HEADER TRANSFERASE 04-JUN-12 4FG7
TITLE CRYSTAL STRUCTURE OF HUMAN CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE
TITLE 2 I 1-293 IN COMPLEX WITH ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-293;
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 4FG7 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. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 8918
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 461
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 609
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 27
REMARK 3 BIN FREE R VALUE : 0.4670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2008
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 79
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.02
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): 0.072
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 : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2087 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2832 ; 1.435 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 246 ; 5.119 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;38.569 ;24.900
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;15.950 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;18.640 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1570 ; 0.006 ; 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 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 9 A 277
REMARK 3 ORIGIN FOR THE GROUP (A): 129.3778 -22.3634 24.2949
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.1690
REMARK 3 T33: 0.0438 T12: -0.0037
REMARK 3 T13: -0.0124 T23: 0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 1.0607 L22: 2.7372
REMARK 3 L33: 0.3986 L12: -0.8340
REMARK 3 L13: -0.2944 L23: -0.2469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0294 S12: 0.0580 S13: 0.1097
REMARK 3 S21: 0.1406 S22: -0.0171 S23: -0.0350
REMARK 3 S31: 0.0706 S32: 0.0583 S33: -0.0122
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 : RESIDUAL ONLY
REMARK 4
REMARK 4 4FG7 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 RCSB072861.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
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 : ADSC QUANTUM 4
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) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 59.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.6000
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
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 1A06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM NH4AC, 100MM (CH3)2ASO2NA, 25%
REMARK 280 PEG 8000, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -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 -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 69.94450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 32.84050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.84050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.97225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.84050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 32.84050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 104.91675
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 32.84050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.84050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 34.97225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 32.84050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.84050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 104.91675
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.94450
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: 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 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 LYS A 53
REMARK 465 GLU A 54
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 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 PRO A 194
REMARK 465 TYR A 195
REMARK 465 GLY A 278
REMARK 465 ASP A 279
REMARK 465 THR A 280
REMARK 465 ALA A 281
REMARK 465 LEU A 282
REMARK 465 ASP A 283
REMARK 465 LYS A 284
REMARK 465 ASN A 285
REMARK 465 ILE A 286
REMARK 465 HIS A 287
REMARK 465 GLN A 288
REMARK 465 SER A 289
REMARK 465 VAL A 290
REMARK 465 SER A 291
REMARK 465 GLU A 292
REMARK 465 GLN A 293
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 ARG A 9 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 17 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 LYS A 193 CG CD CE NZ
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 -126.18 -116.63
REMARK 500 ASP A 83 -175.99 -173.88
REMARK 500 GLU A 109 24.24 -78.79
REMARK 500 LYS A 110 -27.21 -153.08
REMARK 500 ARG A 140 -3.11 76.61
REMARK 500 ASP A 141 39.67 -145.87
REMARK 500 ASP A 162 83.23 56.25
REMARK 500 GLN A 192 -124.09 -141.02
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 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FG8 RELATED DB: PDB
REMARK 900 RELATED ID: 4FG9 RELATED DB: PDB
REMARK 900 RELATED ID: 4FGB RELATED DB: PDB
DBREF 4FG7 A 1 293 UNP Q14012 KCC1A_HUMAN 1 293
SEQRES 1 A 293 MET LEU GLY ALA VAL GLU GLY PRO ARG TRP LYS GLN ALA
SEQRES 2 A 293 GLU ASP ILE ARG ASP ILE TYR ASP PHE ARG ASP VAL LEU
SEQRES 3 A 293 GLY THR GLY ALA PHE SER GLU VAL ILE LEU ALA GLU ASP
SEQRES 4 A 293 LYS ARG THR GLN LYS LEU VAL ALA ILE LYS CYS ILE ALA
SEQRES 5 A 293 LYS GLU ALA LEU GLU GLY LYS GLU GLY SER MET GLU ASN
SEQRES 6 A 293 GLU ILE ALA VAL LEU HIS LYS ILE LYS HIS PRO ASN ILE
SEQRES 7 A 293 VAL ALA LEU ASP ASP ILE TYR GLU SER GLY GLY HIS LEU
SEQRES 8 A 293 TYR LEU ILE MET GLN LEU VAL SER GLY GLY GLU LEU PHE
SEQRES 9 A 293 ASP ARG ILE VAL GLU LYS GLY PHE TYR THR GLU ARG ASP
SEQRES 10 A 293 ALA SER ARG LEU ILE PHE GLN VAL LEU ASP ALA VAL LYS
SEQRES 11 A 293 TYR LEU HIS ASP LEU GLY ILE VAL HIS ARG ASP LEU LYS
SEQRES 12 A 293 PRO GLU ASN LEU LEU TYR TYR SER LEU ASP GLU ASP SER
SEQRES 13 A 293 LYS ILE MET ILE SER ASP PHE GLY LEU SER LYS MET GLU
SEQRES 14 A 293 ASP PRO GLY SER VAL LEU SER THR ALA CYS GLY THR PRO
SEQRES 15 A 293 GLY TYR VAL ALA PRO GLU VAL LEU ALA GLN LYS PRO TYR
SEQRES 16 A 293 SER LYS ALA VAL ASP CYS TRP SER ILE GLY VAL ILE ALA
SEQRES 17 A 293 TYR ILE LEU LEU CYS GLY TYR PRO PRO PHE TYR ASP GLU
SEQRES 18 A 293 ASN ASP ALA LYS LEU PHE GLU GLN ILE LEU LYS ALA GLU
SEQRES 19 A 293 TYR GLU PHE ASP SER PRO TYR TRP ASP ASP ILE SER ASP
SEQRES 20 A 293 SER ALA LYS ASP PHE ILE ARG HIS LEU MET GLU LYS ASP
SEQRES 21 A 293 PRO GLU LYS ARG PHE THR CYS GLU GLN ALA LEU GLN HIS
SEQRES 22 A 293 PRO TRP ILE ALA GLY ASP THR ALA LEU ASP LYS ASN ILE
SEQRES 23 A 293 HIS GLN SER VAL SER GLU GLN
HET ATP A 301 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 ATP C10 H16 N5 O13 P3
FORMUL 3 HOH *79(H2 O)
HELIX 1 1 ASP A 15 ASP A 18 5 4
HELIX 2 2 MET A 63 ILE A 73 1 11
HELIX 3 3 GLU A 102 GLU A 109 1 8
HELIX 4 4 THR A 114 ASP A 134 1 21
HELIX 5 5 ALA A 186 GLN A 192 1 7
HELIX 6 6 LYS A 197 GLY A 214 1 18
HELIX 7 7 ASN A 222 ALA A 233 1 12
HELIX 8 8 SER A 246 MET A 257 1 12
HELIX 9 9 THR A 266 HIS A 273 1 8
SHEET 1 A 6 LYS A 11 GLN A 12 0
SHEET 2 A 6 LEU A 81 SER A 87 1 O GLU A 86 N LYS A 11
SHEET 3 A 6 HIS A 90 MET A 95 -1 O ILE A 94 N ASP A 83
SHEET 4 A 6 LEU A 45 ILE A 51 -1 N ALA A 47 O MET A 95
SHEET 5 A 6 SER A 32 ASP A 39 -1 N GLU A 33 O CYS A 50
SHEET 6 A 6 TYR A 20 THR A 28 -1 N ARG A 23 O LEU A 36
SHEET 1 B 2 ILE A 137 VAL A 138 0
SHEET 2 B 2 LYS A 167 MET A 168 -1 O LYS A 167 N VAL A 138
SHEET 1 C 2 LEU A 147 TYR A 149 0
SHEET 2 C 2 ILE A 158 ILE A 160 -1 O MET A 159 N LEU A 148
CISPEP 1 SER A 239 PRO A 240 0 5.69
SITE 1 AC1 18 GLY A 27 THR A 28 GLY A 29 ALA A 30
SITE 2 AC1 18 PHE A 31 SER A 32 VAL A 34 ALA A 47
SITE 3 AC1 18 LYS A 49 VAL A 79 GLN A 96 VAL A 98
SITE 4 AC1 18 GLU A 102 ASP A 162 HOH A 407 HOH A 427
SITE 5 AC1 18 HOH A 430 HOH A 435
CRYST1 65.681 65.681 139.889 90.00 90.00 90.00 P 41 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 0.015225 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007149 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
