HEADER HYDROLASE/DNA 30-JUL-14 4U7D
TITLE STRUCTURE OF HUMAN RECQ-LIKE HELICASE IN COMPLEX WITH AN
TITLE 2 OLIGONUCLEOTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT DNA HELICASE Q1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 49-616;
COMPND 5 SYNONYM: DNA HELICASE,RECQ-LIKE TYPE 1,RECQ1,DNA-DEPENDENT ATPASE Q1,
COMPND 6 RECQ PROTEIN-LIKE 1;
COMPND 7 EC: 3.6.4.12;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA OLIGONUCLEOTIDE;
COMPND 11 CHAIN: P, Q, R, S;
COMPND 12 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: RECQL, RECQ1, RECQL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630
KEYWDS HYDROLASE-DNA COMPLEX, NUCLEAR PROTEIN, HYDROLASE, DNA STRAND
KEYWDS 2 ANNEALING, DNA BINDING PROTEIN, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.W.PIKE,Y.ZHANG,C.SCHNECKE,C.D.O.COOPER,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.EDWARDS,C.BOUNTRA,O.GILEADI,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 5 20-DEC-23 4U7D 1 REMARK
REVDAT 4 24-JAN-18 4U7D 1 AUTHOR
REVDAT 3 15-APR-15 4U7D 1 JRNL
REVDAT 2 01-APR-15 4U7D 1 JRNL
REVDAT 1 21-JAN-15 4U7D 0
JRNL AUTH A.C.PIKE,S.GOMATHINAYAGAM,P.SWUEC,M.BERTI,Y.ZHANG,
JRNL AUTH 2 C.SCHNECKE,F.MARINO,F.VON DELFT,L.RENAULT,A.COSTA,O.GILEADI,
JRNL AUTH 3 A.VINDIGNI
JRNL TITL HUMAN RECQ1 HELICASE-DRIVEN DNA UNWINDING, ANNEALING, AND
JRNL TITL 2 BRANCH MIGRATION: INSIGHTS FROM DNA COMPLEX STRUCTURES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 4286 2015
JRNL REFN ESSN 1091-6490
JRNL PMID 25831490
JRNL DOI 10.1073/PNAS.1417594112
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1682)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 40919
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.770
REMARK 3 FREE R VALUE TEST SET COUNT : 1951
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 24.9525 - 7.9160 0.90 3016 148 0.1576 0.2381
REMARK 3 2 7.9160 - 6.3168 0.88 2941 146 0.1939 0.2251
REMARK 3 3 6.3168 - 5.5282 0.90 2956 144 0.2138 0.2575
REMARK 3 4 5.5282 - 5.0272 0.90 2989 145 0.1930 0.2146
REMARK 3 5 5.0272 - 4.6694 0.90 2972 141 0.1956 0.2420
REMARK 3 6 4.6694 - 4.3957 0.90 3013 141 0.1983 0.2199
REMARK 3 7 4.3957 - 4.1766 0.91 2969 139 0.2125 0.2599
REMARK 3 8 4.1766 - 3.9956 0.92 3013 149 0.2317 0.2820
REMARK 3 9 3.9956 - 3.8423 0.90 2982 143 0.2472 0.3275
REMARK 3 10 3.8423 - 3.7102 0.93 3040 152 0.2566 0.2886
REMARK 3 11 3.7102 - 3.5945 0.91 3026 140 0.2555 0.2683
REMARK 3 12 3.5945 - 3.4921 0.93 3038 149 0.2659 0.2771
REMARK 3 13 3.4921 - 3.4004 0.90 2992 147 0.2729 0.2520
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 17671
REMARK 3 ANGLE : 1.140 24120
REMARK 3 CHIRALITY : 0.048 2767
REMARK 3 PLANARITY : 0.005 2906
REMARK 3 DIHEDRAL : 17.464 6449
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 283:592)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0009 2.1073 72.1414
REMARK 3 T TENSOR
REMARK 3 T11: 1.7247 T22: 0.9072
REMARK 3 T33: 0.8091 T12: -0.4850
REMARK 3 T13: -0.0820 T23: 0.0953
REMARK 3 L TENSOR
REMARK 3 L11: 2.2032 L22: 2.7344
REMARK 3 L33: 5.6714 L12: -0.5224
REMARK 3 L13: 0.7560 L23: -0.5226
REMARK 3 S TENSOR
REMARK 3 S11: -0.2270 S12: -0.6249 S13: 0.2592
REMARK 3 S21: 0.9694 S22: 0.0717 S23: -0.1044
REMARK 3 S31: -1.6371 S32: 0.4407 S33: -0.0130
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 63:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6349 5.1013 -34.6570
REMARK 3 T TENSOR
REMARK 3 T11: 0.6966 T22: 0.5818
REMARK 3 T33: 0.7875 T12: 0.2826
REMARK 3 T13: 0.0534 T23: -0.1524
REMARK 3 L TENSOR
REMARK 3 L11: 3.1712 L22: 3.2162
REMARK 3 L33: 6.1644 L12: -0.9923
REMARK 3 L13: 2.6925 L23: 0.3685
REMARK 3 S TENSOR
REMARK 3 S11: 0.0401 S12: -0.0192 S13: 0.0877
REMARK 3 S21: 0.2313 S22: -0.2179 S23: 0.1410
REMARK 3 S31: -0.2474 S32: -0.0834 S33: -0.0085
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 63:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6799 31.3229 29.9014
REMARK 3 T TENSOR
REMARK 3 T11: 0.8841 T22: 0.5711
REMARK 3 T33: 0.8970 T12: -0.0287
REMARK 3 T13: 0.1236 T23: 0.0668
REMARK 3 L TENSOR
REMARK 3 L11: 3.9672 L22: 2.5748
REMARK 3 L33: 6.1776 L12: 0.2827
REMARK 3 L13: -0.5214 L23: -2.4019
REMARK 3 S TENSOR
REMARK 3 S11: 0.4512 S12: 0.1721 S13: -0.0526
REMARK 3 S21: -0.3701 S22: -0.3876 S23: 0.0712
REMARK 3 S31: 1.1793 S32: 0.0534 S33: -0.0008
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 63:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7213 -40.1036 67.4081
REMARK 3 T TENSOR
REMARK 3 T11: 0.8061 T22: 0.8170
REMARK 3 T33: 0.7645 T12: -0.4854
REMARK 3 T13: 0.0088 T23: 0.1952
REMARK 3 L TENSOR
REMARK 3 L11: 2.0827 L22: 2.8325
REMARK 3 L33: 5.8021 L12: -0.4405
REMARK 3 L13: -0.3394 L23: 0.5830
REMARK 3 S TENSOR
REMARK 3 S11: 0.3210 S12: -0.2719 S13: 0.0352
REMARK 3 S21: 0.8291 S22: -0.2508 S23: 0.1314
REMARK 3 S31: 1.0247 S32: -0.4676 S33: 0.0196
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'P' OR CHAIN 'Q'
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6055 -33.2323 18.2508
REMARK 3 T TENSOR
REMARK 3 T11: 1.0500 T22: 1.1060
REMARK 3 T33: 1.0778 T12: 0.0167
REMARK 3 T13: 0.0557 T23: 0.0630
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: 2.6280
REMARK 3 L33: 1.2943 L12: 0.0947
REMARK 3 L13: -0.2979 L23: -0.2187
REMARK 3 S TENSOR
REMARK 3 S11: 0.2514 S12: 0.0810 S13: -0.4091
REMARK 3 S21: -0.4728 S22: 0.0714 S23: -0.1566
REMARK 3 S31: 1.4906 S32: -0.3626 S33: 0.0018
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'R' OR CHAIN 'S'
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5164 -11.1250 126.4360
REMARK 3 T TENSOR
REMARK 3 T11: 1.3176 T22: 1.7375
REMARK 3 T33: 1.5556 T12: 0.0096
REMARK 3 T13: -0.3514 T23: -0.1030
REMARK 3 L TENSOR
REMARK 3 L11: 0.1479 L22: -0.0365
REMARK 3 L33: 1.3673 L12: -0.0143
REMARK 3 L13: 0.4934 L23: 0.0317
REMARK 3 S TENSOR
REMARK 3 S11: -1.3233 S12: 0.0316 S13: 0.4121
REMARK 3 S21: -0.4018 S22: -0.4010 S23: 0.3331
REMARK 3 S31: 1.2145 S32: -0.4749 S33: -0.1727
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 283:592)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4311 -12.2896 39.7224
REMARK 3 T TENSOR
REMARK 3 T11: 0.4101 T22: 0.3983
REMARK 3 T33: 0.6166 T12: -0.2246
REMARK 3 T13: -0.0097 T23: 0.0962
REMARK 3 L TENSOR
REMARK 3 L11: 4.5029 L22: 2.4022
REMARK 3 L33: 4.2786 L12: 1.8511
REMARK 3 L13: 1.2392 L23: 0.8576
REMARK 3 S TENSOR
REMARK 3 S11: 0.0538 S12: 0.1145 S13: 0.3296
REMARK 3 S21: 0.0293 S22: -0.0861 S23: 0.0862
REMARK 3 S31: -0.4916 S32: 0.2761 S33: -0.0258
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 283:592)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0667 -10.3221 -1.8817
REMARK 3 T TENSOR
REMARK 3 T11: 0.4246 T22: 0.6453
REMARK 3 T33: 0.6576 T12: 0.0059
REMARK 3 T13: 0.0529 T23: -0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 3.6001 L22: 3.5552
REMARK 3 L33: 6.3007 L12: -1.6644
REMARK 3 L13: 1.1810 L23: -2.0465
REMARK 3 S TENSOR
REMARK 3 S11: -0.2549 S12: -0.3748 S13: 0.3813
REMARK 3 S21: 0.2796 S22: 0.2021 S23: -0.0382
REMARK 3 S31: -0.6109 S32: -0.4982 S33: 0.0087
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 283:592)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.8632 47.5987 63.1974
REMARK 3 T TENSOR
REMARK 3 T11: 1.1530 T22: 0.8043
REMARK 3 T33: 0.6350 T12: -0.4861
REMARK 3 T13: 0.1201 T23: 0.1149
REMARK 3 L TENSOR
REMARK 3 L11: 3.2472 L22: 5.3560
REMARK 3 L33: 5.7864 L12: 0.7330
REMARK 3 L13: 1.2880 L23: 0.8706
REMARK 3 S TENSOR
REMARK 3 S11: 0.2374 S12: -0.6042 S13: -0.1450
REMARK 3 S21: 0.6678 S22: -0.2202 S23: -0.1136
REMARK 3 S31: 0.4535 S32: 0.4826 S33: 0.0006
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 283:592)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9014 -24.2770 100.6505
REMARK 3 T TENSOR
REMARK 3 T11: 1.5526 T22: 1.5643
REMARK 3 T33: 0.7365 T12: -0.4278
REMARK 3 T13: 0.0354 T23: 0.1785
REMARK 3 L TENSOR
REMARK 3 L11: 2.6400 L22: 3.7147
REMARK 3 L33: 3.9631 L12: 0.9526
REMARK 3 L13: 0.7394 L23: 1.4883
REMARK 3 S TENSOR
REMARK 3 S11: 0.0894 S12: -0.9556 S13: -0.3218
REMARK 3 S21: 0.5905 S22: -0.0229 S23: -0.0732
REMARK 3 S31: 0.5769 S32: -0.3858 S33: -0.0000
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 4U7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40962
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 83.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 2V1X
REMARK 200
REMARK 200 REMARK: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.18M POTASSIUM CITRATE, 17% (W/V)
REMARK 280 PEG3350, 5% (V/V) ETHYLENE GLYCOL, 0.1M BIS-TRIS PROPANE PH6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 69.11000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, Q
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, R, S
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 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 55.30754
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -69.11000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 207.58099
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: D, R, S
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 55.30754
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 69.11000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 207.58099
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 MET A 48
REMARK 465 CYS A 49
REMARK 465 LEU A 50
REMARK 465 GLU A 51
REMARK 465 ASP A 52
REMARK 465 SER A 53
REMARK 465 ASP A 54
REMARK 465 ALA A 55
REMARK 465 GLY A 56
REMARK 465 ALA A 57
REMARK 465 SER A 58
REMARK 465 ASN A 59
REMARK 465 GLU A 60
REMARK 465 TYR A 61
REMARK 465 ASP A 62
REMARK 465 ASN A 467
REMARK 465 SER A 468
REMARK 465 GLU A 469
REMARK 465 SER A 593
REMARK 465 THR A 594
REMARK 465 GLN A 595
REMARK 465 ASN A 596
REMARK 465 SER A 597
REMARK 465 PHE A 598
REMARK 465 ARG A 599
REMARK 465 ALA A 600
REMARK 465 GLU A 601
REMARK 465 SER A 602
REMARK 465 SER A 603
REMARK 465 GLN A 604
REMARK 465 THR A 605
REMARK 465 CYS A 606
REMARK 465 HIS A 607
REMARK 465 SER A 608
REMARK 465 GLU A 609
REMARK 465 GLN A 610
REMARK 465 SER A 611
REMARK 465 ASP A 612
REMARK 465 LYS A 613
REMARK 465 LYS A 614
REMARK 465 MET A 615
REMARK 465 GLU A 616
REMARK 465 ALA A 617
REMARK 465 GLU A 618
REMARK 465 ASN A 619
REMARK 465 LEU A 620
REMARK 465 TYR A 621
REMARK 465 PHE A 622
REMARK 465 GLN A 623
REMARK 465 SER A 624
REMARK 465 HIS A 625
REMARK 465 HIS A 626
REMARK 465 HIS A 627
REMARK 465 HIS A 628
REMARK 465 HIS A 629
REMARK 465 HIS A 630
REMARK 465 ASP A 631
REMARK 465 TYR A 632
REMARK 465 LYS A 633
REMARK 465 ASP A 634
REMARK 465 ASP A 635
REMARK 465 ASP A 636
REMARK 465 ASP A 637
REMARK 465 LYS A 638
REMARK 465 MET B 48
REMARK 465 CYS B 49
REMARK 465 LEU B 50
REMARK 465 GLU B 51
REMARK 465 ASP B 52
REMARK 465 SER B 53
REMARK 465 ASP B 54
REMARK 465 ALA B 55
REMARK 465 GLY B 56
REMARK 465 ALA B 57
REMARK 465 SER B 58
REMARK 465 ASN B 59
REMARK 465 GLU B 60
REMARK 465 TYR B 61
REMARK 465 ASP B 62
REMARK 465 ASN B 467
REMARK 465 SER B 468
REMARK 465 GLU B 469
REMARK 465 SER B 593
REMARK 465 THR B 594
REMARK 465 GLN B 595
REMARK 465 ASN B 596
REMARK 465 SER B 597
REMARK 465 PHE B 598
REMARK 465 ARG B 599
REMARK 465 ALA B 600
REMARK 465 GLU B 601
REMARK 465 SER B 602
REMARK 465 SER B 603
REMARK 465 GLN B 604
REMARK 465 THR B 605
REMARK 465 CYS B 606
REMARK 465 HIS B 607
REMARK 465 SER B 608
REMARK 465 GLU B 609
REMARK 465 GLN B 610
REMARK 465 SER B 611
REMARK 465 ASP B 612
REMARK 465 LYS B 613
REMARK 465 LYS B 614
REMARK 465 MET B 615
REMARK 465 GLU B 616
REMARK 465 ALA B 617
REMARK 465 GLU B 618
REMARK 465 ASN B 619
REMARK 465 LEU B 620
REMARK 465 TYR B 621
REMARK 465 PHE B 622
REMARK 465 GLN B 623
REMARK 465 SER B 624
REMARK 465 HIS B 625
REMARK 465 HIS B 626
REMARK 465 HIS B 627
REMARK 465 HIS B 628
REMARK 465 HIS B 629
REMARK 465 HIS B 630
REMARK 465 ASP B 631
REMARK 465 TYR B 632
REMARK 465 LYS B 633
REMARK 465 ASP B 634
REMARK 465 ASP B 635
REMARK 465 ASP B 636
REMARK 465 ASP B 637
REMARK 465 LYS B 638
REMARK 465 MET C 48
REMARK 465 CYS C 49
REMARK 465 LEU C 50
REMARK 465 GLU C 51
REMARK 465 ASP C 52
REMARK 465 SER C 53
REMARK 465 ASP C 54
REMARK 465 ALA C 55
REMARK 465 GLY C 56
REMARK 465 ALA C 57
REMARK 465 SER C 58
REMARK 465 ASN C 59
REMARK 465 GLU C 60
REMARK 465 TYR C 61
REMARK 465 ASP C 62
REMARK 465 SER C 593
REMARK 465 THR C 594
REMARK 465 GLN C 595
REMARK 465 ASN C 596
REMARK 465 SER C 597
REMARK 465 PHE C 598
REMARK 465 ARG C 599
REMARK 465 ALA C 600
REMARK 465 GLU C 601
REMARK 465 SER C 602
REMARK 465 SER C 603
REMARK 465 GLN C 604
REMARK 465 THR C 605
REMARK 465 CYS C 606
REMARK 465 HIS C 607
REMARK 465 SER C 608
REMARK 465 GLU C 609
REMARK 465 GLN C 610
REMARK 465 SER C 611
REMARK 465 ASP C 612
REMARK 465 LYS C 613
REMARK 465 LYS C 614
REMARK 465 MET C 615
REMARK 465 GLU C 616
REMARK 465 ALA C 617
REMARK 465 GLU C 618
REMARK 465 ASN C 619
REMARK 465 LEU C 620
REMARK 465 TYR C 621
REMARK 465 PHE C 622
REMARK 465 GLN C 623
REMARK 465 SER C 624
REMARK 465 HIS C 625
REMARK 465 HIS C 626
REMARK 465 HIS C 627
REMARK 465 HIS C 628
REMARK 465 HIS C 629
REMARK 465 HIS C 630
REMARK 465 ASP C 631
REMARK 465 TYR C 632
REMARK 465 LYS C 633
REMARK 465 ASP C 634
REMARK 465 ASP C 635
REMARK 465 ASP C 636
REMARK 465 ASP C 637
REMARK 465 LYS C 638
REMARK 465 MET D 48
REMARK 465 CYS D 49
REMARK 465 LEU D 50
REMARK 465 GLU D 51
REMARK 465 ASP D 52
REMARK 465 SER D 53
REMARK 465 ASP D 54
REMARK 465 ALA D 55
REMARK 465 GLY D 56
REMARK 465 ALA D 57
REMARK 465 SER D 58
REMARK 465 ASN D 59
REMARK 465 GLU D 60
REMARK 465 TYR D 61
REMARK 465 ASP D 62
REMARK 465 SER D 593
REMARK 465 THR D 594
REMARK 465 GLN D 595
REMARK 465 ASN D 596
REMARK 465 SER D 597
REMARK 465 PHE D 598
REMARK 465 ARG D 599
REMARK 465 ALA D 600
REMARK 465 GLU D 601
REMARK 465 SER D 602
REMARK 465 SER D 603
REMARK 465 GLN D 604
REMARK 465 THR D 605
REMARK 465 CYS D 606
REMARK 465 HIS D 607
REMARK 465 SER D 608
REMARK 465 GLU D 609
REMARK 465 GLN D 610
REMARK 465 SER D 611
REMARK 465 ASP D 612
REMARK 465 LYS D 613
REMARK 465 LYS D 614
REMARK 465 MET D 615
REMARK 465 GLU D 616
REMARK 465 ALA D 617
REMARK 465 GLU D 618
REMARK 465 ASN D 619
REMARK 465 LEU D 620
REMARK 465 TYR D 621
REMARK 465 PHE D 622
REMARK 465 GLN D 623
REMARK 465 SER D 624
REMARK 465 HIS D 625
REMARK 465 HIS D 626
REMARK 465 HIS D 627
REMARK 465 HIS D 628
REMARK 465 HIS D 629
REMARK 465 HIS D 630
REMARK 465 ASP D 631
REMARK 465 TYR D 632
REMARK 465 LYS D 633
REMARK 465 ASP D 634
REMARK 465 ASP D 635
REMARK 465 ASP D 636
REMARK 465 ASP D 637
REMARK 465 LYS D 638
REMARK 465 DC P 18
REMARK 465 DT P 19
REMARK 465 DT P 20
REMARK 465 DC Q 21
REMARK 465 DC Q 25
REMARK 465 DT Q 26
REMARK 465 DT Q 27
REMARK 465 DC R 5
REMARK 465 DT R 6
REMARK 465 DC R 7
REMARK 465 DG R 8
REMARK 465 DA R 9
REMARK 465 DC R 10
REMARK 465 DG R 11
REMARK 465 DC R 17
REMARK 465 DC R 18
REMARK 465 DT R 19
REMARK 465 DT R 20
REMARK 465 DC S 12
REMARK 465 DT S 13
REMARK 465 DC S 14
REMARK 465 DT S 15
REMARK 465 DC S 16
REMARK 465 DC S 17
REMARK 465 DC S 18
REMARK 465 DT S 19
REMARK 465 DT S 20
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 LYS A 80 CG CD CE NZ
REMARK 470 LYS A 91 CD CE NZ
REMARK 470 LYS A 107 NZ
REMARK 470 ILE A 141 CD1
REMARK 470 MET A 149 SD CE
REMARK 470 LYS A 152 CD CE NZ
REMARK 470 GLN A 153 CG CD OE1 NE2
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 LYS A 171 CG CD CE NZ
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 GLU A 192 CD OE1 OE2
REMARK 470 LYS A 196 CE NZ
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 ARG A 211 NE CZ NH1 NH2
REMARK 470 GLN A 226 CG CD OE1 NE2
REMARK 470 HIS A 229 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 230 CG OD1 OD2
REMARK 470 ARG A 232 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 236 CD CE NZ
REMARK 470 ILE A 240 CG1 CG2 CD1
REMARK 470 HIS A 260 ND1 CD2 CE1 NE2
REMARK 470 LYS A 273 CG CD CE NZ
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 GLU A 302 CD OE1 OE2
REMARK 470 LYS A 306 NZ
REMARK 470 LYS A 313 CG CD CE NZ
REMARK 470 GLU A 351 OE1 OE2
REMARK 470 LYS A 353 CG CD CE NZ
REMARK 470 ARG A 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 359 CD CE NZ
REMARK 470 GLU A 364 CD OE1 OE2
REMARK 470 MET A 376 CG SD CE
REMARK 470 ILE A 378 CD1
REMARK 470 LYS A 411 CD CE NZ
REMARK 470 GLN A 438 OE1 NE2
REMARK 470 LYS A 452 NZ
REMARK 470 ASP A 481 CG OD1 OD2
REMARK 470 LYS A 501 CD CE NZ
REMARK 470 ILE A 516 CD1
REMARK 470 LYS A 522 CE NZ
REMARK 470 THR A 536 OG1 CG2
REMARK 470 GLU A 540 CG CD OE1 OE2
REMARK 470 TYR A 564 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 571 NZ
REMARK 470 LYS A 575 NZ
REMARK 470 LYS A 592 CE NZ
REMARK 470 LYS B 80 CG CD CE NZ
REMARK 470 LYS B 91 CD CE NZ
REMARK 470 LYS B 107 NZ
REMARK 470 ILE B 141 CD1
REMARK 470 LYS B 152 CD CE NZ
REMARK 470 GLN B 153 CG CD OE1 NE2
REMARK 470 LYS B 167 CG CD CE NZ
REMARK 470 LYS B 171 CG CD CE NZ
REMARK 470 LYS B 180 CG CD CE NZ
REMARK 470 GLU B 192 CD OE1 OE2
REMARK 470 LYS B 196 CE NZ
REMARK 470 LYS B 198 CG CD CE NZ
REMARK 470 ARG B 211 NE CZ NH1 NH2
REMARK 470 GLN B 226 CG CD OE1 NE2
REMARK 470 HIS B 229 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 230 CG OD1 OD2
REMARK 470 ARG B 232 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 236 CD CE NZ
REMARK 470 HIS B 260 ND1 CD2 CE1 NE2
REMARK 470 LYS B 273 CG CD CE NZ
REMARK 470 GLU B 298 CG CD OE1 OE2
REMARK 470 GLU B 302 CD OE1 OE2
REMARK 470 LYS B 306 NZ
REMARK 470 LYS B 313 CG CD CE NZ
REMARK 470 GLU B 349 CG CD OE1 OE2
REMARK 470 GLU B 351 OE1 OE2
REMARK 470 LYS B 353 CG CD CE NZ
REMARK 470 ARG B 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 359 CD CE NZ
REMARK 470 GLU B 364 CD OE1 OE2
REMARK 470 MET B 376 CG SD CE
REMARK 470 ILE B 378 CD1
REMARK 470 ARG B 407 CD NE CZ NH1 NH2
REMARK 470 LYS B 411 CD CE NZ
REMARK 470 GLN B 438 OE1 NE2
REMARK 470 LYS B 452 NZ
REMARK 470 ASP B 481 CG OD1 OD2
REMARK 470 LYS B 501 CD CE NZ
REMARK 470 ILE B 516 CD1
REMARK 470 LYS B 522 CE NZ
REMARK 470 THR B 536 OG1 CG2
REMARK 470 GLU B 540 CG CD OE1 OE2
REMARK 470 TYR B 564 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 571 NZ
REMARK 470 LYS B 575 NZ
REMARK 470 LYS B 592 CE NZ
REMARK 470 LYS C 80 CG CD CE NZ
REMARK 470 LYS C 91 CD CE NZ
REMARK 470 LYS C 107 NZ
REMARK 470 ILE C 141 CD1
REMARK 470 MET C 149 SD CE
REMARK 470 LYS C 152 CD CE NZ
REMARK 470 GLN C 153 CG CD OE1 NE2
REMARK 470 LYS C 167 CG CD CE NZ
REMARK 470 LYS C 171 CG CD CE NZ
REMARK 470 LYS C 180 CG CD CE NZ
REMARK 470 GLU C 192 CD OE1 OE2
REMARK 470 LYS C 196 CE NZ
REMARK 470 LYS C 198 CG CD CE NZ
REMARK 470 ARG C 211 NE CZ NH1 NH2
REMARK 470 GLN C 226 CG CD OE1 NE2
REMARK 470 HIS C 229 CG ND1 CD2 CE1 NE2
REMARK 470 ASP C 230 CG OD1 OD2
REMARK 470 ARG C 232 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 236 CD CE NZ
REMARK 470 HIS C 260 ND1 CD2 CE1 NE2
REMARK 470 LYS C 273 CG CD CE NZ
REMARK 470 GLU C 298 CG CD OE1 OE2
REMARK 470 GLU C 302 CD OE1 OE2
REMARK 470 LYS C 306 NZ
REMARK 470 LYS C 313 CG CD CE NZ
REMARK 470 GLU C 349 CG CD OE1 OE2
REMARK 470 GLU C 351 OE1 OE2
REMARK 470 LYS C 353 CG CD CE NZ
REMARK 470 ARG C 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 359 CD CE NZ
REMARK 470 GLU C 364 CD OE1 OE2
REMARK 470 MET C 376 CG SD CE
REMARK 470 ILE C 378 CD1
REMARK 470 ARG C 407 CD NE CZ NH1 NH2
REMARK 470 LYS C 411 CD CE NZ
REMARK 470 ASN C 434 CG OD1 ND2
REMARK 470 GLN C 438 OE1 NE2
REMARK 470 LYS C 452 NZ
REMARK 470 ASN C 467 CG OD1 ND2
REMARK 470 SER C 468 OG
REMARK 470 GLU C 469 CG CD OE1 OE2
REMARK 470 ASP C 481 CG OD1 OD2
REMARK 470 LYS C 501 CD CE NZ
REMARK 470 ILE C 516 CD1
REMARK 470 LYS C 522 CE NZ
REMARK 470 THR C 536 OG1 CG2
REMARK 470 GLU C 540 CG CD OE1 OE2
REMARK 470 TYR C 564 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 571 NZ
REMARK 470 LYS C 575 NZ
REMARK 470 LYS C 592 CE NZ
REMARK 470 LYS D 80 CG CD CE NZ
REMARK 470 LYS D 91 CD CE NZ
REMARK 470 LYS D 107 NZ
REMARK 470 ILE D 141 CD1
REMARK 470 MET D 149 SD CE
REMARK 470 LYS D 152 CD CE NZ
REMARK 470 GLN D 153 CG CD OE1 NE2
REMARK 470 LYS D 167 CG CD CE NZ
REMARK 470 LYS D 171 CG CD CE NZ
REMARK 470 LYS D 180 CG CD CE NZ
REMARK 470 GLU D 192 CD OE1 OE2
REMARK 470 LYS D 196 CE NZ
REMARK 470 LYS D 198 CG CD CE NZ
REMARK 470 ARG D 211 NE CZ NH1 NH2
REMARK 470 GLN D 226 CG CD OE1 NE2
REMARK 470 HIS D 229 CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 230 CG OD1 OD2
REMARK 470 ARG D 232 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 236 CD CE NZ
REMARK 470 HIS D 260 ND1 CD2 CE1 NE2
REMARK 470 LYS D 273 CG CD CE NZ
REMARK 470 GLU D 298 CG CD OE1 OE2
REMARK 470 GLU D 302 CD OE1 OE2
REMARK 470 LYS D 306 NZ
REMARK 470 LYS D 313 CG CD CE NZ
REMARK 470 GLU D 349 CG CD OE1 OE2
REMARK 470 GLU D 351 OE1 OE2
REMARK 470 LYS D 353 CG CD CE NZ
REMARK 470 ARG D 358 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 359 CD CE NZ
REMARK 470 GLU D 364 CD OE1 OE2
REMARK 470 MET D 376 CG SD CE
REMARK 470 ILE D 378 CD1
REMARK 470 ARG D 407 CD NE CZ NH1 NH2
REMARK 470 LYS D 411 CD CE NZ
REMARK 470 GLN D 438 OE1 NE2
REMARK 470 LYS D 452 NZ
REMARK 470 ASN D 467 CG OD1 ND2
REMARK 470 ASP D 481 CG OD1 OD2
REMARK 470 LYS D 501 CD CE NZ
REMARK 470 ILE D 516 CD1
REMARK 470 LYS D 522 CE NZ
REMARK 470 THR D 536 OG1 CG2
REMARK 470 GLU D 540 CG CD OE1 OE2
REMARK 470 TYR D 564 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 571 NZ
REMARK 470 LYS D 575 NZ
REMARK 470 LYS D 592 CE NZ
REMARK 470 DC P 14 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC P 14 C6
REMARK 470 DT P 15 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT P 15 C7 C6
REMARK 470 DG Q 8 O5'
REMARK 470 DT Q 22 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT Q 22 C7 C6
REMARK 470 DC R 14 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC R 14 C6
REMARK 470 DC R 16 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DC R 16 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC R 16 C6
REMARK 470 DC S 5 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC S 5 C6
REMARK 470 DG S 8 N9 C8 N7 C5 C6 O6 N1
REMARK 470 DG S 8 C2 N2 N3 C4
REMARK 470 DA S 9 N9 C8 N7 C5 C6 N6 N1
REMARK 470 DA S 9 C2 N3 C4
REMARK 470 DC S 10 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC S 10 C6
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 O SER B 130 NZ LYS B 185 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 DA P 3 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT P 6 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG P 8 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA P 9 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC Q 12 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT Q 13 O4' - C1' - N1 ANGL. DEV. = 2.8 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 LEU A 95 -4.14 64.27
REMARK 500 PRO A 114 152.61 -46.99
REMARK 500 SER A 164 32.53 -81.53
REMARK 500 HIS A 229 40.95 -71.54
REMARK 500 ASP A 230 30.78 -154.06
REMARK 500 GLU A 272 125.58 -175.66
REMARK 500 VAL A 372 -14.57 -49.22
REMARK 500 ASP A 382 42.91 -108.41
REMARK 500 ASN A 434 -71.16 -33.60
REMARK 500 VAL A 465 87.62 -63.53
REMARK 500 LYS A 522 -167.52 -116.16
REMARK 500 THR A 536 37.18 -84.67
REMARK 500 LEU B 95 -5.48 64.03
REMARK 500 PRO B 114 152.64 -47.10
REMARK 500 HIS B 229 40.78 -72.06
REMARK 500 ASP B 230 31.42 -155.64
REMARK 500 GLU B 272 125.33 -174.33
REMARK 500 VAL B 372 -15.71 -49.99
REMARK 500 ASP B 382 43.33 -108.06
REMARK 500 ASN B 434 -71.18 -33.28
REMARK 500 VAL B 465 84.10 -64.08
REMARK 500 LYS B 522 -167.55 -115.66
REMARK 500 THR B 536 37.43 -84.86
REMARK 500 LEU C 95 -4.72 64.48
REMARK 500 PRO C 114 152.07 -47.14
REMARK 500 SER C 164 31.84 -82.15
REMARK 500 HIS C 229 41.41 -71.13
REMARK 500 ASP C 230 31.50 -150.97
REMARK 500 GLU C 272 125.59 -172.03
REMARK 500 VAL C 372 -14.83 -49.36
REMARK 500 ASP C 382 42.69 -108.12
REMARK 500 ASN C 434 -70.97 -32.76
REMARK 500 VAL C 465 83.70 -63.10
REMARK 500 GLU C 469 58.71 -113.47
REMARK 500 LYS C 522 -167.61 -115.82
REMARK 500 THR C 536 37.53 -84.75
REMARK 500 LEU D 95 -4.82 64.14
REMARK 500 PRO D 114 152.58 -46.98
REMARK 500 SER D 164 32.22 -81.53
REMARK 500 HIS D 229 42.23 -69.72
REMARK 500 ASP D 230 31.21 -152.06
REMARK 500 GLU D 272 125.64 -171.98
REMARK 500 ASP D 382 43.22 -108.13
REMARK 500 ASN D 434 -70.97 -32.76
REMARK 500 VAL D 465 90.74 -64.04
REMARK 500 GLU D 469 62.18 -114.50
REMARK 500 LYS D 522 -167.32 -115.42
REMARK 500 THR D 536 37.25 -84.78
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 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 453 SG
REMARK 620 2 CYS A 471 SG 107.7
REMARK 620 3 CYS A 475 SG 123.0 118.7
REMARK 620 4 CYS A 478 SG 92.0 119.2 92.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 453 SG
REMARK 620 2 CYS B 471 SG 94.9
REMARK 620 3 CYS B 475 SG 103.6 120.0
REMARK 620 4 CYS B 478 SG 88.7 126.9 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 453 SG
REMARK 620 2 CYS C 471 SG 100.0
REMARK 620 3 CYS C 475 SG 113.2 124.1
REMARK 620 4 CYS C 478 SG 86.3 125.9 100.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 453 SG
REMARK 620 2 CYS D 471 SG 112.9
REMARK 620 3 CYS D 475 SG 116.8 130.0
REMARK 620 4 CYS D 478 SG 78.5 106.9 88.1
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 701
DBREF 4U7D A 49 616 UNP P46063 RECQ1_HUMAN 49 616
DBREF 4U7D B 49 616 UNP P46063 RECQ1_HUMAN 49 616
DBREF 4U7D C 49 616 UNP P46063 RECQ1_HUMAN 49 616
DBREF 4U7D D 49 616 UNP P46063 RECQ1_HUMAN 49 616
DBREF 4U7D P 1 20 PDB 4U7D 4U7D 1 20
DBREF 4U7D Q 8 27 PDB 4U7D 4U7D 8 27
DBREF 4U7D R 1 20 PDB 4U7D 4U7D 1 20
DBREF 4U7D S 1 20 PDB 4U7D 4U7D 1 20
SEQADV 4U7D MET A 48 UNP P46063 INITIATING METHIONINE
SEQADV 4U7D SER A 611 UNP P46063 GLY 611 CONFLICT
SEQADV 4U7D ALA A 617 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLU A 618 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASN A 619 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LEU A 620 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR A 621 UNP P46063 EXPRESSION TAG
SEQADV 4U7D PHE A 622 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLN A 623 UNP P46063 EXPRESSION TAG
SEQADV 4U7D SER A 624 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS A 625 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS A 626 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS A 627 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS A 628 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS A 629 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS A 630 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP A 631 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR A 632 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS A 633 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP A 634 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP A 635 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP A 636 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP A 637 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS A 638 UNP P46063 EXPRESSION TAG
SEQADV 4U7D MET B 48 UNP P46063 INITIATING METHIONINE
SEQADV 4U7D SER B 611 UNP P46063 GLY 611 CONFLICT
SEQADV 4U7D ALA B 617 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLU B 618 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASN B 619 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LEU B 620 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR B 621 UNP P46063 EXPRESSION TAG
SEQADV 4U7D PHE B 622 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLN B 623 UNP P46063 EXPRESSION TAG
SEQADV 4U7D SER B 624 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS B 625 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS B 626 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS B 627 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS B 628 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS B 629 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS B 630 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP B 631 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR B 632 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS B 633 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP B 634 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP B 635 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP B 636 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP B 637 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS B 638 UNP P46063 EXPRESSION TAG
SEQADV 4U7D MET C 48 UNP P46063 INITIATING METHIONINE
SEQADV 4U7D SER C 611 UNP P46063 GLY 611 CONFLICT
SEQADV 4U7D ALA C 617 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLU C 618 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASN C 619 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LEU C 620 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR C 621 UNP P46063 EXPRESSION TAG
SEQADV 4U7D PHE C 622 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLN C 623 UNP P46063 EXPRESSION TAG
SEQADV 4U7D SER C 624 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS C 625 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS C 626 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS C 627 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS C 628 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS C 629 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS C 630 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP C 631 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR C 632 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS C 633 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP C 634 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP C 635 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP C 636 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP C 637 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS C 638 UNP P46063 EXPRESSION TAG
SEQADV 4U7D MET D 48 UNP P46063 INITIATING METHIONINE
SEQADV 4U7D SER D 611 UNP P46063 GLY 611 CONFLICT
SEQADV 4U7D ALA D 617 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLU D 618 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASN D 619 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LEU D 620 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR D 621 UNP P46063 EXPRESSION TAG
SEQADV 4U7D PHE D 622 UNP P46063 EXPRESSION TAG
SEQADV 4U7D GLN D 623 UNP P46063 EXPRESSION TAG
SEQADV 4U7D SER D 624 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS D 625 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS D 626 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS D 627 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS D 628 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS D 629 UNP P46063 EXPRESSION TAG
SEQADV 4U7D HIS D 630 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP D 631 UNP P46063 EXPRESSION TAG
SEQADV 4U7D TYR D 632 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS D 633 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP D 634 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP D 635 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP D 636 UNP P46063 EXPRESSION TAG
SEQADV 4U7D ASP D 637 UNP P46063 EXPRESSION TAG
SEQADV 4U7D LYS D 638 UNP P46063 EXPRESSION TAG
SEQRES 1 A 591 MET CYS LEU GLU ASP SER ASP ALA GLY ALA SER ASN GLU
SEQRES 2 A 591 TYR ASP SER SER PRO ALA ALA TRP ASN LYS GLU ASP PHE
SEQRES 3 A 591 PRO TRP SER GLY LYS VAL LYS ASP ILE LEU GLN ASN VAL
SEQRES 4 A 591 PHE LYS LEU GLU LYS PHE ARG PRO LEU GLN LEU GLU THR
SEQRES 5 A 591 ILE ASN VAL THR MET ALA GLY LYS GLU VAL PHE LEU VAL
SEQRES 6 A 591 MET PRO THR GLY GLY GLY LYS SER LEU CYS TYR GLN LEU
SEQRES 7 A 591 PRO ALA LEU CYS SER ASP GLY PHE THR LEU VAL ILE CYS
SEQRES 8 A 591 PRO LEU ILE SER LEU MET GLU ASP GLN LEU MET VAL LEU
SEQRES 9 A 591 LYS GLN LEU GLY ILE SER ALA THR MET LEU ASN ALA SER
SEQRES 10 A 591 SER SER LYS GLU HIS VAL LYS TRP VAL HIS ALA GLU MET
SEQRES 11 A 591 VAL ASN LYS ASN SER GLU LEU LYS LEU ILE TYR VAL THR
SEQRES 12 A 591 PRO GLU LYS ILE ALA LYS SER LYS MET PHE MET SER ARG
SEQRES 13 A 591 LEU GLU LYS ALA TYR GLU ALA ARG ARG PHE THR ARG ILE
SEQRES 14 A 591 ALA VAL ASP GLU VAL HIS CYS CYS SER GLN TRP GLY HIS
SEQRES 15 A 591 ASP PHE ARG PRO ASP TYR LYS ALA LEU GLY ILE LEU LYS
SEQRES 16 A 591 ARG GLN PHE PRO ASN ALA SER LEU ILE GLY LEU THR ALA
SEQRES 17 A 591 THR ALA THR ASN HIS VAL LEU THR ASP ALA GLN LYS ILE
SEQRES 18 A 591 LEU CYS ILE GLU LYS CYS PHE THR PHE THR ALA SER PHE
SEQRES 19 A 591 ASN ARG PRO ASN LEU TYR TYR GLU VAL ARG GLN LYS PRO
SEQRES 20 A 591 SER ASN THR GLU ASP PHE ILE GLU ASP ILE VAL LYS LEU
SEQRES 21 A 591 ILE ASN GLY ARG TYR LYS GLY GLN SER GLY ILE ILE TYR
SEQRES 22 A 591 CYS PHE SER GLN LYS ASP SER GLU GLN VAL THR VAL SER
SEQRES 23 A 591 LEU GLN ASN LEU GLY ILE HIS ALA GLY ALA TYR HIS ALA
SEQRES 24 A 591 ASN LEU GLU PRO GLU ASP LYS THR THR VAL HIS ARG LYS
SEQRES 25 A 591 TRP SER ALA ASN GLU ILE GLN VAL VAL VAL ALA THR VAL
SEQRES 26 A 591 ALA PHE GLY MET GLY ILE ASP LYS PRO ASP VAL ARG PHE
SEQRES 27 A 591 VAL ILE HIS HIS SER MET SER LYS SER MET GLU ASN TYR
SEQRES 28 A 591 TYR GLN GLU SER GLY ARG ALA GLY ARG ASP ASP MET LYS
SEQRES 29 A 591 ALA ASP CYS ILE LEU TYR TYR GLY PHE GLY ASP ILE PHE
SEQRES 30 A 591 ARG ILE SER SER MET VAL VAL MET GLU ASN VAL GLY GLN
SEQRES 31 A 591 GLN LYS LEU TYR GLU MET VAL SER TYR CYS GLN ASN ILE
SEQRES 32 A 591 SER LYS CYS ARG ARG VAL LEU MET ALA GLN HIS PHE ASP
SEQRES 33 A 591 GLU VAL TRP ASN SER GLU ALA CYS ASN LYS MET CYS ASP
SEQRES 34 A 591 ASN CYS CYS LYS ASP SER ALA PHE GLU ARG LYS ASN ILE
SEQRES 35 A 591 THR GLU TYR CYS ARG ASP LEU ILE LYS ILE LEU LYS GLN
SEQRES 36 A 591 ALA GLU GLU LEU ASN GLU LYS LEU THR PRO LEU LYS LEU
SEQRES 37 A 591 ILE ASP SER TRP MET GLY LYS GLY ALA ALA LYS LEU ARG
SEQRES 38 A 591 VAL ALA GLY VAL VAL ALA PRO THR LEU PRO ARG GLU ASP
SEQRES 39 A 591 LEU GLU LYS ILE ILE ALA HIS PHE LEU ILE GLN GLN TYR
SEQRES 40 A 591 LEU LYS GLU ASP TYR SER PHE THR ALA TYR ALA THR ILE
SEQRES 41 A 591 SER TYR LEU LYS ILE GLY PRO LYS ALA ASN LEU LEU ASN
SEQRES 42 A 591 ASN GLU ALA HIS ALA ILE THR MET GLN VAL THR LYS SER
SEQRES 43 A 591 THR GLN ASN SER PHE ARG ALA GLU SER SER GLN THR CYS
SEQRES 44 A 591 HIS SER GLU GLN SER ASP LYS LYS MET GLU ALA GLU ASN
SEQRES 45 A 591 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 46 A 591 LYS ASP ASP ASP ASP LYS
SEQRES 1 B 591 MET CYS LEU GLU ASP SER ASP ALA GLY ALA SER ASN GLU
SEQRES 2 B 591 TYR ASP SER SER PRO ALA ALA TRP ASN LYS GLU ASP PHE
SEQRES 3 B 591 PRO TRP SER GLY LYS VAL LYS ASP ILE LEU GLN ASN VAL
SEQRES 4 B 591 PHE LYS LEU GLU LYS PHE ARG PRO LEU GLN LEU GLU THR
SEQRES 5 B 591 ILE ASN VAL THR MET ALA GLY LYS GLU VAL PHE LEU VAL
SEQRES 6 B 591 MET PRO THR GLY GLY GLY LYS SER LEU CYS TYR GLN LEU
SEQRES 7 B 591 PRO ALA LEU CYS SER ASP GLY PHE THR LEU VAL ILE CYS
SEQRES 8 B 591 PRO LEU ILE SER LEU MET GLU ASP GLN LEU MET VAL LEU
SEQRES 9 B 591 LYS GLN LEU GLY ILE SER ALA THR MET LEU ASN ALA SER
SEQRES 10 B 591 SER SER LYS GLU HIS VAL LYS TRP VAL HIS ALA GLU MET
SEQRES 11 B 591 VAL ASN LYS ASN SER GLU LEU LYS LEU ILE TYR VAL THR
SEQRES 12 B 591 PRO GLU LYS ILE ALA LYS SER LYS MET PHE MET SER ARG
SEQRES 13 B 591 LEU GLU LYS ALA TYR GLU ALA ARG ARG PHE THR ARG ILE
SEQRES 14 B 591 ALA VAL ASP GLU VAL HIS CYS CYS SER GLN TRP GLY HIS
SEQRES 15 B 591 ASP PHE ARG PRO ASP TYR LYS ALA LEU GLY ILE LEU LYS
SEQRES 16 B 591 ARG GLN PHE PRO ASN ALA SER LEU ILE GLY LEU THR ALA
SEQRES 17 B 591 THR ALA THR ASN HIS VAL LEU THR ASP ALA GLN LYS ILE
SEQRES 18 B 591 LEU CYS ILE GLU LYS CYS PHE THR PHE THR ALA SER PHE
SEQRES 19 B 591 ASN ARG PRO ASN LEU TYR TYR GLU VAL ARG GLN LYS PRO
SEQRES 20 B 591 SER ASN THR GLU ASP PHE ILE GLU ASP ILE VAL LYS LEU
SEQRES 21 B 591 ILE ASN GLY ARG TYR LYS GLY GLN SER GLY ILE ILE TYR
SEQRES 22 B 591 CYS PHE SER GLN LYS ASP SER GLU GLN VAL THR VAL SER
SEQRES 23 B 591 LEU GLN ASN LEU GLY ILE HIS ALA GLY ALA TYR HIS ALA
SEQRES 24 B 591 ASN LEU GLU PRO GLU ASP LYS THR THR VAL HIS ARG LYS
SEQRES 25 B 591 TRP SER ALA ASN GLU ILE GLN VAL VAL VAL ALA THR VAL
SEQRES 26 B 591 ALA PHE GLY MET GLY ILE ASP LYS PRO ASP VAL ARG PHE
SEQRES 27 B 591 VAL ILE HIS HIS SER MET SER LYS SER MET GLU ASN TYR
SEQRES 28 B 591 TYR GLN GLU SER GLY ARG ALA GLY ARG ASP ASP MET LYS
SEQRES 29 B 591 ALA ASP CYS ILE LEU TYR TYR GLY PHE GLY ASP ILE PHE
SEQRES 30 B 591 ARG ILE SER SER MET VAL VAL MET GLU ASN VAL GLY GLN
SEQRES 31 B 591 GLN LYS LEU TYR GLU MET VAL SER TYR CYS GLN ASN ILE
SEQRES 32 B 591 SER LYS CYS ARG ARG VAL LEU MET ALA GLN HIS PHE ASP
SEQRES 33 B 591 GLU VAL TRP ASN SER GLU ALA CYS ASN LYS MET CYS ASP
SEQRES 34 B 591 ASN CYS CYS LYS ASP SER ALA PHE GLU ARG LYS ASN ILE
SEQRES 35 B 591 THR GLU TYR CYS ARG ASP LEU ILE LYS ILE LEU LYS GLN
SEQRES 36 B 591 ALA GLU GLU LEU ASN GLU LYS LEU THR PRO LEU LYS LEU
SEQRES 37 B 591 ILE ASP SER TRP MET GLY LYS GLY ALA ALA LYS LEU ARG
SEQRES 38 B 591 VAL ALA GLY VAL VAL ALA PRO THR LEU PRO ARG GLU ASP
SEQRES 39 B 591 LEU GLU LYS ILE ILE ALA HIS PHE LEU ILE GLN GLN TYR
SEQRES 40 B 591 LEU LYS GLU ASP TYR SER PHE THR ALA TYR ALA THR ILE
SEQRES 41 B 591 SER TYR LEU LYS ILE GLY PRO LYS ALA ASN LEU LEU ASN
SEQRES 42 B 591 ASN GLU ALA HIS ALA ILE THR MET GLN VAL THR LYS SER
SEQRES 43 B 591 THR GLN ASN SER PHE ARG ALA GLU SER SER GLN THR CYS
SEQRES 44 B 591 HIS SER GLU GLN SER ASP LYS LYS MET GLU ALA GLU ASN
SEQRES 45 B 591 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 46 B 591 LYS ASP ASP ASP ASP LYS
SEQRES 1 C 591 MET CYS LEU GLU ASP SER ASP ALA GLY ALA SER ASN GLU
SEQRES 2 C 591 TYR ASP SER SER PRO ALA ALA TRP ASN LYS GLU ASP PHE
SEQRES 3 C 591 PRO TRP SER GLY LYS VAL LYS ASP ILE LEU GLN ASN VAL
SEQRES 4 C 591 PHE LYS LEU GLU LYS PHE ARG PRO LEU GLN LEU GLU THR
SEQRES 5 C 591 ILE ASN VAL THR MET ALA GLY LYS GLU VAL PHE LEU VAL
SEQRES 6 C 591 MET PRO THR GLY GLY GLY LYS SER LEU CYS TYR GLN LEU
SEQRES 7 C 591 PRO ALA LEU CYS SER ASP GLY PHE THR LEU VAL ILE CYS
SEQRES 8 C 591 PRO LEU ILE SER LEU MET GLU ASP GLN LEU MET VAL LEU
SEQRES 9 C 591 LYS GLN LEU GLY ILE SER ALA THR MET LEU ASN ALA SER
SEQRES 10 C 591 SER SER LYS GLU HIS VAL LYS TRP VAL HIS ALA GLU MET
SEQRES 11 C 591 VAL ASN LYS ASN SER GLU LEU LYS LEU ILE TYR VAL THR
SEQRES 12 C 591 PRO GLU LYS ILE ALA LYS SER LYS MET PHE MET SER ARG
SEQRES 13 C 591 LEU GLU LYS ALA TYR GLU ALA ARG ARG PHE THR ARG ILE
SEQRES 14 C 591 ALA VAL ASP GLU VAL HIS CYS CYS SER GLN TRP GLY HIS
SEQRES 15 C 591 ASP PHE ARG PRO ASP TYR LYS ALA LEU GLY ILE LEU LYS
SEQRES 16 C 591 ARG GLN PHE PRO ASN ALA SER LEU ILE GLY LEU THR ALA
SEQRES 17 C 591 THR ALA THR ASN HIS VAL LEU THR ASP ALA GLN LYS ILE
SEQRES 18 C 591 LEU CYS ILE GLU LYS CYS PHE THR PHE THR ALA SER PHE
SEQRES 19 C 591 ASN ARG PRO ASN LEU TYR TYR GLU VAL ARG GLN LYS PRO
SEQRES 20 C 591 SER ASN THR GLU ASP PHE ILE GLU ASP ILE VAL LYS LEU
SEQRES 21 C 591 ILE ASN GLY ARG TYR LYS GLY GLN SER GLY ILE ILE TYR
SEQRES 22 C 591 CYS PHE SER GLN LYS ASP SER GLU GLN VAL THR VAL SER
SEQRES 23 C 591 LEU GLN ASN LEU GLY ILE HIS ALA GLY ALA TYR HIS ALA
SEQRES 24 C 591 ASN LEU GLU PRO GLU ASP LYS THR THR VAL HIS ARG LYS
SEQRES 25 C 591 TRP SER ALA ASN GLU ILE GLN VAL VAL VAL ALA THR VAL
SEQRES 26 C 591 ALA PHE GLY MET GLY ILE ASP LYS PRO ASP VAL ARG PHE
SEQRES 27 C 591 VAL ILE HIS HIS SER MET SER LYS SER MET GLU ASN TYR
SEQRES 28 C 591 TYR GLN GLU SER GLY ARG ALA GLY ARG ASP ASP MET LYS
SEQRES 29 C 591 ALA ASP CYS ILE LEU TYR TYR GLY PHE GLY ASP ILE PHE
SEQRES 30 C 591 ARG ILE SER SER MET VAL VAL MET GLU ASN VAL GLY GLN
SEQRES 31 C 591 GLN LYS LEU TYR GLU MET VAL SER TYR CYS GLN ASN ILE
SEQRES 32 C 591 SER LYS CYS ARG ARG VAL LEU MET ALA GLN HIS PHE ASP
SEQRES 33 C 591 GLU VAL TRP ASN SER GLU ALA CYS ASN LYS MET CYS ASP
SEQRES 34 C 591 ASN CYS CYS LYS ASP SER ALA PHE GLU ARG LYS ASN ILE
SEQRES 35 C 591 THR GLU TYR CYS ARG ASP LEU ILE LYS ILE LEU LYS GLN
SEQRES 36 C 591 ALA GLU GLU LEU ASN GLU LYS LEU THR PRO LEU LYS LEU
SEQRES 37 C 591 ILE ASP SER TRP MET GLY LYS GLY ALA ALA LYS LEU ARG
SEQRES 38 C 591 VAL ALA GLY VAL VAL ALA PRO THR LEU PRO ARG GLU ASP
SEQRES 39 C 591 LEU GLU LYS ILE ILE ALA HIS PHE LEU ILE GLN GLN TYR
SEQRES 40 C 591 LEU LYS GLU ASP TYR SER PHE THR ALA TYR ALA THR ILE
SEQRES 41 C 591 SER TYR LEU LYS ILE GLY PRO LYS ALA ASN LEU LEU ASN
SEQRES 42 C 591 ASN GLU ALA HIS ALA ILE THR MET GLN VAL THR LYS SER
SEQRES 43 C 591 THR GLN ASN SER PHE ARG ALA GLU SER SER GLN THR CYS
SEQRES 44 C 591 HIS SER GLU GLN SER ASP LYS LYS MET GLU ALA GLU ASN
SEQRES 45 C 591 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 46 C 591 LYS ASP ASP ASP ASP LYS
SEQRES 1 D 591 MET CYS LEU GLU ASP SER ASP ALA GLY ALA SER ASN GLU
SEQRES 2 D 591 TYR ASP SER SER PRO ALA ALA TRP ASN LYS GLU ASP PHE
SEQRES 3 D 591 PRO TRP SER GLY LYS VAL LYS ASP ILE LEU GLN ASN VAL
SEQRES 4 D 591 PHE LYS LEU GLU LYS PHE ARG PRO LEU GLN LEU GLU THR
SEQRES 5 D 591 ILE ASN VAL THR MET ALA GLY LYS GLU VAL PHE LEU VAL
SEQRES 6 D 591 MET PRO THR GLY GLY GLY LYS SER LEU CYS TYR GLN LEU
SEQRES 7 D 591 PRO ALA LEU CYS SER ASP GLY PHE THR LEU VAL ILE CYS
SEQRES 8 D 591 PRO LEU ILE SER LEU MET GLU ASP GLN LEU MET VAL LEU
SEQRES 9 D 591 LYS GLN LEU GLY ILE SER ALA THR MET LEU ASN ALA SER
SEQRES 10 D 591 SER SER LYS GLU HIS VAL LYS TRP VAL HIS ALA GLU MET
SEQRES 11 D 591 VAL ASN LYS ASN SER GLU LEU LYS LEU ILE TYR VAL THR
SEQRES 12 D 591 PRO GLU LYS ILE ALA LYS SER LYS MET PHE MET SER ARG
SEQRES 13 D 591 LEU GLU LYS ALA TYR GLU ALA ARG ARG PHE THR ARG ILE
SEQRES 14 D 591 ALA VAL ASP GLU VAL HIS CYS CYS SER GLN TRP GLY HIS
SEQRES 15 D 591 ASP PHE ARG PRO ASP TYR LYS ALA LEU GLY ILE LEU LYS
SEQRES 16 D 591 ARG GLN PHE PRO ASN ALA SER LEU ILE GLY LEU THR ALA
SEQRES 17 D 591 THR ALA THR ASN HIS VAL LEU THR ASP ALA GLN LYS ILE
SEQRES 18 D 591 LEU CYS ILE GLU LYS CYS PHE THR PHE THR ALA SER PHE
SEQRES 19 D 591 ASN ARG PRO ASN LEU TYR TYR GLU VAL ARG GLN LYS PRO
SEQRES 20 D 591 SER ASN THR GLU ASP PHE ILE GLU ASP ILE VAL LYS LEU
SEQRES 21 D 591 ILE ASN GLY ARG TYR LYS GLY GLN SER GLY ILE ILE TYR
SEQRES 22 D 591 CYS PHE SER GLN LYS ASP SER GLU GLN VAL THR VAL SER
SEQRES 23 D 591 LEU GLN ASN LEU GLY ILE HIS ALA GLY ALA TYR HIS ALA
SEQRES 24 D 591 ASN LEU GLU PRO GLU ASP LYS THR THR VAL HIS ARG LYS
SEQRES 25 D 591 TRP SER ALA ASN GLU ILE GLN VAL VAL VAL ALA THR VAL
SEQRES 26 D 591 ALA PHE GLY MET GLY ILE ASP LYS PRO ASP VAL ARG PHE
SEQRES 27 D 591 VAL ILE HIS HIS SER MET SER LYS SER MET GLU ASN TYR
SEQRES 28 D 591 TYR GLN GLU SER GLY ARG ALA GLY ARG ASP ASP MET LYS
SEQRES 29 D 591 ALA ASP CYS ILE LEU TYR TYR GLY PHE GLY ASP ILE PHE
SEQRES 30 D 591 ARG ILE SER SER MET VAL VAL MET GLU ASN VAL GLY GLN
SEQRES 31 D 591 GLN LYS LEU TYR GLU MET VAL SER TYR CYS GLN ASN ILE
SEQRES 32 D 591 SER LYS CYS ARG ARG VAL LEU MET ALA GLN HIS PHE ASP
SEQRES 33 D 591 GLU VAL TRP ASN SER GLU ALA CYS ASN LYS MET CYS ASP
SEQRES 34 D 591 ASN CYS CYS LYS ASP SER ALA PHE GLU ARG LYS ASN ILE
SEQRES 35 D 591 THR GLU TYR CYS ARG ASP LEU ILE LYS ILE LEU LYS GLN
SEQRES 36 D 591 ALA GLU GLU LEU ASN GLU LYS LEU THR PRO LEU LYS LEU
SEQRES 37 D 591 ILE ASP SER TRP MET GLY LYS GLY ALA ALA LYS LEU ARG
SEQRES 38 D 591 VAL ALA GLY VAL VAL ALA PRO THR LEU PRO ARG GLU ASP
SEQRES 39 D 591 LEU GLU LYS ILE ILE ALA HIS PHE LEU ILE GLN GLN TYR
SEQRES 40 D 591 LEU LYS GLU ASP TYR SER PHE THR ALA TYR ALA THR ILE
SEQRES 41 D 591 SER TYR LEU LYS ILE GLY PRO LYS ALA ASN LEU LEU ASN
SEQRES 42 D 591 ASN GLU ALA HIS ALA ILE THR MET GLN VAL THR LYS SER
SEQRES 43 D 591 THR GLN ASN SER PHE ARG ALA GLU SER SER GLN THR CYS
SEQRES 44 D 591 HIS SER GLU GLN SER ASP LYS LYS MET GLU ALA GLU ASN
SEQRES 45 D 591 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 46 D 591 LYS ASP ASP ASP ASP LYS
SEQRES 1 P 20 DG DG DA DT DC DT DC DG DA DC DG DC DT
SEQRES 2 P 20 DC DT DC DC DC DT DT
SEQRES 1 Q 20 DG DG DA DT DC DT DC DG DA DC DG DC DT
SEQRES 2 Q 20 DC DT DC DC DC DT DT
SEQRES 1 R 20 DG DG DA DT DC DT DC DG DA DC DG DC DT
SEQRES 2 R 20 DC DT DC DC DC DT DT
SEQRES 1 S 20 DG DG DA DT DC DT DC DG DA DC DG DC DT
SEQRES 2 S 20 DC DT DC DC DC DT DT
HET ZN A 701 1
HET ZN B 701 1
HET ZN C 701 1
HET ZN D 701 1
HETNAM ZN ZINC ION
FORMUL 9 ZN 4(ZN 2+)
HELIX 1 AA1 PRO A 65 ASN A 69 5 5
HELIX 2 AA2 TRP A 75 VAL A 86 1 12
HELIX 3 AA3 LEU A 95 ALA A 105 1 11
HELIX 4 AA4 SER A 120 CYS A 129 1 10
HELIX 5 AA5 LEU A 140 GLY A 155 1 16
HELIX 6 AA6 SER A 166 ASN A 179 1 14
HELIX 7 AA7 THR A 190 LYS A 196 1 7
HELIX 8 AA8 SER A 197 ALA A 210 1 14
HELIX 9 AA9 VAL A 221 SER A 225 5 5
HELIX 10 AB1 ARG A 232 LEU A 238 5 7
HELIX 11 AB2 GLY A 239 PHE A 245 1 7
HELIX 12 AB3 THR A 258 LEU A 269 1 12
HELIX 13 AB4 ASN A 296 ASN A 309 1 14
HELIX 14 AB5 SER A 323 LEU A 337 1 15
HELIX 15 AB6 GLU A 349 ALA A 362 1 14
HELIX 16 AB7 SER A 394 GLY A 403 1 10
HELIX 17 AB8 GLY A 419 VAL A 430 1 12
HELIX 18 AB9 VAL A 435 GLN A 448 1 14
HELIX 19 AC1 CYS A 453 ASP A 463 1 11
HELIX 20 AC2 CYS A 475 LYS A 480 1 6
HELIX 21 AC3 ILE A 489 LEU A 506 1 18
HELIX 22 AC4 THR A 511 MET A 520 1 10
HELIX 23 AC5 ALA A 524 ARG A 528 5 5
HELIX 24 AC6 PRO A 538 GLN A 552 1 15
HELIX 25 AC7 PRO A 574 ASN A 581 5 8
HELIX 26 AC8 PRO B 65 ASN B 69 5 5
HELIX 27 AC9 TRP B 75 VAL B 86 1 12
HELIX 28 AD1 LEU B 95 ALA B 105 1 11
HELIX 29 AD2 SER B 120 CYS B 129 1 10
HELIX 30 AD3 LEU B 140 GLY B 155 1 16
HELIX 31 AD4 SER B 166 ASN B 179 1 14
HELIX 32 AD5 THR B 190 LYS B 196 1 7
HELIX 33 AD6 SER B 197 ALA B 210 1 14
HELIX 34 AD7 VAL B 221 SER B 225 5 5
HELIX 35 AD8 ARG B 232 LEU B 238 5 7
HELIX 36 AD9 GLY B 239 PHE B 245 1 7
HELIX 37 AE1 THR B 258 LEU B 269 1 12
HELIX 38 AE2 ASN B 296 ASN B 309 1 14
HELIX 39 AE3 SER B 323 LEU B 337 1 15
HELIX 40 AE4 GLU B 349 ALA B 362 1 14
HELIX 41 AE5 SER B 394 GLY B 403 1 10
HELIX 42 AE6 GLY B 419 VAL B 430 1 12
HELIX 43 AE7 VAL B 435 ASN B 449 1 15
HELIX 44 AE8 CYS B 453 ASP B 463 1 11
HELIX 45 AE9 CYS B 475 LYS B 480 1 6
HELIX 46 AF1 ILE B 489 LEU B 506 1 18
HELIX 47 AF2 THR B 511 MET B 520 1 10
HELIX 48 AF3 ALA B 524 ARG B 528 5 5
HELIX 49 AF4 PRO B 538 GLN B 552 1 15
HELIX 50 AF5 PRO B 574 ASN B 581 5 8
HELIX 51 AF6 SER C 64 ASN C 69 5 6
HELIX 52 AF7 TRP C 75 VAL C 86 1 12
HELIX 53 AF8 LEU C 95 ALA C 105 1 11
HELIX 54 AF9 SER C 120 CYS C 129 1 10
HELIX 55 AG1 LEU C 140 LEU C 154 1 15
HELIX 56 AG2 SER C 166 ASN C 179 1 14
HELIX 57 AG3 THR C 190 LYS C 196 1 7
HELIX 58 AG4 SER C 197 ALA C 210 1 14
HELIX 59 AG5 VAL C 221 SER C 225 5 5
HELIX 60 AG6 ARG C 232 LEU C 238 5 7
HELIX 61 AG7 GLY C 239 PHE C 245 1 7
HELIX 62 AG8 THR C 258 LEU C 269 1 12
HELIX 63 AG9 ASN C 296 ASN C 309 1 14
HELIX 64 AH1 SER C 323 LEU C 337 1 15
HELIX 65 AH2 GLU C 349 ALA C 362 1 14
HELIX 66 AH3 SER C 394 GLY C 403 1 10
HELIX 67 AH4 GLY C 419 VAL C 430 1 12
HELIX 68 AH5 VAL C 435 ASN C 449 1 15
HELIX 69 AH6 CYS C 453 ASP C 463 1 11
HELIX 70 AH7 CYS C 475 LYS C 480 1 6
HELIX 71 AH8 ILE C 489 LEU C 506 1 18
HELIX 72 AH9 THR C 511 MET C 520 1 10
HELIX 73 AI1 ALA C 524 ARG C 528 5 5
HELIX 74 AI2 PRO C 538 GLN C 552 1 15
HELIX 75 AI3 PRO C 574 ASN C 581 5 8
HELIX 76 AI4 SER D 64 ASN D 69 5 6
HELIX 77 AI5 TRP D 75 VAL D 86 1 12
HELIX 78 AI6 LEU D 95 ALA D 105 1 11
HELIX 79 AI7 SER D 120 CYS D 129 1 10
HELIX 80 AI8 LEU D 140 LEU D 154 1 15
HELIX 81 AI9 SER D 166 ASN D 179 1 14
HELIX 82 AJ1 THR D 190 LYS D 196 1 7
HELIX 83 AJ2 SER D 197 ALA D 210 1 14
HELIX 84 AJ3 VAL D 221 SER D 225 5 5
HELIX 85 AJ4 ARG D 232 LEU D 238 5 7
HELIX 86 AJ5 GLY D 239 PHE D 245 1 7
HELIX 87 AJ6 THR D 258 LEU D 269 1 12
HELIX 88 AJ7 ASN D 296 ASN D 309 1 14
HELIX 89 AJ8 SER D 323 LEU D 337 1 15
HELIX 90 AJ9 GLU D 349 ALA D 362 1 14
HELIX 91 AK1 SER D 394 GLY D 403 1 10
HELIX 92 AK2 GLY D 419 VAL D 430 1 12
HELIX 93 AK3 VAL D 435 GLN D 448 1 14
HELIX 94 AK4 CYS D 453 ASP D 463 1 11
HELIX 95 AK5 CYS D 475 LYS D 480 1 6
HELIX 96 AK6 ILE D 489 LEU D 506 1 18
HELIX 97 AK7 THR D 511 MET D 520 1 10
HELIX 98 AK8 ALA D 524 ARG D 528 5 5
HELIX 99 AK9 PRO D 538 GLN D 552 1 15
HELIX 100 AL1 PRO D 574 ASN D 581 5 8
SHEET 1 AA1 7 ALA A 158 MET A 160 0
SHEET 2 AA1 7 LEU A 186 VAL A 189 1 O LEU A 186 N THR A 159
SHEET 3 AA1 7 PHE A 133 ILE A 137 1 N VAL A 136 O ILE A 187
SHEET 4 AA1 7 PHE A 213 ASP A 219 1 O ALA A 217 N LEU A 135
SHEET 5 AA1 7 SER A 249 THR A 254 1 O SER A 249 N ILE A 216
SHEET 6 AA1 7 VAL A 109 VAL A 112 1 N LEU A 111 O GLY A 252
SHEET 7 AA1 7 PHE A 275 THR A 278 1 O PHE A 277 N VAL A 112
SHEET 1 AA2 6 LEU A 286 GLN A 292 0
SHEET 2 AA2 6 ALA A 412 TYR A 418 1 O CYS A 414 N TYR A 287
SHEET 3 AA2 6 VAL A 383 HIS A 388 1 N HIS A 388 O ILE A 415
SHEET 4 AA2 6 SER A 316 TYR A 320 1 N TYR A 320 O ILE A 387
SHEET 5 AA2 6 VAL A 367 ALA A 370 1 O ALA A 370 N ILE A 319
SHEET 6 AA2 6 ALA A 341 TYR A 344 1 N GLY A 342 O VAL A 369
SHEET 1 AA3 2 PHE A 484 ASN A 488 0
SHEET 2 AA3 2 THR A 587 THR A 591 -1 O MET A 588 N LYS A 487
SHEET 1 AA4 2 LEU A 555 PHE A 561 0
SHEET 2 AA4 2 THR A 566 ILE A 572 -1 O LYS A 571 N LYS A 556
SHEET 1 AA5 7 ALA B 158 MET B 160 0
SHEET 2 AA5 7 LEU B 186 VAL B 189 1 O TYR B 188 N THR B 159
SHEET 3 AA5 7 PHE B 133 ILE B 137 1 N VAL B 136 O ILE B 187
SHEET 4 AA5 7 PHE B 213 ASP B 219 1 O ALA B 217 N LEU B 135
SHEET 5 AA5 7 SER B 249 THR B 254 1 O SER B 249 N ILE B 216
SHEET 6 AA5 7 VAL B 109 VAL B 112 1 N LEU B 111 O GLY B 252
SHEET 7 AA5 7 PHE B 275 THR B 278 1 O PHE B 275 N PHE B 110
SHEET 1 AA6 6 LEU B 286 GLN B 292 0
SHEET 2 AA6 6 ALA B 412 TYR B 418 1 O CYS B 414 N TYR B 287
SHEET 3 AA6 6 VAL B 383 HIS B 388 1 N ARG B 384 O ASP B 413
SHEET 4 AA6 6 SER B 316 TYR B 320 1 N ILE B 318 O ILE B 387
SHEET 5 AA6 6 VAL B 367 ALA B 370 1 O VAL B 368 N ILE B 319
SHEET 6 AA6 6 ALA B 341 TYR B 344 1 N GLY B 342 O VAL B 369
SHEET 1 AA7 2 PHE B 484 ASN B 488 0
SHEET 2 AA7 2 THR B 587 THR B 591 -1 O MET B 588 N LYS B 487
SHEET 1 AA8 2 LEU B 555 PHE B 561 0
SHEET 2 AA8 2 THR B 566 ILE B 572 -1 O TYR B 569 N ASP B 558
SHEET 1 AA9 7 ALA C 158 MET C 160 0
SHEET 2 AA9 7 LEU C 186 VAL C 189 1 O TYR C 188 N THR C 159
SHEET 3 AA9 7 PHE C 133 ILE C 137 1 N VAL C 136 O ILE C 187
SHEET 4 AA9 7 PHE C 213 ASP C 219 1 O ALA C 217 N LEU C 135
SHEET 5 AA9 7 SER C 249 THR C 254 1 O ILE C 251 N VAL C 218
SHEET 6 AA9 7 VAL C 109 VAL C 112 1 N LEU C 111 O GLY C 252
SHEET 7 AA9 7 PHE C 275 THR C 278 1 O PHE C 277 N VAL C 112
SHEET 1 AB1 6 LEU C 286 GLN C 292 0
SHEET 2 AB1 6 ALA C 412 TYR C 418 1 O LEU C 416 N GLU C 289
SHEET 3 AB1 6 VAL C 383 HIS C 388 1 N HIS C 388 O TYR C 417
SHEET 4 AB1 6 SER C 316 TYR C 320 1 N ILE C 318 O ILE C 387
SHEET 5 AB1 6 VAL C 367 ALA C 370 1 O ALA C 370 N ILE C 319
SHEET 6 AB1 6 ALA C 341 TYR C 344 1 N GLY C 342 O VAL C 369
SHEET 1 AB2 2 PHE C 484 ASN C 488 0
SHEET 2 AB2 2 THR C 587 THR C 591 -1 O MET C 588 N LYS C 487
SHEET 1 AB3 2 LEU C 555 PHE C 561 0
SHEET 2 AB3 2 THR C 566 ILE C 572 -1 O TYR C 569 N ASP C 558
SHEET 1 AB4 7 ALA D 158 MET D 160 0
SHEET 2 AB4 7 LEU D 186 VAL D 189 1 O TYR D 188 N THR D 159
SHEET 3 AB4 7 PHE D 133 ILE D 137 1 N VAL D 136 O ILE D 187
SHEET 4 AB4 7 PHE D 213 ASP D 219 1 O ALA D 217 N LEU D 135
SHEET 5 AB4 7 SER D 249 THR D 254 1 O ILE D 251 N VAL D 218
SHEET 6 AB4 7 VAL D 109 VAL D 112 1 N LEU D 111 O GLY D 252
SHEET 7 AB4 7 PHE D 275 THR D 278 1 O PHE D 277 N VAL D 112
SHEET 1 AB5 6 LEU D 286 GLN D 292 0
SHEET 2 AB5 6 ALA D 412 TYR D 418 1 O CYS D 414 N TYR D 287
SHEET 3 AB5 6 VAL D 383 HIS D 388 1 N HIS D 388 O TYR D 417
SHEET 4 AB5 6 SER D 316 TYR D 320 1 N ILE D 318 O ILE D 387
SHEET 5 AB5 6 VAL D 367 ALA D 370 1 O ALA D 370 N ILE D 319
SHEET 6 AB5 6 ALA D 341 TYR D 344 1 N GLY D 342 O VAL D 369
SHEET 1 AB6 2 PHE D 484 ASN D 488 0
SHEET 2 AB6 2 THR D 587 THR D 591 -1 O MET D 588 N LYS D 487
SHEET 1 AB7 2 LEU D 555 PHE D 561 0
SHEET 2 AB7 2 THR D 566 ILE D 572 -1 O TYR D 569 N ASP D 558
SSBOND 1 CYS D 453 CYS D 478 1555 1555 2.96
LINK SG CYS A 453 ZN ZN A 701 1555 1555 2.34
LINK SG CYS A 471 ZN ZN A 701 1555 1555 2.34
LINK SG CYS A 475 ZN ZN A 701 1555 1555 2.34
LINK SG CYS A 478 ZN ZN A 701 1555 1555 2.34
LINK SG CYS B 453 ZN ZN B 701 1555 1555 2.34
LINK SG CYS B 471 ZN ZN B 701 1555 1555 2.34
LINK SG CYS B 475 ZN ZN B 701 1555 1555 2.34
LINK SG CYS B 478 ZN ZN B 701 1555 1555 2.34
LINK SG CYS C 453 ZN ZN C 701 1555 1555 2.34
LINK SG CYS C 471 ZN ZN C 701 1555 1555 2.34
LINK SG CYS C 475 ZN ZN C 701 1555 1555 2.34
LINK SG CYS C 478 ZN ZN C 701 1555 1555 2.34
LINK SG CYS D 453 ZN ZN D 701 1555 1555 2.34
LINK SG CYS D 471 ZN ZN D 701 1555 1555 2.34
LINK SG CYS D 475 ZN ZN D 701 1555 1555 2.34
LINK SG CYS D 478 ZN ZN D 701 1555 1555 2.34
CISPEP 1 GLU A 272 LYS A 273 0 14.55
CISPEP 2 GLU B 272 LYS B 273 0 15.11
CISPEP 3 GLU C 272 LYS C 273 0 14.57
CISPEP 4 GLU D 272 LYS D 273 0 15.12
SITE 1 AC1 4 CYS A 453 CYS A 471 CYS A 475 CYS A 478
SITE 1 AC2 4 CYS B 453 CYS B 471 CYS B 475 CYS B 478
SITE 1 AC3 4 CYS C 453 CYS C 471 CYS C 475 CYS C 478
SITE 1 AC4 4 CYS D 453 CYS D 471 CYS D 475 CYS D 478
CRYST1 55.380 138.220 207.581 90.00 90.02 90.00 P 1 21 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 0.018057 0.000000 0.000006 0.00000
SCALE2 0.000000 0.007235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004817 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
