HEADER TRANSFERASE 04-JUN-12 4FG9
TITLE CRYSTAL STRUCTURE OF HUMAN CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE
TITLE 2 I 1-320 IN COMPLEX WITH ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-320;
COMPND 5 SYNONYM: CAM KINASE I, CAM-KI, CAM KINASE I ALPHA, CAMKI-ALPHA;
COMPND 6 EC: 2.7.11.17;
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 GENE: CAMK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1
KEYWDS CAMK, CALMODULIN, AUTOINHIBITION, REGULATION MECHANISM, KINASE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZHA,C.ZHONG,Y.OU,J.WANG,L.HAN,J.DING
REVDAT 1 23-JAN-13 4FG9 0
JRNL AUTH M.ZHA,C.ZHONG,Y.OU,L.HAN,J.WANG,J.DING
JRNL TITL CRYSTAL STRUCTURES OF HUMAN CAMKIALPHA REVEAL INSIGHTS INTO
JRNL TITL 2 THE REGULATION MECHANISM OF CAMKI.
JRNL REF PLOS ONE V. 7 44828 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 23028635
JRNL DOI 10.1371/JOURNAL.PONE.0044828
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 23395
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1188
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1639
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.2110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4420
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 136
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.188
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4586 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6228 ; 1.137 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 551 ; 4.364 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;38.163 ;24.645
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 765 ;16.343 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;12.968 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3433 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.579
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : H+K, -K, -L
REMARK 3 TWIN FRACTION : 0.421
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4FG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 1W2B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 76.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 4FG7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M (NH4)2SO4, 100MM TRI-SODIUM
REMARK 280 CITRATE, 0.8M LI2SO4, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 76.50200
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 76.50200
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 76.50200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 83.09700
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 41.54850
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 71.96411
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 548 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 567 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 561 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 LEU A 2
REMARK 465 GLY A 3
REMARK 465 ALA A 4
REMARK 465 VAL A 5
REMARK 465 GLU A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 8
REMARK 465 ARG A 9
REMARK 465 ALA A 55
REMARK 465 LEU A 56
REMARK 465 GLU A 57
REMARK 465 GLY A 58
REMARK 465 LYS A 59
REMARK 465 GLU A 60
REMARK 465 GLY A 61
REMARK 465 SER A 62
REMARK 465 MET A 63
REMARK 465 GLY A 164
REMARK 465 LEU A 165
REMARK 465 SER A 166
REMARK 465 LYS A 167
REMARK 465 MET A 168
REMARK 465 GLU A 169
REMARK 465 ASP A 170
REMARK 465 PRO A 171
REMARK 465 GLY A 172
REMARK 465 SER A 173
REMARK 465 VAL A 174
REMARK 465 LEU A 175
REMARK 465 SER A 176
REMARK 465 THR A 177
REMARK 465 ALA A 178
REMARK 465 CYS A 179
REMARK 465 GLY A 180
REMARK 465 THR A 181
REMARK 465 HIS A 315
REMARK 465 MET A 316
REMARK 465 ARG A 317
REMARK 465 LYS A 318
REMARK 465 LEU A 319
REMARK 465 GLN A 320
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 GLY B 3
REMARK 465 ALA B 4
REMARK 465 VAL B 5
REMARK 465 GLU B 6
REMARK 465 GLY B 7
REMARK 465 PRO B 8
REMARK 465 ARG B 9
REMARK 465 TRP B 10
REMARK 465 LYS B 11
REMARK 465 GLN B 12
REMARK 465 ALA B 13
REMARK 465 GLU B 54
REMARK 465 ALA B 55
REMARK 465 LEU B 56
REMARK 465 GLU B 57
REMARK 465 GLY B 58
REMARK 465 LYS B 59
REMARK 465 GLU B 60
REMARK 465 GLY B 61
REMARK 465 SER B 62
REMARK 465 MET B 63
REMARK 465 GLU B 64
REMARK 465 ASN B 65
REMARK 465 GLY B 164
REMARK 465 LEU B 165
REMARK 465 SER B 166
REMARK 465 LYS B 167
REMARK 465 MET B 168
REMARK 465 GLU B 169
REMARK 465 ASP B 170
REMARK 465 PRO B 171
REMARK 465 GLY B 172
REMARK 465 SER B 173
REMARK 465 HIS B 315
REMARK 465 MET B 316
REMARK 465 ARG B 317
REMARK 465 LYS B 318
REMARK 465 LEU B 319
REMARK 465 GLN B 320
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 14 CG CD OE1 OE2
REMARK 470 PHE A 31 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 TYR A 219 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 221 CG CD OE1 OE2
REMARK 470 LYS A 232 CG CD CE NZ
REMARK 470 GLU A 262 CG CD OE1 OE2
REMARK 470 ARG A 314 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 14 CG CD OE1 OE2
REMARK 470 ASP B 15 CG OD1 OD2
REMARK 470 GLU B 66 CG CD OE1 OE2
REMARK 470 ILE B 67 CG1 CG2 CD1
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 THR B 181 OG1 CG2
REMARK 470 GLU B 221 CG CD OE1 OE2
REMARK 470 GLU B 234 CG CD OE1 OE2
REMARK 470 ARG B 314 CG CD NE CZ NH1 NH2
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 ARG A 23 -120.30 -116.69
REMARK 500 LYS A 53 93.42 -65.93
REMARK 500 SER A 87 -166.80 -106.78
REMARK 500 ARG A 140 -19.91 75.14
REMARK 500 ASN A 285 95.79 -69.31
REMARK 500 ARG B 23 -124.84 -116.86
REMARK 500 ARG B 140 -17.09 67.77
REMARK 500 SER B 196 -148.09 -143.42
REMARK 500 CYS B 213 -24.09 -142.86
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 ATP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FG7 RELATED DB: PDB
REMARK 900 RELATED ID: 4FG8 RELATED DB: PDB
REMARK 900 RELATED ID: 4FGB RELATED DB: PDB
DBREF 4FG9 A 1 320 UNP Q14012 KCC1A_HUMAN 1 320
DBREF 4FG9 B 1 320 UNP Q14012 KCC1A_HUMAN 1 320
SEQRES 1 A 320 MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA
SEQRES 2 A 320 GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU
SEQRES 3 A 320 GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP
SEQRES 4 A 320 LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA
SEQRES 5 A 320 LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN
SEQRES 6 A 320 GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE
SEQRES 7 A 320 VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU
SEQRES 8 A 320 TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE
SEQRES 9 A 320 ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP
SEQRES 10 A 320 ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS
SEQRES 11 A 320 TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS
SEQRES 12 A 320 PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER
SEQRES 13 A 320 LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU
SEQRES 14 A 320 ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO
SEQRES 15 A 320 GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR
SEQRES 16 A 320 SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA
SEQRES 17 A 320 TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU
SEQRES 18 A 320 ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU
SEQRES 19 A 320 TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP
SEQRES 20 A 320 SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP
SEQRES 21 A 320 PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS
SEQRES 22 A 320 PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE
SEQRES 23 A 320 HIS GLN SER VAL SER GLU GLN ILE LYS LYS ASN PHE ALA
SEQRES 24 A 320 LYS SER LYS TRP LYS GLN ALA PHE ASN ALA THR ALA VAL
SEQRES 25 A 320 VAL ARG HIS MET ARG LYS LEU GLN
SEQRES 1 B 320 MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA
SEQRES 2 B 320 GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU
SEQRES 3 B 320 GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP
SEQRES 4 B 320 LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA
SEQRES 5 B 320 LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN
SEQRES 6 B 320 GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE
SEQRES 7 B 320 VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU
SEQRES 8 B 320 TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE
SEQRES 9 B 320 ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP
SEQRES 10 B 320 ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS
SEQRES 11 B 320 TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS
SEQRES 12 B 320 PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER
SEQRES 13 B 320 LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU
SEQRES 14 B 320 ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO
SEQRES 15 B 320 GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR
SEQRES 16 B 320 SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA
SEQRES 17 B 320 TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU
SEQRES 18 B 320 ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU
SEQRES 19 B 320 TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP
SEQRES 20 B 320 SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP
SEQRES 21 B 320 PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS
SEQRES 22 B 320 PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE
SEQRES 23 B 320 HIS GLN SER VAL SER GLU GLN ILE LYS LYS ASN PHE ALA
SEQRES 24 B 320 LYS SER LYS TRP LYS GLN ALA PHE ASN ALA THR ALA VAL
SEQRES 25 B 320 VAL ARG HIS MET ARG LYS LEU GLN
HET ATP A 401 31
HET ATP B 401 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
FORMUL 5 HOH *136(H2 O)
HELIX 1 1 ASP A 15 ASP A 18 5 4
HELIX 2 2 ASN A 65 LYS A 72 1 8
HELIX 3 3 LEU A 103 LYS A 110 1 8
HELIX 4 4 THR A 114 GLY A 136 1 23
HELIX 5 5 LYS A 143 GLU A 145 5 3
HELIX 6 6 ALA A 186 ALA A 191 1 6
HELIX 7 7 LYS A 197 GLY A 214 1 18
HELIX 8 8 ASN A 222 LYS A 232 1 11
HELIX 9 9 SER A 246 MET A 257 1 12
HELIX 10 10 THR A 266 HIS A 273 1 8
HELIX 11 11 HIS A 273 GLY A 278 1 6
HELIX 12 12 ILE A 286 PHE A 298 1 13
HELIX 13 13 LYS A 300 VAL A 312 1 13
HELIX 14 14 ASP B 15 ASP B 18 5 4
HELIX 15 15 ILE B 67 HIS B 71 1 5
HELIX 16 16 LEU B 103 LYS B 110 1 8
HELIX 17 17 THR B 114 GLY B 136 1 23
HELIX 18 18 LYS B 143 GLU B 145 5 3
HELIX 19 19 LEU B 175 THR B 181 1 7
HELIX 20 20 ALA B 186 ALA B 191 1 6
HELIX 21 21 LYS B 197 GLY B 214 1 18
HELIX 22 22 ASN B 222 LYS B 232 1 11
HELIX 23 23 SER B 246 MET B 257 1 12
HELIX 24 24 THR B 266 GLN B 272 1 7
HELIX 25 25 HIS B 273 GLY B 278 1 6
HELIX 26 26 ILE B 286 PHE B 298 1 13
HELIX 27 27 ALA B 299 ARG B 314 1 16
SHEET 1 A 5 TYR A 20 THR A 28 0
SHEET 2 A 5 SER A 32 ASP A 39 -1 O LEU A 36 N ASP A 24
SHEET 3 A 5 LEU A 45 ALA A 52 -1 O VAL A 46 N ALA A 37
SHEET 4 A 5 HIS A 90 GLN A 96 -1 O MET A 95 N ALA A 47
SHEET 5 A 5 LEU A 81 GLU A 86 -1 N TYR A 85 O TYR A 92
SHEET 1 B 3 GLY A 101 GLU A 102 0
SHEET 2 B 3 LEU A 147 TYR A 149 -1 O TYR A 149 N GLY A 101
SHEET 3 B 3 ILE A 158 ILE A 160 -1 O MET A 159 N LEU A 148
SHEET 1 C 5 TYR B 20 THR B 28 0
SHEET 2 C 5 SER B 32 ASP B 39 -1 O LEU B 36 N ASP B 24
SHEET 3 C 5 LEU B 45 ALA B 52 -1 O VAL B 46 N ALA B 37
SHEET 4 C 5 HIS B 90 MET B 95 -1 O LEU B 91 N ILE B 51
SHEET 5 C 5 LEU B 81 GLU B 86 -1 N ASP B 83 O ILE B 94
SHEET 1 D 3 GLY B 101 GLU B 102 0
SHEET 2 D 3 LEU B 147 TYR B 149 -1 O TYR B 149 N GLY B 101
SHEET 3 D 3 ILE B 158 ILE B 160 -1 O MET B 159 N LEU B 148
CISPEP 1 SER A 239 PRO A 240 0 -0.64
CISPEP 2 SER B 239 PRO B 240 0 -2.51
SITE 1 AC1 18 GLY A 27 THR A 28 GLY A 29 ALA A 30
SITE 2 AC1 18 SER A 32 VAL A 34 ALA A 47 LYS A 49
SITE 3 AC1 18 GLN A 96 VAL A 98 GLU A 102 ASP A 141
SITE 4 AC1 18 LYS A 143 GLU A 145 ASN A 146 LEU A 148
SITE 5 AC1 18 ASP A 162 HOH A 563
SITE 1 AC2 21 LEU B 26 GLY B 27 GLY B 29 ALA B 30
SITE 2 AC2 21 SER B 32 VAL B 34 ALA B 47 LYS B 49
SITE 3 AC2 21 VAL B 79 GLN B 96 VAL B 98 GLU B 102
SITE 4 AC2 21 LYS B 143 ASN B 146 LEU B 148 ASP B 162
SITE 5 AC2 21 HOH B 550 HOH B 551 HOH B 559 HOH B 564
SITE 6 AC2 21 HOH B 565
CRYST1 83.097 83.097 153.004 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 0.012034 0.006948 0.000000 0.00000
SCALE2 0.000000 0.013896 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006536 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
