Header list of 1nmv.pdb file
Complete list - b 23 2 Bytes
HEADER ISOMERASE 11-JAN-03 1NMV
TITLE SOLUTION STRUCTURE OF HUMAN PIN1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ROTAMASE PIN1, PPIASE PIN1;
COMPND 5 EC: 5.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PIN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PPIASE DOMAIN, WW DOMAIN GROUP IV, BETA-ALPHA, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR E.BAYER,S.GOETTSCH,J.W.MUELLER,B.GRIEWEL,E.GUIBERMAN,L.MAYR,P.BAYER
REVDAT 3 23-FEB-22 1NMV 1 REMARK
REVDAT 2 24-FEB-09 1NMV 1 VERSN
REVDAT 1 12-AUG-03 1NMV 0
JRNL AUTH E.BAYER,S.GOETTSCH,J.W.MUELLER,B.GRIEWEL,E.GUIBERMAN,
JRNL AUTH 2 L.M.MAYR,P.BAYER
JRNL TITL STRUCTURAL ANALYSIS OF THE MITOTIC REGULATOR HPIN1 IN
JRNL TITL 2 SOLUTION: INSIGHTS INTO DOMAIN ARCHITECTURE AND SUBSTRATE
JRNL TITL 3 BINDING.
JRNL REF J.BIOL.CHEM. V. 278 26183 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12721297
JRNL DOI 10.1074/JBC.M300721200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.P.LU,S.D.HANNES,T.HUNTER
REMARK 1 TITL A HUMAN PEPTIDYL-PROLYL ISOMERASE ESSENTIAL FOR REGULATION
REMARK 1 TITL 2 OF MITOSIS
REMARK 1 REF NATURE V. 380 544 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/380544A0
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.RANGANATHAN,K.P.LU,T.HUNTER,J.P.NOEL
REMARK 1 TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE MITOTIC ROTAMASE
REMARK 1 TITL 2 PIN1 SUGGESTS SUBSTRATE RECOGNITION IS PHOSPHORYLATION
REMARK 1 TITL 3 DEPENDENT
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 89 875 1997
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)80273-1
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.A.VERDECIA,M.E.BOWMAN,K.P.LU,T.HUNTER,J.P.NOEL
REMARK 1 TITL STRUCTURAL BASIS FOR PHOSPHOSERINE-PROLINE RECOGNITION BY
REMARK 1 TITL 2 GROUP IV WW DOMAINS
REMARK 1 REF NAT.STRUCT.BIOL. V. 7 639 2000
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/77929
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.2, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUENGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NMV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018016.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300
REMARK 210 PH : 6.6; 6.6; 6.6
REMARK 210 IONIC STRENGTH : N.C.; N.C.; N.C.
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6-0.8MM PIN1 U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 1MM DTT, 5MM
REMARK 210 EDTA, 50-100MM NA SULFATE; ~
REMARK 210 0.2MM PIN1 U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 1MM DTT, 5MM
REMARK 210 EDTA, 50-100MM NA SULFATE; 0.6MM
REMARK 210 PIN1 U-15N,13C;50MM TRIS/HCL
REMARK 210 BUFFER, 1MM DTT, 5MM EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HNHA; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.8.11, VNMR 6.18, NDEE
REMARK 210 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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 : 3
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: 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 ALA A 107 N SER A 111 2.16
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 ALA A 2 162.75 -45.33
REMARK 500 1 GLU A 4 89.72 20.89
REMARK 500 1 LYS A 6 -170.05 -175.75
REMARK 500 1 SER A 18 15.62 48.30
REMARK 500 1 SER A 19 -169.36 -115.96
REMARK 500 1 GLU A 35 150.25 63.43
REMARK 500 1 PRO A 37 -89.67 -79.09
REMARK 500 1 SER A 38 -169.56 -102.00
REMARK 500 1 ASN A 40 -80.14 73.12
REMARK 500 1 SER A 41 -84.52 -72.07
REMARK 500 1 SER A 42 -49.44 174.50
REMARK 500 1 GLN A 49 -172.79 57.85
REMARK 500 1 GLU A 51 149.97 62.12
REMARK 500 1 ARG A 69 82.61 -152.15
REMARK 500 1 SER A 71 137.09 -171.62
REMARK 500 1 THR A 79 46.56 -150.65
REMARK 500 1 ASP A 153 -72.89 4.67
REMARK 500 2 ALA A 2 32.36 -146.02
REMARK 500 2 ASP A 3 52.53 -167.79
REMARK 500 2 LYS A 6 124.72 -177.21
REMARK 500 2 LEU A 7 77.40 59.20
REMARK 500 2 PRO A 8 -177.74 -52.12
REMARK 500 2 SER A 18 23.47 40.67
REMARK 500 2 SER A 19 -74.27 -100.18
REMARK 500 2 GLU A 35 164.81 63.06
REMARK 500 2 SER A 38 -165.99 -102.05
REMARK 500 2 SER A 41 139.38 73.93
REMARK 500 2 LYS A 46 -45.02 -161.77
REMARK 500 2 ASN A 47 177.19 62.75
REMARK 500 2 GLN A 49 100.54 -176.40
REMARK 500 2 SER A 114 0.04 -61.52
REMARK 500 3 ALA A 2 -35.38 -177.62
REMARK 500 3 LYS A 6 -174.19 -175.86
REMARK 500 3 LEU A 7 78.14 58.40
REMARK 500 3 PRO A 8 174.17 -58.72
REMARK 500 3 SER A 16 -168.05 -62.21
REMARK 500 3 ARG A 17 85.35 -57.81
REMARK 500 3 SER A 18 22.73 41.45
REMARK 500 3 SER A 19 -78.72 -77.45
REMARK 500 3 GLU A 35 176.13 57.48
REMARK 500 3 ASN A 40 -52.86 -127.47
REMARK 500 3 SER A 41 -164.14 -164.09
REMARK 500 3 SER A 42 140.38 67.52
REMARK 500 3 SER A 43 109.19 -161.61
REMARK 500 3 GLN A 49 -168.51 60.98
REMARK 500 3 THR A 81 -179.97 -56.95
REMARK 500 3 ASP A 153 -46.16 -27.55
REMARK 500 4 ALA A 2 91.27 64.75
REMARK 500 4 ASP A 3 133.76 -178.04
REMARK 500 4 GLU A 4 47.31 -178.34
REMARK 500
REMARK 500 THIS ENTRY HAS 161 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PIN RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HPIN1 WITH ALA-PRO PEPTIDE COMPLEXED TO PPIASE
REMARK 900 DOMAIN
REMARK 900 RELATED ID: 1F8A RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HPIN1 WITH CTD PEPTIDE COMPLEXED TO WW DOMAIN
REMARK 900 RELATED ID: 1I8G RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25
REMARK 900 RELATED ID: 1I6C RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF PIN1 WW DOMAIN
REMARK 900 RELATED ID: 5305 RELATED DB: BMRB
REMARK 900 ASSIGNMENTS OF HPIN1
REMARK 900 RELATED ID: 4882 RELATED DB: BMRB
REMARK 900 ASSIGNMENTS OF THE WW DOMAIN OF HPIN1
REMARK 900 RELATED ID: 1NMW RELATED DB: PDB
DBREF 1NMV A 1 163 UNP Q13526 PIN1_HUMAN 1 163
SEQRES 1 A 163 MET ALA ASP GLU GLU LYS LEU PRO PRO GLY TRP GLU LYS
SEQRES 2 A 163 ARG MET SER ARG SER SER GLY ARG VAL TYR TYR PHE ASN
SEQRES 3 A 163 HIS ILE THR ASN ALA SER GLN TRP GLU ARG PRO SER GLY
SEQRES 4 A 163 ASN SER SER SER GLY GLY LYS ASN GLY GLN GLY GLU PRO
SEQRES 5 A 163 ALA ARG VAL ARG CYS SER HIS LEU LEU VAL LYS HIS SER
SEQRES 6 A 163 GLN SER ARG ARG PRO SER SER TRP ARG GLN GLU LYS ILE
SEQRES 7 A 163 THR ARG THR LYS GLU GLU ALA LEU GLU LEU ILE ASN GLY
SEQRES 8 A 163 TYR ILE GLN LYS ILE LYS SER GLY GLU GLU ASP PHE GLU
SEQRES 9 A 163 SER LEU ALA SER GLN PHE SER ASP CYS SER SER ALA LYS
SEQRES 10 A 163 ALA ARG GLY ASP LEU GLY ALA PHE SER ARG GLY GLN MET
SEQRES 11 A 163 GLN LYS PRO PHE GLU ASP ALA SER PHE ALA LEU ARG THR
SEQRES 12 A 163 GLY GLU MET SER GLY PRO VAL PHE THR ASP SER GLY ILE
SEQRES 13 A 163 HIS ILE ILE LEU ARG THR GLU
HELIX 1 1 THR A 81 GLY A 99 1 19
HELIX 2 2 ASP A 102 SER A 111 1 10
HELIX 3 3 CYS A 113 ARG A 119 5 7
HELIX 4 4 GLN A 131 LEU A 141 1 11
SHEET 1 A 3 TRP A 11 MET A 15 0
SHEET 2 A 3 VAL A 22 ASN A 26 -1 O PHE A 25 N GLU A 12
SHEET 3 A 3 ALA A 31 GLN A 33 -1 O GLN A 33 N TYR A 24
SHEET 1 B 4 ASP A 121 SER A 126 0
SHEET 2 B 4 ARG A 54 LYS A 63 -1 N VAL A 55 O PHE A 125
SHEET 3 B 4 GLY A 155 GLU A 163 -1 O THR A 162 N ARG A 56
SHEET 4 B 4 VAL A 150 PHE A 151 -1 N VAL A 150 O HIS A 157
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