Header list of 1q2n.pdb file
Complete list - 27 20 Bytes
HEADER IMMUNE SYSTEM 25-JUL-03 1Q2N TITLE REFINED SOLUTION NMR STRUCTURE OF THE Z DOMAIN OF STAPHYLOCOCCAL TITLE 2 PROTEIN A COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 212-269; COMPND 5 SYNONYM: IGG BINDING PROTEIN A; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 CELLULAR_LOCATION: CELL WALL; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: RV308; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDHZ KEYWDS IMMUNOGLOBULIN-BINDING PROTEIN, THREE-HELICAL BUNDLE STRUCTURE, KEYWDS 2 RESIDUAL DIPOLAR COUPLINGS, IMMUNE SYSTEM EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR D.ZHENG,M.TASHIRO,J.M.ARAMINI,G.T.MONTELIONE REVDAT 4 27-OCT-21 1Q2N 1 REMARK SEQADV REVDAT 3 24-FEB-09 1Q2N 1 VERSN REVDAT 2 02-MAR-04 1Q2N 1 JRNL REVDAT 1 12-AUG-03 1Q2N 0 JRNL AUTH D.ZHENG,J.M.ARAMINI,G.T.MONTELIONE JRNL TITL VALIDATION OF HELICAL TILT ANGLES IN THE SOLUTION NMR JRNL TITL 2 STRUCTURE OF THE Z DOMAIN OF STAPHYLOCOCCAL PROTEIN A BY JRNL TITL 3 COMBINED ANALYSIS OF RESIDUAL DIPOLAR COUPLING AND NOE DATA. JRNL REF PROTEIN SCI. V. 13 549 2004 JRNL REFN ISSN 0961-8368 JRNL PMID 14718654 JRNL DOI 10.1110/PS.03351704 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.JENDEBERG,M.TASHIRO,R.TEJERO,B.A.LYONS,M.UHLEN, REMARK 1 AUTH 2 G.T.MONTELIONE,B.NILSSON REMARK 1 TITL THE MECHANISM OF BINDING STAPHYLOCOCCAL PROTEIN A TO REMARK 1 TITL 2 IMMUNOGLOBIN G DOES NOT INVOLVE HELIX UNWINDING REMARK 1 REF BIOCHEMISTRY V. 35 22 1996 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI9512814 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.TASHIRO,G.T.MONTELIONE REMARK 1 TITL STRUCTURES OF BACTERIAL IMMUNOGLOBULIN-BINDING DOMAINS AND REMARK 1 TITL 2 THEIR COMPLEXES WITH IMMUNOGLOBULIN REMARK 1 REF CURR.OPIN.STRUCT.BIOL. V. 5 471 1995 REMARK 1 REFN ISSN 0959-440X REMARK 1 DOI 10.1016/0959-440X(95)80031-X REMARK 1 REFERENCE 3 REMARK 1 AUTH B.A.LYONS,M.TASHIRO,L.CEDERGREN,B.NILSSON,G.T.MONTELIONE REMARK 1 TITL AN IMPROVED STRATEGY FOR DETERMINING RESONANCE ASSIGNMENTS REMARK 1 TITL 2 FOR ISOTOPICALLY ENRICHED PROTEINS AND ITS APPLICATION TO AN REMARK 1 TITL 3 ENGINEERED DOMAIN OF STAPHYLOCOCCAL PROTEIN A REMARK 1 REF BIOCHEMISTRY V. 32 7839 1993 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 4 REMARK 1 AUTH M.TASHIRO,R.TEJERO,D.E.ZIMMERMAN,B.CELDA,B.NILSSON, REMARK 1 AUTH 2 G.T.MONTELIONE REMARK 1 TITL HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE Z DOMAIN OF REMARK 1 TITL 2 STAPHYLOCOCCAL PROTEIN A REMARK 1 REF J.MOL.BIOL. V. 272 573 1997 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1997.1265 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER, A.T. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 769 CONFORMATIONAL RESTRAINTS. SUMMARY OF EXPERIMENTAL REMARK 3 CONSTRAINTS: DISTANCE CONSTRAINTS: TOTAL = 536; INTRA-RESIDUE [I= REMARK 3 J] = 224; SEQUENTIAL [(I-J)=1] = 142; MEDIUM RANGE [1<(I-J)<5] REMARK 3 105; LONG RANGE [(I-J)>=5] = 65; NUMBER OF DISTANCE CONSTRAINTS REMARK 3 RESIDUE = 9.2; DIHEDRAL-ANGLE CONSTRAINTS = 107 RESIDUAL DIPOLAR REMARK 3 COUPLING CONSTRAINTS = 126 (34 N-H, 43 HA-CA, 4 TOTAL NUMBER OF REMARK 3 CONSTRAINTS PER RESIDUE = 13.3; NUMBER OF LONG RANGE CONSTRAINTS REMARK 3 PER RESIDUE = 3.3; NUMBER OF STRUCTURES COMPUTED = 100; NUMBER REMARK 3 OF STRUCTURES USED = 10. AVERAGE RESIDUAL CONSTRAINT VIOLATIONS: REMARK 3 DISTANCE VIOLATIONS 0.1-0.2 ANG = 7.7, 0. 0.8, >0.5 ANG = 0.3. REMARK 3 AVERAGE R.M.S. DISTANCE VIOLATION = 0.03 AN AVERAGE DIHEDRAL REMARK 3 ANGLE VIOLATIONS: >0 DEG = 0; RMSD VALUES: BACKBONE ATOMS (N,C,C' REMARK 3 ) = 1.2 ANG; BACKBONE ATOMS(N,C,C') OF ORDERED RESIDUES = 0.4 REMARK 3 ANG; ALL HEAVY = 1.7 ANG; ALL HEAVY ATOMS OF ORDERED RESIDUES = REMARK 3 1.0 ANG. PROCHECK USING ORDERED RESIDUES (5-36,39-57): MOST REMARK 3 FAVORED REGIONS = 91.4%; ADDITIONAL ALLOWED REGIONS = 8.4%; REMARK 3 GENEROUSLY ALLOWED REGIONS = 0.2%; DISALLOWED REGIONS = 0%. REMARK 4 REMARK 4 1Q2N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-03. REMARK 100 THE DEPOSITION ID IS D_1000019838. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303.00 REMARK 210 PH : 6.50 REMARK 210 IONIC STRENGTH : 20 MM NH4OAC REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM Z DOMAIN U-15N,13C; 20MM REMARK 210 NH4OAC BUFFER; 95% H2O, 5% D2O. REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : MODIFIED UNITY 500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING WITH REMARK 210 RESTRAINED MOLECULAR DYNAMICS, REMARK 210 PROTOCAL USED: ANNEAL.INP REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 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: NMR EXPERIMENTS CONDUCTED: 2D PFG-[15N]HSQC, 3D PFG-HNCO, REMARK 210 3D PFG-(HA)CA(CO)NH, 3D PFG-HA(CA)(CO)NH, 3D PFG-HA(CA)NH, 3D REMARK 210 PFG-CBCANH, 3D PFG-CBCA(CO)NH, 3D PFG- (HA)CANH, 3D PFG-HN(CA)CO, REMARK 210 3D PFG-HCCNH-TOCSY, 3D PFG-HCC (CO)NH-TOCSY, 2D [15N]HSQC-IPAP, REMARK 210 3D CA-COUPLED HNCO 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 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 LYS A 4 -82.33 -93.74 REMARK 500 1 GLN A 40 31.11 -95.60 REMARK 500 2 ASP A 2 -89.50 -56.34 REMARK 500 2 ASN A 3 -164.25 -160.09 REMARK 500 2 LYS A 4 -88.90 -87.03 REMARK 500 2 PRO A 38 -135.44 -55.10 REMARK 500 2 GLN A 40 31.62 -84.23 REMARK 500 2 PRO A 57 173.42 -52.75 REMARK 500 3 LYS A 4 45.19 -100.04 REMARK 500 3 PRO A 38 -134.68 -54.61 REMARK 500 3 GLN A 40 41.23 -80.47 REMARK 500 4 ASP A 2 -174.27 -67.74 REMARK 500 4 ASN A 3 -123.00 -69.94 REMARK 500 5 ASN A 3 48.44 -94.54 REMARK 500 5 LYS A 4 61.56 -100.04 REMARK 500 5 ALA A 56 106.62 -53.48 REMARK 500 6 ASP A 2 -172.42 -69.59 REMARK 500 6 PHE A 5 -164.43 -76.31 REMARK 500 7 LYS A 4 -84.66 -51.75 REMARK 500 7 PRO A 38 -136.97 -55.80 REMARK 500 8 PRO A 38 -155.87 -50.40 REMARK 500 8 GLN A 40 33.98 -77.48 REMARK 500 9 ASN A 3 -143.19 -108.31 REMARK 500 9 LYS A 4 -147.70 -100.04 REMARK 500 9 GLU A 25 -72.57 -54.13 REMARK 500 10 LYS A 4 -124.98 -65.52 REMARK 500 10 PHE A 5 -172.07 -69.91 REMARK 500 10 ASN A 6 -104.65 -149.85 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2SPZ RELATED DB: PDB DBREF 1Q2N A 1 58 UNP P38507 SPA2_STAAU 212 269 SEQADV 1Q2N VAL A 1 UNP P38507 ALA 212 ENGINEERED MUTATION SEQADV 1Q2N ALA A 29 UNP P38507 GLY 240 ENGINEERED MUTATION SEQRES 1 A 58 VAL ASP ASN LYS PHE ASN LYS GLU GLN GLN ASN ALA PHE SEQRES 2 A 58 TYR GLU ILE LEU HIS LEU PRO ASN LEU ASN GLU GLU GLN SEQRES 3 A 58 ARG ASN ALA PHE ILE GLN SER LEU LYS ASP ASP PRO SER SEQRES 4 A 58 GLN SER ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN SEQRES 5 A 58 ASP ALA GLN ALA PRO LYS HELIX 1 1 ASN A 6 HIS A 18 1 13 HELIX 2 2 ASN A 23 ASP A 37 1 15 HELIX 3 3 GLN A 40 GLN A 55 1 16 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 - 27 20 Bytes