Header list of 1ss1.pdb file
Complete list - t 27 2 Bytes
HEADER IMMUNE SYSTEM 23-MAR-04 1SS1 TITLE STAPHYLOCOCCAL PROTEIN A, B-DOMAIN, Y15W MUTANT, NMR, 25 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: B DOMAIN; COMPND 5 SYNONYM: IGG BINDING PROTEIN A, STAPHYLOCOCCAL PROTEIN A; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 GENE: SPA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET A KEYWDS IMMUNOGLOBULIN-BINDING PROTEIN, THREE-HELICAL BUNDLE, IMMUNE SYSTEM EXPDTA SOLUTION NMR NUMMDL 26 AUTHOR S.SATO,T.L.RELIGA,V.DAGGETT,A.R.FERSHT REVDAT 4 27-OCT-21 1SS1 1 REMARK SEQADV REVDAT 3 24-FEB-09 1SS1 1 VERSN REVDAT 2 25-MAY-04 1SS1 1 JRNL REVDAT 1 06-APR-04 1SS1 0 JRNL AUTH S.SATO,T.L.RELIGA,V.DAGGETT,A.R.FERSHT JRNL TITL FROM THE COVER: TESTING PROTEIN-FOLDING SIMULATIONS BY JRNL TITL 2 EXPERIMENT: B DOMAIN OF PROTEIN A. JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 6952 2004 JRNL REFN ISSN 0027-8424 JRNL PMID 15069202 JRNL DOI 10.1073/PNAS.0401396101 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2002.044.17.08, CNS 1.1 REMARK 3 AUTHORS : DELAGLIO, F. ET AL (NMRPIPE), BRUNGER, A. T. ET AL REMARK 3 (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1SS1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-04. REMARK 100 THE DEPOSITION ID IS D_1000021952. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : 100 MM NACL / 50 MM ACETATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM SAMPLE, U-13C, U-15N; 50 MM REMARK 210 D-ACETATE BUFFER, 100 MM NACL, REMARK 210 PH 5.5; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY 3.106, CNS 1.1 REMARK 210 METHOD USED : STANDARD ANNEAL.INP CNS SCRIPT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 103 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26 REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH REMARK 210 EXPERIMENTAL NOESY SPECTRUM, REMARK 210 STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS 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 ASN A 7 H GLN A 11 1.54 REMARK 500 O ASN A 4 H PHE A 6 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 SER A 0 -81.28 -167.02 REMARK 500 1 THR A 1 -79.61 -156.94 REMARK 500 1 ASP A 3 26.78 46.98 REMARK 500 1 ASN A 4 66.46 30.86 REMARK 500 1 LYS A 5 53.82 -65.72 REMARK 500 1 ASN A 7 -179.53 -48.25 REMARK 500 1 LEU A 20 61.10 16.79 REMARK 500 1 PRO A 21 93.10 -61.59 REMARK 500 1 ASN A 22 -0.37 133.75 REMARK 500 1 LYS A 59 159.07 -39.83 REMARK 500 2 SER A 0 164.54 58.31 REMARK 500 2 ALA A 2 -160.72 -18.81 REMARK 500 2 ASP A 3 -70.72 40.58 REMARK 500 2 ASN A 4 -129.59 45.99 REMARK 500 2 ASN A 7 -150.95 -59.27 REMARK 500 2 LEU A 20 64.79 10.59 REMARK 500 2 PRO A 21 98.87 -61.61 REMARK 500 2 ASN A 22 -2.89 110.70 REMARK 500 2 SER A 42 -55.21 -28.56 REMARK 500 2 LYS A 59 -60.16 -98.50 REMARK 500 3 THR A 1 -69.74 109.02 REMARK 500 3 ASP A 3 44.71 -107.38 REMARK 500 3 ASN A 4 -102.13 -31.63 REMARK 500 3 LYS A 5 2.76 58.13 REMARK 500 3 PHE A 6 -111.43 26.60 REMARK 500 3 ASN A 7 -160.62 100.01 REMARK 500 3 LEU A 20 64.10 14.90 REMARK 500 3 PRO A 21 96.91 -57.33 REMARK 500 3 ASN A 22 18.58 116.53 REMARK 500 3 ASN A 24 105.41 -55.28 REMARK 500 3 SER A 42 -36.98 -39.85 REMARK 500 3 ALA A 57 99.59 -38.00 REMARK 500 4 SER A 0 129.54 63.41 REMARK 500 4 THR A 1 -63.96 -164.93 REMARK 500 4 ALA A 2 85.84 64.13 REMARK 500 4 ASP A 3 -71.67 -100.04 REMARK 500 4 LYS A 5 93.50 -177.12 REMARK 500 4 PHE A 6 72.60 -66.94 REMARK 500 4 ASN A 7 -167.87 -55.05 REMARK 500 4 PRO A 21 95.02 -66.71 REMARK 500 4 ASN A 22 12.03 104.70 REMARK 500 4 SER A 42 -76.20 -33.27 REMARK 500 4 PRO A 58 82.38 -61.09 REMARK 500 5 ASP A 3 30.80 -169.59 REMARK 500 5 ASN A 4 -78.31 -45.73 REMARK 500 5 LYS A 5 60.76 93.13 REMARK 500 5 ASN A 7 -165.93 -56.79 REMARK 500 5 LEU A 20 67.35 11.81 REMARK 500 5 PRO A 21 98.05 -56.05 REMARK 500 5 ASN A 22 -6.01 111.12 REMARK 500 REMARK 500 THIS ENTRY HAS 266 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1SS1 A 2 60 UNP P38507 SPA2_STAAU 212 270 SEQADV 1SS1 GLY A -1 UNP P38507 CLONING ARTIFACT SEQADV 1SS1 SER A 0 UNP P38507 CLONING ARTIFACT SEQADV 1SS1 THR A 1 UNP P38507 CLONING ARTIFACT SEQADV 1SS1 TRP A 15 UNP P38507 TYR 225 ENGINEERED MUTATION SEQRES 1 A 62 GLY SER THR ALA ASP ASN LYS PHE ASN LYS GLU GLN GLN SEQRES 2 A 62 ASN ALA PHE TRP GLU ILE LEU HIS LEU PRO ASN LEU ASN SEQRES 3 A 62 GLU GLU GLN ARG ASN GLY PHE ILE GLN SER LEU LYS ASP SEQRES 4 A 62 ASP PRO SER GLN SER ALA ASN LEU LEU ALA GLU ALA LYS SEQRES 5 A 62 LYS LEU ASN ASP ALA GLN ALA PRO LYS ALA HELIX 1 1 ASN A 7 LEU A 20 1 14 HELIX 2 2 ASN A 24 ASP A 38 1 15 HELIX 3 3 GLN A 41 ALA A 57 1 17 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