HEADER TRANSCRIPTION/STRUCTURAL PROTEIN 13-DEC-15 5FB1
TITLE CRYSTAL STRUCTURE OF A PHD FINGER BOUND TO HISTONE H3 K9ME3 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR AUTOANTIGEN SP-100;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 696-878;
COMPND 5 SYNONYM: SP100 NUCLEAR ANTIGEN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PEPTIDE FROM HISTONE H3;
COMPND 10 CHAIN: C;
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: SP100;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: CHEMICALLY SYNTHESIZED H3 PEPTIDE 1-15 WITH K9ME3
SOURCE 17 MODIFICATION
KEYWDS ZINC FINGER PROTEIN, BROMODOMAIN, TRANSCRIPTION-STRUCTURAL PROTEIN
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,X.ZHANG
REVDAT 4 20-MAR-24 5FB1 1 REMARK
REVDAT 3 04-OCT-17 5FB1 1 JRNL REMARK
REVDAT 2 22-JUN-16 5FB1 1 JRNL
REVDAT 1 04-MAY-16 5FB1 0
JRNL AUTH X.ZHANG,D.ZHAO,X.XIONG,Z.HE,H.LI
JRNL TITL MULTIFACETED HISTONE H3 METHYLATION AND PHOSPHORYLATION
JRNL TITL 2 READOUT BY THE PLANT HOMEODOMAIN FINGER OF HUMAN NUCLEAR
JRNL TITL 3 ANTIGEN SP100C
JRNL REF J.BIOL.CHEM. V. 291 12786 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27129259
JRNL DOI 10.1074/JBC.M116.721159
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2155: ???
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 14906
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 713
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.2444 - 3.5902 1.00 2978 159 0.1604 0.2065
REMARK 3 2 3.5902 - 2.8501 1.00 2831 157 0.1707 0.2369
REMARK 3 3 2.8501 - 2.4899 1.00 2809 115 0.1657 0.2297
REMARK 3 4 2.4899 - 2.2623 1.00 2802 140 0.1655 0.1971
REMARK 3 5 2.2623 - 2.1002 1.00 2773 142 0.1854 0.2440
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.13
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 1550
REMARK 3 ANGLE : 0.817 2083
REMARK 3 CHIRALITY : 0.049 214
REMARK 3 PLANARITY : 0.005 274
REMARK 3 DIHEDRAL : 17.214 947
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3955 17.7576 -19.2156
REMARK 3 T TENSOR
REMARK 3 T11: 0.1608 T22: 0.1505
REMARK 3 T33: 0.1570 T12: -0.0020
REMARK 3 T13: 0.0030 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 1.2823 L22: 1.1580
REMARK 3 L33: 1.0328 L12: 0.5393
REMARK 3 L13: -0.2108 L23: -0.5029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: -0.0127 S13: -0.2860
REMARK 3 S21: -0.0123 S22: -0.0949 S23: -0.1840
REMARK 3 S31: 0.0071 S32: 0.1026 S33: -0.0044
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5FB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14943
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.66500
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: NULL
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE/CITRIC ACID, PH
REMARK 280 5.5, 10% 2-PROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+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 26.42000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.48200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.42000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.48200
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 TYR A 804
REMARK 465 ASN A 805
REMARK 465 ARG A 806
REMARK 465 GLU A 807
REMARK 465 GLU A 876
REMARK 465 THR A 877
REMARK 465 SER A 878
REMARK 465 LYS C 9
REMARK 465 SER C 10
REMARK 465 THR C 11
REMARK 465 GLY C 12
REMARK 465 GLY C 13
REMARK 465 LYS C 14
REMARK 465 ALA C 15
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 OE1 GLU A 831 O HOH A 1001 2.16
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 LYS A 811 83.55 -156.21
REMARK 500 HIS A 844 72.88 -113.84
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 A 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 705 SG
REMARK 620 2 CYS A 708 SG 111.3
REMARK 620 3 HIS A 725 ND1 103.4 95.0
REMARK 620 4 CYS A 728 SG 111.6 119.4 114.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 717 SG
REMARK 620 2 CYS A 720 SG 112.1
REMARK 620 3 CYS A 742 SG 111.1 108.9
REMARK 620 4 CYS A 745 SG 106.2 101.6 116.7
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 903
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FB0 RELATED DB: PDB
DBREF 5FB1 A 696 878 UNP P23497 SP100_HUMAN 696 878
DBREF 5FB1 C 1 15 UNP K7EMV3 K7EMV3_HUMAN 2 16
SEQADV 5FB1 SER A 695 UNP P23497 EXPRESSION TAG
SEQADV 5FB1 A UNP P23497 GLY 805 DELETION
SEQADV 5FB1 A UNP P23497 SER 806 DELETION
SEQADV 5FB1 A UNP P23497 GLN 807 DELETION
SEQADV 5FB1 THR A 826 UNP P23497 MET 826 ENGINEERED MUTATION
SEQRES 1 A 181 SER ASP PRO CYS PRO GLU ASN SER ASN ILE CYS GLU VAL
SEQRES 2 A 181 CYS ASN LYS TRP GLY ARG LEU PHE CYS CYS ASP THR CYS
SEQRES 3 A 181 PRO ARG SER PHE HIS GLU HIS CYS HIS ILE PRO SER VAL
SEQRES 4 A 181 GLU ALA ASN LYS ASN PRO TRP SER CYS ILE PHE CYS ARG
SEQRES 5 A 181 ILE LYS THR ILE GLN GLU ARG CYS PRO GLU SER GLN SER
SEQRES 6 A 181 GLY HIS GLN GLU SER GLU VAL LEU MET ARG GLN MET LEU
SEQRES 7 A 181 PRO GLU GLU GLN LEU LYS CYS GLU PHE LEU LEU LEU LYS
SEQRES 8 A 181 VAL TYR CYS ASP SER LYS SER CYS PHE PHE ALA SER GLU
SEQRES 9 A 181 PRO TYR TYR ASN ARG GLU GLY PRO GLN LYS PRO MET TRP
SEQRES 10 A 181 LEU ASN LYS VAL LYS THR SER LEU ASN GLU GLN THR TYR
SEQRES 11 A 181 THR ARG VAL GLU GLY PHE VAL GLN ASP MET ARG LEU ILE
SEQRES 12 A 181 PHE HIS ASN HIS LYS GLU PHE TYR ARG GLU ASP LYS PHE
SEQRES 13 A 181 THR ARG LEU GLY ILE GLN VAL GLN ASP ILE PHE GLU LYS
SEQRES 14 A 181 ASN PHE ARG ASN ILE PHE ALA ILE GLN GLU THR SER
SEQRES 1 C 15 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 C 15 LYS ALA
HET ZN A 901 1
HET ZN A 902 1
HET MLI A 903 7
HETNAM ZN ZINC ION
HETNAM MLI MALONATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 MLI C3 H2 O4 2-
FORMUL 6 HOH *155(H2 O)
HELIX 1 AA1 CYS A 742 CYS A 754 1 13
HELIX 2 AA2 GLN A 762 ARG A 769 1 8
HELIX 3 AA3 LEU A 772 CYS A 788 1 17
HELIX 4 AA4 ASP A 789 ALA A 796 5 8
HELIX 5 AA5 TRP A 814 GLU A 824 1 11
HELIX 6 AA6 ARG A 829 ASN A 843 1 15
HELIX 7 AA7 GLU A 850 PHE A 872 1 23
SHEET 1 AA1 3 SER A 723 HIS A 725 0
SHEET 2 AA1 3 ARG A 713 CYS A 716 -1 N PHE A 715 O PHE A 724
SHEET 3 AA1 3 ARG C 2 GLN C 5 -1 O LYS C 4 N LEU A 714
LINK SG CYS A 705 ZN ZN A 901 1555 1555 2.25
LINK SG CYS A 708 ZN ZN A 901 1555 1555 2.37
LINK SG CYS A 717 ZN ZN A 902 1555 1555 2.32
LINK SG CYS A 720 ZN ZN A 902 1555 1555 2.30
LINK ND1 HIS A 725 ZN ZN A 901 1555 1555 2.08
LINK SG CYS A 728 ZN ZN A 901 1555 1555 2.30
LINK SG CYS A 742 ZN ZN A 902 1555 1555 2.27
LINK SG CYS A 745 ZN ZN A 902 1555 1555 2.35
CISPEP 1 ILE A 730 PRO A 731 0 -7.29
CISPEP 2 ASN A 738 PRO A 739 0 -4.76
SITE 1 AC1 4 CYS A 705 CYS A 708 HIS A 725 CYS A 728
SITE 1 AC2 4 CYS A 717 CYS A 720 CYS A 742 CYS A 745
SITE 1 AC3 8 ARG A 713 HIS A 725 GLU A 726 HIS A 727
SITE 2 AC3 8 HOH A1026 HOH A1033 HOH A1035 HOH A1080
CRYST1 52.840 102.964 44.955 90.00 90.00 90.00 P 21 21 2 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 0.018925 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009712 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022244 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
