Header list of 1nsh.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 27-JAN-03 1NSH
TITLE SOLUTION STRUCTURE OF RABBIT APO-S100A11 (19 MODELS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALGIZZARIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100C PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 GENE: S100A11 OR S100C OR PCALG;
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
KEYWDS CALCIUM-BINDING PROTEIN, EF HAND, HELIX-LOOP-HELIX, S100, ANNEXIN,
KEYWDS 2 METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR A.C.DEMPSEY,M.P.WALSH,G.S.SHAW
REVDAT 6 23-FEB-22 1NSH 1 REMARK
REVDAT 5 09-JUN-09 1NSH 1 REVDAT
REVDAT 4 24-FEB-09 1NSH 1 VERSN
REVDAT 3 16-DEC-08 1NSH 1
REVDAT 2 14-FEB-06 1NSH 1 KEYWDS
REVDAT 1 15-JUL-03 1NSH 0
JRNL AUTH A.C.DEMPSEY,M.P.WALSH,G.S.SHAW
JRNL TITL UNMASKING THE ANNEXIN I INTERACTION FROM THE STRUCTURE OF
JRNL TITL 2 APO-S100A11
JRNL REF STRUCTURE V. 11 887 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12842051
JRNL DOI 10.1016/S0969-2126(03)00126-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.1
REMARK 3 AUTHORS : VARIAN INC. (VNMR), A.T.BRUNGER, P.D.ADAMS,
REMARK 3 G.M.CLORE, W.L.DELANO, P.GROS, R.W.GROSSE-
REMARK 3 KUNSTLEVE, J.-S.JIANG, J.KUSZEWSKI, M.NILGES,
REMARK 3 N.S.PANNU, R.J.READ, L.M.RICE, T.SIMONSON,
REMARK 3 G.L.WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED USING 2964
REMARK 3 NOE DERIVED DISTANCE RESTRAINTS: 1336 INTRARESIDUE, 658
REMARK 3 SEQUENTIAL, 594 SHORT RANGE, 264 LONG RANGE AND 112
REMARK 3 INTERMONOMER. THERE WERE 64 HYDROGEN BOND DISTANCE RESTRAINTS
REMARK 3 AND 192 DIHEDRAL RESTRAINTS INCLUDED IN CALCULATIONS.
REMARK 4
REMARK 4 1NSH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018162.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 308
REMARK 210 PH : 7.25; 7.25
REMARK 210 IONIC STRENGTH : 50 MM KCL; 50 MM KCL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM 13C,15N APO-S100A11, 50 MM
REMARK 210 KCL, 10 MM DITHIOTHREITOL, PH
REMARK 210 7.25; 3 MM 13C,15N APO-S100A11,
REMARK 210 3 MM UNLABELLED APO-S100A11, 50
REMARK 210 MM KCL, 10 MM DITHIOTHREITOL, PH
REMARK 210 7.25
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_15N/13C-SIMULTANEOUS_NOESY;
REMARK 210 3D_13C-EDITED/FILTERED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, PIPP/STAPP 4.3.3,
REMARK 210 CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
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: 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: 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 GLN A 74 H ASN A 78 1.49
REMARK 500 O GLN B 74 H ASN B 78 1.49
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 ARG A 2 -65.07 -158.18
REMARK 500 1 HIS A 26 -53.30 -130.24
REMARK 500 1 LEU A 30 -121.77 -142.71
REMARK 500 1 SER A 31 130.96 -172.31
REMARK 500 1 LEU A 43 52.94 -163.18
REMARK 500 1 ASP A 64 85.99 55.29
REMARK 500 1 ASN A 66 33.51 -173.85
REMARK 500 1 GLN A 70 -168.47 -110.32
REMARK 500 1 LEU A 71 -134.91 -62.29
REMARK 500 1 ASP A 72 -171.15 178.58
REMARK 500 1 CYS A 87 -43.32 -154.58
REMARK 500 1 GLU A 89 -163.42 -58.34
REMARK 500 1 SER A 90 -57.45 81.62
REMARK 500 1 LYS A 93 28.02 48.51
REMARK 500 1 ALA A 94 -37.69 -130.80
REMARK 500 1 ARG B 2 -64.97 -158.18
REMARK 500 1 HIS B 26 -53.38 -130.14
REMARK 500 1 LEU B 30 -121.70 -142.83
REMARK 500 1 SER B 31 130.96 -172.38
REMARK 500 1 LEU B 43 52.93 -163.18
REMARK 500 1 ASP B 64 85.94 55.38
REMARK 500 1 ASN B 66 33.48 -173.75
REMARK 500 1 GLN B 70 -168.44 -110.37
REMARK 500 1 LEU B 71 -134.97 -62.36
REMARK 500 1 ASP B 72 -171.12 178.64
REMARK 500 1 CYS B 87 -43.13 -154.65
REMARK 500 1 GLU B 89 -163.43 -58.34
REMARK 500 1 SER B 90 -57.42 81.61
REMARK 500 1 LYS B 93 27.94 48.53
REMARK 500 1 ALA B 94 -37.65 -130.78
REMARK 500 2 PRO A 3 -127.29 -63.53
REMARK 500 2 HIS A 26 112.55 61.36
REMARK 500 2 VAL A 28 -6.97 81.64
REMARK 500 2 LEU A 30 -124.30 -132.01
REMARK 500 2 SER A 31 126.71 -173.63
REMARK 500 2 THR A 47 45.67 -178.45
REMARK 500 2 ASN A 49 28.80 -153.79
REMARK 500 2 ASP A 64 64.18 69.15
REMARK 500 2 ASN A 66 -74.26 -156.23
REMARK 500 2 ASP A 68 99.94 60.74
REMARK 500 2 GLN A 70 -167.78 60.16
REMARK 500 2 LEU A 71 -135.41 -63.27
REMARK 500 2 ASP A 72 -168.70 172.79
REMARK 500 2 CYS A 87 -35.88 -158.38
REMARK 500 2 GLU A 89 156.51 -36.55
REMARK 500 2 SER A 90 66.18 -68.19
REMARK 500 2 PHE A 91 -48.96 -142.41
REMARK 500 2 PRO B 3 -127.25 -63.50
REMARK 500 2 HIS B 26 112.51 61.27
REMARK 500 2 VAL B 28 -6.84 81.58
REMARK 500
REMARK 500 THIS ENTRY HAS 684 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NSH A 1 101 UNP P24480 S10AB_RABIT 2 102
DBREF 1NSH B 1 101 UNP P24480 S10AB_RABIT 2 102
SEQRES 1 A 101 SER ARG PRO THR GLU THR GLU ARG CYS ILE GLU SER LEU
SEQRES 2 A 101 ILE ALA VAL PHE GLN LYS TYR ALA GLY LYS ASP GLY HIS
SEQRES 3 A 101 SER VAL THR LEU SER LYS THR GLU PHE LEU SER PHE MET
SEQRES 4 A 101 ASN THR GLU LEU ALA ALA PHE THR LYS ASN GLN LYS ASP
SEQRES 5 A 101 PRO GLY VAL LEU ASP ARG MET MET LYS LYS LEU ASP LEU
SEQRES 6 A 101 ASN SER ASP GLY GLN LEU ASP PHE GLN GLU PHE LEU ASN
SEQRES 7 A 101 LEU ILE GLY GLY LEU ALA VAL ALA CYS HIS GLU SER PHE
SEQRES 8 A 101 VAL LYS ALA ALA PRO PRO GLN LYS ARG PHE
SEQRES 1 B 101 SER ARG PRO THR GLU THR GLU ARG CYS ILE GLU SER LEU
SEQRES 2 B 101 ILE ALA VAL PHE GLN LYS TYR ALA GLY LYS ASP GLY HIS
SEQRES 3 B 101 SER VAL THR LEU SER LYS THR GLU PHE LEU SER PHE MET
SEQRES 4 B 101 ASN THR GLU LEU ALA ALA PHE THR LYS ASN GLN LYS ASP
SEQRES 5 B 101 PRO GLY VAL LEU ASP ARG MET MET LYS LYS LEU ASP LEU
SEQRES 6 B 101 ASN SER ASP GLY GLN LEU ASP PHE GLN GLU PHE LEU ASN
SEQRES 7 B 101 LEU ILE GLY GLY LEU ALA VAL ALA CYS HIS GLU SER PHE
SEQRES 8 B 101 VAL LYS ALA ALA PRO PRO GLN LYS ARG PHE
HELIX 1 1 THR A 4 ALA A 21 1 18
HELIX 2 2 SER A 31 LEU A 43 1 13
HELIX 3 3 LEU A 43 LYS A 48 1 6
HELIX 4 4 ASN A 49 LYS A 51 5 3
HELIX 5 5 VAL A 55 LEU A 63 1 9
HELIX 6 6 PHE A 73 ALA A 86 1 14
HELIX 7 7 HIS A 88 VAL A 92 5 5
HELIX 8 8 ALA A 95 LYS A 99 5 5
HELIX 9 9 THR B 4 ALA B 21 1 18
HELIX 10 10 SER B 31 LEU B 43 1 13
HELIX 11 11 LEU B 43 LYS B 48 1 6
HELIX 12 12 ASN B 49 LYS B 51 5 3
HELIX 13 13 VAL B 55 LEU B 63 1 9
HELIX 14 14 PHE B 73 ALA B 86 1 14
HELIX 15 15 HIS B 88 VAL B 92 5 5
HELIX 16 16 ALA B 95 LYS B 99 5 5
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