Header list of 2spz.pdb file
Complete list - 3 20 Bytes
HEADER IMMUNE SYSTEM 29-JUL-98 2SPZ
TITLE STAPHYLOCOCCAL PROTEIN A, Z-DOMAIN, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: Z DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 CELLULAR_LOCATION: CELL WALL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: RV308;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDHZ
KEYWDS IMMUNOGLOBULIN-BINDING PROTEIN, THREE-HELICAL BUNDLE STRUCTURE,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.T.MONTELIONE,M.TASHIRO,R.TEJERO,B.A.LYONS
REVDAT 6 03-NOV-21 2SPZ 1 REMARK SEQADV
REVDAT 5 24-FEB-09 2SPZ 1 VERSN
REVDAT 4 01-APR-03 2SPZ 1 JRNL
REVDAT 3 21-APR-00 2SPZ 1 SPRSDE
REVDAT 2 22-DEC-99 2SPZ 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 05-AUG-98 2SPZ 0
SPRSDE 21-APR-00 2SPZ 1SPZ
JRNL AUTH M.TASHIRO,R.TEJERO,D.E.ZIMMERMAN,B.CELDA,B.NILSSON,
JRNL AUTH 2 G.T.MONTELIONE
JRNL TITL HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE Z DOMAIN OF
JRNL TITL 2 STAPHYLOCOCCAL PROTEIN A.
JRNL REF J.MOL.BIOL. V. 272 573 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9325113
JRNL DOI 10.1006/JMBI.1997.1265
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.JENDEBERG,M.TASHIRO,R.TEJERO,B.A.LYONS,M.UHLEN,
REMARK 1 AUTH 2 G.T.MONTELIONE,B.NILSSON
REMARK 1 TITL THE MECHANISM OF BINDING STAPHYLOCOCCAL PROTEIN A TO
REMARK 1 TITL 2 IMMUNOGLOBIN G DOES NOT INVOLVE HELIX UNWINDING
REMARK 1 REF BIOCHEMISTRY V. 35 22 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.TASHIRO,G.T.MONTELIONE
REMARK 1 TITL STRUCTURES OF BACTERIAL IMMUNOGLOBULIN-BINDING DOMAINS AND
REMARK 1 TITL 2 THEIR COMPLEXES WITH IMMUNOGLOBULIN
REMARK 1 REF CURR.OPIN.STRUCT.BIOL. V. 5 471 1995
REMARK 1 REFN ISSN 0959-440X
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.A.LYONS,M.TASHIRO,L.CEDERGREN,B.NILSSON,G.T.MONTELIONE
REMARK 1 TITL AN IMPROVED STRATEGY FOR DETERMINING RESONANCE ASSIGNMENTS
REMARK 1 TITL 2 FOR ISOTOPICALLY ENRICHED PROTEINS AND ITS APPLICATION TO AN
REMARK 1 TITL 3 ENGINEERED DOMAIN OF STAPHYLOCOCCAL PROTEIN A
REMARK 1 REF BIOCHEMISTRY V. 32 7839 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CONGEN
REMARK 3 AUTHORS : BRUCCOLERI,KARPLUS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 2SPZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008044.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 10 MILLIMOLAR K2HPO4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE REMARKS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : MODIFIED UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, CONGEN
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST CONFORMATIONAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL NMR EXPERIMENTS CONDUCTED: 2D PFG-[15N]HSQC, 3D PFG
REMARK 210 -HNCO, 3D PFG-(HA)CA(CO)NH, 3D PFG-HA(CA)(CO)NH, 3D PFG-HA(CA)NH,
REMARK 210 3D PFG-CBCANH, 3D PFG-CBCA(CO)NH, 3D PFG- (HA)CANH, 3D PFG-
REMARK 210 HN(CA)CO, 3D PFG-HCCNH-TOCSY, 3D PFG-HCC (CO)NH-TOCSY, 2D CT
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 2 HIS A 18 NE2 HIS A 18 CD2 -0.066
REMARK 500 3 HIS A 18 NE2 HIS A 18 CD2 -0.068
REMARK 500 6 HIS A 18 NE2 HIS A 18 CD2 -0.066
REMARK 500 7 HIS A 18 NE2 HIS A 18 CD2 -0.068
REMARK 500 8 HIS A 18 NE2 HIS A 18 CD2 -0.067
REMARK 500 9 HIS A 18 NE2 HIS A 18 CD2 -0.066
REMARK 500 10 HIS A 18 NE2 HIS A 18 CD2 -0.068
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 ARG A 27 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 GLN A 32 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 2 PHE A 5 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 2 PHE A 5 CB - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 2 PHE A 5 CB - CG - CD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 2 PHE A 30 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 PHE A 30 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 2 GLN A 32 N - CA - CB ANGL. DEV. = -14.7 DEGREES
REMARK 500 3 GLN A 9 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 3 GLN A 9 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 3 PHE A 13 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 TYR A 14 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 3 TYR A 14 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 PHE A 30 CB - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 3 PHE A 30 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 3 GLN A 32 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 4 TYR A 14 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 4 GLN A 32 N - CA - CB ANGL. DEV. = -10.8 DEGREES
REMARK 500 5 GLN A 9 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 5 ARG A 27 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 5 PHE A 30 CB - CG - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 5 PHE A 30 CB - CG - CD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 6 GLN A 9 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 6 PHE A 30 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 6 LEU A 44 CB - CG - CD1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 7 PHE A 13 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 7 PHE A 13 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 7 PHE A 30 CB - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 7 PHE A 30 CB - CG - CD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 7 GLN A 32 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 8 TYR A 14 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 8 GLN A 32 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 9 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 9 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 PHE A 30 CB - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 9 PHE A 30 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 10 GLN A 9 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 10 PHE A 13 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 10 TYR A 14 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 10 TYR A 14 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 10 PHE A 30 CB - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 10 PHE A 30 CB - CG - CD1 ANGL. DEV. = -4.8 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 ASP A 2 -169.25 -71.92
REMARK 500 1 PHE A 5 82.39 -67.68
REMARK 500 1 ASN A 6 -130.24 -109.89
REMARK 500 1 LYS A 7 -106.55 -39.58
REMARK 500 1 ASN A 23 -19.32 -153.35
REMARK 500 1 GLU A 24 -133.04 -73.36
REMARK 500 1 PRO A 38 -83.48 -71.14
REMARK 500 1 ALA A 56 -111.34 -92.62
REMARK 500 2 ASP A 2 -81.41 -39.49
REMARK 500 2 ASN A 3 -60.91 -160.42
REMARK 500 2 LEU A 19 104.72 -58.56
REMARK 500 2 ASN A 21 44.15 -140.64
REMARK 500 3 PHE A 5 -122.75 -86.54
REMARK 500 3 GLU A 8 33.93 -89.90
REMARK 500 3 GLN A 9 -80.61 -44.63
REMARK 500 3 LEU A 19 102.55 -58.33
REMARK 500 3 ALA A 56 -92.11 -90.15
REMARK 500 4 ASP A 2 -109.69 -67.59
REMARK 500 4 ASN A 3 92.25 -160.36
REMARK 500 4 LYS A 4 43.40 -78.27
REMARK 500 4 LYS A 7 -136.97 -90.24
REMARK 500 4 LEU A 19 104.85 -54.25
REMARK 500 4 ASN A 21 30.70 -83.85
REMARK 500 4 ASP A 37 -58.73 -143.70
REMARK 500 4 ALA A 56 -76.05 -91.14
REMARK 500 5 ASP A 2 -157.23 -68.73
REMARK 500 5 PRO A 38 -72.93 -76.28
REMARK 500 6 ASP A 2 -138.19 -84.74
REMARK 500 6 ASN A 6 -53.84 -139.09
REMARK 500 6 LYS A 7 -141.62 -71.94
REMARK 500 6 LEU A 19 96.35 -53.10
REMARK 500 6 ASN A 23 -155.57 -71.82
REMARK 500 6 GLU A 24 -66.60 -90.58
REMARK 500 6 SER A 39 -88.67 -100.24
REMARK 500 7 ASP A 2 -155.85 -85.50
REMARK 500 7 ASN A 6 -155.01 -93.96
REMARK 500 7 LYS A 7 -89.54 -39.01
REMARK 500 7 LEU A 19 100.80 -54.61
REMARK 500 7 PRO A 38 -96.68 -69.02
REMARK 500 8 ASP A 2 -92.82 -65.52
REMARK 500 8 LYS A 7 -84.28 -53.56
REMARK 500 8 ASN A 23 -34.34 -151.50
REMARK 500 8 GLU A 24 -132.66 -75.00
REMARK 500 8 PRO A 38 -92.66 -102.38
REMARK 500 9 ASP A 2 -91.27 -77.68
REMARK 500 9 LYS A 7 -77.77 -55.27
REMARK 500 9 LEU A 22 111.82 -160.02
REMARK 500 9 ASN A 23 2.94 -154.82
REMARK 500 9 GLU A 24 -132.88 -87.16
REMARK 500 9 PRO A 38 -121.02 -97.19
REMARK 500
REMARK 500 THIS ENTRY HAS 59 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 27 0.29 SIDE CHAIN
REMARK 500 2 ARG A 27 0.32 SIDE CHAIN
REMARK 500 4 ARG A 27 0.29 SIDE CHAIN
REMARK 500 5 ARG A 27 0.17 SIDE CHAIN
REMARK 500 8 ARG A 27 0.26 SIDE CHAIN
REMARK 500 9 ARG A 27 0.20 SIDE CHAIN
REMARK 500 10 ARG A 27 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2SPZ A 1 58 UNP P38507 SPA2_STAAU 212 269
SEQADV 2SPZ VAL A 1 UNP P38507 ALA 212 ENGINEERED MUTATION
SEQADV 2SPZ ALA A 29 UNP P38507 GLY 240 ENGINEERED MUTATION
SEQRES 1 A 58 VAL ASP ASN LYS PHE ASN LYS GLU GLN GLN ASN ALA PHE
SEQRES 2 A 58 TYR GLU ILE LEU HIS LEU PRO ASN LEU ASN GLU GLU GLN
SEQRES 3 A 58 ARG ASN ALA PHE ILE GLN SER LEU LYS ASP ASP PRO SER
SEQRES 4 A 58 GLN SER ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN
SEQRES 5 A 58 ASP ALA GLN ALA PRO LYS
HELIX 1 1 ASN A 6 LEU A 19 1 14
HELIX 2 2 GLU A 24 ASP A 37 1 14
HELIX 3 3 GLN A 40 ALA A 56 1 17
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 - 3 20 Bytes