Header list of 1sw8.pdb file
Complete list - t 27 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 30-MAR-04 1SW8 TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN N60D CALMODULIN TITLE 2 REFINED WITH PARAMAGNETISM BASED STRATEGY COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CALCIUM, CALMODULIN, EF-HAND, LANTHANIDE, STRUCTURAL PROTEOMICS IN KEYWDS 2 EUROPE, SPINE, STRUCTURAL GENOMICS, CALCIUM-BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR I.BERTINI,C.DEL BIANCO,I.GELIS,N.KATSAROS,C.LUCHINAT,G.PARIGI, AUTHOR 2 M.PEANA,A.PROVENZANI,M.A.ZORODDU,STRUCTURAL PROTEOMICS IN EUROPE AUTHOR 3 (SPINE) REVDAT 4 27-OCT-21 1SW8 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1SW8 1 VERSN REVDAT 2 11-MAY-04 1SW8 1 JRNL REVDAT 1 06-APR-04 1SW8 0 JRNL AUTH I.BERTINI,C.DEL BIANCO,I.GELIS,N.KATSAROS,C.LUCHINAT, JRNL AUTH 2 G.PARIGI,M.PEANA,A.PROVENZANI,M.A.ZORODDU JRNL TITL EXPERIMENTALLY EXPLORING THE CONFORMATIONAL SPACE SAMPLED BY JRNL TITL 2 DOMAIN REORIENTATION IN CALMODULIN JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 6841 2004 JRNL REFN ISSN 0027-8424 JRNL PMID 15100408 JRNL DOI 10.1073/PNAS.0308641101 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.1 3.1, DYANA REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WITH PSEUDOCONTACT SHIFTS REMARK 4 REMARK 4 1SW8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-04. REMARK 100 THE DEPOSITION ID IS D_1000022048. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 400 MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM CALMODULIN U-15N, 20 MM REMARK 210 MES, 400 MM KCL, 90% H20, 10% REMARK 210 D20; 1 MM CALMODULIN U-15N-13C, REMARK 210 20 MM MES, 400 MM KCL, 90% H20, REMARK 210 10% D20 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1 3.1, XEASY 1.3, REMARK 210 DYANA REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 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: THE STRUCTURE WAS CALCULATED USING DIMAGNETIC, DIHEDRAL REMARK 210 ANGLE RESTRAINTS AND PSEUDOCONTACT SHIFTS 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 OD1 ASP A 22 CA CA A 80 0.99 REMARK 500 O GLN A 8 H PHE A 12 1.54 REMARK 500 O GLU A 11 H ALA A 15 1.57 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 2 -39.16 88.45 REMARK 500 1 GLN A 3 33.20 -140.69 REMARK 500 1 LEU A 4 28.38 40.43 REMARK 500 1 PHE A 16 -39.18 -37.60 REMARK 500 1 GLN A 41 178.14 -49.95 REMARK 500 1 ASN A 42 64.83 -154.39 REMARK 500 1 ASP A 56 108.35 -43.88 REMARK 500 1 ASP A 58 -35.78 -39.50 REMARK 500 1 ASP A 60 -49.56 176.88 REMARK 500 2 LEU A 4 -38.86 -175.61 REMARK 500 2 THR A 5 -32.45 -37.47 REMARK 500 2 GLN A 41 -174.25 -52.59 REMARK 500 2 ASN A 42 60.60 -163.65 REMARK 500 2 ASP A 56 109.79 -53.12 REMARK 500 2 ASP A 60 -50.66 176.26 REMARK 500 3 GLN A 3 -57.42 -125.69 REMARK 500 3 LEU A 4 -34.21 -176.68 REMARK 500 3 THR A 5 -31.65 -37.58 REMARK 500 3 LEU A 39 -70.78 -81.89 REMARK 500 3 ASN A 42 61.67 -166.39 REMARK 500 3 ASP A 56 109.28 -49.74 REMARK 500 3 ASP A 60 -60.81 168.30 REMARK 500 4 GLN A 3 -72.71 -140.06 REMARK 500 4 LEU A 4 32.13 -173.35 REMARK 500 4 ILE A 9 -39.25 -39.42 REMARK 500 4 GLN A 41 -172.21 -61.06 REMARK 500 4 ASN A 42 60.71 -167.51 REMARK 500 4 ASP A 56 107.94 -51.79 REMARK 500 4 ASP A 60 -67.18 176.22 REMARK 500 5 ASP A 2 19.88 55.05 REMARK 500 5 PHE A 16 -32.18 -36.55 REMARK 500 5 ASP A 20 39.65 -96.59 REMARK 500 5 ILE A 27 77.84 -104.25 REMARK 500 5 ASP A 56 108.19 -50.48 REMARK 500 5 ASP A 58 -35.00 -39.86 REMARK 500 5 ASP A 60 -50.72 -167.64 REMARK 500 6 GLN A 3 20.64 -141.59 REMARK 500 6 LEU A 4 -61.95 69.69 REMARK 500 6 THR A 28 150.76 -46.06 REMARK 500 6 ASN A 42 62.31 -156.41 REMARK 500 6 ASP A 56 106.38 -54.07 REMARK 500 6 ASP A 58 -33.51 -38.93 REMARK 500 6 ASP A 60 -55.43 -164.20 REMARK 500 7 LEU A 4 -60.45 -127.45 REMARK 500 7 ASP A 22 -75.56 -43.59 REMARK 500 7 THR A 28 153.88 -47.57 REMARK 500 7 LEU A 39 35.51 -89.79 REMARK 500 7 GLN A 41 178.31 -49.05 REMARK 500 7 ASN A 42 57.09 -165.08 REMARK 500 7 ASP A 56 108.84 -50.22 REMARK 500 REMARK 500 THIS ENTRY HAS 127 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 CA A 80 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 20 OD1 REMARK 620 2 ASP A 22 OD2 163.9 REMARK 620 3 GLY A 23 N 99.2 90.8 REMARK 620 4 ASP A 24 OD1 109.5 54.4 123.4 REMARK 620 5 ASP A 24 N 98.9 75.6 58.6 69.3 REMARK 620 6 THR A 26 O 73.8 97.0 171.7 64.1 126.2 REMARK 620 7 GLU A 31 OE1 71.0 120.0 99.1 135.8 154.5 74.5 REMARK 620 8 GLU A 31 OE2 107.7 77.3 120.2 96.2 152.9 59.3 46.8 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 81 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 56 OD1 REMARK 620 2 ASP A 58 OD1 55.5 REMARK 620 3 ASP A 60 OD1 80.0 106.3 REMARK 620 4 ASP A 60 OD2 66.0 60.8 47.5 REMARK 620 5 THR A 62 N 77.3 131.5 49.2 92.0 REMARK 620 6 THR A 62 O 88.4 125.3 105.7 144.0 56.5 REMARK 620 7 GLU A 67 OE1 106.0 91.4 161.3 151.1 114.0 57.7 REMARK 620 8 GLU A 67 OE2 71.2 48.6 149.6 109.2 129.5 83.7 44.5 REMARK 620 N 1 2 3 4 5 6 7 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 80 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 81 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: CIRMMP35 RELATED DB: TARGETDB DBREF 1SW8 A 1 79 UNP P62158 CALM_HUMAN 2 80 SEQADV 1SW8 ASP A 60 UNP P62158 ASN 61 ENGINEERED MUTATION SEQRES 1 A 79 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS SEQRES 2 A 79 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR SEQRES 3 A 79 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU SEQRES 4 A 79 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE SEQRES 5 A 79 ASN GLU VAL ASP ALA ASP GLY ASP GLY THR ILE ASP PHE SEQRES 6 A 79 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP SEQRES 7 A 79 THR HET CA A 80 1 HET CA A 81 1 HETNAM CA CALCIUM ION FORMUL 2 CA 2(CA 2+) HELIX 1 1 LEU A 4 ASP A 20 1 17 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 PHE A 65 THR A 79 1 15 SHEET 1 A 2 THR A 26 ILE A 27 0 SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27 LINK OD1 ASP A 20 CA CA A 80 1555 1555 2.30 LINK OD2 ASP A 22 CA CA A 80 1555 1555 2.29 LINK N GLY A 23 CA CA A 80 1555 1555 2.80 LINK OD1 ASP A 24 CA CA A 80 1555 1555 2.79 LINK N ASP A 24 CA CA A 80 1555 1555 2.87 LINK O THR A 26 CA CA A 80 1555 1555 2.37 LINK OE1 GLU A 31 CA CA A 80 1555 1555 2.85 LINK OE2 GLU A 31 CA CA A 80 1555 1555 2.76 LINK OD1 ASP A 56 CA CA A 81 1555 1555 2.19 LINK OD1 ASP A 58 CA CA A 81 1555 1555 2.81 LINK OD1 ASP A 60 CA CA A 81 1555 1555 3.02 LINK OD2 ASP A 60 CA CA A 81 1555 1555 2.19 LINK N THR A 62 CA CA A 81 1555 1555 3.18 LINK O THR A 62 CA CA A 81 1555 1555 2.24 LINK OE1 GLU A 67 CA CA A 81 1555 1555 2.86 LINK OE2 GLU A 67 CA CA A 81 1555 1555 3.01 SITE 1 AC1 6 ASP A 20 ASP A 22 GLY A 23 ASP A 24 SITE 2 AC1 6 THR A 26 GLU A 31 SITE 1 AC2 6 ASP A 56 ASP A 58 ASP A 60 THR A 62 SITE 2 AC2 6 ASP A 64 GLU A 67 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 - t 27 2 Bytes