HEADER METAL BINDING PROTEIN/METAL TRANSPORT 29-OCT-12 2M0K
TITLE 3D STRUCTURE OF CALMODULIN AND CALMODULIN BINDING DOMAIN OF RAT
TITLE 2 OLFACTORY CYCLIC NUCLEOTIDE-GATED ION CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PEPTIDE FROM CYCLIC NUCLEOTIDE-GATED OLFACTORY CHANNEL;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 60-87;
COMPND 10 SYNONYM: CYCLIC NUCLEOTIDE-GATED CATION CHANNEL 2, CYCLIC NUCLEOTIDE-
COMPND 11 GATED CHANNEL ALPHA-2, CNG CHANNEL ALPHA-2, CNG-2, CNG2, CYCLIC
COMPND 12 NUCLEOTIDE-GATED OLFACTORY CHANNEL SUBUNIT OCNC1;
COMPND 13 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;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET29C;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: RAT;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 GENE: CNGA2, CNCG2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR: PET29C
KEYWDS CALMODULIN, CYCLIC OLFACTORY NUCLEOTIDE-GATED ION CHANNEL, METAL
KEYWDS 2 BINDING PROTEIN-METAL TRANSPORT COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.DELI,C.CHYAN
REVDAT 2 11-FEB-15 2M0K 1 JRNL REMARK
REVDAT 1 30-OCT-13 2M0K 0
JRNL AUTH D.IRENE,J.W.HUANG,T.Y.CHUNG,F.Y.LI,J.T.TZEN,T.H.LIN,
JRNL AUTH 2 C.L.CHYAN
JRNL TITL BINDING ORIENTATION AND SPECIFICITY OF CALMODULIN TO RAT
JRNL TITL 2 OLFACTORY CYCLIC NUCLEOTIDE-GATED ION CHANNEL.
JRNL REF J.BIOMOL.STRUCT.DYN. V. 31 414 2013
JRNL REFN ISSN 0739-1102
JRNL PMID 22877078
JRNL DOI 10.1080/07391102.2012.703069
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.IRENE,F.H.SUNG,J.W.HUANG,T.H.LIN,Y.C.CHEN,C.L.CHYAN
REMARK 1 TITL RESONANCE ASSIGNMENTS AND SECONDARY STRUCTURE OF CALMODULIN
REMARK 1 TITL 2 IN COMPLEX WITH ITS TARGET SEQUENCE IN RAT OLFACTORY CYCLIC
REMARK 1 TITL 3 NUCLEOTIDE-GATED ION CHANNEL.
REMARK 1 REF BIOMOL.NMR ASSIGN. V. 8 97 2014
REMARK 1 REFN ISSN 1874-2718
REMARK 1 PMID 23315338
REMARK 1 DOI 10.1007/S12104-013-9461-Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2M0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB103056.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1 MM [U-99% 13C; U-99% 15N] CAM-
REMARK 210 OLFP-1, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-1H TOCSY; 2D DQF-COSY; 2D
REMARK 210 1H-1H NOESY; 3D HNCA; 3D HN(CO)
REMARK 210 CA; 3D HNCO; 3D HN(CA)CO; 3D
REMARK 210 HNCACB; 3D C(CO)NH; 3D HBHA(CO)
REMARK 210 NH; 3D H(CCO)NH; 3D HCCH-TOCSY;
REMARK 210 3D HCCH-COSY; 3D 1H-15N TOCSY; 3D
REMARK 210 1H-13C15N SIMULTANEOUS
REMARK 210 COEVOLUTION NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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: DIMERIC
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 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 2 85.20 -157.06
REMARK 500 1 GLN A 3 -179.92 -177.54
REMARK 500 1 PRO A 43 -169.98 -68.71
REMARK 500 1 MET A 76 89.73 61.84
REMARK 500 1 TYR A 99 116.34 -166.35
REMARK 500 1 TYR A 138 -72.41 -56.82
REMARK 500 1 THR A 146 -51.01 -135.77
REMARK 500 1 PRO B 61 -176.76 -52.02
REMARK 500 1 ARG B 63 30.84 -150.34
REMARK 500 1 ASN B 83 -65.28 -148.23
REMARK 500 1 LYS B 84 66.74 -69.90
REMARK 500 2 ASP A 2 77.60 -66.43
REMARK 500 2 GLN A 3 -175.64 -177.39
REMARK 500 2 MET A 76 93.74 60.71
REMARK 500 2 TYR A 99 116.36 -165.67
REMARK 500 2 TYR A 138 -73.41 -57.06
REMARK 500 2 THR A 146 -51.17 -135.46
REMARK 500 2 PRO B 61 173.89 -52.12
REMARK 500 2 ARG B 63 79.12 -176.83
REMARK 500 2 ASN B 83 -65.87 -145.91
REMARK 500 2 LYS B 84 65.39 -69.62
REMARK 500 3 ASP A 2 78.76 -105.97
REMARK 500 3 GLN A 3 -178.25 -176.98
REMARK 500 3 MET A 76 76.44 57.71
REMARK 500 3 TYR A 99 116.94 -162.99
REMARK 500 3 ASN A 137 -164.73 -102.20
REMARK 500 3 TYR A 138 -73.90 -63.12
REMARK 500 3 THR A 146 -48.83 -141.64
REMARK 500 3 ARG B 63 39.26 -155.20
REMARK 500 3 ASN B 83 -65.40 -148.51
REMARK 500 3 LYS B 84 66.12 -69.88
REMARK 500 4 GLN A 3 -178.59 -173.82
REMARK 500 4 PRO A 43 -169.93 -68.43
REMARK 500 4 MET A 76 73.78 59.92
REMARK 500 4 THR A 79 146.84 -177.23
REMARK 500 4 TYR A 99 116.86 -162.65
REMARK 500 4 ASN A 137 -166.32 -105.31
REMARK 500 4 TYR A 138 -73.90 -59.09
REMARK 500 4 THR A 146 -51.57 -147.84
REMARK 500 4 ALA A 147 74.99 -69.06
REMARK 500 4 PRO B 61 -168.01 -69.79
REMARK 500 4 ARG B 63 38.24 -155.52
REMARK 500 4 ASN B 83 -64.47 -148.50
REMARK 500 5 GLN A 3 -179.59 -177.85
REMARK 500 5 MET A 76 95.10 61.45
REMARK 500 5 TYR A 99 116.97 -162.47
REMARK 500 5 TYR A 138 -73.56 -60.12
REMARK 500 5 THR A 146 -50.01 -146.55
REMARK 500 5 PRO B 61 -168.04 -69.96
REMARK 500 5 ARG B 63 37.69 -155.21
REMARK 500
REMARK 500 THIS ENTRY HAS 232 RAMACHANDRAN OUTLIERS.
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 1 CA A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 97 OD1
REMARK 620 2 ASP A 93 OD1 102.5
REMARK 620 3 ASP A 95 OD1 135.8 82.0
REMARK 620 4 ASP A 95 OD2 87.2 108.9 51.0
REMARK 620 5 ASP A 93 OD2 58.8 50.9 96.3 81.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 60 OD1
REMARK 620 2 ASP A 56 OD2 58.5
REMARK 620 3 ASP A 58 OD1 71.7 65.6
REMARK 620 4 ASP A 58 OD2 120.2 103.9 50.9
REMARK 620 5 THR A 62 O 72.8 59.1 123.9 151.5
REMARK 620 6 ASP A 56 OD1 108.1 50.8 89.6 88.8 62.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 22 OD2
REMARK 620 2 ASP A 20 OD2 71.8
REMARK 620 3 ASP A 24 OD2 66.7 102.3
REMARK 620 4 THR A 26 O 134.9 78.0 88.6
REMARK 620 5 ASP A 22 OD1 50.9 58.5 117.4 132.2
REMARK 620 6 ASP A 20 OD1 121.0 51.0 132.4 51.3 84.0
REMARK 620 7 ASP A 24 OD1 75.6 57.1 50.7 59.9 104.8 84.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CA A 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 133 OD2
REMARK 620 2 ASP A 131 OD2 60.9
REMARK 620 3 ASP A 131 OD1 65.9 50.6
REMARK 620 4 ASP A 129 OD1 123.5 85.0 57.7
REMARK 620 5 ASP A 129 OD2 104.8 116.9 67.1 50.4
REMARK 620 6 GLU A 140 OE2 109.3 54.3 91.2 76.6 126.7
REMARK 620 7 GLN A 135 O 128.8 165.2 119.7 80.3 52.7 120.8
REMARK 620 8 ASP A 133 OD1 51.0 107.3 79.3 111.6 65.4 160.2 78.8
REMARK 620 9 GLU A 140 OE1 155.2 95.1 105.1 54.7 91.4 46.3 76.0 153.0
REMARK 620 N 1 2 3 4 5 6 7 8
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17771 RELATED DB: BMRB
REMARK 900 RELATED ID: 2M0J RELATED DB: PDB
DBREF 2M0K A 1 148 UNP P62158 CALM_HUMAN 2 149
DBREF 2M0K B 60 87 UNP Q00195 CNGA2_RAT 60 87
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
SEQRES 1 B 28 THR PRO ARG ARG GLY ARG GLY GLY PHE GLN ARG ILE VAL
SEQRES 2 B 28 ARG LEU VAL GLY VAL ILE ARG ASP TRP ALA ASN LYS ASN
SEQRES 3 B 28 PHE ARG
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET CA A 204 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 29 GLN A 41 1 13
HELIX 3 3 THR A 44 GLU A 54 1 11
HELIX 4 4 ASP A 64 ARG A 74 1 11
HELIX 5 5 SER A 81 ASP A 93 1 13
HELIX 6 6 SER A 101 GLY A 113 1 13
HELIX 7 7 THR A 117 GLU A 127 1 11
HELIX 8 8 ASN A 137 THR A 146 1 10
HELIX 9 9 ARG B 65 ASN B 83 1 19
SHEET 1 A 2 ILE A 27 THR A 28 0
SHEET 2 A 2 THR A 62 ILE A 63 -1 O ILE A 63 N ILE A 27
LINK OD1 ASN A 97 CA CA A 203 1555 1555 2.51
LINK OD1 ASN A 60 CA CA A 202 1555 1555 2.52
LINK OD2 ASP A 22 CA CA A 201 1555 1555 2.57
LINK OD2 ASP A 56 CA CA A 202 1555 1555 2.57
LINK OD2 ASP A 133 CA CA A 204 1555 1555 2.55
LINK OD1 ASP A 93 CA CA A 203 1555 1555 2.55
LINK OD1 ASP A 95 CA CA A 203 1555 1555 2.55
LINK OD2 ASP A 20 CA CA A 201 1555 1555 2.55
LINK OD2 ASP A 95 CA CA A 203 1555 1555 2.55
LINK OD1 ASP A 58 CA CA A 202 1555 1555 2.55
LINK OD2 ASP A 58 CA CA A 202 1555 1555 2.55
LINK OD2 ASP A 93 CA CA A 203 1555 1555 2.55
LINK OD2 ASP A 24 CA CA A 201 1555 1555 2.56
LINK OD2 ASP A 131 CA CA A 204 1555 1555 2.56
LINK OD1 ASP A 131 CA CA A 204 1555 1555 2.56
LINK OD1 ASP A 129 CA CA A 204 1555 1555 2.56
LINK OD2 ASP A 129 CA CA A 204 1555 1555 2.58
LINK OE2 GLU A 140 CA CA A 204 1555 1555 2.82
LINK O GLN A 135 CA CA A 204 1555 1555 2.81
LINK O THR A 62 CA CA A 202 1555 1555 3.03
LINK O THR A 26 CA CA A 201 1555 1555 3.03
LINK OD1 ASP A 22 CA CA A 201 1555 1555 2.54
LINK OD1 ASP A 56 CA CA A 202 1555 1555 2.54
LINK OD1 ASP A 133 CA CA A 204 1555 1555 2.55
LINK OD1 ASP A 20 CA CA A 201 1555 1555 2.55
LINK OD1 ASP A 24 CA CA A 201 1555 1555 2.57
LINK OE1 GLU A 140 CA CA A 204 1555 1555 2.77
SITE 1 AC1 4 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 1 AC2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 5 ASP A 64
SITE 1 AC3 4 ASP A 93 ASP A 95 ASN A 97 GLU A 104
SITE 1 AC4 6 TYR A 99 ASP A 129 ASP A 131 ASP A 133
SITE 2 AC4 6 GLN A 135 GLU A 140
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