HEADER TRANSFERASE 13-JUL-07 2V62
TITLE STRUCTURE OF VACCINIA-RELATED KINASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE VRK2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 14-335;
COMPND 5 SYNONYM: VACCINIA RELATED PROTEIN KINASE 2;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS TRANSFERASE, ATP-BINDING, MEMBRANE, NUCLEOTIDE-BINDING, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BUNKOCZI,J.ESWARAN,C.COOPER,O.FEDOROV,T.KEATES,P.RELLOS,E.SALAH,
AUTHOR 2 P.SAVITSKY,E.UGOCHUKWU,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,
AUTHOR 3 M.SUNDSTROM,J.WEIGELT,S.KNAPP
REVDAT 6 13-DEC-23 2V62 1 REMARK LINK
REVDAT 5 30-NOV-11 2V62 1 REMARK
REVDAT 4 13-JUL-11 2V62 1 VERSN
REVDAT 3 04-AUG-09 2V62 1 JRNL REMARK
REVDAT 2 24-FEB-09 2V62 1 VERSN
REVDAT 1 21-AUG-07 2V62 0
JRNL AUTH E.D.SCHEEFF,J.ESWARAN,G.BUNKOCZI,S.KNAPP,G.MANNING
JRNL TITL STRUCTURE OF THE PSEUDOKINASE VRK3 REVEALS A DEGRADED
JRNL TITL 2 CATALYTIC SITE, A HIGHLY CONSERVED KINASE FOLD, AND A
JRNL TITL 3 PUTATIVE REGULATORY BINDING SITE.
JRNL REF STRUCTURE V. 17 128 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19141289
JRNL DOI 10.1016/J.STR.2008.10.018
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0034
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 64302
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 + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3413
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4358
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 217
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4756
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : -0.83000
REMARK 3 B33 (A**2) : 0.55000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.559
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4958 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3322 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6727 ; 1.483 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8122 ; 1.012 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 617 ; 5.602 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;33.469 ;24.512
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 801 ;13.311 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.691 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 741 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5519 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 975 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1029 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3320 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2372 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2510 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 235 ; 0.169 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.185 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 100 ; 0.295 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.158 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3193 ; 3.326 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4955 ; 4.590 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2047 ; 7.114 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1772 ; 8.803 ;11.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 15 A 62 5
REMARK 3 1 B 15 B 62 5
REMARK 3 2 A 98 A 122 3
REMARK 3 2 B 98 B 122 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 145 ; 0.04 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 245 ; 0.04 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 419 ; 0.03 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 145 ; 0.19 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 245 ; 0.17 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 419 ; 0.18 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 68 A 97 5
REMARK 3 1 B 68 B 97 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 178 ; 0.12 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 A (A): 238 ; 0.30 ; 5.00
REMARK 3 MEDIUM THERMAL 2 A (A**2): 178 ; 1.07 ; 2.00
REMARK 3 LOOSE THERMAL 2 A (A**2): 238 ; 1.06 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 123 A 330 3
REMARK 3 1 B 123 B 330 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 1220 ; 0.03 ; 0.05
REMARK 3 LOOSE POSITIONAL 3 A (A): 1465 ; 0.05 ; 5.00
REMARK 3 TIGHT THERMAL 3 A (A**2): 1220 ; 0.27 ; 0.50
REMARK 3 LOOSE THERMAL 3 A (A**2): 1465 ; 0.24 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 67
REMARK 3 RESIDUE RANGE : A 98 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4035 -1.7714 28.8268
REMARK 3 T TENSOR
REMARK 3 T11: 0.2811 T22: 0.1399
REMARK 3 T33: 0.0509 T12: 0.0470
REMARK 3 T13: -0.0388 T23: -0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 3.7570 L22: 5.7041
REMARK 3 L33: 1.6924 L12: -2.6505
REMARK 3 L13: 0.9759 L23: -0.5670
REMARK 3 S TENSOR
REMARK 3 S11: 0.3218 S12: 0.4531 S13: -0.3997
REMARK 3 S21: -0.9798 S22: -0.1401 S23: -0.1118
REMARK 3 S31: 0.5739 S32: 0.4571 S33: -0.1816
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 68 A 97
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7818 11.6726 35.4781
REMARK 3 T TENSOR
REMARK 3 T11: -0.0869 T22: -0.1637
REMARK 3 T33: -0.0627 T12: -0.0594
REMARK 3 T13: -0.0206 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 4.7695 L22: 1.5859
REMARK 3 L33: 4.3243 L12: -2.2205
REMARK 3 L13: 1.0702 L23: -0.6609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0336 S12: -0.0893 S13: -0.5311
REMARK 3 S21: 0.0180 S22: 0.1398 S23: 0.2568
REMARK 3 S31: 0.3398 S32: -0.3091 S33: -0.1062
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 123 A 330
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9835 27.7157 30.1806
REMARK 3 T TENSOR
REMARK 3 T11: -0.1358 T22: -0.1262
REMARK 3 T33: -0.1213 T12: 0.0047
REMARK 3 T13: 0.0018 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 1.0556 L22: 1.3213
REMARK 3 L33: 1.4893 L12: -0.0793
REMARK 3 L13: 0.1324 L23: -0.4239
REMARK 3 S TENSOR
REMARK 3 S11: 0.0460 S12: 0.1833 S13: 0.1590
REMARK 3 S21: -0.1844 S22: -0.0333 S23: -0.0163
REMARK 3 S31: 0.0776 S32: 0.0210 S33: -0.0128
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 67
REMARK 3 RESIDUE RANGE : B 98 B 122
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9299 80.0317 56.4216
REMARK 3 T TENSOR
REMARK 3 T11: 0.3050 T22: 0.1216
REMARK 3 T33: 0.0578 T12: 0.0442
REMARK 3 T13: 0.0231 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 3.8714 L22: 5.6988
REMARK 3 L33: 0.9482 L12: -2.2242
REMARK 3 L13: -0.9552 L23: 0.4026
REMARK 3 S TENSOR
REMARK 3 S11: 0.3259 S12: 0.4610 S13: 0.3237
REMARK 3 S21: -1.0514 S22: -0.2104 S23: 0.1798
REMARK 3 S31: -0.5570 S32: -0.3261 S33: -0.1154
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 68 B 97
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7547 66.7924 63.5871
REMARK 3 T TENSOR
REMARK 3 T11: -0.0675 T22: -0.1425
REMARK 3 T33: -0.0108 T12: -0.0690
REMARK 3 T13: 0.0254 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 6.4470 L22: 0.5866
REMARK 3 L33: 3.1432 L12: -1.5562
REMARK 3 L13: -0.7946 L23: 0.9933
REMARK 3 S TENSOR
REMARK 3 S11: 0.1360 S12: -0.0688 S13: 0.5786
REMARK 3 S21: -0.1198 S22: 0.0371 S23: -0.1839
REMARK 3 S31: -0.2966 S32: 0.3520 S33: -0.1731
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 123 B 330
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8436 50.8887 58.3550
REMARK 3 T TENSOR
REMARK 3 T11: -0.1289 T22: -0.1367
REMARK 3 T33: -0.1004 T12: -0.0019
REMARK 3 T13: 0.0096 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 1.1754 L22: 1.4095
REMARK 3 L33: 1.6716 L12: -0.1653
REMARK 3 L13: -0.0948 L23: 0.4885
REMARK 3 S TENSOR
REMARK 3 S11: 0.0351 S12: 0.1720 S13: -0.1430
REMARK 3 S21: -0.1881 S22: -0.0208 S23: -0.0390
REMARK 3 S31: -0.1022 S32: 0.0361 S33: -0.0143
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2V62 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1290033183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67759
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 45.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: PDB ENTRY 2JII
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SUCCINIC ACID PH=7.0 15%
REMARK 280 PEG3350, PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 35.32750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.76600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.32750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.76600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 SER A -2
REMARK 465 SER A -1
REMARK 465 GLY A 0
REMARK 465 VAL A 1
REMARK 465 ASP A 2
REMARK 465 LEU A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 GLU A 6
REMARK 465 ASN A 7
REMARK 465 LEU A 8
REMARK 465 TYR A 9
REMARK 465 PHE A 10
REMARK 465 GLN A 11
REMARK 465 SER A 12
REMARK 465 MET A 13
REMARK 465 PRO A 14
REMARK 465 GLY A 36
REMARK 465 SER A 37
REMARK 465 GLY A 38
REMARK 465 GLY A 39
REMARK 465 PHE A 40
REMARK 465 GLY A 41
REMARK 465 ASN A 67
REMARK 465 SER A 331
REMARK 465 ILE A 332
REMARK 465 ASN A 333
REMARK 465 VAL A 334
REMARK 465 HIS A 335
REMARK 465 MET B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 SER B -2
REMARK 465 SER B -1
REMARK 465 GLY B 0
REMARK 465 VAL B 1
REMARK 465 ASP B 2
REMARK 465 LEU B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 ASN B 7
REMARK 465 LEU B 8
REMARK 465 TYR B 9
REMARK 465 PHE B 10
REMARK 465 GLN B 11
REMARK 465 SER B 12
REMARK 465 MET B 13
REMARK 465 PRO B 14
REMARK 465 GLY B 36
REMARK 465 SER B 37
REMARK 465 GLY B 38
REMARK 465 GLY B 39
REMARK 465 PHE B 40
REMARK 465 ASN B 67
REMARK 465 SER B 331
REMARK 465 ILE B 332
REMARK 465 ASN B 333
REMARK 465 VAL B 334
REMARK 465 HIS B 335
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 GLU A 17 CG CD OE1 OE2
REMARK 470 ASP A 22 CG OD1 OD2
REMARK 470 LYS A 33 CG CD CE NZ
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 LEU A 42 CG CD1 CD2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 GLU A 53 CG CD OE1 OE2
REMARK 470 LYS A 54 CD CE NZ
REMARK 470 ASP A 55 CG OD1 OD2
REMARK 470 ARG A 57 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 64 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 66 CG CD OE1 OE2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 LYS A 87 CG CD CE NZ
REMARK 470 LYS A 88 CG CD CE NZ
REMARK 470 LYS A 93 CE NZ
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 PHE A 111 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 130 CD CE NZ
REMARK 470 GLN A 134 CG CD OE1 NE2
REMARK 470 LYS A 139 CE NZ
REMARK 470 LYS A 177 CD CE NZ
REMARK 470 ASP A 180 CG OD1 OD2
REMARK 470 GLN A 203 CD OE1 NE2
REMARK 470 LYS A 208 CE NZ
REMARK 470 GLU A 251 CD OE1 OE2
REMARK 470 LYS A 255 CD CE NZ
REMARK 470 GLN A 307 CD OE1 NE2
REMARK 470 ILE A 318 CG1 CG2 CD1
REMARK 470 THR A 327 OG1 CG2
REMARK 470 LYS A 328 CE NZ
REMARK 470 GLN A 330 CG CD OE1 NE2
REMARK 470 LYS B 33 CG CD CE NZ
REMARK 470 LYS B 34 CG CD CE NZ
REMARK 470 LEU B 42 CG CD1 CD2
REMARK 470 LYS B 51 CD CE NZ
REMARK 470 LYS B 54 CD CE NZ
REMARK 470 ARG B 57 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 64 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 66 CG CD OE1 OE2
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS B 87 CG CD CE NZ
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 GLU B 110 CD OE1 OE2
REMARK 470 PHE B 111 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 112 CG CD CE NZ
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 130 CD CE NZ
REMARK 470 GLN B 134 CG CD OE1 NE2
REMARK 470 LYS B 139 CE NZ
REMARK 470 LYS B 177 CG CD CE NZ
REMARK 470 ASP B 180 CG OD1 OD2
REMARK 470 LYS B 208 CE NZ
REMARK 470 GLU B 251 CD OE1 OE2
REMARK 470 LYS B 255 CD CE NZ
REMARK 470 GLN B 307 CD OE1 NE2
REMARK 470 THR B 327 OG1 CG2
REMARK 470 LYS B 328 CD CE NZ
REMARK 470 GLN B 330 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 194 CB CYS A 194 SG -0.097
REMARK 500 CYS A 294 CB CYS A 294 SG -0.141
REMARK 500 GLN B 65 CB GLN B 65 CG 8.353
REMARK 500 CYS B 294 CB CYS B 294 SG -0.132
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 GLN B 65 CA - CB - CG ANGL. DEV. = -83.0 DEGREES
REMARK 500 GLN B 65 CB - CG - CD ANGL. DEV. = 27.9 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 ASP A 55 52.66 -94.89
REMARK 500 TYR A 64 177.98 -59.54
REMARK 500 ALA A 81 53.67 -92.39
REMARK 500 LYS A 112 -100.89 -127.41
REMARK 500 GLU A 161 8.70 83.59
REMARK 500 ASP A 166 45.78 -151.06
REMARK 500 TYR A 176 -61.81 -100.69
REMARK 500 ASP A 186 82.15 61.40
REMARK 500 HIS A 210 31.66 71.36
REMARK 500 SER A 283 85.48 -153.63
REMARK 500 ASP B 55 52.34 -93.68
REMARK 500 LYS B 112 -102.57 -127.24
REMARK 500 GLU B 161 6.94 83.73
REMARK 500 ASP B 166 42.25 -151.81
REMARK 500 TYR B 176 -62.42 -98.36
REMARK 500 ASP B 186 82.78 58.38
REMARK 500 SER B 283 82.52 -153.65
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 MG A1331 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 207 O
REMARK 620 2 HOH A1084 O 91.1
REMARK 620 3 HOH A1085 O 92.2 86.4
REMARK 620 4 ARG B 207 O 175.7 89.4 83.5
REMARK 620 5 HOH B1094 O 95.1 167.2 82.2 83.6
REMARK 620 6 HOH B1096 O 90.9 98.9 173.8 93.3 92.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1331
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 1332
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1331
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1334
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 23 RESIDUES BELONG TO AN UNCLEAVED HIS-TAG
DBREF 2V62 A 14 335 UNP Q86Y07 VRK2_HUMAN 14 335
DBREF 2V62 B 14 335 UNP Q86Y07 VRK2_HUMAN 14 335
SEQADV 2V62 MET A -9 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS A -8 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS A -7 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS A -6 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS A -5 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS A -4 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS A -3 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 SER A -2 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 SER A -1 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLY A 0 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 VAL A 1 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 ASP A 2 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 LEU A 3 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLY A 4 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 THR A 5 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLU A 6 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 ASN A 7 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 LEU A 8 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 TYR A 9 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 PHE A 10 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLN A 11 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 SER A 12 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 MET A 13 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 MET B -9 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS B -8 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS B -7 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS B -6 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS B -5 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS B -4 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 HIS B -3 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 SER B -2 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 SER B -1 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLY B 0 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 VAL B 1 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 ASP B 2 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 LEU B 3 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLY B 4 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 THR B 5 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLU B 6 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 ASN B 7 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 LEU B 8 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 TYR B 9 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 PHE B 10 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 GLN B 11 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 SER B 12 UNP Q86Y07 EXPRESSION TAG
SEQADV 2V62 MET B 13 UNP Q86Y07 EXPRESSION TAG
SEQRES 1 A 345 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 345 GLY THR GLU ASN LEU TYR PHE GLN SER MET PRO PHE PRO
SEQRES 3 A 345 GLU GLY LYS VAL LEU ASP ASP MET GLU GLY ASN GLN TRP
SEQRES 4 A 345 VAL LEU GLY LYS LYS ILE GLY SER GLY GLY PHE GLY LEU
SEQRES 5 A 345 ILE TYR LEU ALA PHE PRO THR ASN LYS PRO GLU LYS ASP
SEQRES 6 A 345 ALA ARG HIS VAL VAL LYS VAL GLU TYR GLN GLU ASN GLY
SEQRES 7 A 345 PRO LEU PHE SER GLU LEU LYS PHE TYR GLN ARG VAL ALA
SEQRES 8 A 345 LYS LYS ASP CYS ILE LYS LYS TRP ILE GLU ARG LYS GLN
SEQRES 9 A 345 LEU ASP TYR LEU GLY ILE PRO LEU PHE TYR GLY SER GLY
SEQRES 10 A 345 LEU THR GLU PHE LYS GLY ARG SER TYR ARG PHE MET VAL
SEQRES 11 A 345 MET GLU ARG LEU GLY ILE ASP LEU GLN LYS ILE SER GLY
SEQRES 12 A 345 GLN ASN GLY THR PHE LYS LYS SER THR VAL LEU GLN LEU
SEQRES 13 A 345 GLY ILE ARG MET LEU ASP VAL LEU GLU TYR ILE HIS GLU
SEQRES 14 A 345 ASN GLU TYR VAL HIS GLY ASP ILE LYS ALA ALA ASN LEU
SEQRES 15 A 345 LEU LEU GLY TYR LYS ASN PRO ASP GLN VAL TYR LEU ALA
SEQRES 16 A 345 ASP TYR GLY LEU SER TYR ARG TYR CYS PRO ASN GLY ASN
SEQRES 17 A 345 HIS LYS GLN TYR GLN GLU ASN PRO ARG LYS GLY HIS ASN
SEQRES 18 A 345 GLY THR ILE GLU PHE THR SER LEU ASP ALA HIS LYS GLY
SEQRES 19 A 345 VAL ALA LEU SER ARG ARG SER ASP VAL GLU ILE LEU GLY
SEQRES 20 A 345 TYR CYS MET LEU ARG TRP LEU CYS GLY LYS LEU PRO TRP
SEQRES 21 A 345 GLU GLN ASN LEU LYS ASP PRO VAL ALA VAL GLN THR ALA
SEQRES 22 A 345 LYS THR ASN LEU LEU ASP GLU LEU PRO GLN SER VAL LEU
SEQRES 23 A 345 LYS TRP ALA PRO SER GLY SER SER CYS CYS GLU ILE ALA
SEQRES 24 A 345 GLN PHE LEU VAL CYS ALA HIS SER LEU ALA TYR ASP GLU
SEQRES 25 A 345 LYS PRO ASN TYR GLN ALA LEU LYS LYS ILE LEU ASN PRO
SEQRES 26 A 345 HIS GLY ILE PRO LEU GLY PRO LEU ASP PHE SER THR LYS
SEQRES 27 A 345 GLY GLN SER ILE ASN VAL HIS
SEQRES 1 B 345 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 345 GLY THR GLU ASN LEU TYR PHE GLN SER MET PRO PHE PRO
SEQRES 3 B 345 GLU GLY LYS VAL LEU ASP ASP MET GLU GLY ASN GLN TRP
SEQRES 4 B 345 VAL LEU GLY LYS LYS ILE GLY SER GLY GLY PHE GLY LEU
SEQRES 5 B 345 ILE TYR LEU ALA PHE PRO THR ASN LYS PRO GLU LYS ASP
SEQRES 6 B 345 ALA ARG HIS VAL VAL LYS VAL GLU TYR GLN GLU ASN GLY
SEQRES 7 B 345 PRO LEU PHE SER GLU LEU LYS PHE TYR GLN ARG VAL ALA
SEQRES 8 B 345 LYS LYS ASP CYS ILE LYS LYS TRP ILE GLU ARG LYS GLN
SEQRES 9 B 345 LEU ASP TYR LEU GLY ILE PRO LEU PHE TYR GLY SER GLY
SEQRES 10 B 345 LEU THR GLU PHE LYS GLY ARG SER TYR ARG PHE MET VAL
SEQRES 11 B 345 MET GLU ARG LEU GLY ILE ASP LEU GLN LYS ILE SER GLY
SEQRES 12 B 345 GLN ASN GLY THR PHE LYS LYS SER THR VAL LEU GLN LEU
SEQRES 13 B 345 GLY ILE ARG MET LEU ASP VAL LEU GLU TYR ILE HIS GLU
SEQRES 14 B 345 ASN GLU TYR VAL HIS GLY ASP ILE LYS ALA ALA ASN LEU
SEQRES 15 B 345 LEU LEU GLY TYR LYS ASN PRO ASP GLN VAL TYR LEU ALA
SEQRES 16 B 345 ASP TYR GLY LEU SER TYR ARG TYR CYS PRO ASN GLY ASN
SEQRES 17 B 345 HIS LYS GLN TYR GLN GLU ASN PRO ARG LYS GLY HIS ASN
SEQRES 18 B 345 GLY THR ILE GLU PHE THR SER LEU ASP ALA HIS LYS GLY
SEQRES 19 B 345 VAL ALA LEU SER ARG ARG SER ASP VAL GLU ILE LEU GLY
SEQRES 20 B 345 TYR CYS MET LEU ARG TRP LEU CYS GLY LYS LEU PRO TRP
SEQRES 21 B 345 GLU GLN ASN LEU LYS ASP PRO VAL ALA VAL GLN THR ALA
SEQRES 22 B 345 LYS THR ASN LEU LEU ASP GLU LEU PRO GLN SER VAL LEU
SEQRES 23 B 345 LYS TRP ALA PRO SER GLY SER SER CYS CYS GLU ILE ALA
SEQRES 24 B 345 GLN PHE LEU VAL CYS ALA HIS SER LEU ALA TYR ASP GLU
SEQRES 25 B 345 LYS PRO ASN TYR GLN ALA LEU LYS LYS ILE LEU ASN PRO
SEQRES 26 B 345 HIS GLY ILE PRO LEU GLY PRO LEU ASP PHE SER THR LYS
SEQRES 27 B 345 GLY GLN SER ILE ASN VAL HIS
HET MG A1331 1
HET SIN A1332 8
HET EDO A1333 4
HET EDO A1334 4
HET EDO B1331 4
HETNAM MG MAGNESIUM ION
HETNAM SIN SUCCINIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 MG MG 2+
FORMUL 4 SIN C4 H6 O4
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 8 HOH *334(H2 O)
HELIX 1 1 PRO A 52 ALA A 56 5 5
HELIX 2 2 GLY A 68 ALA A 81 1 14
HELIX 3 3 LYS A 82 GLN A 94 1 13
HELIX 4 4 LEU A 128 SER A 132 1 5
HELIX 5 5 GLN A 134 GLY A 136 5 3
HELIX 6 6 LYS A 139 ASN A 160 1 22
HELIX 7 7 LYS A 168 ALA A 170 5 3
HELIX 8 8 CYS A 194 ASN A 198 5 5
HELIX 9 9 ASN A 205 GLY A 209 5 5
HELIX 10 10 SER A 218 GLY A 224 1 7
HELIX 11 11 SER A 228 GLY A 246 1 19
HELIX 12 12 TRP A 250 LEU A 254 5 5
HELIX 13 13 ASP A 256 GLU A 270 1 15
HELIX 14 14 PRO A 272 ALA A 279 1 8
HELIX 15 15 CYS A 285 SER A 297 1 13
HELIX 16 16 ASN A 305 ASN A 314 1 10
HELIX 17 17 PRO B 52 ALA B 56 5 5
HELIX 18 18 GLY B 68 ALA B 81 1 14
HELIX 19 19 LYS B 82 LYS B 93 1 12
HELIX 20 20 GLN B 134 GLY B 136 5 3
HELIX 21 21 LYS B 139 ASN B 160 1 22
HELIX 22 22 LYS B 168 ALA B 170 5 3
HELIX 23 23 CYS B 194 ASN B 198 5 5
HELIX 24 24 ASN B 205 GLY B 209 5 5
HELIX 25 25 SER B 218 GLY B 224 1 7
HELIX 26 26 SER B 228 GLY B 246 1 19
HELIX 27 27 TRP B 250 LEU B 254 5 5
HELIX 28 28 ASP B 256 GLU B 270 1 15
HELIX 29 29 PRO B 272 LYS B 277 1 6
HELIX 30 30 CYS B 285 SER B 297 1 13
HELIX 31 31 ASN B 305 ASN B 314 1 10
SHEET 1 AA 6 VAL A 20 ASP A 22 0
SHEET 2 AA 6 GLN A 28 LYS A 34 -1 O TRP A 29 N LEU A 21
SHEET 3 AA 6 ILE A 43 PRO A 48 -1 O LEU A 45 N GLY A 32
SHEET 4 AA 6 HIS A 58 TYR A 64 -1 O HIS A 58 N ALA A 46
SHEET 5 AA 6 SER A 115 GLU A 122 -1 O ARG A 117 N GLU A 63
SHEET 6 AA 6 PHE A 103 GLU A 110 -1 N TYR A 104 O VAL A 120
SHEET 1 AB 3 LEU A 124 ASP A 127 0
SHEET 2 AB 3 LEU A 172 GLY A 175 -1 O LEU A 174 N GLY A 125
SHEET 3 AB 3 VAL A 182 LEU A 184 -1 O TYR A 183 N LEU A 173
SHEET 1 AC 2 TYR A 162 VAL A 163 0
SHEET 2 AC 2 TYR A 191 ARG A 192 -1 O TYR A 191 N VAL A 163
SHEET 1 BA 6 VAL B 20 ASP B 22 0
SHEET 2 BA 6 GLN B 28 ILE B 35 -1 O TRP B 29 N LEU B 21
SHEET 3 BA 6 LEU B 42 PRO B 48 -1 O ILE B 43 N ILE B 35
SHEET 4 BA 6 HIS B 58 VAL B 62 -1 O HIS B 58 N ALA B 46
SHEET 5 BA 6 SER B 115 GLU B 122 -1 O MET B 119 N LYS B 61
SHEET 6 BA 6 PHE B 103 GLU B 110 -1 N TYR B 104 O VAL B 120
SHEET 1 BB 3 LEU B 124 ASP B 127 0
SHEET 2 BB 3 LEU B 172 GLY B 175 -1 O LEU B 174 N GLY B 125
SHEET 3 BB 3 VAL B 182 LEU B 184 -1 O TYR B 183 N LEU B 173
SHEET 1 BC 2 TYR B 162 VAL B 163 0
SHEET 2 BC 2 TYR B 191 ARG B 192 -1 O TYR B 191 N VAL B 163
LINK O ARG A 207 MG MG A1331 1555 1555 2.21
LINK O HOH A1084 MG MG A1331 1555 1555 2.31
LINK O HOH A1085 MG MG A1331 1555 1555 2.62
LINK MG MG A1331 O ARG B 207 1555 4557 2.35
LINK MG MG A1331 O HOH B1094 1555 4557 2.45
LINK MG MG A1331 O HOH B1096 1555 4557 2.53
CISPEP 1 LEU A 271 PRO A 272 0 -4.19
CISPEP 2 LEU B 271 PRO B 272 0 -4.10
SITE 1 AC1 6 ARG A 207 HOH A1084 HOH A1085 ARG B 207
SITE 2 AC1 6 HOH B1094 HOH B1096
SITE 1 AC2 10 ARG A 117 HOH A1167 HOH A1168 HOH A1169
SITE 2 AC2 10 MET B 24 LEU B 74 GLN B 78 SER B 106
SITE 3 AC2 10 GLY B 107 ARG B 117
SITE 1 AC3 4 SER A 297 CYS B 245 TRP B 278 PRO B 280
SITE 1 AC4 5 CYS A 245 TRP A 278 PRO A 280 SER B 297
SITE 2 AC4 5 HOH B1150
SITE 1 AC5 5 ARG A 79 ASN A 160 GLU A 161 GLU B 25
SITE 2 AC5 5 ARG B 92
CRYST1 70.655 157.532 56.288 90.00 90.00 90.00 P 21 21 2 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 0.014153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017766 0.00000
MTRIX1 1 -0.999290 0.037720 -0.001270 35.71097 1
MTRIX2 1 -0.037720 -0.999270 0.006050 78.92622 1
MTRIX3 1 -0.001040 0.006100 0.999980 27.94197 1
(ATOM LINES ARE NOT SHOWN.)
END