HEADER CALCIUM-BINDING PROTEIN 07-DEC-04 1Y6W
TITLE TRAPPED INTERMEDIATE OF CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CALM1, CALM2, CALM3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAED4
KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN, ENGINEERED DISULFIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.GRABAREK
REVDAT 3 20-OCT-21 1Y6W 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1Y6W 1 VERSN
REVDAT 1 01-MAR-05 1Y6W 0
JRNL AUTH Z.GRABAREK
JRNL TITL STRUCTURE OF A TRAPPED INTERMEDIATE OF CALMODULIN: CALCIUM
JRNL TITL 2 REGULATION OF EF-HAND PROTEINS FROM A NEW PERSPECTIVE.
JRNL REF J.MOL.BIOL. V. 346 1351 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15713486
JRNL DOI 10.1016/J.JMB.2005.01.004
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1351678.820
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 10322
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 492
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1553
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 79
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 56
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.76000
REMARK 3 B22 (A**2) : -9.76000
REMARK 3 B33 (A**2) : 19.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.540 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.560 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.870 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.120 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 38.89
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : HETERO.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : HETERO.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE N-TERMINAL DOMAIN IS LOCKED IN A
REMARK 3 CLOSED CONFORMATION WITH A DISULFIDE BOND. THIS PREVENTS THE
REMARK 3 GLUTAMATE IN THE 12TH POSITION OF THE LOOP FROM INTERACTING WITH
REMARK 3 THE CALCIUM ION IN SITES I AND II. BOND ANGLES IN RESIDUES 60,
REMARK 3 61, 94 AND 132 DEVIATE BY MORE THAN 6*RMSD RELATIVE TO THE
REMARK 3 STANDARD DICTIONARY (SEE REMARK 500). THESE RESIDUES ARE LOCATED
REMARK 3 IN THE CALCIUM BINDING LOOPS, THUS THEIR CONFORMATION IS
REMARK 3 CONSTRAINED BY THE CALCIUM IONS.
REMARK 4
REMARK 4 1Y6W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031191.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97896, 0.97919, 0.97129
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10558
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
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 (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% (W/V) 2-METHYL-2,4-PENTANEDIOL,
REMARK 280 10% (V/V) T-BUTANOL, 20 MM NA-CACODYLATE, 5 MM CACL2, PH 5.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 21.32000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.93750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.93750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.98000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.93750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.93750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 10.66000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.93750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.93750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.98000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.93750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.93750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 10.66000
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 21.32000
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 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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 LYS A 148
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 114 CG CD OE1 OE2
REMARK 480 LYS A 115 CG CD CE NZ
REMARK 480 LEU A 116 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 42 66.41 -116.25
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 CA A 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 82.1
REMARK 620 3 ASP A 22 OD2 105.0 46.1
REMARK 620 4 ASP A 24 OD2 82.4 110.5 74.5
REMARK 620 5 THR A 26 O 83.1 159.0 153.8 82.1
REMARK 620 6 HOH A 602 O 107.1 84.6 114.6 163.5 85.6
REMARK 620 7 HOH A 606 O 157.2 91.3 56.7 79.6 107.8 93.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 56 OD2 53.7
REMARK 620 3 ASP A 58 OD1 121.0 106.4
REMARK 620 4 ASP A 58 OD2 71.7 75.8 49.4
REMARK 620 5 ASN A 60 OD1 90.6 140.3 75.4 76.8
REMARK 620 6 THR A 62 O 71.8 92.6 160.9 141.2 91.2
REMARK 620 7 MPD A 400 O2 148.8 142.1 84.0 130.9 77.3 79.8
REMARK 620 8 MPD A 400 O4 125.8 73.7 82.9 110.3 143.6 101.2 71.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD2 84.4
REMARK 620 3 ASN A 97 OD1 83.7 72.2
REMARK 620 4 TYR A 99 O 81.6 153.4 83.8
REMARK 620 5 GLU A 104 OE1 105.5 131.4 154.6 74.5
REMARK 620 6 GLU A 104 OE2 100.0 80.6 152.2 124.0 50.9
REMARK 620 7 HOH A 611 O 166.7 88.3 83.5 100.6 87.7 89.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 83.9
REMARK 620 3 ASP A 133 OD1 81.4 97.0
REMARK 620 4 GLN A 135 O 79.0 162.2 75.8
REMARK 620 5 GLU A 140 OE1 111.5 115.4 145.7 75.9
REMARK 620 6 GLU A 140 OE2 84.1 73.0 163.2 109.6 49.0
REMARK 620 7 HOH A 604 O 159.6 96.5 78.3 97.9 86.8 115.6
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBU A 500
DBREF 1Y6W A 1 148 UNP P62158 CALM_HUMAN 1 148
SEQADV 1Y6W MSE A 36 UNP P62158 MET 36 MODIFIED RESIDUE
SEQADV 1Y6W CYS A 41 UNP P62158 GLN 41 ENGINEERED MUTATION
SEQADV 1Y6W MSE A 51 UNP P62158 MET 51 MODIFIED RESIDUE
SEQADV 1Y6W ASN A 64 UNP P62158 ASP 64 ENGINEERED MUTATION
SEQADV 1Y6W MSE A 71 UNP P62158 MET 71 MODIFIED RESIDUE
SEQADV 1Y6W MSE A 72 UNP P62158 MET 72 MODIFIED RESIDUE
SEQADV 1Y6W CYS A 75 UNP P62158 LYS 75 ENGINEERED MUTATION
SEQADV 1Y6W MSE A 76 UNP P62158 MET 76 MODIFIED RESIDUE
SEQADV 1Y6W MSE A 109 UNP P62158 MET 109 MODIFIED RESIDUE
SEQADV 1Y6W MSE A 124 UNP P62158 MET 124 MODIFIED RESIDUE
SEQADV 1Y6W MSE A 144 UNP P62158 MET 144 MODIFIED RESIDUE
SEQADV 1Y6W MSE A 145 UNP P62158 MET 145 MODIFIED RESIDUE
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER LEU
SEQRES 4 A 148 GLY CYS ASN PRO THR GLU ALA GLU LEU GLN ASP MSE ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASN PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MSE MSE ALA ARG CYS MSE LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MSE MSE THR ALA LYS
MODRES 1Y6W MSE A 36 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 51 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 71 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 72 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 76 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 109 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 124 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 144 MET SELENOMETHIONINE
MODRES 1Y6W MSE A 145 MET SELENOMETHIONINE
HET MSE A 36 8
HET MSE A 51 8
HET MSE A 71 8
HET MSE A 72 8
HET MSE A 76 8
HET MSE A 109 8
HET MSE A 124 8
HET MSE A 144 8
HET MSE A 145 8
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HET CA A 152 1
HET MPD A 400 8
HET TBU A 500 5
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM TBU TERTIARY-BUTYL ALCOHOL
HETSYN TBU 2-METHYL-2-PROPANOL
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 2 CA 4(CA 2+)
FORMUL 6 MPD C6 H14 O2
FORMUL 7 TBU C4 H10 O
FORMUL 8 HOH *56(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 29 LEU A 39 1 11
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 ASP A 93 1 29
HELIX 5 5 SER A 101 GLY A 113 1 13
HELIX 6 6 THR A 117 ASP A 129 1 13
HELIX 7 7 TYR A 138 THR A 146 1 9
SHEET 1 A 2 THR A 26 THR A 28 0
SHEET 2 A 2 THR A 62 ASN A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 TYR A 99 ILE A 100 0
SHEET 2 B 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
SSBOND 1 CYS A 41 CYS A 75 1555 1555 2.05
LINK C VAL A 35 N MSE A 36 1555 1555 1.32
LINK C MSE A 36 N ARG A 37 1555 1555 1.34
LINK C ASP A 50 N MSE A 51 1555 1555 1.33
LINK C MSE A 51 N ILE A 52 1555 1555 1.33
LINK C THR A 70 N MSE A 71 1555 1555 1.33
LINK C MSE A 71 N MSE A 72 1555 1555 1.33
LINK C MSE A 72 N ALA A 73 1555 1555 1.33
LINK C CYS A 75 N MSE A 76 1555 1555 1.33
LINK C MSE A 76 N LYS A 77 1555 1555 1.33
LINK C VAL A 108 N MSE A 109 1555 1555 1.33
LINK C MSE A 109 N THR A 110 1555 1555 1.33
LINK C GLU A 123 N MSE A 124 1555 1555 1.33
LINK C MSE A 124 N ILE A 125 1555 1555 1.33
LINK C GLN A 143 N MSE A 144 1555 1555 1.33
LINK C MSE A 144 N MSE A 145 1555 1555 1.33
LINK C MSE A 145 N THR A 146 1555 1555 1.33
LINK OD1 ASP A 20 CA CA A 149 1555 1555 2.35
LINK OD1 ASP A 22 CA CA A 149 1555 1555 2.43
LINK OD2 ASP A 22 CA CA A 149 1555 1555 2.98
LINK OD2 ASP A 24 CA CA A 149 1555 1555 2.43
LINK O THR A 26 CA CA A 149 1555 1555 2.32
LINK OD1 ASP A 56 CA CA A 150 1555 1555 2.57
LINK OD2 ASP A 56 CA CA A 150 1555 1555 2.25
LINK OD1 ASP A 58 CA CA A 150 1555 1555 2.69
LINK OD2 ASP A 58 CA CA A 150 1555 1555 2.46
LINK OD1 ASN A 60 CA CA A 150 1555 1555 2.37
LINK O THR A 62 CA CA A 150 1555 1555 2.49
LINK OD1 ASP A 93 CA CA A 151 1555 1555 2.32
LINK OD2 ASP A 95 CA CA A 151 1555 1555 2.32
LINK OD1 ASN A 97 CA CA A 151 1555 1555 2.38
LINK O TYR A 99 CA CA A 151 1555 1555 2.27
LINK OE1 GLU A 104 CA CA A 151 1555 1555 2.62
LINK OE2 GLU A 104 CA CA A 151 1555 1555 2.46
LINK OD1 ASP A 129 CA CA A 152 1555 1555 2.48
LINK OD1 ASP A 131 CA CA A 152 1555 1555 2.15
LINK OD1 ASP A 133 CA CA A 152 1555 1555 2.53
LINK O GLN A 135 CA CA A 152 1555 1555 2.36
LINK OE1 GLU A 140 CA CA A 152 1555 1555 2.58
LINK OE2 GLU A 140 CA CA A 152 1555 1555 2.70
LINK CA CA A 149 O HOH A 602 1555 1555 2.56
LINK CA CA A 149 O HOH A 606 1555 1555 2.78
LINK CA CA A 150 O2 MPD A 400 1555 1555 2.51
LINK CA CA A 150 O4 MPD A 400 1555 1555 2.36
LINK CA CA A 151 O HOH A 611 1555 1555 2.72
LINK CA CA A 152 O HOH A 604 1555 1555 2.46
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 HOH A 602 HOH A 606
SITE 1 AC2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 5 MPD A 400
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A 611
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 GLU A 140 HOH A 604
SITE 1 AC5 10 THR A 26 ARG A 37 SER A 38 ASP A 56
SITE 2 AC5 10 ASP A 58 ASN A 60 THR A 62 ASN A 64
SITE 3 AC5 10 GLU A 67 CA A 150
SITE 1 AC6 2 LEU A 105 MSE A 144
CRYST1 109.875 109.875 42.640 90.00 90.00 90.00 P 43 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 0.009101 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023452 0.00000
(ATOM LINES ARE NOT SHOWN.)
END