS A 35 AMINO ACID TRUNCATED FORM OF THE
REMARK 400 'NATIVE' MOLECULE.
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 LYS A 32
REMARK 465 ASN A 33
REMARK 465 ASP A 34
REMARK 465 LYS A 35
REMARK 465 GLU A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 GLY A 39
REMARK 465 GLU A 40
REMARK 465 GLY A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
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 LEU A 44 CG CD1 CD2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 SER A 100
REMARK 475 GLU A 101
REMARK 475 ASN A 102
REMARK 475 LYS A 103
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 109 CG CD OE1 NE2
REMARK 480 ASP A 124 CG OD1 OD2
REMARK 480 LYS A 125 CG CD CE NZ
REMARK 480 ARG A 202 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 224 CG CD CE NZ
REMARK 480 LYS A 227 CG CD CE NZ
REMARK 480 LYS A 228 CG CD CE NZ
REMARK 480 ASN A 272 CG OD1 ND2
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 ASP A 308 CB - CG - OD1 ANGL. DEV. = 6.6 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 GLU A 101 -171.45 172.89
REMARK 500 LYS A 125 91.12 -58.60
REMARK 500 SER A 129 -145.21 53.03
REMARK 500 VAL A 213 132.07 -170.79
REMARK 500 PHE A 232 29.33 -145.71
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 SM A 402 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 46 OE1
REMARK 620 2 GLU A 46 OE2 50.0
REMARK 620 3 ASP A 148 OD1 149.7 111.8
REMARK 620 4 GLU A 150 OE2 133.4 105.9 70.4
REMARK 620 5 GLU A 150 OE1 112.3 64.9 66.6 48.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 401 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 70 OD1
REMARK 620 2 GLU A 96 OE2 102.6
REMARK 620 3 GLU A 96 OE1 70.2 49.9
REMARK 620 4 HOH A 563 O 83.2 92.2 123.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 403 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 126 OE2
REMARK 620 2 LEU A 318 O 79.3
REMARK 620 3 LEU A 318 OXT 118.4 50.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SM A 400 SM
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 216 OE2
REMARK 620 2 GLU A 216 OE1 45.4
REMARK 620 3 GLU A 217 OE1 107.6 66.8
REMARK 620 4 GLU A 217 OE2 115.2 74.1 50.5
REMARK 620 5 GLU A 242 OE1 128.9 137.5 116.5 78.2
REMARK 620 6 GLN A 245 OE1 73.0 118.3 156.6 151.5 76.2
REMARK 620 7 HOH A 566 O 128.9 123.5 67.5 100.1 92.4 93.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PT A 404 PT
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 271 SD
REMARK 620 2 LYS A 276 NZ 130.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ROX
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CYS 65 HAS BEEN PROPOSED TO BE INVOLVED IN THE
REMARK 800 REDUCTIVE ACTIVATION OF A NUMBER OF TRANSCRIPTION FACTORS
REMARK 800 INCLUDING FOS/JUN AND P53.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SM A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SM A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SM A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SM A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT A 404
DBREF 1BIX A 32 318 UNP P27695 APEX1_HUMAN 31 317
SEQRES 1 A 287 LYS ASN ASP LYS GLU ALA ALA GLY GLU GLY PRO ALA LEU
SEQRES 2 A 287 TYR GLU ASP PRO PRO ASP GLN LYS THR SER PRO SER GLY
SEQRES 3 A 287 LYS PRO ALA THR LEU LYS ILE CYS SER TRP ASN VAL ASP
SEQRES 4 A 287 GLY LEU ARG ALA TRP ILE LYS LYS LYS GLY LEU ASP TRP
SEQRES 5 A 287 VAL LYS GLU GLU ALA PRO ASP ILE LEU CYS LEU GLN GLU
SEQRES 6 A 287 THR LYS CYS SER GLU ASN LYS LEU PRO ALA GLU LEU GLN
SEQRES 7 A 287 GLU LEU PRO GLY LEU SER HIS GLN TYR TRP SER ALA PRO
SEQRES 8 A 287 SER ASP LYS GLU GLY TYR SER GLY VAL GLY LEU LEU SER
SEQRES 9 A 287 ARG GLN CYS PRO LEU LYS VAL SER TYR GLY ILE GLY ASP
SEQRES 10 A 287 GLU GLU HIS ASP GLN GLU GLY ARG VAL ILE VAL ALA GLU
SEQRES 11 A 287 PHE ASP SER PHE VAL LEU VAL THR ALA TYR VAL PRO ASN
SEQRES 12 A 287 ALA GLY ARG GLY LEU VAL ARG LEU GLU TYR ARG GLN ARG
SEQRES 13 A 287 TRP ASP GLU ALA PHE ARG LYS PHE LEU LYS GLY LEU ALA
SEQRES 14 A 287 SER ARG LYS PRO LEU VAL LEU CYS GLY ASP LEU ASN VAL
SEQRES 15 A 287 ALA HIS GLU GLU ILE ASP LEU ARG ASN PRO LYS GLY ASN
SEQRES 16 A 287 LYS LYS ASN ALA GLY PHE THR PRO GLN GLU ARG GLN GLY
SEQRES 17 A 287 PHE GLY GLU LEU LEU GLN ALA VAL PRO LEU ALA ASP SER
SEQRES 18 A 287 PHE ARG HIS LEU TYR PRO ASN THR PRO TYR ALA TYR THR
SEQRES 19 A 287 PHE TRP THR TYR MET MET ASN ALA ARG SER LYS ASN VAL
SEQRES 20 A 287 GLY TRP ARG LEU ASP TYR PHE LEU LEU SER HIS SER LEU
SEQRES 21 A 287 LEU PRO ALA LEU CYS ASP SER LYS ILE ARG SER LYS ALA
SEQRES 22 A 287 LEU GLY SER ASP HIS CYS PRO ILE THR LEU TYR LEU ALA
SEQRES 23 A 287 LEU
HET SM A 400 1
HET SM A 401 1
HET SM A 402 1
HET SM A 403 1
HET PT A 404 1
HETNAM SM SAMARIUM (III) ION
HETNAM PT PLATINUM (II) ION
FORMUL 2 SM 4(SM 3+)
FORMUL 6 PT PT 2+
FORMUL 7 HOH *155(H2 O)
HELIX 1 1 LEU A 72 LYS A 77 1 6
HELIX 2 2 GLY A 80 GLU A 87 1 8
HELIX 3 3 ALA A 106 GLN A 109 5 4
HELIX 4 4 GLU A 149 HIS A 151 5 3
HELIX 5 5 ARG A 177 LEU A 179 5 3
HELIX 6 6 LEU A 182 ALA A 200 1 19
HELIX 7 7 GLU A 217 ASP A 219 5 3
HELIX 8 8 LYS A 224 ASN A 226 5 3
HELIX 9 9 PRO A 234 ALA A 246 1 13
HELIX 10 10 SER A 252 LEU A 256 1 5
HELIX 11 11 MET A 270 ASN A 272 5 3
HELIX 12 12 HIS A 289 ALA A 294 5 6
SHEET 1 A 6 HIS A 116 SER A 120 0
SHEET 2 A 6 VAL A 131 SER A 135 -1 N SER A 135 O HIS A 116
SHEET 3 A 6 ILE A 91 GLN A 95 -1 N LEU A 94 O GLY A 132
SHEET 4 A 6 LEU A 62 ASN A 68 1 N CYS A 65 O ILE A 91
SHEET 5 A 6 ILE A 312 LEU A 316 -1 N LEU A 316 O LEU A 62
SHEET 6 A 6 LEU A 295 ILE A 300 -1 N LYS A 299 O THR A 313
SHEET 1 B 5 LYS A 141 TYR A 144 0
SHEET 2 B 5 VAL A 157 GLU A 161 -1 N GLU A 161 O LYS A 141
SHEET 3 B 5 VAL A 166 TYR A 171 -1 N THR A 169 O ILE A 158
SHEET 4 B 5 LEU A 205 ASP A 210 1 N VAL A 206 O VAL A 166
SHEET 5 B 5 ASP A 283 LEU A 287 -1 N LEU A 286 O LEU A 207
LINK OE1 GLU A 46 SM SM A 402 3545 1555 2.29
LINK OE2 GLU A 46 SM SM A 402 3545 1555 2.86
LINK OD1 ASP A 70 SM SM A 401 1555 1555 2.52
LINK OE2 GLU A 96 SM SM A 401 1555 1555 2.32
LINK OE1 GLU A 96 SM SM A 401 1555 1555 2.75
LINK OE2 GLU A 126 SM SM A 403 1565 1555 2.54
LINK OD1 ASP A 148 SM SM A 402 1555 1555 2.39
LINK OE2 GLU A 150 SM SM A 402 1555 1555 2.61
LINK OE1 GLU A 150 SM SM A 402 1555 1555 2.71
LINK OE2 GLU A 216 SM SM A 400 1555 1555 2.97
LINK OE1 GLU A 216 SM SM A 400 1555 1555 2.71
LINK OE1 GLU A 217 SM SM A 400 1555 1555 2.35
LINK OE2 GLU A 217 SM SM A 400 1555 1555 2.68
LINK OE1 GLU A 242 SM SM A 400 2656 1555 2.57
LINK OE1 GLN A 245 SM SM A 400 2656 1555 2.18
LINK SD MET A 271 PT PT A 404 1555 1555 1.97
LINK NZ LYS A 276 PT PT A 404 1555 1555 2.92
LINK O LEU A 318 SM SM A 403 1555 1555 2.63
LINK OXT LEU A 318 SM SM A 403 1555 1555 2.57
LINK SM SM A 400 O HOH A 566 1555 2656 2.82
LINK SM SM A 401 O HOH A 563 1555 1555 2.79
CISPEP 1 VAL A 247 PRO A 248 0 -1.57
SITE 1 ROX 1 CYS A 65
SITE 1 AC1 5 GLU A 216 GLU A 217 GLU A 242 GLN A 245
SITE 2 AC1 5 HOH A 566
SITE 1 AC2 3 ASP A 70 GLU A 96 HOH A 563
SITE 1 AC3 3 GLU A 46 ASP A 148 GLU A 150
SITE 1 AC4 3 ASP A 124 GLU A 126 LEU A 318
SITE 1 AC5 2 MET A 271 LYS A 276
CRYST1 87.260 44.701 78.778 90.00 103.45 90.00 C 1 2 1 4
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 0.011460 0.000000 0.002741 0.00000
SCALE2 0.000000 0.022371 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013052 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
