Header list of 1kio.pdb file
Complete list - 27 20 Bytes
HEADER HYDROLASE 03-DEC-01 1KIO
TITLE SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R,
TITLE 2 K31M]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE INHIBITOR I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 57-91;
COMPND 5 SYNONYM: SCHISTOCERCA GREGARIA CHYMOTRYPSIN INHIBITOR (SGCI);
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS, FMOC STRATEGY,
SOURCE 4 SEQUENCE NATURALLY FOUND IN SCHISTOCERCA GREGARIA (DESERT LOCUST)
KEYWDS SPECIFICITY, PROTEASE INHIBITOR, MODIFIED SPECIFICITY, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Z.GASPARI,A.PATTHY,L.GRAF,A.PERCZEL
REVDAT 5 27-OCT-21 1KIO 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1KIO 1 VERSN
REVDAT 3 01-APR-03 1KIO 1 JRNL
REVDAT 2 27-FEB-02 1KIO 1 JRNL
REVDAT 1 12-DEC-01 1KIO 0
JRNL AUTH Z.GASPARI,A.PATTHY,L.GRAF,A.PERCZEL
JRNL TITL COMPARATIVE STRUCTURE ANALYSIS OF PROTEINASE INHIBITORS FROM
JRNL TITL 2 THE DESERT LOCUST, SCHISTOCERCA GREGARIA.
JRNL REF EUR.J.BIOCHEM. V. 269 527 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 11856311
JRNL DOI 10.1046/J.0014-2956.2001.02685.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 526 NMR DISTANCE RESTRAINTS (150 LONG-RANGE)
REMARK 4
REMARK 4 1KIO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000014996.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 292
REMARK 210 PH : 3.03
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.8MM SGCI[L30R, K31M] NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
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: 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 13 -135.63 45.83
REMARK 500 1 THR A 16 179.12 -51.53
REMARK 500 1 CYS A 17 88.24 -168.75
REMARK 500 1 ARG A 18 98.21 -68.00
REMARK 500 1 SER A 25 116.35 -170.23
REMARK 500 1 CYS A 28 136.78 63.78
REMARK 500 1 ARG A 30 -156.83 -155.37
REMARK 500 2 THR A 8 -33.79 -165.39
REMARK 500 2 THR A 9 165.57 51.53
REMARK 500 2 PHE A 10 168.95 176.46
REMARK 500 2 LYS A 13 -102.97 48.33
REMARK 500 2 THR A 16 -174.62 -52.64
REMARK 500 2 CYS A 17 95.43 174.85
REMARK 500 2 LYS A 24 41.35 170.59
REMARK 500 2 SER A 25 100.32 -172.63
REMARK 500 2 ALA A 26 -150.46 -104.63
REMARK 500 2 ALA A 27 -39.38 -147.28
REMARK 500 2 CYS A 28 134.36 63.69
REMARK 500 3 THR A 3 25.53 176.60
REMARK 500 3 ASP A 12 -82.69 -98.90
REMARK 500 3 LYS A 13 -102.41 -68.20
REMARK 500 3 THR A 16 -166.18 -76.00
REMARK 500 3 CYS A 17 107.68 174.38
REMARK 500 3 LYS A 24 43.16 -149.98
REMARK 500 3 SER A 25 109.72 -172.06
REMARK 500 3 CYS A 28 135.93 63.72
REMARK 500 3 ARG A 30 122.81 73.93
REMARK 500 3 MET A 31 -32.74 -165.18
REMARK 500 3 ALA A 32 136.22 72.63
REMARK 500 4 THR A 3 -20.36 158.97
REMARK 500 4 PHE A 10 164.65 178.55
REMARK 500 4 LYS A 11 -149.72 -58.64
REMARK 500 4 ASP A 12 -26.40 174.88
REMARK 500 4 LYS A 13 -51.04 138.92
REMARK 500 4 CYS A 19 129.20 -34.24
REMARK 500 4 LYS A 24 15.60 -150.45
REMARK 500 4 THR A 29 -89.66 -37.24
REMARK 500 4 ARG A 30 -47.21 -172.81
REMARK 500 4 MET A 31 -75.93 -16.35
REMARK 500 4 ALA A 32 -149.58 -148.98
REMARK 500 5 THR A 8 -30.40 -150.68
REMARK 500 5 THR A 9 122.99 57.76
REMARK 500 5 LYS A 13 -76.84 73.94
REMARK 500 5 CYS A 14 -35.55 -134.77
REMARK 500 5 ASN A 15 -169.20 -118.32
REMARK 500 5 CYS A 19 106.29 69.48
REMARK 500 5 THR A 29 -103.54 -51.41
REMARK 500 5 ARG A 30 34.43 -179.36
REMARK 500 5 MET A 31 -82.41 -55.52
REMARK 500 5 ALA A 32 121.76 158.92
REMARK 500
REMARK 500 THIS ENTRY HAS 92 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 18 0.31 SIDE CHAIN
REMARK 500 1 ARG A 30 0.25 SIDE CHAIN
REMARK 500 2 ARG A 18 0.24 SIDE CHAIN
REMARK 500 2 ARG A 30 0.29 SIDE CHAIN
REMARK 500 3 ARG A 18 0.20 SIDE CHAIN
REMARK 500 3 ARG A 30 0.28 SIDE CHAIN
REMARK 500 4 ARG A 30 0.32 SIDE CHAIN
REMARK 500 5 ARG A 18 0.21 SIDE CHAIN
REMARK 500 5 ARG A 30 0.24 SIDE CHAIN
REMARK 500 6 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 30 0.22 SIDE CHAIN
REMARK 500 7 ARG A 18 0.18 SIDE CHAIN
REMARK 500 7 ARG A 30 0.32 SIDE CHAIN
REMARK 500 8 ARG A 18 0.20 SIDE CHAIN
REMARK 500 8 ARG A 30 0.23 SIDE CHAIN
REMARK 500 9 ARG A 18 0.12 SIDE CHAIN
REMARK 500 9 ARG A 30 0.20 SIDE CHAIN
REMARK 500 10 ARG A 18 0.28 SIDE CHAIN
REMARK 500 10 ARG A 30 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KGM RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI
REMARK 900 RELATED ID: 1PMC RELATED DB: PDB
REMARK 900 PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)
REMARK 900 RELATED ID: 1KJ0 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTI
DBREF 1KIO A 1 35 UNP O46162 SGP1_SCHGR 57 91
SEQADV 1KIO ARG A 30 UNP O46162 LEU 86 ENGINEERED MUTATION
SEQADV 1KIO MET A 31 UNP O46162 LYS 87 ENGINEERED MUTATION
SEQRES 1 A 35 GLU VAL THR CYS GLU PRO GLY THR THR PHE LYS ASP LYS
SEQRES 2 A 35 CYS ASN THR CYS ARG CYS GLY SER ASP GLY LYS SER ALA
SEQRES 3 A 35 ALA CYS THR ARG MET ALA CYS PRO GLN
SHEET 1 A 2 THR A 8 THR A 9 0
SHEET 2 A 2 ARG A 18 CYS A 19 -1 O CYS A 19 N THR A 8
SSBOND 1 CYS A 4 CYS A 19 1555 1555 2.02
SSBOND 2 CYS A 14 CYS A 33 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 28 1555 1555 2.02
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 - 27 20 Bytes