Header list of 1kkd.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 07-DEC-01 1KKD TITLE SOLUTION STRUCTURE OF THE CALMODULIN BINDING DOMAIN (CAMBD) OF SMALL TITLE 2 CONDUCTANCE CA2+-ACTIVATED POTASSIUM CHANNELS (SK2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL COMPND 3 PROTEIN 2; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: CYTOPLASMIC CALMODULIN BINDING DOMAIN (CAMBD); COMPND 6 SYNONYM: CALCIUM-ACTIVATED POTASSIUM CHANNEL RSK2; SK2; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: SK2 (KCNN2); SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23B KEYWDS SMALL-CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL, CALMODULIN KEYWDS 2 BINDING DOMAIN (CAMBD), CHANNEL GATING, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 23 AUTHOR R.WISSMANN,W.BILDL,H.NEUMANN,A.F.RIVARD,N.KLOECKER,D.WEITZ,U.SCHULTE, AUTHOR 2 J.P.ADELMAN,D.BENTROP,B.FAKLER REVDAT 5 23-FEB-22 1KKD 1 REMARK SEQADV REVDAT 4 24-FEB-09 1KKD 1 VERSN REVDAT 3 01-APR-03 1KKD 1 JRNL REVDAT 2 08-FEB-02 1KKD 1 JRNL REVDAT 1 14-DEC-01 1KKD 0 JRNL AUTH R.WISSMANN,W.BILDL,H.NEUMANN,A.F.RIVARD,N.KLOCKER,D.WEITZ, JRNL AUTH 2 U.SCHULTE,J.P.ADELMAN,D.BENTROP,B.FAKLER JRNL TITL A HELICAL REGION IN THE C TERMINUS OF SMALL-CONDUCTANCE JRNL TITL 2 CA2+-ACTIVATED K+ CHANNELS CONTROLS ASSEMBLY WITH JRNL TITL 3 APO-CALMODULIN. JRNL REF J.BIOL.CHEM. V. 277 4558 2002 JRNL REFN ISSN 0021-9258 JRNL PMID 11723128 JRNL DOI 10.1074/JBC.M109240200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.E.KEEN,R.KHAWALED,D.L.FARRENS,T.NEELANDS,A.RIVARD, REMARK 1 AUTH 2 C.T.BOND,A.JANOWSKY,B.FAKLER,J.P.ADELMAN,J.MAYLIE REMARK 1 TITL DOMAINS RESPONSIBLE FOR CONSTITUTIVE AND CA2+-DEPENDENT REMARK 1 TITL 2 INTERACTIONS BETWEEN CALMODULIN AND SMALL CONDUCTANCE CA2+- REMARK 1 TITL 3 ACTIVATED POTASSIUM CHANNELS REMARK 1 REF J.NEUROSCI. V. 19 8830 1999 REMARK 1 REFN ISSN 0270-6474 REMARK 1 REFERENCE 2 REMARK 1 AUTH X.-M.XIA,B.FAKLER,A.RIVARD,G.WAYMAN,T.JOHNSON-PAIS,J.E.KEEN, REMARK 1 AUTH 2 T.ISHII,B.HIRSCHBERG,C.T.BOND,S.LUTSENKO,J.MAYLIE, REMARK 1 AUTH 3 J.P.ADELMAN REMARK 1 TITL MECHANISM OF CALCIUM GATING IN SMALL-CONDUCTANCE REMARK 1 TITL 2 CALCIUM-ACTIVATED POTASSIUM CHANNELS REMARK 1 REF NATURE V. 395 503 1998 REMARK 1 REFN ISSN 0028-0836 REMARK 1 DOI 10.1038/26758 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.A.SCHUMACHER,A.F.RIVARD,H.P.BAECHINGER,J.P.ADELMAN REMARK 1 TITL STRUCTURE OF THE GATING DOMAIN OF A CA2+-ACTIVATED K+ REMARK 1 TITL 2 CHANNEL COMPLEXED WITH CA2+/CALMODULIN REMARK 1 REF NATURE V. 410 1120 2001 REMARK 1 REFN ISSN 0028-0836 REMARK 1 DOI 10.1038/35074145 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.5 REMARK 3 AUTHORS : BRUKER (XWINNMR), MUMENTHALER, GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SEE TABLE 1 IN THE PRIMARY CITATION FOR REMARK 3 STRUCTURAL STATISTICS REMARK 4 REMARK 4 1KKD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-01. REMARK 100 THE DEPOSITION ID IS D_1000015045. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298 REMARK 210 PH : 3.5; 3.5; 3.5; 3.5 REMARK 210 IONIC STRENGTH : 250 MM; 250 MM; 250 MM; 250 MM REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM U-15N,13C CAMBD (RESIDUES REMARK 210 396-487 OF RAT SK2); 250 MM NACL, REMARK 210 0.05 % NA-AZIDE; 1.2 MM U-15N REMARK 210 CAMBD (RESIDUES 396-487 OF RAT REMARK 210 SK2); 250 MM NACL, 0.05 % NA- REMARK 210 AZIDE; 1 MM CAMBD (RESIDUES 396- REMARK 210 487 OF RAT SK2); 250 MM NACL, REMARK 210 0.05 % NA-AZIDE; 1 MM CAMBD REMARK 210 (RESIDUES 396-487 OF RAT SK2); REMARK 210 250 MM NACL, 0.05 % NA-AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; 2D REMARK 210 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 2.7.5, XEASY 1.3.13, REMARK 210 DYANA 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,TARGET REMARK 210 FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 22 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-23 REMARK 465 RES C SSSEQI REMARK 465 MET A -1 REMARK 465 GLY A 0 REMARK 465 LEU A 93 REMARK 465 GLU A 94 REMARK 465 HIS A 95 REMARK 465 HIS A 96 REMARK 465 HIS A 97 REMARK 465 HIS A 98 REMARK 465 HIS A 99 REMARK 465 HIS A 100 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 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 GLU A 4 -173.80 47.26 REMARK 500 1 LEU A 5 177.85 62.06 REMARK 500 1 THR A 6 58.88 37.51 REMARK 500 1 ALA A 8 126.71 66.27 REMARK 500 1 GLU A 9 13.80 -140.47 REMARK 500 1 HIS A 11 131.80 66.71 REMARK 500 1 VAL A 12 130.74 -177.92 REMARK 500 1 ASN A 14 37.64 -92.74 REMARK 500 1 PHE A 15 171.91 -52.31 REMARK 500 1 MET A 17 -54.75 76.41 REMARK 500 1 ASP A 18 105.15 178.41 REMARK 500 1 THR A 19 60.53 -111.97 REMARK 500 1 ARG A 24 -156.95 -79.48 REMARK 500 1 VAL A 25 48.74 -85.51 REMARK 500 1 LYS A 26 29.41 82.61 REMARK 500 1 ALA A 30 -83.50 62.60 REMARK 500 1 LEU A 33 -59.91 69.79 REMARK 500 1 LEU A 38 -44.71 -141.06 REMARK 500 1 TYR A 40 142.12 -34.47 REMARK 500 1 ASN A 42 -60.96 73.81 REMARK 500 1 LYS A 44 58.19 -168.45 REMARK 500 1 LEU A 45 68.66 -104.83 REMARK 500 1 ILE A 49 164.29 -44.33 REMARK 500 1 ASP A 50 112.91 64.00 REMARK 500 1 HIS A 51 -41.99 -170.15 REMARK 500 1 VAL A 54 101.86 66.12 REMARK 500 1 ARG A 55 -150.15 -129.99 REMARK 500 1 HIS A 57 104.56 -174.24 REMARK 500 1 GLN A 58 -59.32 72.33 REMARK 500 1 LYS A 60 165.01 -44.84 REMARK 500 1 ILE A 65 -109.79 -100.97 REMARK 500 1 LEU A 68 177.66 67.98 REMARK 500 1 ARG A 69 80.75 65.87 REMARK 500 1 SER A 70 80.43 -172.60 REMARK 500 1 LYS A 72 117.23 -164.87 REMARK 500 1 GLU A 74 172.99 54.19 REMARK 500 1 GLN A 75 174.43 -48.11 REMARK 500 1 ARG A 76 82.90 62.13 REMARK 500 1 ASN A 79 -39.57 -171.88 REMARK 500 1 GLN A 81 97.37 53.58 REMARK 500 1 ASN A 83 118.12 -171.46 REMARK 500 1 VAL A 86 55.34 -114.80 REMARK 500 1 LEU A 88 31.25 37.70 REMARK 500 1 ALA A 89 -69.39 -155.88 REMARK 500 2 LYS A 2 147.55 69.41 REMARK 500 2 LEU A 5 145.49 -177.14 REMARK 500 2 THR A 6 87.94 39.51 REMARK 500 2 ALA A 8 126.74 -176.56 REMARK 500 2 GLU A 9 13.89 -140.53 REMARK 500 2 VAL A 12 130.09 -175.98 REMARK 500 REMARK 500 THIS ENTRY HAS 1058 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1G4Y RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH CA2+- REMARK 900 LOADED CALMODULIN DBREF 1KKD A 1 92 UNP P70604 KCNN2_RAT 396 487 SEQADV 1KKD MET A -1 UNP P70604 CLONING ARTIFACT SEQADV 1KKD GLY A 0 UNP P70604 CLONING ARTIFACT SEQADV 1KKD LEU A 93 UNP P70604 EXPRESSION TAG SEQADV 1KKD GLU A 94 UNP P70604 EXPRESSION TAG SEQADV 1KKD HIS A 95 UNP P70604 EXPRESSION TAG SEQADV 1KKD HIS A 96 UNP P70604 EXPRESSION TAG SEQADV 1KKD HIS A 97 UNP P70604 EXPRESSION TAG SEQADV 1KKD HIS A 98 UNP P70604 EXPRESSION TAG SEQADV 1KKD HIS A 99 UNP P70604 EXPRESSION TAG SEQADV 1KKD HIS A 100 UNP P70604 EXPRESSION TAG SEQRES 1 A 102 MET GLY ARG LYS LEU GLU LEU THR LYS ALA GLU LYS HIS SEQRES 2 A 102 VAL HIS ASN PHE MET MET ASP THR GLN LEU THR LYS ARG SEQRES 3 A 102 VAL LYS ASN ALA ALA ALA ASN VAL LEU ARG GLU THR TRP SEQRES 4 A 102 LEU ILE TYR LYS ASN THR LYS LEU VAL LYS LYS ILE ASP SEQRES 5 A 102 HIS ALA LYS VAL ARG LYS HIS GLN ARG LYS PHE LEU GLN SEQRES 6 A 102 ALA ILE HIS GLN LEU ARG SER VAL LYS MET GLU GLN ARG SEQRES 7 A 102 LYS LEU ASN ASP GLN ALA ASN THR LEU VAL ASP LEU ALA SEQRES 8 A 102 LYS THR GLN LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 GLU A 35 TYR A 40 1 6 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
Complete list - b 23 2 Bytes