Header list of 1zxh.pdb file
Complete list - t 20 2 Bytes
HEADER IMMUNE SYSTEM/PROTEIN BINDING 08-JUN-05 1ZXH TITLE G311 MUTANT PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN G; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IGG BINDING PROTEIN G; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP.; SOURCE 3 ORGANISM_TAXID: 1306; SOURCE 4 GENE: SPG; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PG58-G311 KEYWDS IGG-BINDING, PROTEIN G, PHAGE DISPLAY, IMMUNE SYSTEM-PROTEIN BINDING KEYWDS 2 COMPLEX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.HE,D.C.YEH,P.ALEXANDER,P.N.BRYAN,J.ORBAN REVDAT 3 20-OCT-21 1ZXH 1 REMARK SEQADV REVDAT 2 24-FEB-09 1ZXH 1 VERSN REVDAT 1 08-NOV-05 1ZXH 0 JRNL AUTH Y.HE,D.C.YEH,P.ALEXANDER,P.N.BRYAN,J.ORBAN JRNL TITL SOLUTION NMR STRUCTURES OF IGG BINDING DOMAINS WITH JRNL TITL 2 ARTIFICIALLY EVOLVED HIGH LEVELS OF SEQUENCE IDENTITY BUT JRNL TITL 3 DIFFERENT FOLDS. JRNL REF BIOCHEMISTRY V. 44 14055 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 16245921 JRNL DOI 10.1021/BI051232J REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.5, CNS 1.1 REMARK 3 AUTHORS : BRUKER CO. (XWINNMR), 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: SIMULATED ANNEALING REMARK 4 REMARK 4 1ZXH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1000033233. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 275 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 0.1M REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : G311 MUTANT PROTEIN, 0.1 M KPI, REMARK 210 PH7.0, ~0.6 M GUHCL. REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D HNCACB, 3D REMARK 210 HNCO, 3DCBCACONH, 3D HBHA(CBCACO) REMARK 210 NH, 3D (H)C(CO)NH-TOCSY, H(CCO) REMARK 210 NH-TOCSY, 2D TOCSY, 2D-CBHD, REMARK 210 2DCBHE, 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, SPARKY 3, CNS 1.1 REMARK 210 METHOD USED : CNS 1.1 REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS REMARK 210 ARE THOSE WITH THE FEWEST NUMBER REMARK 210 OF CONSTRAINT 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 H ASN A 7 O TYR A 14 1.51 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 ASN A 11 42.22 -149.95 REMARK 500 1 VAL A 21 -63.19 68.22 REMARK 500 1 ASP A 22 -164.85 -124.84 REMARK 500 1 ALA A 23 -72.48 -82.10 REMARK 500 1 GLN A 40 -30.56 -31.99 REMARK 500 1 LYS A 50 36.26 77.49 REMARK 500 2 ASN A 11 44.62 -151.10 REMARK 500 2 VAL A 21 -70.00 58.74 REMARK 500 2 ASP A 22 -161.43 -114.58 REMARK 500 2 ALA A 23 -73.09 -87.73 REMARK 500 2 GLN A 40 -30.35 -31.92 REMARK 500 2 LYS A 50 37.80 78.61 REMARK 500 3 ASN A 11 42.28 -145.87 REMARK 500 3 ALA A 12 122.19 -176.42 REMARK 500 3 VAL A 21 -65.07 68.75 REMARK 500 3 ASP A 22 -163.90 -116.66 REMARK 500 3 ALA A 23 -73.02 -87.11 REMARK 500 3 GLN A 40 -30.46 -31.97 REMARK 500 3 LYS A 50 38.31 77.79 REMARK 500 4 TYR A 2 82.91 -161.30 REMARK 500 4 ASN A 11 42.83 -150.06 REMARK 500 4 VAL A 21 -67.51 61.99 REMARK 500 4 ASP A 22 -159.75 -125.73 REMARK 500 4 ALA A 23 -71.38 -85.46 REMARK 500 4 GLN A 40 -30.41 -31.95 REMARK 500 4 LYS A 50 36.96 77.71 REMARK 500 5 ASN A 11 43.13 -150.07 REMARK 500 5 ALA A 12 128.86 -172.64 REMARK 500 5 VAL A 21 -69.42 59.62 REMARK 500 5 ASP A 22 -159.40 -122.39 REMARK 500 5 ALA A 23 -71.49 -86.41 REMARK 500 5 GLN A 40 -30.52 -31.85 REMARK 500 5 LYS A 50 36.82 77.91 REMARK 500 6 ASN A 11 43.59 -146.91 REMARK 500 6 ALA A 12 127.60 -173.94 REMARK 500 6 VAL A 21 -68.80 67.39 REMARK 500 6 ASP A 22 -158.81 -121.95 REMARK 500 6 ALA A 23 -70.13 -86.12 REMARK 500 6 GLN A 40 -30.56 -31.65 REMARK 500 6 LYS A 50 37.40 80.29 REMARK 500 7 TYR A 2 67.79 -66.19 REMARK 500 7 ASN A 11 43.54 -147.95 REMARK 500 7 ALA A 12 127.46 -172.64 REMARK 500 7 VAL A 21 -70.20 62.40 REMARK 500 7 ASP A 22 -161.62 -118.02 REMARK 500 7 ALA A 23 -71.72 -87.49 REMARK 500 7 GLN A 40 -30.27 -32.05 REMARK 500 7 LYS A 50 39.59 82.09 REMARK 500 8 ASN A 11 43.90 -147.07 REMARK 500 8 ALA A 12 127.95 -174.81 REMARK 500 REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ZXG RELATED DB: PDB DBREF 1ZXH A 2 56 UNP P19909 SPG2_STRSG 443 497 SEQADV 1ZXH TYR A 2 UNP P19909 THR 443 ENGINEERED MUTATION SEQADV 1ZXH LEU A 4 UNP P19909 LYS 445 ENGINEERED MUTATION SEQADV 1ZXH VAL A 5 UNP P19909 LEU 446 ENGINEERED MUTATION SEQADV 1ZXH ASN A 7 UNP P19909 ILE 448 ENGINEERED MUTATION SEQADV 1ZXH LYS A 8 UNP P19909 ASN 449 ENGINEERED MUTATION SEQADV 1ZXH GLN A 10 UNP P19909 LYS 451 ENGINEERED MUTATION SEQADV 1ZXH ASN A 11 UNP P19909 THR 452 ENGINEERED MUTATION SEQADV 1ZXH ALA A 12 UNP P19909 LEU 453 ENGINEERED MUTATION SEQADV 1ZXH PHE A 13 UNP P19909 LYS 454 ENGINEERED MUTATION SEQADV 1ZXH TYR A 14 UNP P19909 GLY 455 ENGINEERED MUTATION SEQADV 1ZXH LEU A 17 UNP P19909 THR 458 ENGINEERED MUTATION SEQADV 1ZXH ARG A 27 UNP P19909 GLU 468 ENGINEERED MUTATION SEQADV 1ZXH ASN A 28 UNP P19909 LYS 469 ENGINEERED MUTATION SEQADV 1ZXH ILE A 31 UNP P19909 LYS 472 ENGINEERED MUTATION SEQADV 1ZXH SER A 33 UNP P19909 TYR 474 ENGINEERED MUTATION SEQADV 1ZXH LEU A 34 UNP P19909 ALA 475 ENGINEERED MUTATION SEQADV 1ZXH LYS A 35 UNP P19909 ASN 476 ENGINEERED MUTATION SEQADV 1ZXH ASP A 37 UNP P19909 ASN 478 ENGINEERED MUTATION SEQADV 1ZXH GLN A 40 UNP P19909 ASP 481 ENGINEERED MUTATION SEQADV 1ZXH GLN A 55 UNP P19909 THR 496 ENGINEERED MUTATION SEQADV 1ZXH ALA A 56 UNP P19909 GLU 497 ENGINEERED MUTATION SEQRES 1 A 56 MET TYR TYR LEU VAL VAL ASN LYS GLY GLN ASN ALA PHE SEQRES 2 A 56 TYR GLU THR LEU THR LYS ALA VAL ASP ALA GLU THR ALA SEQRES 3 A 56 ARG ASN ALA PHE ILE GLN SER LEU LYS ASP ASP GLY VAL SEQRES 4 A 56 GLN GLY VAL TRP THR TYR ASP ASP ALA THR LYS THR PHE SEQRES 5 A 56 THR VAL GLN ALA HELIX 1 1 ASP A 22 VAL A 39 1 18 SHEET 1 A 3 PHE A 13 LYS A 19 0 SHEET 2 A 3 TYR A 2 LYS A 8 -1 N ASN A 7 O TYR A 14 SHEET 3 A 3 THR A 51 PHE A 52 1 O PHE A 52 N VAL A 6 SHEET 1 B 2 VAL A 42 TRP A 43 0 SHEET 2 B 2 VAL A 54 GLN A 55 -1 O GLN A 55 N VAL A 42 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 20 2 Bytes