HEADER METAL BINDING PROTEIN 02-FEB-08 2K0E
TITLE A COUPLED EQUILIBRIUM SHIFT MECHANISM IN CALMODULIN-MEDIATED SIGNAL
TITLE 2 TRANSDUCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: CALM1, CALM, CAM, CAM1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: AR58
KEYWDS EF HANDS, ENSEMBLE, HELIX BUNDLE, CALCIUM BINDING, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 160
AUTHOR J.GSPONER,J.CHRISTODOULOU,A.CAVALLI,J.M.BUI,B.RICHTER,C.M.DOBSON,
AUTHOR 2 M.VENDRUSCOLO
REVDAT 3 16-MAR-22 2K0E 1 REMARK
REVDAT 2 24-FEB-09 2K0E 1 VERSN
REVDAT 1 10-JUN-08 2K0E 0
JRNL AUTH J.GSPONER,J.CHRISTODOULOU,A.CAVALLI,J.M.BUI,B.RICHTER,
JRNL AUTH 2 C.M.DOBSON,M.VENDRUSCOLO
JRNL TITL A COUPLED EQUILIBRIUM SHIFT MECHANISM IN CALMODULIN-MEDIATED
JRNL TITL 2 SIGNAL TRANSDUCTION
JRNL REF STRUCTURE V. 16 736 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18462678
JRNL DOI 10.1016/J.STR.2008.02.017
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CHARMM C30
REMARK 3 AUTHORS : B.R.BROOKS, R.E.BRUCCOLERI,
REMARK 3 B.D.OLAFSON,D.J.STATES, S.SWAMINATHAN, M.KARLPLUS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PROGRAM : CHARMM C30 AUTHORS :
REMARK 3 B.R.BROOKS, R.E.BRUCCOLERI, B.D.OLAFSON,D.J.STATES,
REMARK 3 S.SWAMINATHAN, M.KARLPLUS
REMARK 4
REMARK 4 2K0E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000100517.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.5 MM CALMODULIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : CHARMM
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 160
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 160
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 24 HG1 THR A 26 1.60
REMARK 500 O VAL A 142 HG1 THR A 146 1.60
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 1 ASP A 22 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 1 THR A 62 CA - CB - CG2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 1 ASP A 80 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 ASP A 80 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 1 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 PHE A 89 CB - CG - CD2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 PHE A 89 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 LEU A 112 O - C - N ANGL. DEV. = -10.5 DEGREES
REMARK 500 1 ASP A 118 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 1 GLU A 120 O - C - N ANGL. DEV. = -10.1 DEGREES
REMARK 500 1 VAL A 121 CA - CB - CG2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 1 ARG A 126 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ASP A 129 O - C - N ANGL. DEV. = -9.9 DEGREES
REMARK 500 1 ASP A 131 CB - CG - OD1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 1 TYR A 138 CB - CG - CD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 1 GLU A 140 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 2 PHE A 19 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 THR A 26 CA - CB - CG2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 2 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 2 MET A 72 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 2 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 2 ARG A 106 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 MET A 109 CG - SD - CE ANGL. DEV. = -15.0 DEGREES
REMARK 500 2 MET A 145 CG - SD - CE ANGL. DEV. = -11.3 DEGREES
REMARK 500 3 ASP A 2 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 PHE A 12 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 3 PHE A 16 CB - CG - CD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 3 PHE A 16 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 PHE A 19 CB - CG - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 3 PHE A 19 CB - CG - CD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 3 GLY A 25 O - C - N ANGL. DEV. = -10.2 DEGREES
REMARK 500 3 THR A 26 N - CA - CB ANGL. DEV. = 11.4 DEGREES
REMARK 500 3 GLU A 31 OE1 - CD - OE2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 3 ASP A 64 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 3 ASP A 64 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 PHE A 68 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 PHE A 68 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 3 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 3 ARG A 90 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 3 ASP A 95 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 3 TYR A 99 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 3 TYR A 99 CD1 - CG - CD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 3 TYR A 99 CG - CD1 - CE1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ASP A 129 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 VAL A 136 CB - CA - C ANGL. DEV. = 13.4 DEGREES
REMARK 500 3 PHE A 141 CB - CG - CD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 3 MET A 145 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 2628 ANGLE DEVIATIONS.
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 1 ASP A 24 -141.95 -93.04
REMARK 500 1 ASN A 42 70.57 -161.45
REMARK 500 1 LYS A 75 -74.17 -62.92
REMARK 500 1 ASP A 78 -71.06 -57.51
REMARK 500 1 SER A 81 -57.71 81.62
REMARK 500 1 GLU A 82 -32.64 105.08
REMARK 500 3 ASP A 20 107.61 -54.67
REMARK 500 3 ASN A 42 64.41 -150.36
REMARK 500 3 ASP A 93 87.86 -65.03
REMARK 500 3 ASP A 129 106.96 -55.06
REMARK 500 5 ASN A 42 69.15 -159.75
REMARK 500 5 THR A 79 35.05 -88.20
REMARK 500 5 ASP A 80 -47.99 -152.85
REMARK 500 5 ASP A 131 -103.20 -99.84
REMARK 500 6 ASP A 2 -143.62 -102.72
REMARK 500 6 SER A 81 101.83 -4.17
REMARK 500 6 ASP A 95 -84.96 -80.07
REMARK 500 6 THR A 146 -78.95 -56.67
REMARK 500 7 ASP A 64 -155.60 -89.43
REMARK 500 7 THR A 79 51.41 -91.90
REMARK 500 7 ASP A 80 -42.79 -150.16
REMARK 500 8 SER A 81 -139.41 53.58
REMARK 500 8 ILE A 130 -70.84 -104.79
REMARK 500 8 ASP A 131 23.90 -74.00
REMARK 500 8 THR A 146 -71.12 -65.84
REMARK 500 8 ALA A 147 134.17 79.62
REMARK 500 9 ASP A 80 -66.34 -175.70
REMARK 500 9 ASN A 137 -165.70 -104.83
REMARK 500 10 ASP A 20 107.86 -56.98
REMARK 500 10 ASN A 42 57.87 -142.86
REMARK 500 10 SER A 81 -162.42 55.58
REMARK 500 10 ILE A 85 -56.92 -127.78
REMARK 500 10 ALA A 128 -73.98 -67.12
REMARK 500 10 ILE A 130 -63.38 -102.16
REMARK 500 11 ASP A 56 95.39 -62.96
REMARK 500 11 MET A 76 -58.10 63.39
REMARK 500 11 ASP A 78 -131.84 -111.70
REMARK 500 11 THR A 79 83.88 -69.77
REMARK 500 11 ASP A 80 -40.30 -163.85
REMARK 500 11 THR A 146 -71.10 -55.03
REMARK 500 12 LYS A 21 -71.38 -57.86
REMARK 500 12 ASP A 56 93.67 -68.54
REMARK 500 12 THR A 79 49.43 -88.78
REMARK 500 12 ASP A 80 83.90 -150.02
REMARK 500 12 SER A 81 -154.84 58.01
REMARK 500 12 ILE A 130 -67.16 -90.28
REMARK 500 13 MET A 76 63.51 -103.82
REMARK 500 13 ALA A 147 -67.20 -21.03
REMARK 500 14 THR A 28 -169.77 -102.22
REMARK 500 14 ASP A 56 93.67 -69.46
REMARK 500
REMARK 500 THIS ENTRY HAS 542 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 32 GLY A 33 2 144.35
REMARK 500 SER A 81 GLU A 82 2 -146.88
REMARK 500 SER A 81 GLU A 82 4 -140.39
REMARK 500 ALA A 128 ASP A 129 10 -144.87
REMARK 500 ASN A 42 PRO A 43 17 -148.91
REMARK 500 SER A 81 GLU A 82 20 -145.01
REMARK 500 ALA A 128 ASP A 129 27 -143.35
REMARK 500 GLN A 135 VAL A 136 31 -148.88
REMARK 500 ASN A 42 PRO A 43 33 141.69
REMARK 500 ASP A 131 GLY A 132 34 143.45
REMARK 500 ASN A 42 PRO A 43 44 147.42
REMARK 500 PRO A 43 THR A 44 50 149.40
REMARK 500 SER A 81 GLU A 82 54 -149.83
REMARK 500 ASP A 78 THR A 79 58 -145.66
REMARK 500 ASP A 131 GLY A 132 58 146.44
REMARK 500 SER A 81 GLU A 82 65 -146.36
REMARK 500 GLY A 132 ASP A 133 67 -147.52
REMARK 500 SER A 81 GLU A 82 68 148.28
REMARK 500 GLU A 120 VAL A 121 71 146.27
REMARK 500 MET A 76 LYS A 77 76 149.00
REMARK 500 MET A 109 THR A 110 79 149.86
REMARK 500 PRO A 43 THR A 44 80 149.64
REMARK 500 ASN A 42 PRO A 43 106 149.58
REMARK 500 ALA A 147 LYS A 148 116 143.36
REMARK 500 ALA A 128 ASP A 129 117 -149.34
REMARK 500 SER A 81 GLU A 82 119 -141.64
REMARK 500 ASN A 42 PRO A 43 122 149.63
REMARK 500 GLU A 82 GLU A 83 126 -148.35
REMARK 500 THR A 146 ALA A 147 129 -145.12
REMARK 500 ASP A 131 GLY A 132 158 147.84
REMARK 500 ASP A 80 SER A 81 159 -142.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 PHE A 12 0.08 SIDE CHAIN
REMARK 500 1 ARG A 106 0.10 SIDE CHAIN
REMARK 500 1 ARG A 126 0.10 SIDE CHAIN
REMARK 500 3 PHE A 19 0.10 SIDE CHAIN
REMARK 500 3 TYR A 99 0.07 SIDE CHAIN
REMARK 500 3 ARG A 106 0.09 SIDE CHAIN
REMARK 500 4 ARG A 106 0.10 SIDE CHAIN
REMARK 500 4 TYR A 138 0.17 SIDE CHAIN
REMARK 500 6 PHE A 68 0.08 SIDE CHAIN
REMARK 500 6 ARG A 86 0.08 SIDE CHAIN
REMARK 500 7 ARG A 86 0.10 SIDE CHAIN
REMARK 500 7 TYR A 138 0.13 SIDE CHAIN
REMARK 500 8 PHE A 16 0.09 SIDE CHAIN
REMARK 500 8 ARG A 74 0.10 SIDE CHAIN
REMARK 500 8 PHE A 89 0.07 SIDE CHAIN
REMARK 500 8 ARG A 106 0.09 SIDE CHAIN
REMARK 500 9 ARG A 86 0.11 SIDE CHAIN
REMARK 500 9 ARG A 126 0.14 SIDE CHAIN
REMARK 500 9 TYR A 138 0.08 SIDE CHAIN
REMARK 500 10 PHE A 19 0.07 SIDE CHAIN
REMARK 500 10 PHE A 68 0.11 SIDE CHAIN
REMARK 500 10 PHE A 92 0.07 SIDE CHAIN
REMARK 500 10 ARG A 126 0.13 SIDE CHAIN
REMARK 500 10 TYR A 138 0.07 SIDE CHAIN
REMARK 500 11 ARG A 37 0.09 SIDE CHAIN
REMARK 500 11 TYR A 99 0.12 SIDE CHAIN
REMARK 500 11 ARG A 106 0.18 SIDE CHAIN
REMARK 500 11 TYR A 138 0.07 SIDE CHAIN
REMARK 500 12 ARG A 74 0.09 SIDE CHAIN
REMARK 500 12 ARG A 86 0.12 SIDE CHAIN
REMARK 500 12 ARG A 90 0.15 SIDE CHAIN
REMARK 500 12 TYR A 99 0.09 SIDE CHAIN
REMARK 500 12 ARG A 106 0.09 SIDE CHAIN
REMARK 500 12 PHE A 141 0.11 SIDE CHAIN
REMARK 500 13 PHE A 16 0.08 SIDE CHAIN
REMARK 500 13 ARG A 37 0.10 SIDE CHAIN
REMARK 500 13 TYR A 99 0.09 SIDE CHAIN
REMARK 500 14 ARG A 106 0.09 SIDE CHAIN
REMARK 500 15 PHE A 12 0.07 SIDE CHAIN
REMARK 500 15 ARG A 126 0.09 SIDE CHAIN
REMARK 500 15 TYR A 138 0.08 SIDE CHAIN
REMARK 500 16 ARG A 86 0.12 SIDE CHAIN
REMARK 500 16 ARG A 106 0.13 SIDE CHAIN
REMARK 500 17 ARG A 86 0.09 SIDE CHAIN
REMARK 500 17 ARG A 90 0.08 SIDE CHAIN
REMARK 500 17 TYR A 138 0.10 SIDE CHAIN
REMARK 500 18 PHE A 19 0.12 SIDE CHAIN
REMARK 500 18 ARG A 37 0.10 SIDE CHAIN
REMARK 500 18 ARG A 126 0.07 SIDE CHAIN
REMARK 500 18 PHE A 141 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 454 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 6 ALA A 15 -10.57
REMARK 500 16 ASP A 50 -10.69
REMARK 500 23 LYS A 75 -10.72
REMARK 500 29 ILE A 125 -10.37
REMARK 500 35 ALA A 102 -11.74
REMARK 500 42 GLU A 127 -10.43
REMARK 500 44 LYS A 75 -10.84
REMARK 500 45 GLU A 84 -10.57
REMARK 500 46 ILE A 100 -10.12
REMARK 500 50 MET A 124 -10.08
REMARK 500 56 VAL A 108 -13.26
REMARK 500 59 MET A 36 -10.19
REMARK 500 67 GLY A 132 10.49
REMARK 500 84 GLY A 33 10.74
REMARK 500 84 VAL A 136 -10.89
REMARK 500 19 TYR A 99 -11.56
REMARK 500 26 LEU A 32 -11.48
REMARK 500 50 MET A 144 -10.11
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 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 20 OD2 50.3
REMARK 620 3 ASP A 22 OD2 93.5 143.8
REMARK 620 4 ASP A 24 OD1 71.4 75.4 94.5
REMARK 620 5 THR A 26 O 110.2 61.4 152.4 80.4
REMARK 620 6 GLU A 31 OE1 115.9 99.5 97.1 165.7 85.4
REMARK 620 7 GLU A 31 OE2 71.8 90.7 75.4 141.0 124.7 51.0
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 56 OD1
REMARK 620 2 ASP A 56 OD2 52.0
REMARK 620 3 ASP A 58 OD2 79.5 123.2
REMARK 620 4 ASN A 60 OD1 92.6 70.7 86.1
REMARK 620 5 THR A 62 O 123.7 72.2 149.3 74.0
REMARK 620 6 ASP A 64 OD1 157.7 150.2 82.0 98.4 78.2
REMARK 620 7 GLU A 67 OE1 98.1 97.4 119.2 153.9 80.2 80.3
REMARK 620 8 GLU A 67 OE2 68.2 107.0 73.3 153.7 131.2 94.7 51.1
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 153 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 85.9
REMARK 620 3 TYR A 99 O 70.7 149.2
REMARK 620 4 GLU A 104 OE1 109.8 121.6 85.9
REMARK 620 5 GLU A 104 OE2 77.6 79.6 113.0 52.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 154 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 84.4
REMARK 620 3 ASP A 133 OD1 78.8 82.0
REMARK 620 4 GLN A 135 O 98.8 154.8 74.2
REMARK 620 5 GLU A 140 OE1 108.5 124.5 152.5 78.4
REMARK 620 6 GLU A 140 OE2 79.3 78.4 151.8 126.8 53.4
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 CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 154
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J7O RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CALCIUM-CALMODULIN N-TERMINAL DOMAIN
REMARK 900 RELATED ID: 1J7P RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CALCIUM-CALMODULIN C-TERMINAL DOMAIN
REMARK 900 RELATED ID: 2K0F RELATED DB: PDB
DBREF 2K0E A 1 148 UNP P62158 CALM_HUMAN 2 149
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 MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET 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 MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET 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 MET MET THR ALA LYS
HET CA A 151 1
HET CA A 152 1
HET CA A 153 1
HET CA A 154 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 4(CA 2+)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 ASP A 64 THR A 79 1 16
HELIX 5 5 GLU A 82 ASP A 93 1 12
HELIX 6 6 ALA A 102 GLY A 113 1 12
HELIX 7 7 THR A 117 GLU A 127 1 11
HELIX 8 8 ASN A 137 LYS A 148 1 12
SHEET 1 A 2 ILE A 100 SER A 101 0
SHEET 2 A 2 GLN A 135 VAL A 136 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 151 1555 1555 2.66
LINK OD2 ASP A 20 CA CA A 151 1555 1555 2.46
LINK OD2 ASP A 22 CA CA A 151 1555 1555 2.56
LINK OD1 ASP A 24 CA CA A 151 1555 1555 2.35
LINK O THR A 26 CA CA A 151 1555 1555 2.49
LINK OE1 GLU A 31 CA CA A 151 1555 1555 2.60
LINK OE2 GLU A 31 CA CA A 151 1555 1555 2.58
LINK OD1 ASP A 56 CA CA A 152 1555 1555 2.52
LINK OD2 ASP A 56 CA CA A 152 1555 1555 2.53
LINK OD2 ASP A 58 CA CA A 152 1555 1555 2.40
LINK OD1 ASN A 60 CA CA A 152 1555 1555 2.57
LINK O THR A 62 CA CA A 152 1555 1555 2.48
LINK OD1 ASP A 64 CA CA A 152 1555 1555 2.47
LINK OE1 GLU A 67 CA CA A 152 1555 1555 2.42
LINK OE2 GLU A 67 CA CA A 152 1555 1555 2.64
LINK OD1 ASP A 93 CA CA A 153 1555 1555 2.37
LINK OD1 ASP A 95 CA CA A 153 1555 1555 2.41
LINK O TYR A 99 CA CA A 153 1555 1555 2.58
LINK OE1 GLU A 104 CA CA A 153 1555 1555 2.45
LINK OE2 GLU A 104 CA CA A 153 1555 1555 2.54
LINK OD1 ASP A 129 CA CA A 154 1555 1555 2.44
LINK OD1 ASP A 131 CA CA A 154 1555 1555 2.47
LINK OD1 ASP A 133 CA CA A 154 1555 1555 2.33
LINK O GLN A 135 CA CA A 154 1555 1555 2.67
LINK OE1 GLU A 140 CA CA A 154 1555 1555 2.36
LINK OE2 GLU A 140 CA CA A 154 1555 1555 2.39
SITE 1 AC1 3 ASP A 20 LYS A 21 ASP A 22
SITE 1 AC2 4 ILE A 52 ASP A 56 ASP A 58 ILE A 63
SITE 1 AC3 6 ASP A 93 LYS A 94 ASP A 95 TYR A 99
SITE 2 AC3 6 SER A 101 GLU A 104
SITE 1 AC4 3 TYR A 99 ILE A 125 ASP A 129
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END