HEADER TRANSCRIPTION 09-MAY-07 2PUY
TITLE CRYSTAL STRUCTURE OF THE BHC80 PHD FINGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHD FINGER PROTEIN 21A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PHD FINGER RESIDUES: 486-543;
COMPND 5 SYNONYM: BRAF35-HDAC COMPLEX PROTEIN BHC80, BHC80A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE H3;
COMPND 9 CHAIN: E;
COMPND 10 FRAGMENT: H3 1-10;
COMPND 11 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: PHF21A, BHC80, KIAA1696;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHESIZED PEPTIDE
KEYWDS PHD FINGER, HISTONE CODE, BRAF-HDAC COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.HORTON,X.CHENG,R.E.COLLINS
REVDAT 4 21-FEB-24 2PUY 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2PUY 1 VERSN
REVDAT 2 20-NOV-07 2PUY 1 JRNL
REVDAT 1 14-AUG-07 2PUY 0
JRNL AUTH F.LAN,R.E.COLLINS,R.DE CEGLI,R.ALPATOV,J.R.HORTON,X.SHI,
JRNL AUTH 2 O.GOZANI,X.CHENG,Y.SHI
JRNL TITL RECOGNITION OF UNMETHYLATED HISTONE H3 LYSINE 4 LINKS BHC80
JRNL TITL 2 TO LSD1-MEDIATED GENE REPRESSION.
JRNL REF NATURE V. 448 718 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 17687328
JRNL DOI 10.1038/NATURE06034
REMARK 2
REMARK 2 RESOLUTION. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23287
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) : 0.206
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1114
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) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE : 0.2080
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 98
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 : 1018
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.84000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : -0.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.41000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : -0.0
REMARK 3 LOW RESOLUTION CUTOFF (A) : 40.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
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) : 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 : 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 173
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 : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97917, 1.28295, 1.28341
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23287
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.23700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ISOPROPANOL, 5-10% POLYETHYLENE
REMARK 280 GLYCOL 4000, 100MM MES 6.2-6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K, PH 6.5
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 39.75550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 12.69300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.75550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 12.69300
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: TRIMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 43 LIES ON A SPECIAL POSITION.
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 HIS A 484
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 541 CG CD OE1 OE2
REMARK 470 ILE A 543 CG1 CG2 CD1
REMARK 470 GLU B 541 CG CD OE1 OE2
REMARK 470 ILE B 543 CG1 CG2 CD1
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 A 355 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 491 SG
REMARK 620 2 CYS A 494 SG 113.1
REMARK 620 3 HIS A 511 ND1 101.5 95.4
REMARK 620 4 CYS A 514 SG 115.0 114.5 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 356 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 503 SG
REMARK 620 2 CYS A 506 SG 112.1
REMARK 620 3 CYS A 529 SG 107.9 108.0
REMARK 620 4 CYS A 532 SG 110.9 103.7 114.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 357 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 491 SG
REMARK 620 2 CYS B 494 SG 111.0
REMARK 620 3 HIS B 511 ND1 102.9 94.2
REMARK 620 4 CYS B 514 SG 112.4 118.5 115.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 358 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 503 SG
REMARK 620 2 CYS B 506 SG 113.5
REMARK 620 3 CYS B 529 SG 106.0 108.6
REMARK 620 4 CYS B 532 SG 111.3 103.2 114.5
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 A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 358
DBREF 2PUY A 486 543 UNP Q96BD5 PF21A_HUMAN 486 543
DBREF 2PUY B 486 543 UNP Q96BD5 PF21A_HUMAN 486 543
DBREF 2PUY E 1 10 UNP P61836 H3_ZYGBA 2 11
SEQADV 2PUY HIS A 484 UNP Q96BD5 EXPRESSION TAG
SEQADV 2PUY MET A 485 UNP Q96BD5 EXPRESSION TAG
SEQADV 2PUY HIS B 484 UNP Q96BD5 EXPRESSION TAG
SEQADV 2PUY MET B 485 UNP Q96BD5 EXPRESSION TAG
SEQRES 1 A 60 HIS MET ILE HIS GLU ASP PHE CYS SER VAL CYS ARG LYS
SEQRES 2 A 60 SER GLY GLN LEU LEU MET CYS ASP THR CYS SER ARG VAL
SEQRES 3 A 60 TYR HIS LEU ASP CYS LEU ASP PRO PRO LEU LYS THR ILE
SEQRES 4 A 60 PRO LYS GLY MET TRP ILE CYS PRO ARG CYS GLN ASP GLN
SEQRES 5 A 60 MET LEU LYS LYS GLU GLU ALA ILE
SEQRES 1 B 60 HIS MET ILE HIS GLU ASP PHE CYS SER VAL CYS ARG LYS
SEQRES 2 B 60 SER GLY GLN LEU LEU MET CYS ASP THR CYS SER ARG VAL
SEQRES 3 B 60 TYR HIS LEU ASP CYS LEU ASP PRO PRO LEU LYS THR ILE
SEQRES 4 B 60 PRO LYS GLY MET TRP ILE CYS PRO ARG CYS GLN ASP GLN
SEQRES 5 B 60 MET LEU LYS LYS GLU GLU ALA ILE
SEQRES 1 E 10 ALA ARG THR LYS GLN THR ALA ARG LYS SER
HET ZN A 355 1
HET ZN A 356 1
HET ZN B 357 1
HET ZN B 358 1
HETNAM ZN ZINC ION
FORMUL 4 ZN 4(ZN 2+)
FORMUL 8 HOH *88(H2 O)
HELIX 1 1 HIS A 511 LEU A 515 5 5
HELIX 2 2 CYS A 529 LYS A 539 1 11
HELIX 3 3 HIS B 511 LEU B 515 5 5
HELIX 4 4 CYS B 529 ILE B 543 1 15
SHEET 1 A 2 LEU A 501 MET A 502 0
SHEET 2 A 2 VAL A 509 TYR A 510 -1 O TYR A 510 N LEU A 501
SHEET 1 B 3 VAL B 509 TYR B 510 0
SHEET 2 B 3 GLY B 498 MET B 502 -1 N LEU B 501 O TYR B 510
SHEET 3 B 3 THR E 3 THR E 6 -1 O LYS E 4 N LEU B 500
LINK ZN ZN A 355 SG CYS A 491 1555 1555 2.38
LINK ZN ZN A 355 SG CYS A 494 1555 1555 2.30
LINK ZN ZN A 355 ND1 HIS A 511 1555 1555 2.12
LINK ZN ZN A 355 SG CYS A 514 1555 1555 2.26
LINK ZN ZN A 356 SG CYS A 503 1555 1555 2.31
LINK ZN ZN A 356 SG CYS A 506 1555 1555 2.36
LINK ZN ZN A 356 SG CYS A 529 1555 1555 2.41
LINK ZN ZN A 356 SG CYS A 532 1555 1555 2.27
LINK ZN ZN B 357 SG CYS B 491 1555 1555 2.29
LINK ZN ZN B 357 SG CYS B 494 1555 1555 2.31
LINK ZN ZN B 357 ND1 HIS B 511 1555 1555 2.11
LINK ZN ZN B 357 SG CYS B 514 1555 1555 2.30
LINK ZN ZN B 358 SG CYS B 503 1555 1555 2.33
LINK ZN ZN B 358 SG CYS B 506 1555 1555 2.33
LINK ZN ZN B 358 SG CYS B 529 1555 1555 2.36
LINK ZN ZN B 358 SG CYS B 532 1555 1555 2.32
CISPEP 1 ASP A 516 PRO A 517 0 0.20
CISPEP 2 ASP B 516 PRO B 517 0 -0.19
SITE 1 AC1 4 CYS A 491 CYS A 494 HIS A 511 CYS A 514
SITE 1 AC2 4 CYS A 503 CYS A 506 CYS A 529 CYS A 532
SITE 1 AC3 4 CYS B 491 CYS B 494 HIS B 511 CYS B 514
SITE 1 AC4 4 CYS B 503 CYS B 506 CYS B 529 CYS B 532
CRYST1 79.511 25.386 62.282 90.00 96.93 90.00 C 1 2 1 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 0.012577 0.000000 0.001529 0.00000
SCALE2 0.000000 0.039392 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016174 0.00000
(ATOM LINES ARE NOT SHOWN.)
END