Header list of 1ytp.pdb file
Complete list - v 10 2 Bytes
HEADER HYDROLASE INHIBITOR 10-FEB-05 1YTP TITLE SOLUTION STRUCTURE OF THE C4A/C41A VARIANT OF THE NICOTIANA ALATA TITLE 2 PROTEINASE INHIBITOR T1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEINASE INHIBITOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-53; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NICOTIANA ALATA; SOURCE 3 ORGANISM_COMMON: PERSIAN TOBACCO; SOURCE 4 ORGANISM_TAXID: 4087; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30 KEYWDS BETA-SHEET, POTII INHIBITOR, HYDROLASE INHIBITOR EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.J.SCHIRRA,R.R.RENDA,M.A.ANDERSON,D.J.CRAIK REVDAT 3 10-NOV-21 1YTP 1 REMARK SEQADV REVDAT 2 24-FEB-09 1YTP 1 VERSN REVDAT 1 21-MAR-06 1YTP 0 JRNL AUTH H.J.SCHIRRA,R.R.RENDA,M.A.ANDERSON,D.J.CRAIK JRNL TITL THE STRUCTURE OF A DISULFIDE MUTANT OF THE NICOTIANA ALATA JRNL TITL 2 PROTEINASE INHIBITOR T1 --- STABILISATION OF THE REACTIVE JRNL TITL 3 SITE LOOP IS CRITICAL FOR ACTIVITY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1YTP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-05. REMARK 100 THE DEPOSITION ID IS D_1000031913. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313 REMARK 210 PH : 5.8 REMARK 210 IONIC STRENGTH : 1MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM C4A/C41A-T1; 1MM C4A/C41A-T1 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : ARX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, CCNMR/GLXCC N.A. REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS, EXPLICIT REMARK 210 INCLUSION OF WATER MOLECULES REMARK 210 (LINGE & NILGES, 1999) REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES. 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: 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 THR A 5 -158.61 -166.49 REMARK 500 1 VAL A 24 -65.73 -90.54 REMARK 500 1 PRO A 38 40.65 -82.29 REMARK 500 2 THR A 5 -148.61 -175.93 REMARK 500 2 VAL A 24 -67.43 -103.98 REMARK 500 2 CYS A 25 147.19 -179.11 REMARK 500 2 ASP A 30 130.37 61.42 REMARK 500 2 ASN A 33 -36.60 142.86 REMARK 500 2 PRO A 34 68.71 -69.79 REMARK 500 2 PRO A 38 39.86 -78.32 REMARK 500 2 ASN A 40 152.16 178.14 REMARK 500 3 THR A 5 -154.45 -178.03 REMARK 500 3 VAL A 24 -63.81 -92.98 REMARK 500 3 CYS A 25 149.18 -177.18 REMARK 500 3 ASP A 30 71.20 64.92 REMARK 500 3 ARG A 32 -37.53 76.33 REMARK 500 3 ARG A 39 46.11 -90.11 REMARK 500 4 THR A 5 -158.89 -178.52 REMARK 500 4 VAL A 24 -67.46 -99.11 REMARK 500 4 CYS A 25 143.94 -176.71 REMARK 500 4 PRO A 31 32.49 -76.18 REMARK 500 5 THR A 5 -163.11 -178.19 REMARK 500 5 LYS A 12 97.97 -61.95 REMARK 500 5 VAL A 24 -60.31 -93.16 REMARK 500 5 CYS A 25 148.21 -176.33 REMARK 500 5 GLU A 26 42.23 -99.55 REMARK 500 5 GLU A 28 -42.08 -148.56 REMARK 500 5 ARG A 32 40.56 -141.93 REMARK 500 5 PRO A 38 40.28 -79.47 REMARK 500 5 ASN A 40 154.44 173.18 REMARK 500 6 THR A 5 -158.51 -178.20 REMARK 500 6 ALA A 9 33.58 -96.45 REMARK 500 6 VAL A 24 -68.11 -103.32 REMARK 500 6 CYS A 25 146.05 -179.66 REMARK 500 6 PRO A 38 43.70 -82.05 REMARK 500 6 PRO A 43 47.58 -71.88 REMARK 500 6 ARG A 44 -30.80 -156.53 REMARK 500 7 THR A 5 -166.18 -179.77 REMARK 500 7 ASN A 6 -156.46 -161.97 REMARK 500 7 VAL A 24 -60.55 -101.15 REMARK 500 7 ASN A 33 109.46 -162.38 REMARK 500 7 ALA A 41 110.54 178.82 REMARK 500 8 THR A 5 -172.96 -176.95 REMARK 500 8 ASN A 6 -168.57 -161.41 REMARK 500 8 GLU A 26 39.54 -96.70 REMARK 500 8 ASP A 30 -55.36 -174.96 REMARK 500 8 ARG A 32 -37.35 86.33 REMARK 500 8 ASN A 33 126.45 -171.78 REMARK 500 8 PRO A 38 30.65 -88.16 REMARK 500 8 ARG A 39 50.55 -174.61 REMARK 500 REMARK 500 THIS ENTRY HAS 135 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1TIH RELATED DB: PDB REMARK 900 WILD-TYPE PARENT PROTEIN OF THIS VARIANT DBREF 1YTP A 1 53 GB 473591 AAA17739 112 164 SEQADV 1YTP ALA A 4 GB 473591 CYS 115 ENGINEERED MUTATION SEQADV 1YTP ALA A 41 GB 473591 CYS 152 ENGINEERED MUTATION SEQRES 1 A 53 ASP ARG ILE ALA THR ASN CYS CYS ALA GLY THR LYS GLY SEQRES 2 A 53 CYS LYS TYR PHE SER ASP ASP GLY THR PHE VAL CYS GLU SEQRES 3 A 53 GLY GLU SER ASP PRO ARG ASN PRO LYS ALA CYS PRO ARG SEQRES 4 A 53 ASN ALA ASP PRO ARG ILE ALA TYR GLY ILE CYS PRO LEU SEQRES 5 A 53 ALA SHEET 1 A 3 PHE A 23 GLU A 26 0 SHEET 2 A 3 LYS A 15 PHE A 17 -1 N TYR A 16 O CYS A 25 SHEET 3 A 3 TYR A 47 ILE A 49 -1 O TYR A 47 N PHE A 17 SSBOND 1 CYS A 7 CYS A 25 1555 1555 2.03 SSBOND 2 CYS A 8 CYS A 37 1555 1555 2.03 SSBOND 3 CYS A 14 CYS A 50 1555 1555 2.03 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 10 2 Bytes