Header list of 1cir.pdb file
Complete list - b 16 2 Bytes
HEADER SERINE PROTEASE INHIBITOR 02-OCT-95 1CIR TITLE COMPLEX OF TWO FRAGMENTS OF CI2 [(1-40)(DOT)(41-64)] COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHYMOTRYPSIN INHIBITOR 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CI2; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: CLEAVED BETWEEN RESIDUES 40 AND 41; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: CHYMOTRYPSIN INHIBITOR 2; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: CI2; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: CLEAVED BETWEEN RESIDUES 40 AND 41 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HORDEUM VULGARE; SOURCE 3 ORGANISM_TAXID: 4513; SOURCE 4 STRAIN: HIPROLY; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTZ18U; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HORDEUM VULGARE; SOURCE 10 ORGANISM_TAXID: 4513; SOURCE 11 STRAIN: HIPROLY; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PTZ18U KEYWDS SERINE PROTEASE INHIBITOR EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.J.DAVIS,A.R.FERSHT REVDAT 4 16-FEB-22 1CIR 1 REMARK REVDAT 3 24-FEB-09 1CIR 1 VERSN REVDAT 2 01-APR-03 1CIR 1 JRNL REVDAT 1 29-JAN-96 1CIR 0 JRNL AUTH J.L.NEIRA,B.DAVIS,A.G.LADURNER,A.M.BUCKLE,P.GAY GDE, JRNL AUTH 2 A.R.FERSHT JRNL TITL TOWARDS THE COMPLETE STRUCTURAL CHARACTERIZATION OF A JRNL TITL 2 PROTEIN FOLDING PATHWAY: THE STRUCTURES OF THE DENATURED, JRNL TITL 3 TRANSITION AND NATIVE STATES FOR THE ASSOCIATION/FOLDING OF JRNL TITL 4 TWO COMPLEMENTARY FRAGMENTS OF CLEAVED CHYMOTRYPSIN JRNL TITL 5 INHIBITOR 2. DIRECT EVIDENCE FOR A NUCLEATION-CONDENSATION JRNL TITL 6 MECHANISM JRNL REF STRUCTURE FOLD.DES. V. 1 189 1996 JRNL REFN ISSN 0969-2126 JRNL PMID 9079381 JRNL DOI 10.1016/S1359-0278(96)00031-4 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.DE PRAT GAY,J.RUIZ-SANZ,B.DAVIS,A.R.FERSHT REMARK 1 TITL THE STRUCTURE OF THE TRANSITION STATE FOR THE ASSOCIATION OF REMARK 1 TITL 2 TWO FRAGMENTS OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 TO REMARK 1 TITL 3 GENERATE NATIVE-LIKE PROTEIN: IMPLICATIONS FOR MECHANISMS OF REMARK 1 TITL 4 PROTEIN FOLDING REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 10943 1994 REMARK 1 REFN ISSN 0027-8424 REMARK 1 REFERENCE 2 REMARK 1 AUTH G.DE PRAT GAY,A.R.FERSHT REMARK 1 TITL GENERATION OF A FAMILY OF PROTEIN FRAGMENTS FOR REMARK 1 TITL 2 STRUCTURE-FOLDING STUDIES. 1. FOLDING COMPLEMENTATION OF TWO REMARK 1 TITL 3 FRAGMENTS OF CHYMOTRYPSIN INHIBITOR-2 FORMED BY CLEAVAGE AT REMARK 1 TITL 4 ITS UNIQUE METHIONINE RESIDUE REMARK 1 REF BIOCHEMISTRY V. 33 7957 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CIR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000172349. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 HSE A 40 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 GLU A 4 -30.76 -131.53 REMARK 500 1 LYS A 11 -144.28 -91.49 REMARK 500 1 GLU A 14 -75.52 -44.60 REMARK 500 1 ALA A 16 -80.66 -62.45 REMARK 500 1 LYS A 18 -81.20 -51.53 REMARK 500 1 LEU A 21 -23.82 -38.84 REMARK 500 1 GLN A 22 -81.22 -135.37 REMARK 500 1 ASP A 23 -94.82 37.77 REMARK 500 1 LYS A 24 -163.76 -58.48 REMARK 500 1 VAL A 34 -91.85 50.38 REMARK 500 1 THR A 36 -167.12 -76.15 REMARK 500 1 ILE A 37 65.33 -112.40 REMARK 500 1 VAL A 38 81.53 58.53 REMARK 500 1 TYR B 42 -148.12 -136.18 REMARK 500 1 ASP B 45 46.43 -107.66 REMARK 500 1 ARG B 48 87.95 -53.35 REMARK 500 1 ASP B 52 -151.34 -93.52 REMARK 500 1 ILE B 57 87.09 -31.94 REMARK 500 1 ARG B 62 -49.15 -140.58 REMARK 500 1 VAL B 63 -3.14 76.04 REMARK 500 2 LYS A 2 98.87 -52.81 REMARK 500 2 GLU A 4 -44.20 -148.45 REMARK 500 2 LYS A 11 -146.88 -94.54 REMARK 500 2 GLU A 14 -73.75 -44.07 REMARK 500 2 ALA A 16 -83.40 -61.39 REMARK 500 2 LYS A 18 -77.37 -44.57 REMARK 500 2 LYS A 24 -153.87 -68.23 REMARK 500 2 GLU A 26 52.33 -166.34 REMARK 500 2 TYR B 42 -148.72 -75.31 REMARK 500 2 ARG B 43 62.66 -104.59 REMARK 500 2 ILE B 44 160.13 -44.88 REMARK 500 2 ASP B 52 -154.30 -124.86 REMARK 500 2 LEU B 54 44.58 -99.58 REMARK 500 2 ILE B 57 86.98 -34.34 REMARK 500 3 GLU A 4 -57.75 -125.50 REMARK 500 3 TRP A 5 39.78 70.30 REMARK 500 3 LYS A 11 78.14 -154.30 REMARK 500 3 SER A 12 46.73 -153.18 REMARK 500 3 VAL A 13 -73.03 -77.28 REMARK 500 3 ALA A 16 -71.62 -62.69 REMARK 500 3 LYS A 18 -90.29 -62.17 REMARK 500 3 LEU A 21 -29.99 -35.13 REMARK 500 3 LYS A 24 -147.00 69.86 REMARK 500 3 GLU A 26 64.66 -161.06 REMARK 500 3 VAL A 34 -71.37 81.24 REMARK 500 3 THR A 36 120.68 -33.14 REMARK 500 3 VAL A 38 -175.80 -57.86 REMARK 500 3 TYR B 42 -145.39 -127.36 REMARK 500 3 ARG B 43 67.33 -114.91 REMARK 500 3 ASP B 45 43.05 -105.86 REMARK 500 REMARK 500 THIS ENTRY HAS 359 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG B 43 0.22 SIDE CHAIN REMARK 500 1 ARG B 46 0.28 SIDE CHAIN REMARK 500 1 ARG B 48 0.32 SIDE CHAIN REMARK 500 1 ARG B 62 0.32 SIDE CHAIN REMARK 500 2 ARG B 43 0.26 SIDE CHAIN REMARK 500 2 ARG B 46 0.31 SIDE CHAIN REMARK 500 2 ARG B 48 0.32 SIDE CHAIN REMARK 500 2 ARG B 62 0.32 SIDE CHAIN REMARK 500 3 ARG B 43 0.31 SIDE CHAIN REMARK 500 3 ARG B 46 0.23 SIDE CHAIN REMARK 500 3 ARG B 48 0.24 SIDE CHAIN REMARK 500 3 ARG B 62 0.24 SIDE CHAIN REMARK 500 4 ARG B 43 0.22 SIDE CHAIN REMARK 500 4 ARG B 46 0.31 SIDE CHAIN REMARK 500 4 ARG B 48 0.31 SIDE CHAIN REMARK 500 4 ARG B 62 0.22 SIDE CHAIN REMARK 500 5 ARG B 43 0.19 SIDE CHAIN REMARK 500 5 ARG B 46 0.23 SIDE CHAIN REMARK 500 5 ARG B 62 0.32 SIDE CHAIN REMARK 500 6 ARG B 43 0.20 SIDE CHAIN REMARK 500 6 ARG B 46 0.14 SIDE CHAIN REMARK 500 6 ARG B 48 0.12 SIDE CHAIN REMARK 500 6 ARG B 62 0.20 SIDE CHAIN REMARK 500 7 ARG B 43 0.31 SIDE CHAIN REMARK 500 7 ARG B 46 0.28 SIDE CHAIN REMARK 500 7 ARG B 48 0.29 SIDE CHAIN REMARK 500 7 ARG B 62 0.19 SIDE CHAIN REMARK 500 8 ARG B 43 0.23 SIDE CHAIN REMARK 500 8 ARG B 46 0.14 SIDE CHAIN REMARK 500 8 ARG B 48 0.30 SIDE CHAIN REMARK 500 9 ARG B 43 0.30 SIDE CHAIN REMARK 500 9 ARG B 46 0.26 SIDE CHAIN REMARK 500 9 ARG B 48 0.32 SIDE CHAIN REMARK 500 9 ARG B 62 0.29 SIDE CHAIN REMARK 500 10 ARG B 43 0.31 SIDE CHAIN REMARK 500 10 ARG B 46 0.11 SIDE CHAIN REMARK 500 10 ARG B 48 0.32 SIDE CHAIN REMARK 500 10 ARG B 62 0.29 SIDE CHAIN REMARK 500 11 ARG B 43 0.27 SIDE CHAIN REMARK 500 11 ARG B 46 0.12 SIDE CHAIN REMARK 500 11 ARG B 48 0.17 SIDE CHAIN REMARK 500 11 ARG B 62 0.17 SIDE CHAIN REMARK 500 12 ARG B 43 0.19 SIDE CHAIN REMARK 500 12 ARG B 46 0.23 SIDE CHAIN REMARK 500 12 ARG B 48 0.31 SIDE CHAIN REMARK 500 13 ARG B 43 0.28 SIDE CHAIN REMARK 500 13 ARG B 46 0.19 SIDE CHAIN REMARK 500 13 ARG B 48 0.29 SIDE CHAIN REMARK 500 13 ARG B 62 0.30 SIDE CHAIN REMARK 500 14 ARG B 43 0.26 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 76 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1CIR A 2 39 UNP P01053 ICI2_HORVU 21 58 DBREF 1CIR B 41 64 UNP P01053 ICI2_HORVU 60 83 SEQRES 1 A 40 MET LYS THR GLU TRP PRO GLU LEU VAL GLY LYS SER VAL SEQRES 2 A 40 GLU GLU ALA LYS LYS VAL ILE LEU GLN ASP LYS PRO GLU SEQRES 3 A 40 ALA GLN ILE ILE VAL LEU PRO VAL GLY THR ILE VAL THR SEQRES 4 A 40 HSE SEQRES 1 B 24 GLU TYR ARG ILE ASP ARG VAL ARG LEU PHE VAL ASP LYS SEQRES 2 B 24 LEU ASP ASN ILE ALA GLN VAL PRO ARG VAL GLY HELIX 1 1 PRO A 6 LEU A 8 5 3 HELIX 2 2 VAL A 13 ILE A 20 1 8 SHEET 1 A 2 ILE A 30 LEU A 32 0 SHEET 2 A 2 ARG B 48 PHE B 50 1 N LEU B 49 O ILE A 30 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 16 2 Bytes