HEADER TRANSFERASE 27-APR-16 5JLE
TITLE CRYSTAL STRUCTURE OF SETD2 BOUND TO SAH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 1434-1711;
COMPND 5 SYNONYM: HIF-1,HUNTINGTIN YEAST PARTNER B,HUNTINGTIN-INTERACTING
COMPND 6 PROTEIN 1,HIP-1,HUNTINGTIN-INTERACTING PROTEIN B,LYSINE N-
COMPND 7 METHYLTRANSFERASE 3A,SET DOMAIN-CONTAINING PROTEIN 2,HSET2,P231HBP;
COMPND 8 EC: 2.1.1.43;
COMPND 9 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: SETD2;
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
KEYWDS SET DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,S.YANG,X.ZHENG
REVDAT 3 08-NOV-23 5JLE 1 REMARK
REVDAT 2 30-AUG-17 5JLE 1 JRNL REMARK
REVDAT 1 02-NOV-16 5JLE 0
JRNL AUTH S.YANG,X.ZHENG,C.LU,G.M.LI,C.D.ALLIS,H.LI
JRNL TITL MOLECULAR BASIS FOR ONCOHISTONE H3 RECOGNITION BY SETD2
JRNL TITL 2 METHYLTRANSFERASE
JRNL REF GENES DEV. V. 30 1611 2016
JRNL REFN ISSN 0890-9369
JRNL PMID 27474439
JRNL DOI 10.1101/GAD.284323.116
REMARK 2
REMARK 2 RESOLUTION. 2.40 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 12819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.220
REMARK 3 FREE R VALUE TEST SET COUNT : 926
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 30.8861 - 4.5594 0.97 1767 151 0.1811 0.2043
REMARK 3 2 4.5594 - 3.6208 1.00 1742 131 0.1851 0.2294
REMARK 3 3 3.6208 - 3.1636 1.00 1718 129 0.2231 0.2821
REMARK 3 4 3.1636 - 2.8746 1.00 1675 156 0.2461 0.2972
REMARK 3 5 2.8746 - 2.6687 1.00 1745 101 0.2536 0.3356
REMARK 3 6 2.6687 - 2.5114 1.00 1674 116 0.2840 0.3211
REMARK 3 7 2.5114 - 2.3857 0.94 1572 142 0.3053 0.4088
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.70
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 : 0.007 1939
REMARK 3 ANGLE : 0.876 2605
REMARK 3 CHIRALITY : 0.050 265
REMARK 3 PLANARITY : 0.005 342
REMARK 3 DIHEDRAL : 17.572 1177
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5JLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220726.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 0.9952
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12885
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.84100
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: MOLREP
REMARK 200 STARTING MODEL: 4H12
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M KSCN, 30% PEG2000MME, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.34650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.57600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.34650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.57600
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 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 SER A 1433
REMARK 465 GLY A 1434
REMARK 465 GLU A 1435
REMARK 465 THR A 1436
REMARK 465 SER A 1437
REMARK 465 VAL A 1438
REMARK 465 PRO A 1439
REMARK 465 PRO A 1440
REMARK 465 GLY A 1441
REMARK 465 SER A 1442
REMARK 465 ALA A 1443
REMARK 465 LEU A 1444
REMARK 465 VAL A 1445
REMARK 465 ARG A 1485
REMARK 465 LYS A 1486
REMARK 465 LYS A 1487
REMARK 465 ASN A 1488
REMARK 465 LYS A 1489
REMARK 465 SER A 1490
REMARK 465 HIS A 1491
REMARK 465 ARG A 1492
REMARK 465 ASP A 1493
REMARK 465 ILE A 1494
REMARK 465 LYS A 1495
REMARK 465 ARG A 1496
REMARK 465 GLY A 1690
REMARK 465 GLY A 1691
REMARK 465 GLU A 1692
REMARK 465 ASN A 1693
REMARK 465 ARG A 1694
REMARK 465 VAL A 1695
REMARK 465 SER A 1696
REMARK 465 ILE A 1697
REMARK 465 ARG A 1698
REMARK 465 ALA A 1699
REMARK 465 ALA A 1700
REMARK 465 GLY A 1701
REMARK 465 GLY A 1702
REMARK 465 LYS A 1703
REMARK 465 MET A 1704
REMARK 465 LYS A 1705
REMARK 465 LYS A 1706
REMARK 465 GLU A 1707
REMARK 465 ARG A 1708
REMARK 465 SER A 1709
REMARK 465 ARG A 1710
REMARK 465 LYS A 1711
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 CYS A1516 64.89 61.03
REMARK 500 SER A1530 -166.93 -105.03
REMARK 500 ASN A1541 41.40 -92.36
REMARK 500 LYS A1559 -3.66 -143.53
REMARK 500 VAL A1576 -63.78 -99.10
REMARK 500 ARG A1670 -59.61 -125.66
REMARK 500 TYR A1671 165.97 66.71
REMARK 500 LYS A1673 63.25 -53.87
REMARK 500 GLU A1674 174.41 61.06
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 A1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1499 SG
REMARK 620 2 CYS A1501 SG 117.1
REMARK 620 3 CYS A1516 SG 109.9 105.7
REMARK 620 4 CYS A1520 SG 114.8 102.0 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1516 SG
REMARK 620 2 CYS A1529 SG 122.4
REMARK 620 3 CYS A1533 SG 100.1 113.8
REMARK 620 4 CYS A1539 SG 105.9 104.8 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1803 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1631 SG
REMARK 620 2 CYS A1678 SG 116.2
REMARK 620 3 CYS A1680 SG 114.5 107.9
REMARK 620 4 CYS A1685 SG 101.6 98.6 117.0
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 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1804
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JJY RELATED DB: PDB
REMARK 900 RELATED ID: 5JLB RELATED DB: PDB
DBREF 5JLE A 1434 1711 UNP Q9BYW2 SETD2_HUMAN 1434 1711
SEQADV 5JLE SER A 1433 UNP Q9BYW2 EXPRESSION TAG
SEQRES 1 A 279 SER GLY GLU THR SER VAL PRO PRO GLY SER ALA LEU VAL
SEQRES 2 A 279 GLY PRO SER CYS VAL MET ASP ASP PHE ARG ASP PRO GLN
SEQRES 3 A 279 ARG TRP LYS GLU CYS ALA LYS GLN GLY LYS MET PRO CYS
SEQRES 4 A 279 TYR PHE ASP LEU ILE GLU GLU ASN VAL TYR LEU THR GLU
SEQRES 5 A 279 ARG LYS LYS ASN LYS SER HIS ARG ASP ILE LYS ARG MET
SEQRES 6 A 279 GLN CYS GLU CYS THR PRO LEU SER LYS ASP GLU ARG ALA
SEQRES 7 A 279 GLN GLY GLU ILE ALA CYS GLY GLU ASP CYS LEU ASN ARG
SEQRES 8 A 279 LEU LEU MET ILE GLU CYS SER SER ARG CYS PRO ASN GLY
SEQRES 9 A 279 ASP TYR CYS SER ASN ARG ARG PHE GLN ARG LYS GLN HIS
SEQRES 10 A 279 ALA ASP VAL GLU VAL ILE LEU THR GLU LYS LYS GLY TRP
SEQRES 11 A 279 GLY LEU ARG ALA ALA LYS ASP LEU PRO SER ASN THR PHE
SEQRES 12 A 279 VAL LEU GLU TYR CYS GLY GLU VAL LEU ASP HIS LYS GLU
SEQRES 13 A 279 PHE LYS ALA ARG VAL LYS GLU TYR ALA ARG ASN LYS ASN
SEQRES 14 A 279 ILE HIS TYR TYR PHE MET ALA LEU LYS ASN ASP GLU ILE
SEQRES 15 A 279 ILE ASP ALA THR GLN LYS GLY ASN CYS SER ARG PHE MET
SEQRES 16 A 279 ASN HIS SER CYS GLU PRO ASN CYS GLU THR GLN LYS TRP
SEQRES 17 A 279 THR VAL ASN GLY GLN LEU ARG VAL GLY PHE PHE THR THR
SEQRES 18 A 279 LYS LEU VAL PRO SER GLY SER GLU LEU THR PHE ASP TYR
SEQRES 19 A 279 GLN PHE GLN ARG TYR GLY LYS GLU ALA GLN LYS CYS PHE
SEQRES 20 A 279 CYS GLY SER ALA ASN CYS ARG GLY TYR LEU GLY GLY GLU
SEQRES 21 A 279 ASN ARG VAL SER ILE ARG ALA ALA GLY GLY LYS MET LYS
SEQRES 22 A 279 LYS GLU ARG SER ARG LYS
HET ZN A1801 1
HET ZN A1802 1
HET ZN A1803 1
HET SAH A1804 26
HETNAM ZN ZINC ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 2 ZN 3(ZN 2+)
FORMUL 5 SAH C14 H20 N6 O5 S
FORMUL 6 HOH *32(H2 O)
HELIX 1 AA1 ASP A 1452 ARG A 1455 5 4
HELIX 2 AA2 ASP A 1456 GLN A 1466 1 11
HELIX 3 AA3 SER A 1505 GLN A 1511 1 7
HELIX 4 AA4 CYS A 1520 LEU A 1525 1 6
HELIX 5 AA5 ASN A 1535 CYS A 1539 5 5
HELIX 6 AA6 ASP A 1585 ASN A 1599 1 15
HELIX 7 AA7 ASN A 1622 MET A 1627 5 6
SHEET 1 AA1 5 SER A1448 VAL A1450 0
SHEET 2 AA1 5 VAL A1552 LEU A1556 -1 O VAL A1554 N CYS A1449
SHEET 3 AA1 5 TRP A1562 ALA A1566 -1 O ARG A1565 N GLU A1553
SHEET 4 AA1 5 GLU A1661 PHE A1664 -1 O LEU A1662 N LEU A1564
SHEET 5 AA1 5 ASN A1628 HIS A1629 1 N ASN A1628 O PHE A1664
SHEET 1 AA2 2 ASP A1474 LEU A1475 0
SHEET 2 AA2 2 LYS A1620 GLY A1621 1 O GLY A1621 N ASP A1474
SHEET 1 AA3 4 VAL A1480 TYR A1481 0
SHEET 2 AA3 4 GLU A1582 LEU A1584 1 O VAL A1583 N VAL A1480
SHEET 3 AA3 4 GLU A1613 ASP A1616 -1 O ASP A1616 N GLU A1582
SHEET 4 AA3 4 PHE A1606 LYS A1610 -1 N MET A1607 O ILE A1615
SHEET 1 AA4 3 PHE A1575 GLU A1578 0
SHEET 2 AA4 3 GLN A1645 THR A1652 -1 O PHE A1650 N VAL A1576
SHEET 3 AA4 3 CYS A1635 VAL A1642 -1 N VAL A1642 O GLN A1645
LINK SG CYS A1499 ZN ZN A1801 1555 1555 2.33
LINK SG CYS A1501 ZN ZN A1801 1555 1555 2.33
LINK SG CYS A1516 ZN ZN A1801 1555 1555 2.58
LINK SG CYS A1516 ZN ZN A1802 1555 1555 2.28
LINK SG CYS A1520 ZN ZN A1801 1555 1555 2.55
LINK SG CYS A1529 ZN ZN A1802 1555 1555 2.31
LINK SG CYS A1533 ZN ZN A1802 1555 1555 2.37
LINK SG CYS A1539 ZN ZN A1802 1555 1555 2.29
LINK SG CYS A1631 ZN ZN A1803 1555 1555 2.36
LINK SG CYS A1678 ZN ZN A1803 1555 1555 2.20
LINK SG CYS A1680 ZN ZN A1803 1555 1555 2.30
LINK SG CYS A1685 ZN ZN A1803 1555 1555 2.63
SITE 1 AC1 4 CYS A1499 CYS A1501 CYS A1516 CYS A1520
SITE 1 AC2 4 CYS A1516 CYS A1529 CYS A1533 CYS A1539
SITE 1 AC3 4 CYS A1631 CYS A1678 CYS A1680 CYS A1685
SITE 1 AC4 19 LYS A1560 GLY A1561 TRP A1562 ILE A1602
SITE 2 AC4 19 HIS A1603 TYR A1604 TYR A1605 ARG A1625
SITE 3 AC4 19 PHE A1626 MET A1627 ASN A1628 HIS A1629
SITE 4 AC4 19 TYR A1666 GLN A1676 LYS A1677 CYS A1678
SITE 5 AC4 19 PHE A1679 HOH A1911 HOH A1916
CRYST1 51.540 77.152 78.693 90.00 90.00 90.00 P 21 21 21 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 0.019402 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012961 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012708 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
