Header list of 1m0v.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 14-JUN-02 1M0V
TITLE NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH
TITLE 2 COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-ACETYL-DEPYDDPF-NH2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE YOPH;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AMINO-TERMINAL DOMAIN (RESIDUES 1-129);
COMPND 5 SYNONYM: VIRULENCE PROTEIN;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SKAP55 HOMOLOGUE;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: SKAP-HOM PEPTIDE;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 633;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. IT IS
SOURCE 9 NATURALLY FOUND IN MUS MUSCULUS (MOUSE).
KEYWDS HIGH RESOLUTION STRUCTURE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.KHANDELWAL,K.KELIIKULI,C.L.SMITH,M.A.SAPER,E.R.P.ZUIDERWEG
REVDAT 4 23-FEB-22 1M0V 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1M0V 1 VERSN
REVDAT 2 11-DEC-02 1M0V 1 JRNL
REVDAT 1 24-JUL-02 1M0V 0
JRNL AUTH P.KHANDELWAL,K.KELIIKULI,C.L.SMITH,M.A.SAPER,E.R.P.ZUIDERWEG
JRNL TITL SOLUTION STRUCTURE AND PHOSPHOPEPTIDE BINDING TO THE
JRNL TITL 2 N-TERMINAL DOMAIN OF YERSINIA YOPH: COMPARISON WITH A
JRNL TITL 3 CRYSTAL STRUCTURE
JRNL REF BIOCHEMISTRY V. 41 11425 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12234185
JRNL DOI 10.1021/BI026333L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.L.SMITH,P.KHANDELWAL,K.KELIIKULI,E.R.P.ZUIDERWEG,M.A.SAPER
REMARK 1 TITL STRUCTURE OF THE TYPE III SECRETION AND SUBSTRATE-BINDING
REMARK 1 TITL 2 DOMAIN OF YERSINIA YOPH PHOSPHATASE
REMARK 1 REF MOL.MICROBIOL. V. 42 967 2001
REMARK 1 REFN ISSN 0950-382X
REMARK 1 DOI 10.1046/J.0950-382X.2001.02711.X
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.KHANDELWAL,K.KELIIKULI,C.L.SMITH,M.A.SAPER,E.R.P.ZUIDERWEG
REMARK 1 TITL 1H, 15N AND 13C ASSIGNMENTS OF THE N-TERMINAL DOMAIN OF
REMARK 1 TITL 2 YERSINIA OUTER PROTEIN H IN ITS APO FORM AND IN COMPLEX WITH
REMARK 1 TITL 3 A PHOSPHOTYROSINE PEPTIDE
REMARK 1 REF J.BIOMOL.NMR V. 21 69 2001
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1011971202626
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, ARIA 1.0
REMARK 3 AUTHORS : NILGES, M. AND O'DONOGHUE, S.I. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 3472 RESTRAINTS, 3222 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 152
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 98 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1M0V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016458.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM YOPHNT U-15N,13C
REMARK 210 COMPLEXED WITH 0.72 MM UNLABELED
REMARK 210 PEPTIDE; 50MM PHOSPHATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-RESOLVED_NOESY; 3D_15N
REMARK 210 -RESOLVED_NOESY; 3D HCCH; 3D 15N/
REMARK 210 13C FILTERED/EDITED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, CNS
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 360
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK: 15N HSQC TITRATIONS
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: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 HIS A 133
REMARK 465 HIS A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
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 O GLY A 94 H GLY A 96 1.51
REMARK 500 O SER A 4 H LEU A 8 1.59
REMARK 500 O ARG A 91 H VAL A 99 1.59
REMARK 500 O ASP A 89 O VAL A 101 2.19
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 2 -163.71 -161.36
REMARK 500 1 GLN A 18 71.44 -170.39
REMARK 500 1 GLU A 19 -38.18 170.30
REMARK 500 1 ASP A 22 82.90 59.97
REMARK 500 1 CYS A 23 -151.90 -133.97
REMARK 500 1 ARG A 28 61.35 161.20
REMARK 500 1 GLU A 36 -72.60 -48.60
REMARK 500 1 THR A 37 -103.43 -86.95
REMARK 500 1 THR A 38 -111.69 164.66
REMARK 500 1 PHE A 39 -164.61 172.54
REMARK 500 1 GLN A 40 37.60 160.34
REMARK 500 1 LEU A 42 135.03 -32.62
REMARK 500 1 THR A 43 36.08 -95.39
REMARK 500 1 SER A 46 -66.01 -101.33
REMARK 500 1 VAL A 63 -74.48 -68.38
REMARK 500 1 ASN A 65 -66.47 159.72
REMARK 500 1 VAL A 66 -127.66 48.11
REMARK 500 1 VAL A 67 -18.83 -174.54
REMARK 500 1 LEU A 68 105.05 32.81
REMARK 500 1 THR A 69 -153.42 -66.12
REMARK 500 1 LYS A 82 -74.49 -48.66
REMARK 500 1 HIS A 83 -80.04 -93.29
REMARK 500 1 ASN A 84 -161.11 -178.36
REMARK 500 1 LEU A 85 87.40 61.91
REMARK 500 1 VAL A 93 -126.01 -164.80
REMARK 500 1 ASN A 95 -56.42 66.22
REMARK 500 1 LEU A 103 -91.38 166.81
REMARK 500 1 SER A 105 157.82 102.53
REMARK 500 1 GLU A 124 -66.65 -96.06
REMARK 500 1 SER A 125 -65.86 -95.72
REMARK 500 1 ARG A 128 105.82 72.08
REMARK 500 1 GLU B 203 -162.62 -65.96
REMARK 500 1 PRO B 207 -163.06 -78.43
REMARK 500 2 ASN A 2 -72.30 -101.92
REMARK 500 2 LEU A 3 -75.23 -164.05
REMARK 500 2 SER A 4 -170.34 171.07
REMARK 500 2 LEU A 5 -63.26 -95.52
REMARK 500 2 GLN A 18 23.90 -140.38
REMARK 500 2 GLU A 19 -69.85 -177.69
REMARK 500 2 CYS A 23 -151.97 -76.28
REMARK 500 2 ARG A 28 54.23 169.77
REMARK 500 2 PHE A 39 -84.87 -68.45
REMARK 500 2 LEU A 42 125.75 3.94
REMARK 500 2 THR A 43 56.98 -91.20
REMARK 500 2 ILE A 44 9.26 49.55
REMARK 500 2 VAL A 63 -82.19 -75.64
REMARK 500 2 ALA A 64 -6.72 72.62
REMARK 500 2 ASN A 65 -61.52 153.46
REMARK 500 2 VAL A 66 -100.96 44.23
REMARK 500 2 VAL A 67 107.87 167.38
REMARK 500
REMARK 500 THIS ENTRY HAS 595 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 209
DBREF 1M0V A 1 129 UNP P08538 YOPH_YERPS 1 129
DBREF 1M0V B 202 208 GB 13277602 AAH03711 73 79
SEQADV 1M0V SER A 130 UNP P08538 EXPRESSION TAG
SEQADV 1M0V HIS A 131 UNP P08538 EXPRESSION TAG
SEQADV 1M0V HIS A 132 UNP P08538 EXPRESSION TAG
SEQADV 1M0V HIS A 133 UNP P08538 EXPRESSION TAG
SEQADV 1M0V HIS A 134 UNP P08538 EXPRESSION TAG
SEQADV 1M0V HIS A 135 UNP P08538 EXPRESSION TAG
SEQADV 1M0V HIS A 136 UNP P08538 EXPRESSION TAG
SEQADV 1M0V PTR B 204 GB 13277602 TYR 75 MODIFIED RESIDUE
SEQRES 1 A 136 MET ASN LEU SER LEU SER ASP LEU HIS ARG GLN VAL SER
SEQRES 2 A 136 ARG LEU VAL GLN GLN GLU SER GLY ASP CYS THR GLY LYS
SEQRES 3 A 136 LEU ARG GLY ASN VAL ALA ALA ASN LYS GLU THR THR PHE
SEQRES 4 A 136 GLN GLY LEU THR ILE ALA SER GLY ALA ARG GLU SER GLU
SEQRES 5 A 136 LYS VAL PHE ALA GLN THR VAL LEU SER HIS VAL ALA ASN
SEQRES 6 A 136 VAL VAL LEU THR GLN GLU ASP THR ALA LYS LEU LEU GLN
SEQRES 7 A 136 SER THR VAL LYS HIS ASN LEU ASN ASN TYR ASP LEU ARG
SEQRES 8 A 136 SER VAL GLY ASN GLY ASN SER VAL LEU VAL SER LEU ARG
SEQRES 9 A 136 SER ASP GLN MET THR LEU GLN ASP ALA LYS VAL LEU LEU
SEQRES 10 A 136 GLU ALA ALA LEU ARG GLN GLU SER GLY ALA ARG GLY SER
SEQRES 11 A 136 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 9 ACE ASP GLU PTR ASP ASP PRO PHE NH2
MODRES 1M0V PTR B 204 TYR O-PHOSPHOTYROSINE
HET ACE B 201 6
HET PTR B 204 24
HET NH2 B 209 3
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM NH2 AMINO GROUP
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 ACE C2 H4 O
FORMUL 2 PTR C9 H12 N O6 P
FORMUL 2 NH2 H2 N
HELIX 1 1 SER A 4 GLN A 17 1 14
HELIX 2 2 ARG A 49 ALA A 64 1 16
HELIX 3 3 THR A 69 HIS A 83 1 15
HELIX 4 4 THR A 109 GLU A 124 1 16
SHEET 1 A 2 THR A 24 LEU A 27 0
SHEET 2 A 2 VAL A 31 ASN A 34 -1 O ASN A 34 N THR A 24
SHEET 1 B 2 TYR A 88 VAL A 93 0
SHEET 2 B 2 ASN A 97 SER A 102 -1 O VAL A 99 N ARG A 91
LINK C ACE B 201 N ASP B 202 1555 1555 1.33
LINK C GLU B 203 N PTR B 204 1555 1555 1.33
LINK C PTR B 204 N ASP B 205 1555 1555 1.33
LINK C PHE B 208 N NH2 B 209 1555 1555 1.33
SITE 1 AC2 1 PHE B 208
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 - b 23 2 Bytes