Header list of 1bip.pdb file
Complete list - v 29 2 Bytes
HEADER SERINE PROTEINASE INHIBITOR 31-MAR-95 1BIP
TITLE BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI
TITLE 2 (ELEUSINE CORACANA GAERTNERI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE/TRYPSIN INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ELEUSINE CORACANA;
SOURCE 3 ORGANISM_COMMON: FINGER MILLET;
SOURCE 4 ORGANISM_TAXID: 4511;
SOURCE 5 ORGAN: SEED;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRBI-PDI
KEYWDS SERINE PROTEINASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.STROBL,P.MUEHLHAHN,T.HOLAK
REVDAT 3 29-NOV-17 1BIP 1 REMARK HELIX
REVDAT 2 24-FEB-09 1BIP 1 VERSN
REVDAT 1 10-JUL-95 1BIP 0
JRNL AUTH S.STROBL,P.MUHLHAHN,R.BERNSTEIN,R.WILTSCHECK,K.MASKOS,
JRNL AUTH 2 M.WUNDERLICH,R.HUBER,R.GLOCKSHUBER,T.A.HOLAK
JRNL TITL DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE
JRNL TITL 2 BIFUNCTIONAL ALPHA-AMYLASE/TRYPSIN INHIBITOR FROM RAGI SEEDS
JRNL TITL 3 BY NMR SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 34 8281 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7599120
JRNL DOI 10.1021/BI00026A009
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 1BIP 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_1000171804.
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: 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: 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 VAL A 2 -90.85 -133.38
REMARK 500 1 SER A 5 171.64 -56.06
REMARK 500 1 CYS A 6 118.79 64.39
REMARK 500 1 PRO A 8 -96.03 -77.84
REMARK 500 1 ALA A 11 -47.59 84.35
REMARK 500 1 THR A 28 -62.84 -97.05
REMARK 500 1 ARG A 56 -93.19 -50.22
REMARK 500 1 CYS A 57 -36.29 -31.63
REMARK 500 1 LEU A 79 92.48 -58.72
REMARK 500 1 LEU A 97 -75.89 -74.13
REMARK 500 1 VAL A 98 1.18 -64.56
REMARK 500 1 GLU A 102 -83.01 -140.25
REMARK 500 1 CYS A 103 42.28 -146.28
REMARK 500 1 LEU A 105 25.06 45.92
REMARK 500 1 ALA A 106 141.73 64.02
REMARK 500 1 THR A 107 -161.80 -112.50
REMARK 500 1 PHE A 113 161.29 174.05
REMARK 500 1 LEU A 115 -176.88 52.11
REMARK 500 1 SER A 116 24.87 46.79
REMARK 500 1 LEU A 117 -155.56 -63.59
REMARK 500 2 THR A 4 52.27 -151.32
REMARK 500 2 SER A 5 -170.39 -58.38
REMARK 500 2 ALA A 11 -57.11 87.20
REMARK 500 2 THR A 28 -61.09 -93.77
REMARK 500 2 TYR A 54 -71.90 -45.67
REMARK 500 2 ARG A 56 -83.44 -40.38
REMARK 500 2 CYS A 57 -35.88 -32.28
REMARK 500 2 LEU A 79 92.90 -61.04
REMARK 500 2 PRO A 83 99.81 -68.60
REMARK 500 2 LYS A 96 57.28 164.62
REMARK 500 2 GLU A 102 -90.50 -133.71
REMARK 500 2 CYS A 103 37.98 -143.63
REMARK 500 2 ALA A 106 124.08 63.23
REMARK 500 2 PHE A 113 149.75 173.99
REMARK 500 2 LEU A 115 178.84 53.32
REMARK 500 2 SER A 116 19.09 58.68
REMARK 500 2 LEU A 117 -97.81 -62.26
REMARK 500 3 ALA A 11 -56.94 85.72
REMARK 500 3 ASN A 15 61.94 63.36
REMARK 500 3 THR A 28 -64.11 -97.23
REMARK 500 3 ARG A 56 -85.23 -49.21
REMARK 500 3 LEU A 79 91.99 -57.26
REMARK 500 3 PRO A 83 99.40 -66.75
REMARK 500 3 PRO A 95 -164.10 -70.98
REMARK 500 3 GLU A 100 -4.16 -59.06
REMARK 500 3 GLU A 102 -89.39 -140.82
REMARK 500 3 CYS A 103 42.38 -145.02
REMARK 500 3 LEU A 105 27.76 46.30
REMARK 500 3 ALA A 106 150.34 70.34
REMARK 500 3 THR A 107 -163.78 -123.16
REMARK 500
REMARK 500 THIS ENTRY HAS 418 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 A 21 0.25 SIDE CHAIN
REMARK 500 1 ARG A 27 0.22 SIDE CHAIN
REMARK 500 1 ARG A 34 0.25 SIDE CHAIN
REMARK 500 1 ARG A 43 0.25 SIDE CHAIN
REMARK 500 1 ARG A 46 0.26 SIDE CHAIN
REMARK 500 1 ARG A 56 0.16 SIDE CHAIN
REMARK 500 1 ARG A 61 0.27 SIDE CHAIN
REMARK 500 1 ARG A 77 0.28 SIDE CHAIN
REMARK 500 1 ARG A 87 0.30 SIDE CHAIN
REMARK 500 1 ARG A 91 0.31 SIDE CHAIN
REMARK 500 2 ARG A 21 0.19 SIDE CHAIN
REMARK 500 2 ARG A 27 0.31 SIDE CHAIN
REMARK 500 2 ARG A 34 0.27 SIDE CHAIN
REMARK 500 2 ARG A 43 0.24 SIDE CHAIN
REMARK 500 2 ARG A 46 0.22 SIDE CHAIN
REMARK 500 2 ARG A 56 0.24 SIDE CHAIN
REMARK 500 2 ARG A 61 0.29 SIDE CHAIN
REMARK 500 2 ARG A 77 0.30 SIDE CHAIN
REMARK 500 2 ARG A 87 0.32 SIDE CHAIN
REMARK 500 2 ARG A 91 0.15 SIDE CHAIN
REMARK 500 3 ARG A 21 0.23 SIDE CHAIN
REMARK 500 3 ARG A 27 0.20 SIDE CHAIN
REMARK 500 3 ARG A 34 0.32 SIDE CHAIN
REMARK 500 3 ARG A 43 0.28 SIDE CHAIN
REMARK 500 3 ARG A 46 0.23 SIDE CHAIN
REMARK 500 3 ARG A 56 0.13 SIDE CHAIN
REMARK 500 3 ARG A 61 0.23 SIDE CHAIN
REMARK 500 3 ARG A 77 0.24 SIDE CHAIN
REMARK 500 3 ARG A 87 0.23 SIDE CHAIN
REMARK 500 3 ARG A 91 0.27 SIDE CHAIN
REMARK 500 4 ARG A 21 0.31 SIDE CHAIN
REMARK 500 4 ARG A 27 0.22 SIDE CHAIN
REMARK 500 4 ARG A 34 0.32 SIDE CHAIN
REMARK 500 4 ARG A 43 0.30 SIDE CHAIN
REMARK 500 4 ARG A 46 0.23 SIDE CHAIN
REMARK 500 4 ARG A 56 0.31 SIDE CHAIN
REMARK 500 4 ARG A 61 0.26 SIDE CHAIN
REMARK 500 4 ARG A 77 0.23 SIDE CHAIN
REMARK 500 4 ARG A 87 0.24 SIDE CHAIN
REMARK 500 4 ARG A 91 0.25 SIDE CHAIN
REMARK 500 5 ARG A 21 0.18 SIDE CHAIN
REMARK 500 5 ARG A 27 0.22 SIDE CHAIN
REMARK 500 5 ARG A 34 0.22 SIDE CHAIN
REMARK 500 5 ARG A 43 0.20 SIDE CHAIN
REMARK 500 5 ARG A 46 0.31 SIDE CHAIN
REMARK 500 5 ARG A 61 0.32 SIDE CHAIN
REMARK 500 5 ARG A 77 0.29 SIDE CHAIN
REMARK 500 5 ARG A 87 0.20 SIDE CHAIN
REMARK 500 5 ARG A 91 0.22 SIDE CHAIN
REMARK 500 6 ARG A 21 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 195 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: BND
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1BIP A 1 122 UNP P01087 IAAT_ELECO 1 122
SEQADV 1BIP SER A 70 UNP P01087 PRO 70 CONFLICT
SEQRES 1 A 122 SER VAL GLY THR SER CYS ILE PRO GLY MET ALA ILE PRO
SEQRES 2 A 122 HIS ASN PRO LEU ASP SER CYS ARG TRP TYR VAL SER THR
SEQRES 3 A 122 ARG THR CYS GLY VAL GLY PRO ARG LEU ALA THR GLN GLU
SEQRES 4 A 122 MET LYS ALA ARG CYS CYS ARG GLN LEU GLU ALA ILE PRO
SEQRES 5 A 122 ALA TYR CYS ARG CYS GLU ALA VAL ARG ILE LEU MET ASP
SEQRES 6 A 122 GLY VAL VAL THR SER SER GLY GLN HIS GLU GLY ARG LEU
SEQRES 7 A 122 LEU GLN ASP LEU PRO GLY CYS PRO ARG GLN VAL GLN ARG
SEQRES 8 A 122 ALA PHE ALA PRO LYS LEU VAL THR GLU VAL GLU CYS ASN
SEQRES 9 A 122 LEU ALA THR ILE HIS GLY GLY PRO PHE CYS LEU SER LEU
SEQRES 10 A 122 LEU GLY ALA GLY GLU
HELIX 1 H1 ASP A 18 CYS A 29 1 12
HELIX 2 H2 THR A 37 ILE A 51 1 15
HELIX 3 H3 GLU A 58 ASP A 65 1 8
HELIX 4 H4 ARG A 87 ALA A 94 1 8
SHEET 1 S1 2 VAL A 67 THR A 69 0
SHEET 2 S1 2 GLN A 73 GLU A 75 -1 N GLN A 73 O THR A 69
SSBOND 1 CYS A 6 CYS A 55 1555 1555 2.02
SSBOND 2 CYS A 20 CYS A 44 1555 1555 2.03
SSBOND 3 CYS A 29 CYS A 85 1555 1555 2.01
SSBOND 4 CYS A 45 CYS A 103 1555 1555 2.03
SSBOND 5 CYS A 57 CYS A 114 1555 1555 2.02
SITE 1 BND 6 GLY A 32 PRO A 33 ARG A 34 LEU A 35
SITE 2 BND 6 ALA A 36 THR A 37
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 - v 29 2 Bytes