Header list of 2bbi.pdb file
Complete list - v 29 2 Bytes
HEADER SERINE PROTEASE INHIBITOR 19-SEP-91 2BBI TITLE THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN TITLE 2 BOWMAN-BIRK INHIBITOR IN SOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRYPSIN/CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX; SOURCE 3 ORGANISM_COMMON: SOYBEAN; SOURCE 4 ORGANISM_TAXID: 3847 KEYWDS SERINE PROTEASE INHIBITOR EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR M.H.WERNER,D.E.WEMMER REVDAT 5 29-NOV-17 2BBI 1 HELIX REVDAT 4 25-SEP-13 2BBI 1 REMARK SHEET VERSN REVDAT 3 24-FEB-09 2BBI 1 VERSN REVDAT 2 01-APR-03 2BBI 1 JRNL REVDAT 1 31-OCT-93 2BBI 0 JRNL AUTH M.H.WERNER,D.E.WEMMER JRNL TITL THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN/CHYMOTRYPSIN JRNL TITL 2 BOWMAN-BIRK INHIBITOR IN SOLUTION. JRNL REF BIOCHEMISTRY V. 31 999 1992 JRNL REFN ISSN 0006-2960 JRNL PMID 1734975 JRNL DOI 10.1021/BI00119A008 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.H.WERNER,D.E.WEMMER REMARK 1 TITL 1H ASSIGNMENTS AND SECONDARY STRUCTURE DETERMINATION OF THE REMARK 1 TITL 2 SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR REMARK 1 REF BIOCHEMISTRY V. 30 3356 1991 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2BBI 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_1000177811. 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 : 16 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: 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: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 HIS A 33 CG HIS A 33 ND1 -0.114 REMARK 500 2 HIS A 33 CG HIS A 33 ND1 -0.116 REMARK 500 3 HIS A 33 CG HIS A 33 ND1 -0.123 REMARK 500 4 HIS A 33 CG HIS A 33 ND1 -0.117 REMARK 500 5 HIS A 33 CG HIS A 33 ND1 -0.120 REMARK 500 6 HIS A 33 CG HIS A 33 ND1 -0.120 REMARK 500 7 HIS A 33 CG HIS A 33 ND1 -0.119 REMARK 500 8 HIS A 33 CG HIS A 33 ND1 -0.119 REMARK 500 9 HIS A 33 CG HIS A 33 ND1 -0.118 REMARK 500 10 HIS A 33 CG HIS A 33 ND1 -0.119 REMARK 500 11 HIS A 33 CG HIS A 33 ND1 -0.118 REMARK 500 12 HIS A 33 CG HIS A 33 ND1 -0.117 REMARK 500 13 HIS A 33 CG HIS A 33 ND1 -0.123 REMARK 500 14 HIS A 33 CG HIS A 33 ND1 -0.116 REMARK 500 15 HIS A 33 CG HIS A 33 ND1 -0.117 REMARK 500 16 HIS A 33 CG HIS A 33 ND1 -0.114 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 ASP A 2 -109.93 -111.41 REMARK 500 1 GLU A 3 -175.09 -68.73 REMARK 500 1 ASP A 10 -55.27 -145.10 REMARK 500 1 SER A 17 -141.54 -127.19 REMARK 500 1 ASN A 18 91.21 -160.90 REMARK 500 1 ASP A 26 -81.75 -46.95 REMARK 500 1 LEU A 29 47.08 -78.34 REMARK 500 1 ASN A 30 -97.36 -161.27 REMARK 500 1 CYS A 32 -141.95 -83.99 REMARK 500 1 CYS A 36 -155.45 -104.41 REMARK 500 1 LYS A 37 -60.48 -104.12 REMARK 500 1 LEU A 43 35.41 -73.01 REMARK 500 1 PHE A 57 -2.79 -157.67 REMARK 500 1 CYS A 58 104.60 58.02 REMARK 500 1 LYS A 63 68.66 69.84 REMARK 500 1 SER A 65 136.51 -174.02 REMARK 500 1 ASP A 68 -94.79 -66.08 REMARK 500 1 GLU A 70 21.86 -161.25 REMARK 500 2 GLU A 3 -172.90 -63.63 REMARK 500 2 SER A 4 60.67 -100.37 REMARK 500 2 SER A 5 70.08 -15.30 REMARK 500 2 ASP A 10 -77.71 -133.21 REMARK 500 2 SER A 17 -145.77 -82.61 REMARK 500 2 ASN A 18 92.19 -160.85 REMARK 500 2 ASP A 26 -71.24 -36.97 REMARK 500 2 LEU A 29 -162.54 -58.45 REMARK 500 2 SER A 31 -16.80 -164.97 REMARK 500 2 CYS A 32 162.85 -36.48 REMARK 500 2 HIS A 33 -114.44 -156.30 REMARK 500 2 CYS A 41 138.82 -172.91 REMARK 500 2 LEU A 43 41.72 -73.79 REMARK 500 2 PHE A 57 3.33 -170.05 REMARK 500 2 CYS A 58 97.90 50.71 REMARK 500 2 TYR A 59 146.11 -36.61 REMARK 500 2 CYS A 62 -141.95 -102.68 REMARK 500 2 SER A 65 -75.21 -153.49 REMARK 500 2 GLU A 66 91.85 -40.93 REMARK 500 2 ASP A 68 93.99 -47.41 REMARK 500 2 GLU A 70 -67.41 -93.78 REMARK 500 3 SER A 4 2.53 -67.99 REMARK 500 3 SER A 5 5.25 -67.12 REMARK 500 3 LYS A 6 99.89 -33.25 REMARK 500 3 CYS A 8 -158.25 -135.72 REMARK 500 3 ASP A 10 -47.95 -150.83 REMARK 500 3 SER A 17 -154.88 -156.38 REMARK 500 3 ASN A 18 97.56 -160.25 REMARK 500 3 ASP A 26 -70.74 -37.71 REMARK 500 3 LEU A 29 -86.36 -91.18 REMARK 500 3 ASN A 30 -120.70 -113.50 REMARK 500 3 SER A 34 74.90 -14.12 REMARK 500 REMARK 500 THIS ENTRY HAS 320 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 23 0.31 SIDE CHAIN REMARK 500 1 ARG A 28 0.14 SIDE CHAIN REMARK 500 2 ARG A 23 0.32 SIDE CHAIN REMARK 500 2 ARG A 28 0.27 SIDE CHAIN REMARK 500 3 ARG A 23 0.24 SIDE CHAIN REMARK 500 3 ARG A 28 0.23 SIDE CHAIN REMARK 500 4 ARG A 23 0.32 SIDE CHAIN REMARK 500 4 ARG A 28 0.20 SIDE CHAIN REMARK 500 5 ARG A 23 0.23 SIDE CHAIN REMARK 500 5 ARG A 28 0.31 SIDE CHAIN REMARK 500 6 ARG A 23 0.20 SIDE CHAIN REMARK 500 6 ARG A 28 0.15 SIDE CHAIN REMARK 500 7 ARG A 23 0.29 SIDE CHAIN REMARK 500 7 ARG A 28 0.30 SIDE CHAIN REMARK 500 8 ARG A 23 0.32 SIDE CHAIN REMARK 500 8 ARG A 28 0.10 SIDE CHAIN REMARK 500 9 ARG A 23 0.25 SIDE CHAIN REMARK 500 9 ARG A 28 0.32 SIDE CHAIN REMARK 500 10 ARG A 23 0.27 SIDE CHAIN REMARK 500 10 ARG A 28 0.16 SIDE CHAIN REMARK 500 11 ARG A 23 0.23 SIDE CHAIN REMARK 500 11 ARG A 28 0.14 SIDE CHAIN REMARK 500 12 ARG A 23 0.09 SIDE CHAIN REMARK 500 12 ARG A 28 0.17 SIDE CHAIN REMARK 500 13 ARG A 23 0.32 SIDE CHAIN REMARK 500 13 ARG A 28 0.31 SIDE CHAIN REMARK 500 14 ARG A 23 0.30 SIDE CHAIN REMARK 500 14 ARG A 28 0.28 SIDE CHAIN REMARK 500 15 ARG A 23 0.23 SIDE CHAIN REMARK 500 15 ARG A 28 0.12 SIDE CHAIN REMARK 500 16 ARG A 23 0.27 SIDE CHAIN REMARK 500 16 ARG A 28 0.18 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: T1 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: C1 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1BBI RELATED DB: PDB DBREF 2BBI A 1 71 UNP P01055 IBB1_SOYBN 40 110 SEQRES 1 A 71 ASP ASP GLU SER SER LYS PRO CYS CYS ASP GLN CYS ALA SEQRES 2 A 71 CYS THR LYS SER ASN PRO PRO GLN CYS ARG CYS SER ASP SEQRES 3 A 71 MET ARG LEU ASN SER CYS HIS SER ALA CYS LYS SER CYS SEQRES 4 A 71 ILE CYS ALA LEU SER TYR PRO ALA GLN CYS PHE CYS VAL SEQRES 5 A 71 ASP ILE THR ASP PHE CYS TYR GLU PRO CYS LYS PRO SER SEQRES 6 A 71 GLU ASP ASP LYS GLU ASN SHEET 1 A 2 CYS A 12 THR A 15 0 SHEET 2 A 2 GLN A 21 CYS A 24 -1 O ARG A 23 N ALA A 13 SHEET 1 B 3 MET A 27 ARG A 28 0 SHEET 2 B 3 GLN A 48 CYS A 51 -1 N CYS A 49 O ARG A 28 SHEET 3 B 3 CYS A 39 ALA A 42 -1 N ILE A 40 O PHE A 50 SSBOND 1 CYS A 8 CYS A 62 1555 1555 2.02 SSBOND 2 CYS A 9 CYS A 24 1555 1555 2.00 SSBOND 3 CYS A 12 CYS A 58 1555 1555 2.02 SSBOND 4 CYS A 14 CYS A 22 1555 1555 2.02 SSBOND 5 CYS A 32 CYS A 39 1555 1555 2.02 SSBOND 6 CYS A 36 CYS A 51 1555 1555 2.02 SSBOND 7 CYS A 41 CYS A 49 1555 1555 2.02 CISPEP 1 ASN A 18 PRO A 19 1 -1.42 CISPEP 2 TYR A 45 PRO A 46 1 -0.64 CISPEP 3 ASN A 18 PRO A 19 2 -0.97 CISPEP 4 TYR A 45 PRO A 46 2 -0.27 CISPEP 5 ASN A 18 PRO A 19 3 -1.64 CISPEP 6 TYR A 45 PRO A 46 3 -0.33 CISPEP 7 ASN A 18 PRO A 19 4 -0.34 CISPEP 8 TYR A 45 PRO A 46 4 0.27 CISPEP 9 ASN A 18 PRO A 19 5 -0.38 CISPEP 10 TYR A 45 PRO A 46 5 0.44 CISPEP 11 ASN A 18 PRO A 19 6 -0.80 CISPEP 12 TYR A 45 PRO A 46 6 -0.84 CISPEP 13 ASN A 18 PRO A 19 7 -0.83 CISPEP 14 TYR A 45 PRO A 46 7 -1.27 CISPEP 15 ASN A 18 PRO A 19 8 -0.78 CISPEP 16 TYR A 45 PRO A 46 8 -0.31 CISPEP 17 ASN A 18 PRO A 19 9 -0.18 CISPEP 18 TYR A 45 PRO A 46 9 -0.02 CISPEP 19 ASN A 18 PRO A 19 10 -1.34 CISPEP 20 TYR A 45 PRO A 46 10 -0.15 CISPEP 21 ASN A 18 PRO A 19 11 -0.91 CISPEP 22 TYR A 45 PRO A 46 11 -0.36 CISPEP 23 ASN A 18 PRO A 19 12 -0.52 CISPEP 24 TYR A 45 PRO A 46 12 0.05 CISPEP 25 ASN A 18 PRO A 19 13 -0.31 CISPEP 26 TYR A 45 PRO A 46 13 -1.30 CISPEP 27 ASN A 18 PRO A 19 14 -0.52 CISPEP 28 TYR A 45 PRO A 46 14 0.16 CISPEP 29 ASN A 18 PRO A 19 15 -0.71 CISPEP 30 TYR A 45 PRO A 46 15 0.61 CISPEP 31 ASN A 18 PRO A 19 16 -1.05 CISPEP 32 TYR A 45 PRO A 46 16 0.02 SITE 1 T1 2 LYS A 16 SER A 17 SITE 1 C1 2 LEU A 43 SER A 44 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