HEADER TRANSFERASE/HYDROLASE 11-MAR-15 4YOC
TITLE CRYSTAL STRUCTURE OF HUMAN DNMT1 AND USP7/HAUSP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 600-1600;
COMPND 5 SYNONYM: DNMT1,CXXC-TYPE ZINC FINGER PROTEIN 9,DNA METHYLTRANSFERASE
COMPND 6 HSAI,M.HSAI,MCMT;
COMPND 7 EC: 2.1.1.37;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7;
COMPND 11 CHAIN: C;
COMPND 12 FRAGMENT: UNP RESIDUES 560-1102;
COMPND 13 SYNONYM: DEUBIQUITINATING ENZYME 7,HERPESVIRUS-ASSOCIATED UBIQUITIN-
COMPND 14 SPECIFIC PROTEASE,UBIQUITIN THIOESTERASE 7,UBIQUITIN-SPECIFIC-
COMPND 15 PROCESSING PROTEASE 7;
COMPND 16 EC: 3.4.19.12;
COMPND 17 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: DNMT1, AIM, CXXC9, DNMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: USP7, HAUSP;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA METHYLATION, DEUBIQUITINATION, DNA METHYLTRANSFERASE,
KEYWDS 2 MODIFICATION, TRANSFERASE-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHENG,H.YANG,J.FANG,R.GONG,P.WANG,Z.LI,Y.XU
REVDAT 2 08-NOV-23 4YOC 1 SOURCE REMARK
REVDAT 1 27-MAY-15 4YOC 0
JRNL AUTH J.CHENG,H.YANG,J.FANG,L.MA,R.GONG,P.WANG,Z.LI,Y.XU
JRNL TITL MOLECULAR MECHANISM FOR USP7-MEDIATED DNMT1 STABILIZATION BY
JRNL TITL 2 ACETYLATION.
JRNL REF NAT COMMUN V. 6 7023 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 25960197
JRNL DOI 10.1038/NCOMMS8023
REMARK 2
REMARK 2 RESOLUTION. 2.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 44396
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.480
REMARK 3 FREE R VALUE TEST SET COUNT : 1991
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 49.4262 - 7.0222 0.99 3240 155 0.2009 0.2536
REMARK 3 2 7.0222 - 5.5762 1.00 3121 143 0.2103 0.2567
REMARK 3 3 5.5762 - 4.8720 1.00 3085 139 0.1799 0.2241
REMARK 3 4 4.8720 - 4.4269 1.00 3063 140 0.1610 0.1768
REMARK 3 5 4.4269 - 4.1098 1.00 3039 143 0.1762 0.2180
REMARK 3 6 4.1098 - 3.8675 1.00 3064 142 0.1967 0.2552
REMARK 3 7 3.8675 - 3.6739 1.00 3015 141 0.2148 0.2548
REMARK 3 8 3.6739 - 3.5140 1.00 3052 146 0.2234 0.2941
REMARK 3 9 3.5140 - 3.3788 1.00 3013 141 0.2266 0.2730
REMARK 3 10 3.3788 - 3.2622 1.00 3010 148 0.2409 0.2726
REMARK 3 11 3.2622 - 3.1602 1.00 3004 139 0.2528 0.3418
REMARK 3 12 3.1602 - 3.0699 1.00 3015 146 0.2660 0.3311
REMARK 3 13 3.0699 - 2.9891 1.00 2995 144 0.2772 0.3739
REMARK 3 14 2.9891 - 2.9162 0.89 2689 124 0.2899 0.4148
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.890
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.19
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 : 0.003 11649
REMARK 3 ANGLE : 0.892 15743
REMARK 3 CHIRALITY : 0.035 1662
REMARK 3 PLANARITY : 0.004 2066
REMARK 3 DIHEDRAL : 14.800 4420
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 4YOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207740.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-7.0
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) : 1.0000
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44471
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.80
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 0.85800
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: 3SWR, 2YLM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6-8% PEG 3350, 200 MM POTASSIUM
REMARK 280 ACETATE, 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 55.11550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.93400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.80950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.93400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.11550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.80950
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 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 SER A 597
REMARK 465 GLU A 598
REMARK 465 PHE A 599
REMARK 465 ARG A 600
REMARK 465 ARG A 601
REMARK 465 GLN A 602
REMARK 465 THR A 603
REMARK 465 ILE A 604
REMARK 465 ARG A 605
REMARK 465 HIS A 606
REMARK 465 SER A 607
REMARK 465 THR A 608
REMARK 465 ARG A 609
REMARK 465 GLU A 610
REMARK 465 LYS A 611
REMARK 465 ASP A 612
REMARK 465 ARG A 613
REMARK 465 GLY A 614
REMARK 465 GLU A 634
REMARK 465 GLN A 635
REMARK 465 ILE A 636
REMARK 465 GLU A 637
REMARK 465 LYS A 638
REMARK 465 ASP A 639
REMARK 465 ASP A 640
REMARK 465 ARG A 641
REMARK 465 GLU A 642
REMARK 465 ASP A 643
REMARK 465 LYS A 644
REMARK 465 GLU A 645
REMARK 465 ASN A 646
REMARK 465 ALA A 647
REMARK 465 PHE A 648
REMARK 465 LYS A 649
REMARK 465 ARG A 650
REMARK 465 ARG A 651
REMARK 465 ARG A 652
REMARK 465 CYS A 653
REMARK 465 GLY A 654
REMARK 465 VAL A 655
REMARK 465 CYS A 656
REMARK 465 GLU A 657
REMARK 465 VAL A 658
REMARK 465 CYS A 659
REMARK 465 GLN A 660
REMARK 465 GLN A 661
REMARK 465 PRO A 662
REMARK 465 GLU A 663
REMARK 465 CYS A 664
REMARK 465 GLY A 665
REMARK 465 LYS A 666
REMARK 465 CYS A 667
REMARK 465 LYS A 668
REMARK 465 ALA A 669
REMARK 465 CYS A 670
REMARK 465 LYS A 671
REMARK 465 ASP A 672
REMARK 465 MET A 673
REMARK 465 VAL A 674
REMARK 465 LYS A 675
REMARK 465 PHE A 676
REMARK 465 GLY A 677
REMARK 465 GLY A 678
REMARK 465 SER A 679
REMARK 465 GLY A 680
REMARK 465 ARG A 681
REMARK 465 SER A 682
REMARK 465 LYS A 683
REMARK 465 GLN A 684
REMARK 465 ALA A 685
REMARK 465 CYS A 686
REMARK 465 GLN A 687
REMARK 465 GLU A 688
REMARK 465 ARG A 689
REMARK 465 ARG A 690
REMARK 465 CYS A 691
REMARK 465 PRO A 692
REMARK 465 ASN A 693
REMARK 465 MET A 694
REMARK 465 ALA A 695
REMARK 465 MET A 696
REMARK 465 LYS A 697
REMARK 465 GLU A 698
REMARK 465 ALA A 699
REMARK 465 ASP A 700
REMARK 465 ASP A 701
REMARK 465 LEU A 854
REMARK 465 LEU A 855
REMARK 465 GLU A 856
REMARK 465 GLY A 857
REMARK 465 ASP A 858
REMARK 465 ASP A 859
REMARK 465 SER A 953
REMARK 465 SER A 954
REMARK 465 PRO A 955
REMARK 465 VAL A 956
REMARK 465 LYS A 957
REMARK 465 ARG A 958
REMARK 465 PRO A 959
REMARK 465 ARG A 960
REMARK 465 LYS A 961
REMARK 465 ILE A 980
REMARK 465 LYS A 981
REMARK 465 GLY A 982
REMARK 465 SER A 983
REMARK 465 GLY A 1116
REMARK 465 LYS A 1117
REMARK 465 GLY A 1118
REMARK 465 LYS A 1119
REMARK 465 PRO A 1120
REMARK 465 LYS A 1121
REMARK 465 SER A 1122
REMARK 465 GLN A 1123
REMARK 465 ALA A 1124
REMARK 465 CYS A 1125
REMARK 465 GLU A 1126
REMARK 465 PRO A 1127
REMARK 465 SER A 1128
REMARK 465 GLU A 1129
REMARK 465 PRO A 1130
REMARK 465 GLU A 1131
REMARK 465 ILE A 1132
REMARK 465 LYS C 1084
REMARK 465 ALA C 1085
REMARK 465 PRO C 1086
REMARK 465 LYS C 1087
REMARK 465 ARG C 1088
REMARK 465 SER C 1089
REMARK 465 ARG C 1090
REMARK 465 TYR C 1091
REMARK 465 THR C 1092
REMARK 465 TYR C 1093
REMARK 465 LEU C 1094
REMARK 465 GLU C 1095
REMARK 465 LYS C 1096
REMARK 465 ALA C 1097
REMARK 465 ILE C 1098
REMARK 465 LYS C 1099
REMARK 465 ILE C 1100
REMARK 465 HIS C 1101
REMARK 465 ASN C 1102
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 GLN A 1340 OG SER A 1342 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 VAL A 705 70.57 43.01
REMARK 500 SER A 714 168.57 68.53
REMARK 500 PRO A 715 68.29 -64.81
REMARK 500 LYS A 716 77.80 42.74
REMARK 500 LYS A 743 -9.23 -143.32
REMARK 500 ASP A 753 60.14 34.15
REMARK 500 GLU A 819 107.03 177.11
REMARK 500 GLN A 866 -17.30 -142.59
REMARK 500 LEU A 911 -75.02 -116.35
REMARK 500 LEU A 914 -5.29 -142.81
REMARK 500 TYR A 969 76.68 -119.99
REMARK 500 ASP A1013 53.80 -111.67
REMARK 500 THR A1027 -169.89 -75.01
REMARK 500 SER A1030 -158.68 60.10
REMARK 500 LYS A1111 -69.64 -98.29
REMARK 500 ASN A1270 -2.91 -57.71
REMARK 500 ARG A1310 86.07 -154.82
REMARK 500 LEU A1357 -63.65 -108.85
REMARK 500 MET A1371 28.24 -146.61
REMARK 500 ASP A1435 -152.24 -141.88
REMARK 500 ALA A1481 1.90 59.12
REMARK 500 ALA A1484 -62.02 -120.46
REMARK 500 CYS A1485 70.07 61.73
REMARK 500 ASP A1486 103.64 -43.93
REMARK 500 GLU A1543 -62.98 -128.68
REMARK 500 ARG A1546 164.00 174.73
REMARK 500 GLU C 560 39.22 -147.81
REMARK 500 ASP C 582 -145.86 55.44
REMARK 500 ASN C 654 -3.69 66.39
REMARK 500 ASN C 656 129.40 -175.80
REMARK 500 LEU C 836 32.36 -90.48
REMARK 500 PRO C 964 75.01 -66.21
REMARK 500 VAL C 980 -72.27 -57.34
REMARK 500 PHE C 995 141.85 -170.60
REMARK 500 LYS C 997 -115.40 56.29
REMARK 500 HIS C1012 -158.78 -88.20
REMARK 500 HIS C1016 83.84 66.10
REMARK 500 ASP C1029 75.01 58.30
REMARK 500 GLU C1032 30.94 -89.09
REMARK 500 LYS C1033 8.93 113.49
REMARK 500 PRO C1065 -169.95 -72.35
REMARK 500 MET C1070 -55.46 -128.60
REMARK 500 HIS C1081 -10.37 -173.94
REMARK 500 PHE C1082 -141.43 59.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 707 ASN A 708 146.88
REMARK 500 ASN A 708 ILE A 709 -146.23
REMARK 500 SER A 714 PRO A 715 -103.01
REMARK 500 PRO A 715 LYS A 716 110.08
REMARK 500 GLN A 1536 GLY A 1537 -145.94
REMARK 500 GLU C 1032 LYS C 1033 -149.46
REMARK 500 LYS C 1033 GLU C 1034 144.09
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 A1702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 793 NE2
REMARK 620 2 CYS A 820 SG 103.8
REMARK 620 3 CYS A 893 SG 109.2 136.2
REMARK 620 4 CYS A 896 SG 88.7 97.4 111.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1476 SG
REMARK 620 2 CYS A1478 SG 102.9
REMARK 620 3 CYS A1485 SG 120.7 117.8
REMARK 620 4 HIS A1502 NE2 115.0 89.3 107.2
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 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1702
DBREF 4YOC A 600 1600 UNP P26358 DNMT1_HUMAN 600 1600
DBREF 4YOC C 560 1102 UNP Q93009 UBP7_HUMAN 560 1102
SEQADV 4YOC SER A 597 UNP P26358 EXPRESSION TAG
SEQADV 4YOC GLU A 598 UNP P26358 EXPRESSION TAG
SEQADV 4YOC PHE A 599 UNP P26358 EXPRESSION TAG
SEQADV 4YOC GLY C 555 UNP Q93009 EXPRESSION TAG
SEQADV 4YOC PRO C 556 UNP Q93009 EXPRESSION TAG
SEQADV 4YOC LEU C 557 UNP Q93009 EXPRESSION TAG
SEQADV 4YOC GLY C 558 UNP Q93009 EXPRESSION TAG
SEQADV 4YOC SER C 559 UNP Q93009 EXPRESSION TAG
SEQRES 1 A 1004 SER GLU PHE ARG ARG GLN THR ILE ARG HIS SER THR ARG
SEQRES 2 A 1004 GLU LYS ASP ARG GLY PRO THR LYS ALA THR THR THR LYS
SEQRES 3 A 1004 LEU VAL TYR GLN ILE PHE ASP THR PHE PHE ALA GLU GLN
SEQRES 4 A 1004 ILE GLU LYS ASP ASP ARG GLU ASP LYS GLU ASN ALA PHE
SEQRES 5 A 1004 LYS ARG ARG ARG CYS GLY VAL CYS GLU VAL CYS GLN GLN
SEQRES 6 A 1004 PRO GLU CYS GLY LYS CYS LYS ALA CYS LYS ASP MET VAL
SEQRES 7 A 1004 LYS PHE GLY GLY SER GLY ARG SER LYS GLN ALA CYS GLN
SEQRES 8 A 1004 GLU ARG ARG CYS PRO ASN MET ALA MET LYS GLU ALA ASP
SEQRES 9 A 1004 ASP ASP GLU GLU VAL ASP ASP ASN ILE PRO GLU MET PRO
SEQRES 10 A 1004 SER PRO LYS LYS MET HIS GLN GLY LYS LYS LYS LYS GLN
SEQRES 11 A 1004 ASN LYS ASN ARG ILE SER TRP VAL GLY GLU ALA VAL LYS
SEQRES 12 A 1004 THR ASP GLY LYS LYS SER TYR TYR LYS LYS VAL CYS ILE
SEQRES 13 A 1004 ASP ALA GLU THR LEU GLU VAL GLY ASP CYS VAL SER VAL
SEQRES 14 A 1004 ILE PRO ASP ASP SER SER LYS PRO LEU TYR LEU ALA ARG
SEQRES 15 A 1004 VAL THR ALA LEU TRP GLU ASP SER SER ASN GLY GLN MET
SEQRES 16 A 1004 PHE HIS ALA HIS TRP PHE CYS ALA GLY THR ASP THR VAL
SEQRES 17 A 1004 LEU GLY ALA THR SER ASP PRO LEU GLU LEU PHE LEU VAL
SEQRES 18 A 1004 ASP GLU CYS GLU ASP MET GLN LEU SER TYR ILE HIS SER
SEQRES 19 A 1004 LYS VAL LYS VAL ILE TYR LYS ALA PRO SER GLU ASN TRP
SEQRES 20 A 1004 ALA MET GLU GLY GLY MET ASP PRO GLU SER LEU LEU GLU
SEQRES 21 A 1004 GLY ASP ASP GLY LYS THR TYR PHE TYR GLN LEU TRP TYR
SEQRES 22 A 1004 ASP GLN ASP TYR ALA ARG PHE GLU SER PRO PRO LYS THR
SEQRES 23 A 1004 GLN PRO THR GLU ASP ASN LYS PHE LYS PHE CYS VAL SER
SEQRES 24 A 1004 CYS ALA ARG LEU ALA GLU MET ARG GLN LYS GLU ILE PRO
SEQRES 25 A 1004 ARG VAL LEU GLU GLN LEU GLU ASP LEU ASP SER ARG VAL
SEQRES 26 A 1004 LEU TYR TYR SER ALA THR LYS ASN GLY ILE LEU TYR ARG
SEQRES 27 A 1004 VAL GLY ASP GLY VAL TYR LEU PRO PRO GLU ALA PHE THR
SEQRES 28 A 1004 PHE ASN ILE LYS LEU SER SER PRO VAL LYS ARG PRO ARG
SEQRES 29 A 1004 LYS GLU PRO VAL ASP GLU ASP LEU TYR PRO GLU HIS TYR
SEQRES 30 A 1004 ARG LYS TYR SER ASP TYR ILE LYS GLY SER ASN LEU ASP
SEQRES 31 A 1004 ALA PRO GLU PRO TYR ARG ILE GLY ARG ILE LYS GLU ILE
SEQRES 32 A 1004 PHE CYS PRO LYS LYS SER ASN GLY ARG PRO ASN GLU THR
SEQRES 33 A 1004 ASP ILE LYS ILE ARG VAL ASN LYS PHE TYR ARG PRO GLU
SEQRES 34 A 1004 ASN THR HIS LYS SER THR PRO ALA SER TYR HIS ALA ASP
SEQRES 35 A 1004 ILE ASN LEU LEU TYR TRP SER ASP GLU GLU ALA VAL VAL
SEQRES 36 A 1004 ASP PHE LYS ALA VAL GLN GLY ARG CYS THR VAL GLU TYR
SEQRES 37 A 1004 GLY GLU ASP LEU PRO GLU CYS VAL GLN VAL TYR SER MET
SEQRES 38 A 1004 GLY GLY PRO ASN ARG PHE TYR PHE LEU GLU ALA TYR ASN
SEQRES 39 A 1004 ALA LYS SER LYS SER PHE GLU ASP PRO PRO ASN HIS ALA
SEQRES 40 A 1004 ARG SER PRO GLY ASN LYS GLY LYS GLY LYS GLY LYS GLY
SEQRES 41 A 1004 LYS GLY LYS PRO LYS SER GLN ALA CYS GLU PRO SER GLU
SEQRES 42 A 1004 PRO GLU ILE GLU ILE LYS LEU PRO LYS LEU ARG THR LEU
SEQRES 43 A 1004 ASP VAL PHE SER GLY CYS GLY GLY LEU SER GLU GLY PHE
SEQRES 44 A 1004 HIS GLN ALA GLY ILE SER ASP THR LEU TRP ALA ILE GLU
SEQRES 45 A 1004 MET TRP ASP PRO ALA ALA GLN ALA PHE ARG LEU ASN ASN
SEQRES 46 A 1004 PRO GLY SER THR VAL PHE THR GLU ASP CYS ASN ILE LEU
SEQRES 47 A 1004 LEU LYS LEU VAL MET ALA GLY GLU THR THR ASN SER ARG
SEQRES 48 A 1004 GLY GLN ARG LEU PRO GLN LYS GLY ASP VAL GLU MET LEU
SEQRES 49 A 1004 CYS GLY GLY PRO PRO CYS GLN GLY PHE SER GLY MET ASN
SEQRES 50 A 1004 ARG PHE ASN SER ARG THR TYR SER LYS PHE LYS ASN SER
SEQRES 51 A 1004 LEU VAL VAL SER PHE LEU SER TYR CYS ASP TYR TYR ARG
SEQRES 52 A 1004 PRO ARG PHE PHE LEU LEU GLU ASN VAL ARG ASN PHE VAL
SEQRES 53 A 1004 SER PHE LYS ARG SER MET VAL LEU LYS LEU THR LEU ARG
SEQRES 54 A 1004 CYS LEU VAL ARG MET GLY TYR GLN CYS THR PHE GLY VAL
SEQRES 55 A 1004 LEU GLN ALA GLY GLN TYR GLY VAL ALA GLN THR ARG ARG
SEQRES 56 A 1004 ARG ALA ILE ILE LEU ALA ALA ALA PRO GLY GLU LYS LEU
SEQRES 57 A 1004 PRO LEU PHE PRO GLU PRO LEU HIS VAL PHE ALA PRO ARG
SEQRES 58 A 1004 ALA CYS GLN LEU SER VAL VAL VAL ASP ASP LYS LYS PHE
SEQRES 59 A 1004 VAL SER ASN ILE THR ARG LEU SER SER GLY PRO PHE ARG
SEQRES 60 A 1004 THR ILE THR VAL ARG ASP THR MET SER ASP LEU PRO GLU
SEQRES 61 A 1004 VAL ARG ASN GLY ALA SER ALA LEU GLU ILE SER TYR ASN
SEQRES 62 A 1004 GLY GLU PRO GLN SER TRP PHE GLN ARG GLN LEU ARG GLY
SEQRES 63 A 1004 ALA GLN TYR GLN PRO ILE LEU ARG ASP HIS ILE CYS LYS
SEQRES 64 A 1004 ASP MET SER ALA LEU VAL ALA ALA ARG MET ARG HIS ILE
SEQRES 65 A 1004 PRO LEU ALA PRO GLY SER ASP TRP ARG ASP LEU PRO ASN
SEQRES 66 A 1004 ILE GLU VAL ARG LEU SER ASP GLY THR MET ALA ARG LYS
SEQRES 67 A 1004 LEU ARG TYR THR HIS HIS ASP ARG LYS ASN GLY ARG SER
SEQRES 68 A 1004 SER SER GLY ALA LEU ARG GLY VAL CYS SER CYS VAL GLU
SEQRES 69 A 1004 ALA GLY LYS ALA CYS ASP PRO ALA ALA ARG GLN PHE ASN
SEQRES 70 A 1004 THR LEU ILE PRO TRP CYS LEU PRO HIS THR GLY ASN ARG
SEQRES 71 A 1004 HIS ASN HIS TRP ALA GLY LEU TYR GLY ARG LEU GLU TRP
SEQRES 72 A 1004 ASP GLY PHE PHE SER THR THR VAL THR ASN PRO GLU PRO
SEQRES 73 A 1004 MET GLY LYS GLN GLY ARG VAL LEU HIS PRO GLU GLN HIS
SEQRES 74 A 1004 ARG VAL VAL SER VAL ARG GLU CYS ALA ARG SER GLN GLY
SEQRES 75 A 1004 PHE PRO ASP THR TYR ARG LEU PHE GLY ASN ILE LEU ASP
SEQRES 76 A 1004 LYS HIS ARG GLN VAL GLY ASN ALA VAL PRO PRO PRO LEU
SEQRES 77 A 1004 ALA LYS ALA ILE GLY LEU GLU ILE LYS LEU CYS MET LEU
SEQRES 78 A 1004 ALA LYS ALA
SEQRES 1 C 548 GLY PRO LEU GLY SER GLU ALA HIS LEU TYR MET GLN VAL
SEQRES 2 C 548 GLN ILE VAL ALA GLU ASP GLN PHE CYS GLY HIS GLN GLY
SEQRES 3 C 548 ASN ASP MET TYR ASP GLU GLU LYS VAL LYS TYR THR VAL
SEQRES 4 C 548 PHE LYS VAL LEU LYS ASN SER SER LEU ALA GLU PHE VAL
SEQRES 5 C 548 GLN SER LEU SER GLN THR MET GLY PHE PRO GLN ASP GLN
SEQRES 6 C 548 ILE ARG LEU TRP PRO MET GLN ALA ARG SER ASN GLY THR
SEQRES 7 C 548 LYS ARG PRO ALA MET LEU ASP ASN GLU ALA ASP GLY ASN
SEQRES 8 C 548 LYS THR MET ILE GLU LEU SER ASP ASN GLU ASN PRO TRP
SEQRES 9 C 548 THR ILE PHE LEU GLU THR VAL ASP PRO GLU LEU ALA ALA
SEQRES 10 C 548 SER GLY ALA THR LEU PRO LYS PHE ASP LYS ASP HIS ASP
SEQRES 11 C 548 VAL MET LEU PHE LEU LYS MET TYR ASP PRO LYS THR ARG
SEQRES 12 C 548 SER LEU ASN TYR CYS GLY HIS ILE TYR THR PRO ILE SER
SEQRES 13 C 548 CYS LYS ILE ARG ASP LEU LEU PRO VAL MET CYS ASP ARG
SEQRES 14 C 548 ALA GLY PHE ILE GLN ASP THR SER LEU ILE LEU TYR GLU
SEQRES 15 C 548 GLU VAL LYS PRO ASN LEU THR GLU ARG ILE GLN ASP TYR
SEQRES 16 C 548 ASP VAL SER LEU ASP LYS ALA LEU ASP GLU LEU MET ASP
SEQRES 17 C 548 GLY ASP ILE ILE VAL PHE GLN LYS ASP ASP PRO GLU ASN
SEQRES 18 C 548 ASP ASN SER GLU LEU PRO THR ALA LYS GLU TYR PHE ARG
SEQRES 19 C 548 ASP LEU TYR HIS ARG VAL ASP VAL ILE PHE CYS ASP LYS
SEQRES 20 C 548 THR ILE PRO ASN ASP PRO GLY PHE VAL VAL THR LEU SER
SEQRES 21 C 548 ASN ARG MET ASN TYR PHE GLN VAL ALA LYS THR VAL ALA
SEQRES 22 C 548 GLN ARG LEU ASN THR ASP PRO MET LEU LEU GLN PHE PHE
SEQRES 23 C 548 LYS SER GLN GLY TYR ARG ASP GLY PRO GLY ASN PRO LEU
SEQRES 24 C 548 ARG HIS ASN TYR GLU GLY THR LEU ARG ASP LEU LEU GLN
SEQRES 25 C 548 PHE PHE LYS PRO ARG GLN PRO LYS LYS LEU TYR TYR GLN
SEQRES 26 C 548 GLN LEU LYS MET LYS ILE THR ASP PHE GLU ASN ARG ARG
SEQRES 27 C 548 SER PHE LYS CYS ILE TRP LEU ASN SER GLN PHE ARG GLU
SEQRES 28 C 548 GLU GLU ILE THR LEU TYR PRO ASP LYS HIS GLY CYS VAL
SEQRES 29 C 548 ARG ASP LEU LEU GLU GLU CYS LYS LYS ALA VAL GLU LEU
SEQRES 30 C 548 GLY GLU LYS ALA SER GLY LYS LEU ARG LEU LEU GLU ILE
SEQRES 31 C 548 VAL SER TYR LYS ILE ILE GLY VAL HIS GLN GLU ASP GLU
SEQRES 32 C 548 LEU LEU GLU CYS LEU SER PRO ALA THR SER ARG THR PHE
SEQRES 33 C 548 ARG ILE GLU GLU ILE PRO LEU ASP GLN VAL ASP ILE ASP
SEQRES 34 C 548 LYS GLU ASN GLU MET LEU VAL THR VAL ALA HIS PHE HIS
SEQRES 35 C 548 LYS GLU VAL PHE GLY THR PHE GLY ILE PRO PHE LEU LEU
SEQRES 36 C 548 ARG ILE HIS GLN GLY GLU HIS PHE ARG GLU VAL MET LYS
SEQRES 37 C 548 ARG ILE GLN SER LEU LEU ASP ILE GLN GLU LYS GLU PHE
SEQRES 38 C 548 GLU LYS PHE LYS PHE ALA ILE VAL MET MET GLY ARG HIS
SEQRES 39 C 548 GLN TYR ILE ASN GLU ASP GLU TYR GLU VAL ASN LEU LYS
SEQRES 40 C 548 ASP PHE GLU PRO GLN PRO GLY ASN MET SER HIS PRO ARG
SEQRES 41 C 548 PRO TRP LEU GLY LEU ASP HIS PHE ASN LYS ALA PRO LYS
SEQRES 42 C 548 ARG SER ARG TYR THR TYR LEU GLU LYS ALA ILE LYS ILE
SEQRES 43 C 548 HIS ASN
HET ZN A1701 1
HET ZN A1702 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 HOH *11(H2 O)
HELIX 1 AA1 THR A 621 THR A 630 1 10
HELIX 2 AA2 THR A 801 THR A 803 5 3
HELIX 3 AA3 LEU A 805 SER A 809 5 5
HELIX 4 AA4 ASN A 842 GLU A 846 5 5
HELIX 5 AA5 CYS A 893 GLU A 906 1 14
HELIX 6 AA6 GLU A 971 TYR A 976 5 6
HELIX 7 AA7 ARG A 1023 THR A 1027 5 5
HELIX 8 AA8 SER A 1030 TYR A 1035 5 6
HELIX 9 AA9 LYS A 1054 VAL A 1056 5 3
HELIX 10 AB1 CYS A 1071 MET A 1077 1 7
HELIX 11 AB2 PRO A 1100 ARG A 1104 5 5
HELIX 12 AB3 GLY A 1149 GLY A 1159 1 11
HELIX 13 AB4 TRP A 1170 ASN A 1181 1 12
HELIX 14 AB5 ASP A 1190 ALA A 1200 1 11
HELIX 15 AB6 ASN A 1236 ASN A 1245 1 10
HELIX 16 AB7 SER A 1246 ARG A 1259 1 14
HELIX 17 AB8 ASN A 1270 PHE A 1274 5 5
HELIX 18 AB9 SER A 1277 GLY A 1291 1 15
HELIX 19 AC1 GLY A 1302 GLY A 1305 5 4
HELIX 20 AC2 ALA A 1335 CYS A 1339 5 5
HELIX 21 AC3 THR A 1366 SER A 1372 1 7
HELIX 22 AC4 SER A 1394 GLY A 1402 1 9
HELIX 23 AC5 SER A 1418 HIS A 1427 1 10
HELIX 24 AC6 ASP A 1435 LEU A 1439 5 5
HELIX 25 AC7 CYS A 1476 ALA A 1481 5 6
HELIX 26 AC8 ASP A 1486 ARG A 1490 5 5
HELIX 27 AC9 TRP A 1498 THR A 1503 1 6
HELIX 28 AD1 GLY A 1504 ALA A 1511 5 8
HELIX 29 AD2 SER A 1549 GLN A 1557 1 9
HELIX 30 AD3 ASN A 1568 ASN A 1578 1 11
HELIX 31 AD4 PRO A 1581 LYS A 1599 1 19
HELIX 32 AD5 GLU C 560 HIS C 562 5 3
HELIX 33 AD6 ASP C 573 PHE C 575 5 3
HELIX 34 AD7 SER C 601 GLY C 614 1 14
HELIX 35 AD8 PRO C 616 ASP C 618 5 3
HELIX 36 AD9 THR C 647 SER C 652 1 6
HELIX 37 AE1 ASP C 666 ALA C 671 1 6
HELIX 38 AE2 LYS C 712 ASP C 715 5 4
HELIX 39 AE3 LEU C 716 ALA C 724 1 9
HELIX 40 AE4 SER C 752 LEU C 757 1 6
HELIX 41 AE5 ASP C 772 SER C 778 5 7
HELIX 42 AE6 THR C 782 HIS C 792 1 11
HELIX 43 AE7 ASN C 818 ASN C 831 1 14
HELIX 44 AE8 ASP C 833 MET C 835 5 3
HELIX 45 AE9 THR C 860 GLN C 866 1 7
HELIX 46 AF1 LYS C 884 ASN C 890 1 7
HELIX 47 AF2 CYS C 917 VAL C 929 1 13
HELIX 48 AF3 LEU C 958 LEU C 962 5 5
HELIX 49 AF4 PRO C 976 ASP C 981 1 6
HELIX 50 AF5 HIS C 1016 ASP C 1029 1 14
HELIX 51 AF6 GLU C 1034 PHE C 1038 5 5
HELIX 52 AF7 ASN C 1059 PHE C 1063 5 5
SHEET 1 AA1 3 ILE A 731 VAL A 734 0
SHEET 2 AA1 3 LYS A 749 ILE A 752 -1 O LYS A 749 N VAL A 734
SHEET 3 AA1 3 GLU A 755 GLU A 758 -1 O LEU A 757 N VAL A 750
SHEET 1 AA2 7 LYS A 739 THR A 740 0
SHEET 2 AA2 7 LYS A 744 TYR A 747 -1 O TYR A 746 N LYS A 739
SHEET 3 AA2 7 TYR A 775 ASP A 785 -1 O GLU A 784 N SER A 745
SHEET 4 AA2 7 GLY A 789 ALA A 799 -1 O GLY A 789 N ASP A 785
SHEET 5 AA2 7 GLU A 813 GLN A 824 -1 O MET A 823 N PHE A 792
SHEET 6 AA2 7 TYR A 863 ASP A 870 1 O TYR A 869 N LEU A 816
SHEET 7 AA2 7 VAL A 834 TYR A 836 1 N ILE A 835 O TYR A 863
SHEET 1 AA3 7 ILE A 828 VAL A 832 0
SHEET 2 AA3 7 CYS A 762 VAL A 765 -1 N SER A 764 O SER A 830
SHEET 3 AA3 7 TYR A 775 ASP A 785 -1 O TYR A 775 N VAL A 765
SHEET 4 AA3 7 GLY A 789 ALA A 799 -1 O GLY A 789 N ASP A 785
SHEET 5 AA3 7 GLU A 813 GLN A 824 -1 O MET A 823 N PHE A 792
SHEET 6 AA3 7 TYR A 863 ASP A 870 1 O TYR A 869 N LEU A 816
SHEET 7 AA3 7 ARG A 875 GLU A 877 -1 O ARG A 875 N ASP A 870
SHEET 1 AA4 3 ARG A 909 VAL A 910 0
SHEET 2 AA4 3 SER A 925 LYS A 928 -1 O THR A 927 N ARG A 909
SHEET 3 AA4 3 ILE A 931 ARG A 934 -1 O TYR A 933 N ALA A 926
SHEET 1 AA5 7 GLN A 913 ASP A 916 0
SHEET 2 AA5 7 ARG A 920 TYR A 923 -1 O LEU A 922 N GLU A 915
SHEET 3 AA5 7 ARG A 992 PRO A1002 -1 O ILE A 999 N TYR A 923
SHEET 4 AA5 7 GLY A 938 LEU A 941 -1 N VAL A 939 O GLY A 994
SHEET 5 AA5 7 GLY A1058 TYR A1064 -1 O GLY A1058 N TYR A 940
SHEET 6 AA5 7 ARG A1082 ASN A1090 1 O PHE A1083 N THR A1061
SHEET 7 AA5 7 SER A1095 GLU A1097 -1 O SER A1095 N ASN A1090
SHEET 1 AA6 7 GLN A 913 ASP A 916 0
SHEET 2 AA6 7 ARG A 920 TYR A 923 -1 O LEU A 922 N GLU A 915
SHEET 3 AA6 7 ARG A 992 PRO A1002 -1 O ILE A 999 N TYR A 923
SHEET 4 AA6 7 LYS A1015 TYR A1022 -1 O LYS A1015 N PHE A1000
SHEET 5 AA6 7 LEU A1041 ASP A1052 -1 O VAL A1051 N ILE A1016
SHEET 6 AA6 7 ARG A1082 ASN A1090 1 O TYR A1089 N TRP A1044
SHEET 7 AA6 7 SER A1095 GLU A1097 -1 O SER A1095 N ASN A1090
SHEET 1 AA7 7 THR A1185 PHE A1187 0
SHEET 2 AA7 7 SER A1161 ILE A1167 1 N LEU A1164 O THR A1185
SHEET 3 AA7 7 LEU A1139 VAL A1144 1 N LEU A1139 O ASP A1162
SHEET 4 AA7 7 MET A1219 GLY A1222 1 O MET A1219 N LEU A1142
SHEET 5 AA7 7 PHE A1262 VAL A1268 1 O GLU A1266 N GLY A1222
SHEET 6 AA7 7 ARG A1311 ALA A1318 -1 O ILE A1315 N LEU A1265
SHEET 7 AA7 7 GLN A1293 GLN A1300 -1 N GLY A1297 O ILE A1314
SHEET 1 AA8 2 VAL A1343 VAL A1345 0
SHEET 2 AA8 2 LYS A1348 PHE A1350 -1 O PHE A1350 N VAL A1343
SHEET 1 AA9 2 GLU A1385 ILE A1386 0
SHEET 2 AA9 2 LEU A1409 ARG A1410 -1 O LEU A1409 N ILE A1386
SHEET 1 AB1 2 VAL A1444 ARG A1445 0
SHEET 2 AB1 2 MET A1451 ALA A1452 -1 O ALA A1452 N VAL A1444
SHEET 1 AB2 5 THR C 592 LEU C 597 0
SHEET 2 AB2 5 TYR C 564 ALA C 571 -1 N MET C 565 O VAL C 596
SHEET 3 AB2 5 TRP C 658 THR C 664 1 O TRP C 658 N GLN C 566
SHEET 4 AB2 5 ILE C 620 ALA C 627 -1 N TRP C 623 O PHE C 661
SHEET 5 AB2 5 LYS C 633 PRO C 635 -1 O ARG C 634 N GLN C 626
SHEET 1 AB3 5 SER C 698 PRO C 708 0
SHEET 2 AB3 5 ASP C 684 ASP C 693 -1 N LEU C 689 O CYS C 702
SHEET 3 AB3 5 ILE C 765 LYS C 770 1 O ILE C 766 N PHE C 688
SHEET 4 AB3 5 LEU C 732 LYS C 739 -1 N TYR C 735 O VAL C 767
SHEET 5 AB3 5 LEU C 742 ARG C 745 -1 O GLU C 744 N GLU C 736
SHEET 1 AB4 5 PHE C 809 SER C 814 0
SHEET 2 AB4 5 ARG C 793 ASP C 800 -1 N VAL C 794 O LEU C 813
SHEET 3 AB4 5 LYS C 874 GLN C 880 1 O LYS C 874 N ILE C 797
SHEET 4 AB4 5 LEU C 837 SER C 842 -1 N GLN C 838 O GLN C 879
SHEET 5 AB4 5 PRO C 849 PRO C 852 -1 O GLY C 850 N LYS C 841
SHEET 1 AB5 5 GLU C 905 LEU C 910 0
SHEET 2 AB5 5 PHE C 894 LEU C 899 -1 N CYS C 896 O ILE C 908
SHEET 3 AB5 5 THR C 969 GLU C 974 1 O ILE C 972 N ILE C 897
SHEET 4 AB5 5 LEU C 939 VAL C 945 -1 N ILE C 944 O THR C 969
SHEET 5 AB5 5 LYS C 948 HIS C 953 -1 O LYS C 948 N VAL C 945
SHEET 1 AB6 5 THR C1002 ILE C1011 0
SHEET 2 AB6 5 MET C 988 PHE C 995 -1 N VAL C 990 O LEU C1009
SHEET 3 AB6 5 TRP C1076 ASP C1080 1 O LEU C1077 N THR C 991
SHEET 4 AB6 5 LYS C1039 MET C1044 -1 N VAL C1043 O TRP C1076
SHEET 5 AB6 5 ARG C1047 TYR C1050 -1 O ARG C1047 N MET C1044
LINK NE2 HIS A 793 ZN ZN A1702 1555 1555 2.08
LINK SG CYS A 820 ZN ZN A1702 1555 1555 2.33
LINK SG CYS A 893 ZN ZN A1702 1555 1555 2.30
LINK SG CYS A 896 ZN ZN A1702 1555 1555 2.37
LINK SG CYS A1476 ZN ZN A1701 1555 1555 2.47
LINK SG CYS A1478 ZN ZN A1701 1555 1555 2.43
LINK SG CYS A1485 ZN ZN A1701 1555 1555 2.53
LINK NE2 HIS A1502 ZN ZN A1701 1555 1555 2.22
CISPEP 1 ASN C 656 PRO C 657 0 -6.40
SITE 1 AC1 4 CYS A1476 CYS A1478 CYS A1485 HIS A1502
SITE 1 AC2 4 HIS A 793 CYS A 820 CYS A 893 CYS A 896
CRYST1 110.231 111.619 163.868 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 0.009072 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END