Header list of 1paj.pdb file
Complete list - 29 20 Bytes
HEADER FIMBRIAL PROTEIN 25-AUG-93 1PAJ
TITLE NMR SOLUTION STRUCTURE AND FLEXIBILITY OF A PEPTIDE ANTIGEN
TITLE 2 REPRESENTING THE RECEPTOR BINDING DOMAIN OF PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIMBRIAL PROTEIN PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287
KEYWDS FIMBRIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR C.MCINNES,F.D.SONNICHSEN,C.M.KAY,R.S.HODGES,B.D.SYKES
REVDAT 3 29-NOV-17 1PAJ 1 REMARK HELIX
REVDAT 2 24-FEB-09 1PAJ 1 VERSN
REVDAT 1 31-JAN-94 1PAJ 0
JRNL AUTH C.MCINNES,F.D.SONNICHSEN,C.M.KAY,R.S.HODGES,B.D.SYKES
JRNL TITL NMR SOLUTION STRUCTURE AND FLEXIBILITY OF A PEPTIDE ANTIGEN
JRNL TITL 2 REPRESENTING THE RECEPTOR BINDING DOMAIN OF PSEUDOMONAS
JRNL TITL 3 AERUGINOSA.
JRNL REF BIOCHEMISTRY V. 32 13432 1993
JRNL REFN ISSN 0006-2960
JRNL PMID 8257679
JRNL DOI 10.1021/BI00212A008
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.MCINNES,C.M.KAY,R.S.HODGES,B.D.SYKES
REMARK 1 TITL CONFORMATIONAL DIFFERENCES BETWEEN THE CIS AND TRANS PROLINE
REMARK 1 TITL 2 ISOMERS OF A PEPTIDE ANTIGEN REPRESENTING THE RECEPTOR
REMARK 1 TITL 3 BINDING DOMAIN OF PSEUDOMONAS AERUGINOSA
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PAJ 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_1000175566.
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 : 12
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: 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 135 CD GLU A 135 OE2 0.120
REMARK 500 2 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 3 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 4 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 5 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 6 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 7 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 8 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 9 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 10 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 11 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500 12 GLU A 135 CD GLU A 135 OE2 0.120
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ASP A 134 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 1 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 ASP A 132 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 6 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 6 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 7 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 7 ASP A 134 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 8 ASP A 132 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 8 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 9 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 9 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 10 ASP A 132 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 10 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 11 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 11 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 12 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 12 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
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 CYS A 129 -86.21 -74.53
REMARK 500 1 SER A 131 -73.86 -167.50
REMARK 500 1 GLN A 133 49.16 -90.85
REMARK 500 1 ASP A 134 152.79 65.13
REMARK 500 1 CYS A 142 -75.35 -64.68
REMARK 500 2 CYS A 129 -85.80 -88.82
REMARK 500 2 ASP A 132 -111.68 -115.25
REMARK 500 3 ASP A 132 -103.53 -97.96
REMARK 500 3 GLN A 133 79.01 -116.88
REMARK 500 4 CYS A 129 -105.72 -116.78
REMARK 500 4 THR A 130 117.45 -166.01
REMARK 500 4 ASP A 132 -106.51 -144.07
REMARK 500 4 GLN A 133 74.61 -118.00
REMARK 500 4 ASP A 134 -64.97 70.67
REMARK 500 5 CYS A 129 -81.67 -73.42
REMARK 500 5 ASP A 132 -20.92 76.12
REMARK 500 5 ASP A 134 132.86 69.16
REMARK 500 6 CYS A 129 -71.44 -100.86
REMARK 500 6 SER A 143 82.33 60.67
REMARK 500 7 CYS A 129 -78.81 -115.47
REMARK 500 7 ASP A 132 -99.32 -138.20
REMARK 500 7 GLN A 133 51.81 -112.63
REMARK 500 7 ASP A 134 62.52 -160.65
REMARK 500 7 CYS A 142 -87.06 -69.06
REMARK 500 8 CYS A 129 -108.14 -115.05
REMARK 500 8 SER A 131 85.34 56.26
REMARK 500 9 CYS A 129 -92.92 -92.88
REMARK 500 9 SER A 131 -101.59 -116.83
REMARK 500 9 ASP A 132 -25.36 -157.25
REMARK 500 9 GLN A 133 69.18 -105.53
REMARK 500 9 ASP A 134 -81.98 65.25
REMARK 500 9 PRO A 139 -176.26 -63.94
REMARK 500 9 SER A 143 96.87 70.14
REMARK 500 10 ASP A 132 -97.61 -103.67
REMARK 500 10 GLN A 133 77.36 -115.03
REMARK 500 10 ASP A 134 69.03 -115.46
REMARK 500 11 CYS A 129 -69.95 -102.02
REMARK 500 12 CYS A 129 -74.57 -114.69
REMARK 500 12 ASP A 132 -102.11 -117.22
REMARK 500 12 GLN A 133 78.25 -116.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 135 GLN A 136 4 147.07
REMARK 500 PHE A 137 ILE A 138 6 144.43
REMARK 500 PHE A 137 ILE A 138 8 144.96
REMARK 500 PHE A 137 ILE A 138 11 144.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH A 145
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PAK RELATED DB: PDB
DBREF 1PAJ A 128 144 UNP P02973 FMPA_PSEAE 134 150
SEQRES 1 A 18 ACE LYS CYS THR SER ASP GLN ASP GLU GLN PHE ILE PRO
SEQRES 2 A 18 LYS GLY CYS SER LYS
HET ACE A 127 6
HET OH A 145 2
HETNAM ACE ACETYL GROUP
HETNAM OH HYDROXIDE ION
FORMUL 1 ACE C2 H4 O
FORMUL 2 OH H O 1-
SSBOND 1 CYS A 129 CYS A 142 1555 1555 2.00
LINK C ACE A 127 N LYS A 128 1555 1555 1.34
LINK C LYS A 144 O OH A 145 1555 1555 1.38
SITE 1 AC1 2 SER A 143 LYS A 144
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 - 29 20 Bytes