HEADER SIGNALING PROTEIN 19-OCT-16 5TP5
TITLE SOLUTION STRUCTURE OF THE CALCIUM DEFICIENT MUTANT CALMODULIN CAM1234
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 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: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALCIUM DEFICIENT, CALMODULIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.PIAZZA,T.DIECKMANN,J.G.GUILLEMETTE
REVDAT 3 14-JUN-23 5TP5 1 REMARK
REVDAT 2 08-JAN-20 5TP5 1 REMARK
REVDAT 1 27-SEP-17 5TP5 0
JRNL AUTH M.PIAZZA,V.TAIAKINA,T.DIECKMANN,J.G.GUILLEMETTE
JRNL TITL STRUCTURAL CONSEQUENCES OF CALMODULIN EF HAND MUTATIONS.
JRNL REF BIOCHEMISTRY V. 56 944 2017
JRNL REFN ISSN 1520-4995
JRNL PMID 28121131
JRNL DOI 10.1021/ACS.BIOCHEM.6B01296
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224581.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 150
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 100 MM POTASSIUM CHLORIDE, 1 MM
REMARK 210 [U-99% 13C; U-99% 15N] CAM1234,
REMARK 210 0.2 MM SODIUM AZIDE, 0.2 MM EDTA,
REMARK 210 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCA; 3D
REMARK 210 CBCA(CO)NH; 3D HCCH-TOCSY; 3D 1H-
REMARK 210 15N NOESY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS, CARA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 O ILE A 52 H ALA A 56 1.51
REMARK 500 O GLY A 33 H ARG A 37 1.52
REMARK 500 H ILE A 27 O ILE A 63 1.55
REMARK 500 HA ARG A 37 O GLN A 41 1.57
REMARK 500 O ARG A 106 HG1 THR A 110 1.60
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 58 -11.94 167.97
REMARK 500 1 PHE A 89 -17.83 -43.27
REMARK 500 1 ALA A 93 68.26 -100.20
REMARK 500 1 LYS A 94 30.59 -178.41
REMARK 500 1 ASP A 95 21.04 -79.85
REMARK 500 1 ALA A 129 -56.20 80.15
REMARK 500 1 ILE A 130 -42.50 70.22
REMARK 500 2 ASP A 2 126.95 63.07
REMARK 500 2 PHE A 89 -18.03 -43.45
REMARK 500 2 ILE A 100 102.49 81.54
REMARK 500 2 ALA A 129 -52.74 79.30
REMARK 500 2 ILE A 130 -40.55 69.25
REMARK 500 3 GLN A 3 152.64 62.63
REMARK 500 3 ALA A 20 -163.02 -62.58
REMARK 500 3 ASP A 58 -11.09 168.19
REMARK 500 3 LYS A 94 49.53 80.45
REMARK 500 3 ASN A 97 -30.00 65.11
REMARK 500 3 ALA A 129 -60.05 77.87
REMARK 500 3 ILE A 130 -34.07 68.22
REMARK 500 4 ASP A 58 -11.66 167.51
REMARK 500 4 PHE A 89 -18.06 -48.26
REMARK 500 4 ALA A 93 75.53 -101.29
REMARK 500 4 ILE A 100 136.41 178.20
REMARK 500 4 ALA A 129 -59.78 76.31
REMARK 500 4 ILE A 130 -31.48 70.32
REMARK 500 4 GLN A 135 -163.39 -117.70
REMARK 500 5 ALA A 20 84.67 -66.62
REMARK 500 5 ASP A 58 -7.82 130.11
REMARK 500 5 ASN A 60 -44.09 71.84
REMARK 500 5 PHE A 89 -17.78 -43.10
REMARK 500 5 LYS A 94 42.48 -176.59
REMARK 500 5 ASN A 97 -24.20 65.59
REMARK 500 5 ALA A 129 -48.99 80.45
REMARK 500 5 ILE A 130 -163.17 50.11
REMARK 500 5 ASP A 131 164.66 65.15
REMARK 500 6 ALA A 20 91.54 -68.02
REMARK 500 6 ASP A 58 -13.25 163.31
REMARK 500 6 ASP A 80 40.23 -82.72
REMARK 500 6 LYS A 94 9.84 -175.45
REMARK 500 6 ILE A 100 80.44 97.30
REMARK 500 6 LYS A 115 142.73 54.01
REMARK 500 6 ALA A 129 -49.99 81.65
REMARK 500 6 ILE A 130 -42.08 73.17
REMARK 500 6 GLN A 135 -169.38 -120.00
REMARK 500 7 ASP A 58 -13.33 162.98
REMARK 500 7 PHE A 89 -18.23 -49.07
REMARK 500 7 ASN A 97 -28.75 64.54
REMARK 500 7 LYS A 115 -4.26 54.36
REMARK 500 7 ALA A 129 -58.89 79.84
REMARK 500 7 ILE A 130 -37.64 69.62
REMARK 500
REMARK 500 THIS ENTRY HAS 133 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 30195 RELATED DB: BMRB
REMARK 900 SOLUTION STRUCTURE OF THE CALCIUM DEFICIENT MUTANT CALMODULIN
REMARK 900 CAM1234
REMARK 900 RELATED ID: 5TP6 RELATED DB: PDB
DBREF 5TP5 A 1 148 UNP P62158 CALM_HUMAN 2 149
SEQADV 5TP5 ALA A 20 UNP P62158 ASP 21 ENGINEERED MUTATION
SEQADV 5TP5 ALA A 56 UNP P62158 ASP 57 ENGINEERED MUTATION
SEQADV 5TP5 ALA A 93 UNP P62158 ASP 94 ENGINEERED MUTATION
SEQADV 5TP5 ALA A 129 UNP P62158 ASP 130 ENGINEERED MUTATION
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 ALA 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 ALA 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 ALA 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 ALA 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
HELIX 1 AA1 GLN A 8 SER A 17 1 10
HELIX 2 AA2 LEU A 32 ARG A 37 1 6
HELIX 3 AA3 ALA A 46 MET A 51 1 6
HELIX 4 AA4 ILE A 52 VAL A 55 5 4
HELIX 5 AA5 PHE A 65 MET A 71 1 7
HELIX 6 AA6 MET A 71 MET A 76 1 6
HELIX 7 AA7 SER A 81 ALA A 93 1 13
HELIX 8 AA8 SER A 101 GLY A 113 1 13
HELIX 9 AA9 THR A 117 ALA A 129 1 13
HELIX 10 AB1 ASN A 137 VAL A 142 1 6
HELIX 11 AB2 VAL A 142 LYS A 148 1 7
SHEET 1 AA1 2 THR A 26 ILE A 27 0
SHEET 2 AA1 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
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