HEADER TRANSFERASE 31-JAN-08 2VN9
TITLE CRYSTAL STRUCTURE OF HUMAN CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE
TITLE 2 II DELTA ISOFORM 1, CAMKD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA
COMPND 3 CHAIN;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: KINASE DOMAIN, RESIDUES 11-309;
COMPND 6 SYNONYM: CAM-KINASE II DELTA CHAIN, CAM KINASE II SUBUNIT DELTA,
COMPND 7 CAMK-II SUBUNIT DELTA, CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II
COMPND 8 DELTA ISOFORM 1;
COMPND 9 EC: 2.7.11.17;
COMPND 10 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS SERINE/THREONINE-PROTEIN KINASE, SERINE-THREONINE KINASE, CELLULAR
KEYWDS 2 DIFFERENTIATION, VASCULAR SMOOTH MUSCLE, KINASE, TRANSFERASE, ATP-
KEYWDS 3 BINDING, PHOSPHOPROTEIN, CALMODULIN-BINDING, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.ROOS,P.RELLOS,E.SALAH,A.C.W.PIKE,O.FEDOROV,E.S.PILKA,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,S.KNAPP
REVDAT 6 13-DEC-23 2VN9 1 REMARK
REVDAT 5 13-DEC-17 2VN9 1 SOURCE JRNL
REVDAT 4 10-AUG-11 2VN9 1 JRNL REMARK HETSYN FORMUL
REVDAT 3 13-JUL-11 2VN9 1 VERSN
REVDAT 2 24-FEB-09 2VN9 1 VERSN
REVDAT 1 26-FEB-08 2VN9 0
JRNL AUTH P.RELLOS,A.C.W.PIKE,F.H.NIESEN,E.SALAH,W.H.LEE,F.VON DELFT,
JRNL AUTH 2 S.KNAPP
JRNL TITL STRUCTURE OF THE CAMKIIDELTA/CALMODULIN COMPLEX REVEALS THE
JRNL TITL 2 MOLECULAR MECHANISM OF CAMKII KINASE ACTIVATION.
JRNL REF PLOS BIOL. V. 8 426 2010
JRNL REFN ISSN 1544-9173
JRNL PMID 20668654
JRNL DOI 10.1371/JOURNAL.PBIO.1000426
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0066
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 37042
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1960
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2704
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4721
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 58.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.15000
REMARK 3 B22 (A**2) : 1.15000
REMARK 3 B33 (A**2) : -1.72000
REMARK 3 B12 (A**2) : 0.57000
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): 0.262
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.212
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.193
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.783
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4928 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3332 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6686 ; 1.425 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8071 ; 0.976 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 600 ; 5.808 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 216 ;33.025 ;23.796
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 820 ;14.525 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;21.522 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 725 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5440 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 980 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3000 ; 1.684 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1210 ; 0.870 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4823 ; 2.481 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1928 ; 4.495 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1857 ; 5.576 ;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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
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 -1 A 309 1
REMARK 3 1 B -1 B 309 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3959 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 3959 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3959 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 3959 ; 0.16 ; 0.50
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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -1 A 39
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4802 37.9307 55.7746
REMARK 3 T TENSOR
REMARK 3 T11: -0.4185 T22: 0.1348
REMARK 3 T33: 0.0596 T12: -0.0372
REMARK 3 T13: 0.0242 T23: -0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 4.7580 L22: 8.4180
REMARK 3 L33: 11.6520 L12: 0.4387
REMARK 3 L13: 0.7231 L23: 1.9160
REMARK 3 S TENSOR
REMARK 3 S11: -0.3062 S12: -0.3087 S13: 0.5231
REMARK 3 S21: -0.0987 S22: 0.1327 S23: 0.2238
REMARK 3 S31: -0.7694 S32: -0.4147 S33: 0.1735
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 40 A 83
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2753 30.2185 53.5075
REMARK 3 T TENSOR
REMARK 3 T11: -0.4955 T22: 0.1371
REMARK 3 T33: -0.1308 T12: -0.0343
REMARK 3 T13: 0.0055 T23: 0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 6.7529 L22: 1.8197
REMARK 3 L33: 1.3251 L12: -3.0149
REMARK 3 L13: -0.3544 L23: 0.9449
REMARK 3 S TENSOR
REMARK 3 S11: -0.1694 S12: -0.3660 S13: 0.4505
REMARK 3 S21: 0.0963 S22: 0.0796 S23: 0.0180
REMARK 3 S31: -0.0176 S32: -0.1205 S33: 0.0898
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 84 A 309
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0084 15.6757 36.1947
REMARK 3 T TENSOR
REMARK 3 T11: -0.2976 T22: 0.1063
REMARK 3 T33: -0.1776 T12: -0.1446
REMARK 3 T13: 0.0777 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 3.3598 L22: 1.9079
REMARK 3 L33: 2.0951 L12: 0.5050
REMARK 3 L13: -0.2368 L23: 1.2558
REMARK 3 S TENSOR
REMARK 3 S11: -0.2771 S12: 0.6060 S13: -0.3184
REMARK 3 S21: -0.4213 S22: 0.2423 S23: -0.1134
REMARK 3 S31: 0.1423 S32: -0.0756 S33: 0.0348
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -1 B 39
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5939 57.9775 -6.0806
REMARK 3 T TENSOR
REMARK 3 T11: 0.1722 T22: -0.0916
REMARK 3 T33: 0.0591 T12: -0.2799
REMARK 3 T13: -0.1864 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 7.4621 L22: 7.4556
REMARK 3 L33: 10.1546 L12: 0.7162
REMARK 3 L13: 1.0051 L23: -0.3826
REMARK 3 S TENSOR
REMARK 3 S11: -0.2801 S12: -0.0299 S13: 0.4969
REMARK 3 S21: -0.4617 S22: 0.2955 S23: 0.2677
REMARK 3 S31: -0.3389 S32: -0.6191 S33: -0.0155
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 40 B 83
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7954 65.3807 -1.3540
REMARK 3 T TENSOR
REMARK 3 T11: 0.2174 T22: -0.1521
REMARK 3 T33: -0.1419 T12: -0.3370
REMARK 3 T13: -0.1012 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 0.2188 L22: 8.9965
REMARK 3 L33: 3.5945 L12: 0.3249
REMARK 3 L13: 0.7225 L23: -2.1354
REMARK 3 S TENSOR
REMARK 3 S11: -0.3533 S12: 0.0536 S13: 0.2378
REMARK 3 S21: -0.9819 S22: 0.1194 S23: 0.2851
REMARK 3 S31: -0.1204 S32: 0.0687 S33: 0.2339
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 84 B 309
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0597 54.9420 19.5083
REMARK 3 T TENSOR
REMARK 3 T11: -0.1601 T22: 0.0152
REMARK 3 T33: -0.2501 T12: -0.1217
REMARK 3 T13: 0.0039 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.5556 L22: 4.0334
REMARK 3 L33: 5.6129 L12: 0.1549
REMARK 3 L13: 1.6079 L23: -2.5982
REMARK 3 S TENSOR
REMARK 3 S11: -0.2961 S12: -0.5224 S13: 0.1137
REMARK 3 S21: 0.1363 S22: 0.1430 S23: 0.0182
REMARK 3 S31: -0.4519 S32: -0.3415 S33: 0.1531
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 2VN9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1290035204.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.98248
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39106
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
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: PDB ENTRY 2V7O
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M NAKPO4 HEPES PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 208.96667
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 104.48333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 104.48333
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 208.96667
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 SER A -1 OG
REMARK 470 LYS A 22 CE NZ
REMARK 470 PHE A 25 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 49 CE NZ
REMARK 470 LYS A 69 CE NZ
REMARK 470 GLN A 165 CD OE1 NE2
REMARK 470 GLN A 168 CD OE1 NE2
REMARK 470 ARG A 187 CZ NH1 NH2
REMARK 470 LYS A 188 NZ
REMARK 470 ARG A 221 CZ NH1 NH2
REMARK 470 GLN A 224 CD OE1 NE2
REMARK 470 LYS A 259 NZ
REMARK 470 LYS A 292 CE NZ
REMARK 470 LYS A 299 CE NZ
REMARK 470 LEU A 309 CG CD1 CD2
REMARK 470 SER B -1 OG
REMARK 470 LEU B 16 CG CD1 CD2
REMARK 470 LYS B 22 CE NZ
REMARK 470 PHE B 25 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 48 CD CE NZ
REMARK 470 LYS B 49 CG CD CE NZ
REMARK 470 LYS B 69 CE NZ
REMARK 470 GLN B 165 CG CD OE1 NE2
REMARK 470 GLN B 168 CD OE1 NE2
REMARK 470 LYS B 188 CE NZ
REMARK 470 GLN B 224 CG CD OE1 NE2
REMARK 470 LYS B 259 CD CE NZ
REMARK 470 LYS B 268 CE NZ
REMARK 470 LYS B 292 CD CE NZ
REMARK 470 LYS B 293 CD CE NZ
REMARK 470 LYS B 299 CE NZ
REMARK 470 LYS B 301 CG CD CE NZ
REMARK 470 LEU B 309 CG CD1 CD2
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 ARG A 298 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 298 NE - CZ - NH2 ANGL. DEV. = 3.3 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 PHE A 17 -136.38 -116.79
REMARK 500 PHE A 25 31.13 -171.85
REMARK 500 ASP A 136 46.64 -149.72
REMARK 500 ASP A 157 92.42 55.20
REMARK 500 LYS A 301 -143.04 67.00
REMARK 500 PHE B 17 -135.64 -118.09
REMARK 500 PHE B 25 29.91 -171.19
REMARK 500 ASP B 136 47.14 -147.49
REMARK 500 ASP B 157 92.45 57.38
REMARK 500 PHE B 233 68.62 -119.10
REMARK 500 ARG B 284 62.05 -117.61
REMARK 500 LYS B 301 -150.37 68.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVD B 1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVD A 1314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1313
DBREF 2VN9 A -1 0 PDB 2VN9 2VN9 -1 0
DBREF 2VN9 A 11 309 UNP Q13557 KCC2D_HUMAN 11 309
DBREF 2VN9 B -1 0 PDB 2VN9 2VN9 -1 0
DBREF 2VN9 B 11 309 UNP Q13557 KCC2D_HUMAN 11 309
SEQRES 1 A 301 SER MET THR ASP GLU TYR GLN LEU PHE GLU GLU LEU GLY
SEQRES 2 A 301 LYS GLY ALA PHE SER VAL VAL ARG ARG CYS MET LYS ILE
SEQRES 3 A 301 PRO THR GLY GLN GLU TYR ALA ALA LYS ILE ILE ASN THR
SEQRES 4 A 301 LYS LYS LEU SER ALA ARG ASP HIS GLN LYS LEU GLU ARG
SEQRES 5 A 301 GLU ALA ARG ILE CYS ARG LEU LEU LYS HIS PRO ASN ILE
SEQRES 6 A 301 VAL ARG LEU HIS ASP SER ILE SER GLU GLU GLY PHE HIS
SEQRES 7 A 301 TYR LEU VAL PHE ASP LEU VAL THR GLY GLY GLU LEU PHE
SEQRES 8 A 301 GLU ASP ILE VAL ALA ARG GLU TYR TYR SER GLU ALA ASP
SEQRES 9 A 301 ALA SER HIS CYS ILE GLN GLN ILE LEU GLU SER VAL ASN
SEQRES 10 A 301 HIS CYS HIS LEU ASN GLY ILE VAL HIS ARG ASP LEU LYS
SEQRES 11 A 301 PRO GLU ASN LEU LEU LEU ALA SER LYS SER LYS GLY ALA
SEQRES 12 A 301 ALA VAL LYS LEU ALA ASP PHE GLY LEU ALA ILE GLU VAL
SEQRES 13 A 301 GLN GLY ASP GLN GLN ALA TRP PHE GLY PHE ALA GLY THR
SEQRES 14 A 301 PRO GLY TYR LEU SER PRO GLU VAL LEU ARG LYS ASP PRO
SEQRES 15 A 301 TYR GLY LYS PRO VAL ASP MET TRP ALA CYS GLY VAL ILE
SEQRES 16 A 301 LEU TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP ASP
SEQRES 17 A 301 GLU ASP GLN HIS ARG LEU TYR GLN GLN ILE LYS ALA GLY
SEQRES 18 A 301 ALA TYR ASP PHE PRO SER PRO GLU TRP ASP THR VAL THR
SEQRES 19 A 301 PRO GLU ALA LYS ASP LEU ILE ASN LYS MET LEU THR ILE
SEQRES 20 A 301 ASN PRO ALA LYS ARG ILE THR ALA SER GLU ALA LEU LYS
SEQRES 21 A 301 HIS PRO TRP ILE CYS GLN ARG SER THR VAL ALA SER MET
SEQRES 22 A 301 MET HIS ARG GLN GLU THR VAL ASP CYS LEU LYS LYS PHE
SEQRES 23 A 301 ASN ALA ARG ARG LYS LEU LYS GLY ALA ILE LEU THR THR
SEQRES 24 A 301 MET LEU
SEQRES 1 B 301 SER MET THR ASP GLU TYR GLN LEU PHE GLU GLU LEU GLY
SEQRES 2 B 301 LYS GLY ALA PHE SER VAL VAL ARG ARG CYS MET LYS ILE
SEQRES 3 B 301 PRO THR GLY GLN GLU TYR ALA ALA LYS ILE ILE ASN THR
SEQRES 4 B 301 LYS LYS LEU SER ALA ARG ASP HIS GLN LYS LEU GLU ARG
SEQRES 5 B 301 GLU ALA ARG ILE CYS ARG LEU LEU LYS HIS PRO ASN ILE
SEQRES 6 B 301 VAL ARG LEU HIS ASP SER ILE SER GLU GLU GLY PHE HIS
SEQRES 7 B 301 TYR LEU VAL PHE ASP LEU VAL THR GLY GLY GLU LEU PHE
SEQRES 8 B 301 GLU ASP ILE VAL ALA ARG GLU TYR TYR SER GLU ALA ASP
SEQRES 9 B 301 ALA SER HIS CYS ILE GLN GLN ILE LEU GLU SER VAL ASN
SEQRES 10 B 301 HIS CYS HIS LEU ASN GLY ILE VAL HIS ARG ASP LEU LYS
SEQRES 11 B 301 PRO GLU ASN LEU LEU LEU ALA SER LYS SER LYS GLY ALA
SEQRES 12 B 301 ALA VAL LYS LEU ALA ASP PHE GLY LEU ALA ILE GLU VAL
SEQRES 13 B 301 GLN GLY ASP GLN GLN ALA TRP PHE GLY PHE ALA GLY THR
SEQRES 14 B 301 PRO GLY TYR LEU SER PRO GLU VAL LEU ARG LYS ASP PRO
SEQRES 15 B 301 TYR GLY LYS PRO VAL ASP MET TRP ALA CYS GLY VAL ILE
SEQRES 16 B 301 LEU TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP ASP
SEQRES 17 B 301 GLU ASP GLN HIS ARG LEU TYR GLN GLN ILE LYS ALA GLY
SEQRES 18 B 301 ALA TYR ASP PHE PRO SER PRO GLU TRP ASP THR VAL THR
SEQRES 19 B 301 PRO GLU ALA LYS ASP LEU ILE ASN LYS MET LEU THR ILE
SEQRES 20 B 301 ASN PRO ALA LYS ARG ILE THR ALA SER GLU ALA LEU LYS
SEQRES 21 B 301 HIS PRO TRP ILE CYS GLN ARG SER THR VAL ALA SER MET
SEQRES 22 B 301 MET HIS ARG GLN GLU THR VAL ASP CYS LEU LYS LYS PHE
SEQRES 23 B 301 ASN ALA ARG ARG LYS LEU LYS GLY ALA ILE LEU THR THR
SEQRES 24 B 301 MET LEU
HET PO4 A1310 5
HET PO4 A1311 5
HET CL A1312 1
HET EPE A1313 15
HET GVD A1314 29
HET GVD B1310 29
HET PO4 B1311 5
HET PO4 B1312 5
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM GVD [4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)
HETNAM 2 GVD AMINO]QUINAZOLIN-2-YL}IMINO)CYCLOHEXA-2,5-DIEN-1-
HETNAM 3 GVD YL]ACETONITRILE
HETSYN EPE HEPES
FORMUL 3 PO4 4(O4 P 3-)
FORMUL 5 CL CL 1-
FORMUL 6 EPE C8 H18 N2 O4 S
FORMUL 7 GVD 2(C22 H19 N7)
FORMUL 11 HOH *97(H2 O)
HELIX 1 1 SER A -1 GLU A 13 1 5
HELIX 2 2 SER A 51 LEU A 68 1 18
HELIX 3 3 GLU A 97 ARG A 105 1 9
HELIX 4 4 SER A 109 ASN A 130 1 22
HELIX 5 5 LYS A 138 GLU A 140 5 3
HELIX 6 6 THR A 177 LEU A 181 5 5
HELIX 7 7 SER A 182 ARG A 187 1 6
HELIX 8 8 LYS A 193 GLY A 210 1 18
HELIX 9 9 ASP A 218 GLY A 229 1 12
HELIX 10 10 PRO A 236 VAL A 241 5 6
HELIX 11 11 THR A 242 LEU A 253 1 12
HELIX 12 12 THR A 262 LEU A 267 1 6
HELIX 13 13 HIS A 269 GLN A 274 1 6
HELIX 14 14 GLN A 274 ALA A 279 1 6
HELIX 15 15 ARG A 284 LEU A 300 1 17
HELIX 16 16 SER B -1 GLU B 13 1 5
HELIX 17 17 SER B 51 LEU B 68 1 18
HELIX 18 18 GLU B 97 ALA B 104 1 8
HELIX 19 19 SER B 109 ASN B 130 1 22
HELIX 20 20 LYS B 138 GLU B 140 5 3
HELIX 21 21 THR B 177 LEU B 181 5 5
HELIX 22 22 SER B 182 ARG B 187 1 6
HELIX 23 23 LYS B 193 GLY B 210 1 18
HELIX 24 24 ASP B 218 ALA B 228 1 11
HELIX 25 25 THR B 242 LEU B 253 1 12
HELIX 26 26 THR B 262 LEU B 267 1 6
HELIX 27 27 HIS B 269 GLN B 274 1 6
HELIX 28 28 GLN B 274 ALA B 279 1 6
HELIX 29 29 ARG B 284 LEU B 300 1 17
SHEET 1 AA 5 TYR A 14 LYS A 22 0
SHEET 2 AA 5 SER A 26 LYS A 33 -1 O VAL A 28 N LEU A 20
SHEET 3 AA 5 GLU A 39 ASN A 46 -1 O TYR A 40 N CYS A 31
SHEET 4 AA 5 PHE A 85 ASP A 91 -1 O HIS A 86 N ILE A 45
SHEET 5 AA 5 LEU A 76 GLU A 82 -1 N HIS A 77 O VAL A 89
SHEET 1 AB 2 ILE A 132 VAL A 133 0
SHEET 2 AB 2 ILE A 162 GLU A 163 -1 O ILE A 162 N VAL A 133
SHEET 1 AC 2 LEU A 142 LEU A 144 0
SHEET 2 AC 2 VAL A 153 LEU A 155 -1 O LYS A 154 N LEU A 143
SHEET 1 BA 5 TYR B 14 LYS B 22 0
SHEET 2 BA 5 SER B 26 LYS B 33 -1 O VAL B 28 N LEU B 20
SHEET 3 BA 5 GLU B 39 ASN B 46 -1 O TYR B 40 N CYS B 31
SHEET 4 BA 5 PHE B 85 ASP B 91 -1 O HIS B 86 N ILE B 45
SHEET 5 BA 5 LEU B 76 GLU B 82 -1 N HIS B 77 O VAL B 89
SHEET 1 BB 2 ILE B 132 VAL B 133 0
SHEET 2 BB 2 ILE B 162 GLU B 163 -1 O ILE B 162 N VAL B 133
SHEET 1 BC 2 LEU B 142 LEU B 144 0
SHEET 2 BC 2 VAL B 153 LEU B 155 -1 O LYS B 154 N LEU B 143
CISPEP 1 ILE A 34 PRO A 35 0 -3.92
CISPEP 2 SER A 235 PRO A 236 0 -0.64
CISPEP 3 ILE B 34 PRO B 35 0 -5.67
CISPEP 4 SER B 235 PRO B 236 0 0.43
SITE 1 AC1 9 LEU B 20 LYS B 22 ALA B 41 LYS B 43
SITE 2 AC1 9 ASP B 91 LEU B 92 VAL B 93 ASP B 157
SITE 3 AC1 9 PO4 B1312
SITE 1 AC2 11 LEU A 20 LYS A 22 VAL A 28 ALA A 41
SITE 2 AC2 11 LYS A 43 PHE A 90 ASP A 91 LEU A 92
SITE 3 AC2 11 VAL A 93 ASP A 157 PO4 A1311
SITE 1 AC3 9 THR A 47 HIS A 55 SER A 81 GLU A 82
SITE 2 AC3 9 PHE A 85 HIS A 86 SER A 148 LYS A 149
SITE 3 AC3 9 HOH A2072
SITE 1 AC4 8 THR B 47 HIS B 55 SER B 81 GLU B 82
SITE 2 AC4 8 PHE B 85 HIS B 86 SER B 148 LYS B 149
SITE 1 AC5 2 LEU B 20 GVD B1310
SITE 1 AC6 4 LEU A 20 GLY A 21 GVD A1314 HOH A2073
SITE 1 AC7 2 ARG A 75 HIS A 77
SITE 1 AC8 8 TYR A 107 SER A 109 ALA A 111 ASP A 112
SITE 2 AC8 8 ARG A 275 SER A 276 MET A 281 HOH A2029
CRYST1 68.276 68.276 313.450 90.00 90.00 120.00 P 32 2 1 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 0.014646 0.008456 0.000000 0.00000
SCALE2 0.000000 0.016912 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003190 0.00000
MTRIX1 1 -0.501000 -0.820000 0.275000 13.43522 1
MTRIX2 1 -0.865000 0.480000 -0.145000 58.73976 1
MTRIX3 1 -0.013000 -0.311000 -0.950000 58.85304 1
(ATOM LINES ARE NOT SHOWN.)
END