Header list of 1mvz.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE INHIBITOR 27-SEP-02 1MVZ TITLE NMR SOLUTION STRUCTURE OF A BOWMAN BIRK INHIBITOR ISOLATED FROM SNAIL TITLE 2 MEDIC SEEDS (MEDICAGO SCUTELLATA) COMPND MOL_ID: 1; COMPND 2 MOLECULE: BOWMAN-BIRK TYPE PROTEASE INHIBITOR, (MSTI); COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MSTI SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MEDICAGO SCUTELLATA; SOURCE 3 ORGANISM_TAXID: 36901; SOURCE 4 TISSUE: SEEDS KEYWDS SERINE PROTEASE INHIBITOR, THREE STRANDED BETA-SHEET, VIB TYPE TURN, KEYWDS 2 HYDROLASE INHIBITOR EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR M.CATALANO,L.RAGONA,H.MOLINARI,A.TAVA,L.ZETTA REVDAT 4 23-FEB-22 1MVZ 1 REMARK REVDAT 3 24-FEB-09 1MVZ 1 VERSN REVDAT 2 02-DEC-03 1MVZ 1 DBREF SEQADV REVDAT 1 22-APR-03 1MVZ 0 JRNL AUTH M.CATALANO,L.RAGONA,H.MOLINARI,A.TAVA,L.ZETTA JRNL TITL ANTICARCINOGENIC BOWMAN BIRK INHIBITOR ISOLATED FROM SNAIL JRNL TITL 2 MEDIC SEEDS (MEDICAGO SCUTELLATA): SOLUTION STRUCTURE AND JRNL TITL 3 ANALYSIS OF SELF-ASSOCIATION BEHAVIOUR JRNL REF BIOCHEMISTRY V. 42 2836 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12627949 JRNL DOI 10.1021/BI020576W REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, DISCOVER 98 REMARK 3 AUTHORS : BRUKER (XWINNMR), MSI (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1MVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-02. REMARK 100 THE DEPOSITION ID IS D_1000017233. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290; 300; 310; 320 REMARK 210 PH : 5.6; 5.6; 5.6; 5.6 REMARK 210 IONIC STRENGTH : 20MM NA; 20MM NA; 20MM NA; 20MM REMARK 210 NA REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM MSTI, 20MM PHOSPHATE BUFFER REMARK 210 NA; 1MM MSTI, 20MM PHOSPHATE REMARK 210 BUFFER NA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 700 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION REMARK 210 ANGLE DYNAMICS ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 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: 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: 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 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 2 GLU A 29 CD GLU A 29 OE2 0.111 REMARK 500 3 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 4 GLU A 29 CD GLU A 29 OE2 0.111 REMARK 500 5 GLU A 29 CD GLU A 29 OE2 0.110 REMARK 500 6 GLU A 29 CD GLU A 29 OE2 0.111 REMARK 500 7 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 8 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 9 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 10 GLU A 29 CD GLU A 29 OE2 0.111 REMARK 500 11 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 12 GLU A 29 CD GLU A 29 OE2 0.110 REMARK 500 13 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 14 GLU A 29 CD GLU A 29 OE2 0.112 REMARK 500 15 GLU A 29 CD GLU A 29 OE2 0.112 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 2 -58.16 -159.37 REMARK 500 1 CYS A 8 -168.75 -122.49 REMARK 500 1 ASP A 10 -74.94 -132.71 REMARK 500 1 CYS A 12 72.52 -119.96 REMARK 500 1 ARG A 28 -150.25 -162.91 REMARK 500 1 GLU A 29 -142.96 -68.72 REMARK 500 1 SER A 33 21.59 -78.48 REMARK 500 1 ALA A 34 64.34 -155.30 REMARK 500 1 SER A 43 -178.09 -69.33 REMARK 500 2 THR A 5 44.68 -155.06 REMARK 500 2 ALA A 7 95.89 -66.37 REMARK 500 2 ASP A 10 -77.01 -108.44 REMARK 500 2 CYS A 12 67.08 -118.14 REMARK 500 2 ARG A 28 -156.37 -165.06 REMARK 500 2 GLU A 29 -137.89 -78.67 REMARK 500 3 ALA A 7 101.66 -58.68 REMARK 500 3 ASP A 10 -62.99 -142.84 REMARK 500 3 CYS A 12 75.01 -118.04 REMARK 500 3 GLU A 29 -144.92 -71.99 REMARK 500 3 ALA A 34 44.59 -105.96 REMARK 500 4 CYS A 9 142.02 -171.35 REMARK 500 4 ASP A 10 -73.02 -103.61 REMARK 500 4 GLU A 29 -132.86 -77.26 REMARK 500 5 THR A 6 173.70 -59.85 REMARK 500 5 ALA A 7 109.15 -48.39 REMARK 500 5 ASP A 10 -60.91 -105.67 REMARK 500 5 ARG A 28 -150.47 -160.84 REMARK 500 5 GLU A 29 -150.48 -80.05 REMARK 500 5 ALA A 34 48.59 -107.86 REMARK 500 6 ALA A 7 86.24 -69.46 REMARK 500 6 CYS A 8 -168.12 -120.17 REMARK 500 6 ASP A 10 -56.61 -140.34 REMARK 500 6 CYS A 12 68.38 -113.20 REMARK 500 6 GLU A 29 -153.60 -68.38 REMARK 500 6 SER A 33 26.42 -75.05 REMARK 500 6 ALA A 34 62.79 -157.03 REMARK 500 7 LYS A 2 -57.10 -164.29 REMARK 500 7 THR A 5 79.06 1.52 REMARK 500 7 ASP A 10 -70.79 -107.26 REMARK 500 7 ARG A 28 -153.63 -160.07 REMARK 500 7 GLU A 29 -153.83 -76.72 REMARK 500 8 SER A 3 75.48 -114.20 REMARK 500 8 THR A 5 84.64 -1.14 REMARK 500 8 ASP A 10 -68.20 -104.22 REMARK 500 8 CYS A 12 77.49 -117.14 REMARK 500 8 ARG A 28 -153.30 -144.07 REMARK 500 8 GLU A 29 -131.03 -76.20 REMARK 500 8 ALA A 34 46.23 -108.59 REMARK 500 9 LYS A 2 117.59 -167.27 REMARK 500 9 THR A 5 67.41 -150.25 REMARK 500 REMARK 500 THIS ENTRY HAS 89 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 11 TYR A 58 0.09 SIDE CHAIN REMARK 500 15 ARG A 49 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHOR INDICATES THAT THE SEQUENCE IN THE DATABASE REMARK 999 IS INCORRECT DBREF 1MVZ A 1 62 UNP P80321 IBB_MEDSC 1 62 SEQADV 1MVZ ARG A 42 UNP P80321 LEU 42 SEE REMARK 999 SEQADV 1MVZ PHE A 44 UNP P80321 ILE 44 SEE REMARK 999 SEQADV 1MVZ ARG A 49 UNP P80321 HIS 49 SEE REMARK 999 SEQADV 1MVZ SER A 62 UNP P80321 ARG 62 SEE REMARK 999 SEQRES 1 A 62 THR LYS SER THR THR THR ALA CYS CYS ASP PHE CYS PRO SEQRES 2 A 62 CYS THR ARG SER ILE PRO PRO GLN CYS GLN CYS THR ASP SEQRES 3 A 62 VAL ARG GLU LYS CYS HIS SER ALA CYS LYS SER CYS LEU SEQRES 4 A 62 CYS THR ARG SER PHE PRO PRO GLN CYS ARG CYS TYR ASP SEQRES 5 A 62 ILE THR ASP PHE CYS TYR PRO SER CYS SER SHEET 1 A 3 VAL A 27 ARG A 28 0 SHEET 2 A 3 CYS A 48 CYS A 50 -1 O CYS A 48 N ARG A 28 SHEET 3 A 3 CYS A 38 CYS A 40 -1 N LEU A 39 O ARG A 49 SSBOND 1 CYS A 8 CYS A 61 1555 1555 2.04 SSBOND 2 CYS A 9 CYS A 24 1555 1555 2.05 SSBOND 3 CYS A 12 CYS A 57 1555 1555 2.05 SSBOND 4 CYS A 14 CYS A 22 1555 1555 2.05 SSBOND 5 CYS A 31 CYS A 38 1555 1555 2.05 SSBOND 6 CYS A 35 CYS A 50 1555 1555 2.05 SSBOND 7 CYS A 40 CYS A 48 1555 1555 2.05 CISPEP 1 ILE A 18 PRO A 19 1 -3.64 CISPEP 2 PHE A 44 PRO A 45 1 0.24 CISPEP 3 ILE A 18 PRO A 19 2 -9.91 CISPEP 4 PHE A 44 PRO A 45 2 -1.34 CISPEP 5 ILE A 18 PRO A 19 3 -3.58 CISPEP 6 PHE A 44 PRO A 45 3 -2.48 CISPEP 7 ILE A 18 PRO A 19 4 -4.20 CISPEP 8 PHE A 44 PRO A 45 4 -1.47 CISPEP 9 ILE A 18 PRO A 19 5 -6.29 CISPEP 10 PHE A 44 PRO A 45 5 0.86 CISPEP 11 ILE A 18 PRO A 19 6 -1.62 CISPEP 12 PHE A 44 PRO A 45 6 -1.30 CISPEP 13 ILE A 18 PRO A 19 7 -5.64 CISPEP 14 PHE A 44 PRO A 45 7 -2.94 CISPEP 15 ILE A 18 PRO A 19 8 -2.23 CISPEP 16 PHE A 44 PRO A 45 8 0.89 CISPEP 17 ILE A 18 PRO A 19 9 -5.18 CISPEP 18 PHE A 44 PRO A 45 9 -0.37 CISPEP 19 ILE A 18 PRO A 19 10 -3.65 CISPEP 20 PHE A 44 PRO A 45 10 2.36 CISPEP 21 ILE A 18 PRO A 19 11 -1.75 CISPEP 22 PHE A 44 PRO A 45 11 1.67 CISPEP 23 ILE A 18 PRO A 19 12 0.57 CISPEP 24 PHE A 44 PRO A 45 12 -0.13 CISPEP 25 ILE A 18 PRO A 19 13 0.66 CISPEP 26 PHE A 44 PRO A 45 13 -4.72 CISPEP 27 ILE A 18 PRO A 19 14 -5.41 CISPEP 28 PHE A 44 PRO A 45 14 -5.66 CISPEP 29 ILE A 18 PRO A 19 15 -4.96 CISPEP 30 PHE A 44 PRO A 45 15 -0.39 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 23 2 Bytes