Header list of 1s7p.pdb file
Complete list - 25 20 Bytes
HEADER ANTIBIOTIC 30-JAN-04 1S7P
TITLE SOLUTION STRUCTURE OF THERMOLYSIN DIGESTED MICROCIN J25
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROCIN J25;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: RESIDUES 48-58;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MICROCIN J25;
COMPND 8 CHAIN: A;
COMPND 9 FRAGMENT: RESIDUES 38-47;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MCJ25A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: MC4100;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTUC202;
SOURCE 10 OTHER_DETAILS: DIGESTED WITH THERMOLYSIN;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 562;
SOURCE 14 GENE: MCJ25A;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: MC4100;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PTUC202;
SOURCE 20 OTHER_DETAILS: DIGESTED WITH THERMOLYSIN
KEYWDS THERMOLYSIN DIGESTED MICROCIN J25, T-MCCJ25, THERMOLYSIN DIGEST, TWO-
KEYWDS 2 CHAIN PEPTIDE, STERIC LINK, ANTIMICROBIAL PROTEIN, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.ROSENGREN,A.BLOND,C.AFONSO,J.C.TABET,S.REBUFFAT,D.J.CRAIK
REVDAT 4 27-JUL-11 1S7P 1 HEADER KEYWDS REMARK REVDAT
REVDAT 3 13-JUL-11 1S7P 1 VERSN
REVDAT 2 24-FEB-09 1S7P 1 VERSN
REVDAT 1 15-JUN-04 1S7P 0
JRNL AUTH K.J.ROSENGREN,A.BLOND,C.AFONSO,J.C.TABET,S.REBUFFAT,
JRNL AUTH 2 D.J.CRAIK
JRNL TITL STRUCTURE OF THERMOLYSIN CLEAVED MICROCIN J25: EXTREME
JRNL TITL 2 STABILITY OF A TWO-CHAIN ANTIMICROBIAL PEPTIDE DEVOID OF
JRNL TITL 3 COVALENT LINKS
JRNL REF BIOCHEMISTRY V. 43 4696 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15096038
JRNL DOI 10.1021/BI0361261
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S7P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-04.
REMARK 100 THE RCSB ID CODE IS RCSB021471.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 6MM T-MCCJ25
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, XEASY 1.3.7, CNS 1.0
REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED USING
REMARK 210 TORSION ANGLE DYNAMICS IN CNS AND
REMARK 210 REFINED IN EXPLICIT SOLVENT.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLU A 8 OE2
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 H2 VAL B 11 O PHE A 10 1.57
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 SER B 18 -159.85 -160.40
REMARK 500 2 PRO B 16 -131.88 -74.63
REMARK 500 2 GLU A 8 58.36 -104.75
REMARK 500 3 HIS A 5 -42.41 -131.22
REMARK 500 3 GLU A 8 55.68 -108.46
REMARK 500 4 THR B 15 132.94 71.05
REMARK 500 4 HIS A 5 -44.54 -133.16
REMARK 500 5 HIS A 5 -44.59 -130.77
REMARK 500 6 ILE B 13 49.92 -77.26
REMARK 500 6 ILE B 17 142.20 71.36
REMARK 500 6 HIS A 5 -44.91 -132.58
REMARK 500 6 GLU A 8 56.78 -115.67
REMARK 500 8 SER B 18 -167.60 -161.79
REMARK 500 8 HIS A 5 -46.42 -132.77
REMARK 500 9 SER B 18 -163.28 -161.51
REMARK 500 9 HIS A 5 -45.61 -132.08
REMARK 500 10 SER B 18 -165.80 -79.34
REMARK 500 10 HIS A 5 -45.14 -132.84
REMARK 500 12 HIS A 5 -45.97 -131.51
REMARK 500 13 PRO B 16 -138.81 -83.16
REMARK 500 13 SER B 18 -159.95 -160.24
REMARK 500 13 HIS A 5 -43.88 -131.74
REMARK 500 14 PRO B 16 44.27 -70.85
REMARK 500 14 SER B 18 -153.68 -159.05
REMARK 500 14 HIS A 5 -43.25 -131.36
REMARK 500 14 GLU A 8 75.73 -105.80
REMARK 500 15 PRO B 16 -148.91 -82.34
REMARK 500 15 HIS A 5 -45.94 -132.52
REMARK 500 16 HIS A 5 -44.33 -132.17
REMARK 500 17 THR B 15 56.48 -148.91
REMARK 500 17 HIS A 5 -45.60 -133.12
REMARK 500 18 HIS A 5 -44.36 -130.29
REMARK 500 18 GLU A 8 61.54 -112.85
REMARK 500 19 HIS A 5 -44.73 -130.05
REMARK 500 20 HIS A 5 -44.23 -132.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q71 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF NATIVE MICROCIN J25
DBREF 1S7P A 1 10 UNP Q9X2V7 MCJA_ECOLI 38 47
DBREF 1S7P B 11 21 UNP Q9X2V7 MCJA_ECOLI 48 58
SEQRES 1 B 11 VAL GLY ILE GLY THR PRO ILE SER PHE TYR GLY
SEQRES 1 A 10 GLY GLY ALA GLY HIS VAL PRO GLU TYR PHE
SHEET 1 A 2 PHE B 19 TYR B 20 0
SHEET 2 A 2 VAL A 6 PRO A 7 -1 O VAL A 6 N TYR B 20
LINK N GLY A 1 CD GLU A 8 1555 1555 1.32
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 - 25 20 Bytes