HEADER HYDROLASE 28-AUG-14 4R7Y
TITLE CRYSTAL STRUCTURE OF AN ACTIVE MCM HEXAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MINICHROMOSOME MAINTENANCE PROTEIN MCM, CELL DIVISION
COMPND 3 CONTROL PROTEIN 21;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: CHIMERA FUSION OF SSOMCM-N AND PFMCM-AAA;
COMPND 6 EC: 3.6.4.12;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS, PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 273057, 186497;
SOURCE 4 STRAIN: ATCC 35092 / DSM 1617 / JCM 11322 / P2, ATCC 43587 / DSM
SOURCE 5 3638 / JCM 8422 / VC1;
SOURCE 6 GENE: MCM, SSO0774, PF0482;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSF-DUET
KEYWDS AAA+, OB-FOLD, MCM, HELICASE, ATPASE, DNA REPLICATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MILLER,B.T.ARACHEA,L.B.EPLING,E.J.ENEMARK
REVDAT 6 20-SEP-23 4R7Y 1 REMARK SEQADV LINK
REVDAT 5 02-AUG-17 4R7Y 1 SOURCE REMARK
REVDAT 4 19-NOV-14 4R7Y 1 JRNL
REVDAT 3 12-NOV-14 4R7Y 1 JRNL
REVDAT 2 15-OCT-14 4R7Y 1 JRNL
REVDAT 1 08-OCT-14 4R7Y 0
JRNL AUTH J.M.MILLER,B.T.ARACHEA,L.B.EPLING,E.J.ENEMARK
JRNL TITL ANALYSIS OF THE CRYSTAL STRUCTURE OF AN ACTIVE MCM HEXAMER.
JRNL REF ELIFE V. 3 03433 2014
JRNL REFN ESSN 2050-084X
JRNL PMID 25262915
JRNL DOI 10.7554/ELIFE.03433
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3602734.230
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.7
REMARK 3 NUMBER OF REFLECTIONS : 39044
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.263
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1976
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.80
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2042
REMARK 3 BIN R VALUE (WORKING SET) : 0.3600
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 123
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9430
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.32000
REMARK 3 B22 (A**2) : -2.32000
REMARK 3 B33 (A**2) : 4.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.47
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.100
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.460 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.600 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.730 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.750 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 29.06
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : ADP.PARAM
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : ADP.TOP
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 4R7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000087012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43329
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.75000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.790
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: SSOMCM N-TERMINAL DOMAIN (2VL6), PFMCM ATPASE
REMARK 200 DOMAIN (RELATED ENTRY 4R7Z)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10.8 MG/ML SSO-PFMCM; 5 MM ADP MIXED
REMARK 280 1:1 WITH 100 MM HEPES, PH 7.6; 350 MM MGCL2; 3 % (W/V) PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 99.65850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 99.65850
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 99.65850
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 39150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 157040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -338.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 BIOMT1 2 -0.500000 -0.866025 0.000000 -59.45100
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 102.97215
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -118.90200
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 0
REMARK 465 LEU A 1
REMARK 465 GLU A 2
REMARK 465 ILE A 3
REMARK 465 PRO A 4
REMARK 465 SER A 5
REMARK 465 LYS A 6
REMARK 465 VAL A 1905
REMARK 465 LYS A 1906
REMARK 465 LYS A 1907
REMARK 465 THR A 1908
REMARK 465 LYS A 1909
REMARK 465 GLY A 1910
REMARK 465 GLU A 1911
REMARK 465 GLU A 1912
REMARK 465 GLU A 1913
REMARK 465 GLY A 1914
REMARK 465 ILE A 1915
REMARK 465 PRO A 1916
REMARK 465 PRO A 1917
REMARK 465 ILE A 1918
REMARK 465 ASP A 1966
REMARK 465 SER B 0
REMARK 465 LEU B 1
REMARK 465 GLU B 2
REMARK 465 ILE B 3
REMARK 465 PRO B 4
REMARK 465 SER B 5
REMARK 465 LYS B 6
REMARK 465 VAL B 1905
REMARK 465 LYS B 1906
REMARK 465 LYS B 1907
REMARK 465 THR B 1908
REMARK 465 LYS B 1909
REMARK 465 GLY B 1910
REMARK 465 GLU B 1911
REMARK 465 GLU B 1912
REMARK 465 GLU B 1913
REMARK 465 GLY B 1914
REMARK 465 ILE B 1915
REMARK 465 PRO B 1916
REMARK 465 PRO B 1917
REMARK 465 ILE B 1918
REMARK 465 ASP B 1966
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 ASN A 26 14.63 57.62
REMARK 500 LYS A 129 136.90 -170.72
REMARK 500 LYS A 139 112.85 176.40
REMARK 500 ILE A 145 104.26 -59.33
REMARK 500 CYS A 149 -69.52 -105.54
REMARK 500 MET A 150 39.88 35.35
REMARK 500 TRP A 155 -98.89 -60.00
REMARK 500 PRO A 156 91.67 -40.10
REMARK 500 LEU A 182 131.24 -34.88
REMARK 500 ASP A 219 -124.78 55.44
REMARK 500 VAL A 245 -0.37 48.33
REMARK 500 ARG A 247 -110.59 -67.97
REMARK 500 ARG A 250 -154.86 -177.15
REMARK 500 ALA A1287 72.79 -152.65
REMARK 500 ALA A1289 34.22 -66.10
REMARK 500 THR A1316 -132.43 39.45
REMARK 500 LYS A1334 -74.23 -58.23
REMARK 500 THR A1729 -98.71 -113.80
REMARK 500 ASP A1752 141.53 -35.78
REMARK 500 ALA A1786 -132.22 53.50
REMARK 500 MET A1812 -26.30 -38.27
REMARK 500 ASP A1841 -61.39 -6.61
REMARK 500 GLU A1858 -161.18 -60.29
REMARK 500 HIS A1868 -77.26 -45.21
REMARK 500 PRO A1884 146.12 -39.28
REMARK 500 LEU A1940 17.24 53.11
REMARK 500 ASP A1948 -71.17 -58.80
REMARK 500 ASN B 26 2.69 59.59
REMARK 500 ASN B 56 91.41 -164.31
REMARK 500 TYR B 89 -29.12 -39.60
REMARK 500 ILE B 145 99.05 -61.93
REMARK 500 CYS B 149 -74.28 -107.28
REMARK 500 PHE B 153 142.67 -177.26
REMARK 500 TRP B 155 -99.94 -74.76
REMARK 500 PRO B 156 95.31 -37.51
REMARK 500 PRO B 177 177.64 -59.31
REMARK 500 ASP B 219 -120.70 58.13
REMARK 500 VAL B 245 -21.84 43.05
REMARK 500 ALA B 251 46.05 -105.02
REMARK 500 PRO B1263 -18.80 -48.17
REMARK 500 ARG B1275 151.87 -41.69
REMARK 500 ASP B1277 41.99 -101.57
REMARK 500 ALA B1287 74.60 -163.25
REMARK 500 ALA B1289 6.41 -56.22
REMARK 500 SER B1309 96.30 62.60
REMARK 500 THR B1316 -128.22 39.65
REMARK 500 ALA B1333 7.23 80.84
REMARK 500 THR B1729 -101.70 -105.73
REMARK 500 ASP B1752 141.25 -38.13
REMARK 500 SER B1765 162.50 -47.54
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
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 A2003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 144 ND1
REMARK 620 2 CYS A 149 SG 97.7
REMARK 620 3 CYS A 171 SG 92.3 127.0
REMARK 620 4 CYS A 174 SG 87.3 150.8 81.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A1335 OG
REMARK 620 2 ADP A2001 O3B 90.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 144 ND1
REMARK 620 2 CYS B 149 SG 109.7
REMARK 620 3 CYS B 171 SG 92.8 119.5
REMARK 620 4 CYS B 174 SG 86.9 154.4 77.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B1335 OG
REMARK 620 2 ADP B2001 O3B 97.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4R7Z RELATED DB: PDB
REMARK 900 PFMCM AAA+ DOMAIN DOUBLE-OCTAMER
DBREF 4R7Y A 2 269 UNP Q9UXG1 MCM_SULSO 2 269
DBREF 4R7Y A 1257 1361 UNP Q8U3I4 Q8U3I4_PYRFU 257 361
DBREF 4R7Y A 1729 1966 UNP Q8U3I4 Q8U3I4_PYRFU 729 966
DBREF 4R7Y B 2 269 UNP Q9UXG1 MCM_SULSO 2 269
DBREF 4R7Y B 1257 1361 UNP Q8U3I4 Q8U3I4_PYRFU 257 361
DBREF 4R7Y B 1729 1966 UNP Q8U3I4 Q8U3I4_PYRFU 729 966
SEQADV 4R7Y SER A 0 UNP Q9UXG1 EXPRESSION TAG
SEQADV 4R7Y LEU A 1 UNP Q9UXG1 EXPRESSION TAG
SEQADV 4R7Y SER B 0 UNP Q9UXG1 EXPRESSION TAG
SEQADV 4R7Y LEU B 1 UNP Q9UXG1 EXPRESSION TAG
SEQRES 1 A 613 SER LEU GLU ILE PRO SER LYS GLN ILE ASP TYR ARG ASP
SEQRES 2 A 613 VAL PHE ILE GLU PHE LEU THR THR PHE LYS GLY ASN ASN
SEQRES 3 A 613 ASN GLN ASN LYS TYR ILE GLU ARG ILE ASN GLU LEU VAL
SEQRES 4 A 613 ALA TYR ARG LYS LYS SER LEU ILE ILE GLU PHE SER ASP
SEQRES 5 A 613 VAL LEU SER PHE ASN GLU ASN LEU ALA TYR GLU ILE ILE
SEQRES 6 A 613 ASN ASN THR LYS ILE ILE LEU PRO ILE LEU GLU GLY ALA
SEQRES 7 A 613 LEU TYR ASP HIS ILE LEU GLN LEU ASP PRO THR TYR GLN
SEQRES 8 A 613 ARG ASP ILE GLU LYS VAL HIS VAL ARG ILE VAL GLY ILE
SEQRES 9 A 613 PRO ARG VAL ILE GLU LEU ARG LYS ILE ARG SER THR ASP
SEQRES 10 A 613 ILE GLY LYS LEU ILE THR ILE ASP GLY ILE LEU VAL LYS
SEQRES 11 A 613 VAL THR PRO VAL LYS GLU ARG ILE TYR LYS ALA THR TYR
SEQRES 12 A 613 LYS HIS ILE HIS PRO ASP CYS MET GLN GLU PHE GLU TRP
SEQRES 13 A 613 PRO GLU ASP GLU GLU MET PRO GLU VAL LEU GLU MET PRO
SEQRES 14 A 613 THR ILE CYS PRO LYS CYS GLY LYS PRO GLY GLN PHE ARG
SEQRES 15 A 613 LEU ILE PRO GLU LYS THR LYS LEU ILE ASP TRP GLN LYS
SEQRES 16 A 613 ALA VAL ILE GLN GLU ARG PRO GLU GLU VAL PRO SER GLY
SEQRES 17 A 613 GLN LEU PRO ARG GLN LEU GLU ILE ILE LEU GLU ASP ASP
SEQRES 18 A 613 LEU VAL ASP SER ALA ARG PRO GLY ASP ARG VAL LYS VAL
SEQRES 19 A 613 THR GLY ILE LEU ASP ILE LYS GLN ASP SER PRO VAL LYS
SEQRES 20 A 613 ARG GLY SER ARG ALA VAL PHE ASP ILE TYR MET LYS VAL
SEQRES 21 A 613 SER SER ILE GLU VAL SER GLN LYS VAL LEU GLN GLU LEU
SEQRES 22 A 613 GLU ILE SER PRO GLU GLU GLU GLN ILE ILE LYS GLU LEU
SEQRES 23 A 613 ALA LYS ARG LYS ASP ILE VAL ASP ALA ILE VAL ASP SER
SEQRES 24 A 613 ILE ALA PRO ALA ILE TYR GLY TYR LYS GLU VAL LYS LYS
SEQRES 25 A 613 GLY ILE ALA LEU ALA LEU PHE GLY GLY VAL SER ARG LYS
SEQRES 26 A 613 LEU PRO ASP GLY THR ARG LEU ARG GLY ASP ILE HIS VAL
SEQRES 27 A 613 LEU LEU VAL GLY ASP PRO GLY VAL ALA LYS SER GLN ILE
SEQRES 28 A 613 LEU ARG TYR VAL ALA ASN LEU ALA PRO ARG ALA ILE TYR
SEQRES 29 A 613 THR SER GLY LYS SER SER SER ALA ALA GLY LEU THR ALA
SEQRES 30 A 613 ALA ALA VAL ARG ASP GLU PHE THR GLY GLY TRP VAL LEU
SEQRES 31 A 613 GLU ALA GLY ALA LEU VAL LEU ALA ASP GLY GLY TYR ALA
SEQRES 32 A 613 LEU ILE ASP GLU LEU ASP LYS MET SER ASP ARG ASP ARG
SEQRES 33 A 613 SER VAL ILE HIS GLU ALA LEU GLU GLN GLN THR ILE SER
SEQRES 34 A 613 ILE SER LYS ALA GLY ILE THR ALA THR LEU ASN ALA ARG
SEQRES 35 A 613 THR THR VAL ILE ALA ALA ALA ASN PRO LYS GLN GLY ARG
SEQRES 36 A 613 PHE ASN ARG MET LYS ASN PRO PHE GLU GLN ILE ASP LEU
SEQRES 37 A 613 PRO PRO THR LEU LEU SER ARG PHE ASP LEU ILE PHE VAL
SEQRES 38 A 613 LEU ILE ASP GLU PRO ASP ASP LYS ILE ASP SER GLU VAL
SEQRES 39 A 613 ALA ARG HIS ILE LEU ARG VAL ARG ARG GLY GLU SER GLU
SEQRES 40 A 613 VAL VAL ALA PRO LYS ILE PRO HIS GLU ILE LEU ARG LYS
SEQRES 41 A 613 TYR ILE ALA TYR ALA ARG LYS ASN ILE HIS PRO VAL ILE
SEQRES 42 A 613 SER GLU GLU ALA MET GLU GLU ILE GLU LYS TYR TYR VAL
SEQRES 43 A 613 ARG MET ARG LYS SER VAL LYS LYS THR LYS GLY GLU GLU
SEQRES 44 A 613 GLU GLY ILE PRO PRO ILE PRO ILE THR ALA ARG GLN LEU
SEQRES 45 A 613 GLU ALA LEU ILE ARG LEU SER GLU ALA HIS ALA ARG MET
SEQRES 46 A 613 ARG LEU SER PRO ILE VAL THR ARG GLU ASP ALA ARG GLU
SEQRES 47 A 613 ALA ILE LYS LEU MET GLU TYR THR LEU LYS GLN ILE ALA
SEQRES 48 A 613 MET ASP
SEQRES 1 B 613 SER LEU GLU ILE PRO SER LYS GLN ILE ASP TYR ARG ASP
SEQRES 2 B 613 VAL PHE ILE GLU PHE LEU THR THR PHE LYS GLY ASN ASN
SEQRES 3 B 613 ASN GLN ASN LYS TYR ILE GLU ARG ILE ASN GLU LEU VAL
SEQRES 4 B 613 ALA TYR ARG LYS LYS SER LEU ILE ILE GLU PHE SER ASP
SEQRES 5 B 613 VAL LEU SER PHE ASN GLU ASN LEU ALA TYR GLU ILE ILE
SEQRES 6 B 613 ASN ASN THR LYS ILE ILE LEU PRO ILE LEU GLU GLY ALA
SEQRES 7 B 613 LEU TYR ASP HIS ILE LEU GLN LEU ASP PRO THR TYR GLN
SEQRES 8 B 613 ARG ASP ILE GLU LYS VAL HIS VAL ARG ILE VAL GLY ILE
SEQRES 9 B 613 PRO ARG VAL ILE GLU LEU ARG LYS ILE ARG SER THR ASP
SEQRES 10 B 613 ILE GLY LYS LEU ILE THR ILE ASP GLY ILE LEU VAL LYS
SEQRES 11 B 613 VAL THR PRO VAL LYS GLU ARG ILE TYR LYS ALA THR TYR
SEQRES 12 B 613 LYS HIS ILE HIS PRO ASP CYS MET GLN GLU PHE GLU TRP
SEQRES 13 B 613 PRO GLU ASP GLU GLU MET PRO GLU VAL LEU GLU MET PRO
SEQRES 14 B 613 THR ILE CYS PRO LYS CYS GLY LYS PRO GLY GLN PHE ARG
SEQRES 15 B 613 LEU ILE PRO GLU LYS THR LYS LEU ILE ASP TRP GLN LYS
SEQRES 16 B 613 ALA VAL ILE GLN GLU ARG PRO GLU GLU VAL PRO SER GLY
SEQRES 17 B 613 GLN LEU PRO ARG GLN LEU GLU ILE ILE LEU GLU ASP ASP
SEQRES 18 B 613 LEU VAL ASP SER ALA ARG PRO GLY ASP ARG VAL LYS VAL
SEQRES 19 B 613 THR GLY ILE LEU ASP ILE LYS GLN ASP SER PRO VAL LYS
SEQRES 20 B 613 ARG GLY SER ARG ALA VAL PHE ASP ILE TYR MET LYS VAL
SEQRES 21 B 613 SER SER ILE GLU VAL SER GLN LYS VAL LEU GLN GLU LEU
SEQRES 22 B 613 GLU ILE SER PRO GLU GLU GLU GLN ILE ILE LYS GLU LEU
SEQRES 23 B 613 ALA LYS ARG LYS ASP ILE VAL ASP ALA ILE VAL ASP SER
SEQRES 24 B 613 ILE ALA PRO ALA ILE TYR GLY TYR LYS GLU VAL LYS LYS
SEQRES 25 B 613 GLY ILE ALA LEU ALA LEU PHE GLY GLY VAL SER ARG LYS
SEQRES 26 B 613 LEU PRO ASP GLY THR ARG LEU ARG GLY ASP ILE HIS VAL
SEQRES 27 B 613 LEU LEU VAL GLY ASP PRO GLY VAL ALA LYS SER GLN ILE
SEQRES 28 B 613 LEU ARG TYR VAL ALA ASN LEU ALA PRO ARG ALA ILE TYR
SEQRES 29 B 613 THR SER GLY LYS SER SER SER ALA ALA GLY LEU THR ALA
SEQRES 30 B 613 ALA ALA VAL ARG ASP GLU PHE THR GLY GLY TRP VAL LEU
SEQRES 31 B 613 GLU ALA GLY ALA LEU VAL LEU ALA ASP GLY GLY TYR ALA
SEQRES 32 B 613 LEU ILE ASP GLU LEU ASP LYS MET SER ASP ARG ASP ARG
SEQRES 33 B 613 SER VAL ILE HIS GLU ALA LEU GLU GLN GLN THR ILE SER
SEQRES 34 B 613 ILE SER LYS ALA GLY ILE THR ALA THR LEU ASN ALA ARG
SEQRES 35 B 613 THR THR VAL ILE ALA ALA ALA ASN PRO LYS GLN GLY ARG
SEQRES 36 B 613 PHE ASN ARG MET LYS ASN PRO PHE GLU GLN ILE ASP LEU
SEQRES 37 B 613 PRO PRO THR LEU LEU SER ARG PHE ASP LEU ILE PHE VAL
SEQRES 38 B 613 LEU ILE ASP GLU PRO ASP ASP LYS ILE ASP SER GLU VAL
SEQRES 39 B 613 ALA ARG HIS ILE LEU ARG VAL ARG ARG GLY GLU SER GLU
SEQRES 40 B 613 VAL VAL ALA PRO LYS ILE PRO HIS GLU ILE LEU ARG LYS
SEQRES 41 B 613 TYR ILE ALA TYR ALA ARG LYS ASN ILE HIS PRO VAL ILE
SEQRES 42 B 613 SER GLU GLU ALA MET GLU GLU ILE GLU LYS TYR TYR VAL
SEQRES 43 B 613 ARG MET ARG LYS SER VAL LYS LYS THR LYS GLY GLU GLU
SEQRES 44 B 613 GLU GLY ILE PRO PRO ILE PRO ILE THR ALA ARG GLN LEU
SEQRES 45 B 613 GLU ALA LEU ILE ARG LEU SER GLU ALA HIS ALA ARG MET
SEQRES 46 B 613 ARG LEU SER PRO ILE VAL THR ARG GLU ASP ALA ARG GLU
SEQRES 47 B 613 ALA ILE LYS LEU MET GLU TYR THR LEU LYS GLN ILE ALA
SEQRES 48 B 613 MET ASP
HET ADP A2001 27
HET MG A2002 1
HET ZN A2003 1
HET CL A2004 1
HET CL A2005 1
HET CL A2006 1
HET ADP B2001 27
HET MG B2002 1
HET ZN B2003 1
HET CL B2004 1
HET CL B2005 1
HET CL B2006 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 CL 6(CL 1-)
HELIX 1 1 ASP A 9 PHE A 21 1 13
HELIX 2 2 ASN A 28 TYR A 40 1 13
HELIX 3 3 PHE A 49 ASN A 56 1 8
HELIX 4 4 ASN A 56 ASN A 66 1 11
HELIX 5 5 ASN A 66 ASP A 86 1 21
HELIX 6 6 THR A 88 ILE A 93 1 6
HELIX 7 7 GLU A 108 ILE A 112 5 5
HELIX 8 8 ARG A 113 ILE A 117 5 5
HELIX 9 9 ARG A 200 VAL A 204 5 5
HELIX 10 10 ASP A 220 VAL A 222 5 3
HELIX 11 11 SER A 1262 ARG A 1275 1 14
HELIX 12 12 ASP A 1277 ALA A 1287 1 11
HELIX 13 13 TYR A 1293 GLY A 1306 1 14
HELIX 14 14 ALA A 1333 ASN A 1343 1 11
HELIX 15 15 GLY A 1746 ALA A 1751 1 6
HELIX 16 16 GLU A 1760 MET A 1764 5 5
HELIX 17 17 SER A 1765 GLN A 1778 1 14
HELIX 18 18 PRO A 1822 SER A 1827 1 6
HELIX 19 19 ASP A 1840 ARG A 1856 1 17
HELIX 20 20 PRO A 1867 ASN A 1881 1 15
HELIX 21 21 SER A 1887 SER A 1904 1 18
HELIX 22 22 THR A 1921 LEU A 1940 1 20
HELIX 23 23 THR A 1945 ALA A 1964 1 20
HELIX 24 24 ASP B 9 PHE B 21 1 13
HELIX 25 25 ASN B 28 TYR B 40 1 13
HELIX 26 26 PHE B 49 ASN B 56 1 8
HELIX 27 27 ASN B 56 ASN B 66 1 11
HELIX 28 28 ASN B 66 ASP B 86 1 21
HELIX 29 29 THR B 88 ILE B 93 1 6
HELIX 30 30 GLU B 108 ILE B 112 5 5
HELIX 31 31 ARG B 113 ILE B 117 5 5
HELIX 32 32 PRO B 184 THR B 187 5 4
HELIX 33 33 ARG B 200 VAL B 204 5 5
HELIX 34 34 ASP B 220 VAL B 222 5 3
HELIX 35 35 SER B 1262 ARG B 1275 1 14
HELIX 36 36 ASP B 1277 ALA B 1287 1 11
HELIX 37 37 TYR B 1293 GLY B 1306 1 14
HELIX 38 38 LEU B 1312 THR B 1316 5 5
HELIX 39 39 ALA B 1333 LEU B 1344 1 12
HELIX 40 40 GLY B 1746 ALA B 1751 1 6
HELIX 41 41 SER B 1765 GLN B 1778 1 14
HELIX 42 42 ASN B 1814 ILE B 1819 1 6
HELIX 43 43 PRO B 1822 SER B 1827 1 6
HELIX 44 44 ASP B 1841 ARG B 1855 1 15
HELIX 45 45 PRO B 1867 ILE B 1882 1 16
HELIX 46 46 SER B 1887 LYS B 1903 1 17
HELIX 47 47 THR B 1921 LEU B 1940 1 20
HELIX 48 48 THR B 1945 ALA B 1964 1 20
SHEET 1 A 2 SER A 44 GLU A 48 0
SHEET 2 A 2 HIS A 97 VAL A 101 1 O ARG A 99 N ILE A 47
SHEET 1 B12 LYS A 134 LYS A 139 0
SHEET 2 B12 LYS A 188 GLN A 198 -1 O LYS A 188 N LYS A 139
SHEET 3 B12 LEU A 120 VAL A 130 -1 N VAL A 128 O VAL A 196
SHEET 4 B12 ARG A 230 LYS A 240 -1 O VAL A 233 N ILE A 123
SHEET 5 B12 VAL A 252 VAL A 264 -1 O SER A 260 N THR A 234
SHEET 6 B12 LYS B 134 LYS B 139 -1 O GLU B 135 N PHE A 253
SHEET 7 B12 LYS B 188 GLN B 198 -1 O LYS B 188 N LYS B 139
SHEET 8 B12 GLN B 212 GLU B 218 -1 O LEU B 217 N GLN B 193
SHEET 9 B12 ASP B 254 VAL B 264 1 O MET B 257 N ILE B 216
SHEET 10 B12 ARG B 230 LYS B 240 -1 N THR B 234 O SER B 260
SHEET 11 B12 LEU B 120 VAL B 130 -1 N ILE B 123 O VAL B 233
SHEET 12 B12 ARG B 105 ILE B 107 1 N ARG B 105 O THR B 122
SHEET 1 C 9 VAL A 106 ILE A 107 0
SHEET 2 C 9 LEU A 120 VAL A 130 1 O THR A 122 N ILE A 107
SHEET 3 C 9 LYS A 188 GLN A 198 -1 O VAL A 196 N VAL A 128
SHEET 4 C 9 GLN A 212 GLU A 218 -1 O LEU A 217 N GLN A 193
SHEET 5 C 9 VAL A 252 VAL A 264 1 O MET A 257 N ILE A 216
SHEET 6 C 9 LYS B 134 LYS B 139 -1 O GLU B 135 N PHE A 253
SHEET 7 C 9 LYS B 188 GLN B 198 -1 O LYS B 188 N LYS B 139
SHEET 8 C 9 LEU B 120 VAL B 130 -1 N VAL B 128 O VAL B 196
SHEET 9 C 9 ARG B 105 ILE B 107 1 N ARG B 105 O THR B 122
SHEET 1 D 3 GLU A 152 GLU A 154 0
SHEET 2 D 3 THR A 141 ILE A 145 -1 N TYR A 142 O PHE A 153
SHEET 3 D 3 GLN A 179 PHE A 180 -1 O GLN A 179 N ILE A 145
SHEET 1 E 5 ALA A1348 SER A1352 0
SHEET 2 E 5 TYR A1755 ASP A1759 1 O ASP A1759 N THR A1351
SHEET 3 E 5 THR A1797 ALA A1802 1 O THR A1797 N ALA A1756
SHEET 4 E 5 VAL A1324 GLY A1328 1 N LEU A1326 O ALA A1802
SHEET 5 E 5 LEU A1831 LEU A1835 1 O LEU A1831 N LEU A1325
SHEET 1 F 2 ALA A1730 ARG A1734 0
SHEET 2 F 2 TRP A1741 ALA A1745 -1 O VAL A1742 N VAL A1733
SHEET 1 G 2 THR A1780 LYS A1785 0
SHEET 2 G 2 ILE A1788 ASN A1793 -1 O ILE A1788 N LYS A1785
SHEET 1 H 2 SER B 44 GLU B 48 0
SHEET 2 H 2 HIS B 97 VAL B 101 1 O ARG B 99 N ILE B 47
SHEET 1 I 3 GLU B 152 GLU B 154 0
SHEET 2 I 3 THR B 141 ILE B 145 -1 N TYR B 142 O PHE B 153
SHEET 3 I 3 GLN B 179 LEU B 182 -1 O ARG B 181 N LYS B 143
SHEET 1 J 5 ALA B1348 SER B1352 0
SHEET 2 J 5 TYR B1755 ASP B1759 1 O LEU B1757 N THR B1351
SHEET 3 J 5 THR B1797 ALA B1802 1 O THR B1797 N ALA B1756
SHEET 4 J 5 VAL B1324 VAL B1327 1 N LEU B1326 O ALA B1802
SHEET 5 J 5 LEU B1831 VAL B1834 1 O PHE B1833 N LEU B1325
SHEET 1 K 2 ALA B1730 ARG B1734 0
SHEET 2 K 2 TRP B1741 ALA B1745 -1 O VAL B1742 N VAL B1733
SHEET 1 L 2 THR B1780 LYS B1785 0
SHEET 2 L 2 ILE B1788 ASN B1793 -1 O ILE B1788 N LYS B1785
LINK ND1 HIS A 144 ZN ZN A2003 1555 1555 2.06
LINK SG CYS A 149 ZN ZN A2003 1555 1555 2.21
LINK SG CYS A 171 ZN ZN A2003 1555 1555 2.11
LINK SG CYS A 174 ZN ZN A2003 1555 1555 2.55
LINK OG SER A1335 MG MG A2002 1555 1555 1.93
LINK O3B ADP A2001 MG MG A2002 1555 1555 2.26
LINK ND1 HIS B 144 ZN ZN B2003 1555 1555 1.95
LINK SG CYS B 149 ZN ZN B2003 1555 1555 2.41
LINK SG CYS B 171 ZN ZN B2003 1555 1555 2.34
LINK SG CYS B 174 ZN ZN B2003 1555 1555 2.66
LINK OG SER B1335 MG MG B2002 1555 1555 1.94
LINK O3B ADP B2001 MG MG B2002 1555 1555 2.20
CISPEP 1 SER A 1941 PRO A 1942 0 -0.07
CISPEP 2 SER B 1941 PRO B 1942 0 0.06
SITE 1 AC1 14 ALA A1289 ILE A1290 TYR A1291 PRO A1330
SITE 2 AC1 14 GLY A1331 VAL A1332 ALA A1333 LYS A1334
SITE 3 AC1 14 SER A1335 GLN A1336 ASN A1803 ILE A1851
SITE 4 AC1 14 MG A2002 ALA B1922
SITE 1 AC2 2 SER A1335 ADP A2001
SITE 1 AC3 4 HIS A 144 CYS A 149 CYS A 171 CYS A 174
SITE 1 AC4 1 VAL A 106
SITE 1 AC5 2 ARG A 230 ASN A1793
SITE 1 AC6 2 ARG A 105 LYS A 119
SITE 1 AC7 14 ALA B1289 ILE B1290 TYR B1291 TYR B1293
SITE 2 AC7 14 ASP B1329 PRO B1330 GLY B1331 VAL B1332
SITE 3 AC7 14 ALA B1333 LYS B1334 SER B1335 ASN B1803
SITE 4 AC7 14 ILE B1851 MG B2002
SITE 1 AC8 2 SER B1335 ADP B2001
SITE 1 AC9 4 HIS B 144 CYS B 149 CYS B 171 CYS B 174
SITE 1 BC1 1 VAL B 106
SITE 1 BC2 2 ARG B 230 ASN B1793
SITE 1 BC3 2 ARG B 105 LYS B 119
CRYST1 118.902 118.902 199.317 90.00 90.00 120.00 P 63 12
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 0.008410 0.004856 0.000000 0.00000
SCALE2 0.000000 0.009711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005017 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
