Header list of 1zgg.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 21-APR-05 1ZGG
TITLE SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE
TITLE 2 PHOSPHATASE FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LOW MOLECULAR WEIGHT PROTEIN-TYROSINE-PHOSPHATASE
COMPND 3 YWLE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ALPHA/BETA, FOUR-STRANDED PARALLEL BETA SHEET, STRUCTURAL GENOMICS,
KEYWDS 2 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.XU,B.XIA,C.JIN
REVDAT 3 02-MAR-22 1ZGG 1 REMARK
REVDAT 2 24-FEB-09 1ZGG 1 VERSN
REVDAT 1 28-MAR-06 1ZGG 0
JRNL AUTH H.XU,B.XIA,C.JIN
JRNL TITL SOLUTION STRUCTURE OF A LOW-MOLECULAR-WEIGHT PROTEIN
JRNL TITL 2 TYROSINE PHOSPHATASE FROM BACILLUS SUBTILIS
JRNL REF J.BACTERIOL. V. 188 1509 2006
JRNL REFN ISSN 0021-9193
JRNL PMID 16452434
JRNL DOI 10.1128/JB.188.4.1509-1517.2006
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), DAVID CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZGG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032691.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 0.1M
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM LMW-PTPASE U-15N,13C; 50MM
REMARK 210 SODIUM CHLORIDE 50MM TRIS BUFFER;
REMARK 210 30MM DTT; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR 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: 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 3 ARG A 35 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 8 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 19 ARG A 131 NE - CZ - NH1 ANGL. DEV. = 3.5 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 ASN A 10 -57.56 62.82
REMARK 500 1 ARG A 13 -28.23 -163.28
REMARK 500 1 PRO A 43 6.25 -59.84
REMARK 500 1 TYR A 98 21.77 -75.82
REMARK 500 1 ASP A 148 26.21 -156.56
REMARK 500 1 ARG A 149 15.76 43.79
REMARK 500 2 ASN A 10 -65.11 57.77
REMARK 500 2 ARG A 13 -26.73 -162.43
REMARK 500 2 PRO A 43 8.87 -58.92
REMARK 500 2 ASN A 44 10.91 -140.01
REMARK 500 2 ALA A 47 -155.85 42.99
REMARK 500 2 ASN A 63 21.55 -153.48
REMARK 500 2 TYR A 98 25.09 -75.61
REMARK 500 2 VAL A 109 -57.64 -123.11
REMARK 500 2 ARG A 149 74.74 45.11
REMARK 500 3 ASN A 10 -85.71 33.52
REMARK 500 3 ARG A 13 -28.17 -162.59
REMARK 500 3 PHE A 40 32.42 -141.72
REMARK 500 3 PRO A 43 -0.16 -55.06
REMARK 500 3 ARG A 97 44.31 -66.60
REMARK 500 3 ASP A 148 11.43 -140.43
REMARK 500 4 ASN A 10 -61.28 63.34
REMARK 500 4 ARG A 13 -21.77 -162.53
REMARK 500 4 PRO A 43 13.80 -57.83
REMARK 500 4 ALA A 47 -153.37 41.93
REMARK 500 4 VAL A 109 -50.02 -120.52
REMARK 500 5 ARG A 13 -3.09 -160.60
REMARK 500 5 PRO A 43 8.97 -58.59
REMARK 500 5 ASN A 44 11.97 -140.64
REMARK 500 5 ARG A 149 90.84 -69.83
REMARK 500 6 ARG A 13 -23.71 85.84
REMARK 500 6 PRO A 43 3.46 -57.60
REMARK 500 6 ASN A 44 18.89 -141.79
REMARK 500 6 TYR A 98 23.27 -72.23
REMARK 500 7 ASN A 10 -65.38 -2.03
REMARK 500 7 ARG A 13 -31.22 -159.00
REMARK 500 7 PRO A 43 12.13 -58.61
REMARK 500 7 ALA A 47 -163.00 42.87
REMARK 500 7 ALA A 61 73.39 54.44
REMARK 500 7 TYR A 98 21.29 -71.97
REMARK 500 7 ASP A 148 -154.34 -122.06
REMARK 500 8 ASN A 10 -53.84 61.15
REMARK 500 8 ARG A 13 -27.53 -161.84
REMARK 500 8 PRO A 43 5.97 -61.30
REMARK 500 8 ASN A 44 21.15 -143.25
REMARK 500 8 SER A 66 171.84 -59.78
REMARK 500 9 ASN A 10 -55.84 62.51
REMARK 500 9 ARG A 13 -28.15 -162.15
REMARK 500 9 PRO A 43 2.53 -58.91
REMARK 500 9 ASN A 44 19.59 -141.59
REMARK 500
REMARK 500 THIS ENTRY HAS 124 RAMACHANDRAN OUTLIERS.
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 VAL A 32 ASN A 33 1 149.53
REMARK 500 ASP A 148 ARG A 149 1 -148.77
REMARK 500 VAL A 32 ASN A 33 7 149.30
REMARK 500 VAL A 32 ASN A 33 11 148.68
REMARK 500 ASN A 44 GLY A 45 13 145.44
REMARK 500 VAL A 32 ASN A 33 14 149.01
REMARK 500 VAL A 32 ASN A 33 15 148.74
REMARK 500 ARG A 97 TYR A 98 16 149.99
REMARK 500 VAL A 32 ASN A 33 18 147.56
REMARK 500 ASN A 44 GLY A 45 20 149.24
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 9 ARG A 149 0.15 SIDE CHAIN
REMARK 500 13 ARG A 13 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZGG A 1 150 UNP P39155 YWLE_BACSU 1 150
SEQRES 1 A 150 MET ASP ILE ILE PHE VAL CYS THR GLY ASN THR CYS ARG
SEQRES 2 A 150 SER PRO MET ALA GLU ALA LEU PHE LYS SER ILE ALA GLU
SEQRES 3 A 150 ARG GLU GLY LEU ASN VAL ASN VAL ARG SER ALA GLY VAL
SEQRES 4 A 150 PHE ALA SER PRO ASN GLY LYS ALA THR PRO HIS ALA VAL
SEQRES 5 A 150 GLU ALA LEU PHE GLU LYS HIS ILE ALA LEU ASN HIS VAL
SEQRES 6 A 150 SER SER PRO LEU THR GLU GLU LEU MET GLU SER ALA ASP
SEQRES 7 A 150 LEU VAL LEU ALA MET THR HIS GLN HIS LYS GLN ILE ILE
SEQRES 8 A 150 ALA SER GLN PHE GLY ARG TYR ARG ASP LYS VAL PHE THR
SEQRES 9 A 150 LEU LYS GLU TYR VAL THR GLY SER HIS GLY ASP VAL LEU
SEQRES 10 A 150 ASP PRO PHE GLY GLY SER ILE ASP ILE TYR LYS GLN THR
SEQRES 11 A 150 ARG ASP GLU LEU GLU GLU LEU LEU ARG GLN LEU ALA LYS
SEQRES 12 A 150 GLN LEU LYS LYS ASP ARG ARG
HELIX 1 1 ARG A 13 GLY A 29 1 17
HELIX 2 2 HIS A 50 LYS A 58 1 9
HELIX 3 3 THR A 70 ALA A 77 1 8
HELIX 4 4 THR A 84 GLY A 96 1 13
HELIX 5 5 TYR A 98 ASP A 100 5 3
HELIX 6 6 LYS A 106 GLY A 111 1 6
HELIX 7 7 SER A 123 LYS A 146 1 24
SHEET 1 A 4 ASN A 33 ALA A 37 0
SHEET 2 A 4 ASP A 2 VAL A 6 1 N ILE A 3 O ARG A 35
SHEET 3 A 4 LEU A 79 ALA A 82 1 O LEU A 81 N ILE A 4
SHEET 4 A 4 VAL A 102 THR A 104 1 O PHE A 103 N ALA A 82
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 - r 2 2 Bytes