Header list of 1d8v.pdb file
Complete list - 16 20 Bytes
HEADER ANTITUMOR PROTEIN 26-OCT-99 1D8V
TITLE THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTI-HIV AND ANTI-TUMOR PROTEIN MAP30;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MOMORDICA CHARANTIA;
SOURCE 3 ORGANISM_COMMON: BALSAM PEAR;
SOURCE 4 ORGANISM_TAXID: 3673
KEYWDS SINGLE CHAIN, ANTITUMOR PROTEIN
EXPDTA SOLUTION NMR
AUTHOR Y.-X.WANG,N.NEAMATI,J.JACOB,I.PALMER,S.J.STAHL
REVDAT 5 16-FEB-22 1D8V 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1D8V 1 VERSN
REVDAT 3 01-APR-03 1D8V 1 JRNL
REVDAT 2 10-MAY-00 1D8V 1 DBREF SEQADV REMARK
REVDAT 1 19-NOV-99 1D8V 0
JRNL AUTH Y.X.WANG,N.NEAMATI,J.JACOB,I.PALMER,S.J.STAHL,J.D.KAUFMAN,
JRNL AUTH 2 P.L.HUANG,P.L.HUANG,H.E.WINSLOW,Y.POMMIER,P.T.WINGFIELD,
JRNL AUTH 3 S.LEE-HUANG,A.BAX,D.A.TORCHIA
JRNL TITL SOLUTION STRUCTURE OF ANTI-HIV-1 AND ANTI-TUMOR PROTEIN
JRNL TITL 2 MAP30: STRUCTURAL INSIGHTS INTO ITS MULTIPLE FUNCTIONS.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 99 433 1999
JRNL REFN ISSN 0092-8674
JRNL PMID 10571185
JRNL DOI 10.1016/S0092-8674(00)81529-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : MODIFIED X-PLOR 3.5
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 WE CALCULATED THE STRUCTURE OF MAP30 USING SIMULATED ANNEALING IN
REMARK 3 TORSION ANGLE SPACE STARTING FROM AN EXTENDED STRAND, FOLLOWED BY
REMARK 3 SIMULATED ANEALING IN CARTESIAN SPACE USING A MODIFIED XPLOR 3.5,
REMARK 3 CONTAINING PSEUDOPOTENTIALS FOR RESIDUAL DIPOLAR COUPLING AND A
REMARK 3 CONFORMATIONAL DATABASE. HYDROGEN BOND CONSTRAINTS, TWO FOR EACH
REMARK 3 HYDROGEN BOND (NH-O = 1.5-2.8 A AND N-O = 2.4-3.5 A), WERE DERIVED
REMARK 3 FROM NH EXCHANGE EXPERIMENTS, BACKBONE NOE PATTERNS, BACKBONE CA/
REMARK 3 CB CHEMICAL SHIFTS AND DIRECT MEASUREMENTS OF 3HJNC CONNECTIVITY
REMARK 3 ACROSS HYDROGEN BONDS, AND APPLIED IN THE LATER STAGE OF THE
REMARK 3 STRUCTURE CALCULATION. PHI AND PSI ANGLES WERE DERIVED FROM THREE-
REMARK 3 BOND 3JHNHA COUPLING CONSTANTS,
REMARK 3 MEASURED WITH THE 3D HNHA EXPERIMENT AND A DATABASE ANALYSIS OF
REMARK 3 BACKBONE (1H, 15N, 13CA, 13CB AND C) CHEMICAL SHIFTS, USING THE
REMARK 3 PROGRAM TALOS. THE PHI DIHEDRAL ANGLE WAS RESTRAINED TO -60
REMARK 3 DEGREES PLUS-MINUS 30 DEGREES IF JHNHA < 5.5 HZ OR TO 110 DEGREES
REMARK 3 PLUS-MINUS 50 DEGREES IF
REMARK 3 JHNHA >8.0 HZ. CHI 1 DIHEDRAL ANGLES AND STEREOSPECIFIC
REMARK 3 ASSIGNMENTS OF BETA-
REMARK 3 METHYLENE PROTONS WERE DERIVED FROM JHNHB AND JHAHB SCALAR
REMARK 3 COUPLING CONSTANTS
REMARK 3 OBTAINED FROM 3D HNHB AND HACAHB-COSY EXPERIMENTS. TIGHT TURNS
REMARK 3 CLEARLY
REMARK 3 IDENTIFIED BY NOE PATTERNS AND J-COUPLING CONSTANTS, PHI AND PSI
REMARK 3 ANGLES WERE
REMARK 3 RESTRAINED TO THEIR STANDARD VALUES WITH PLUS-MINUS 30 DEGREES
REMARK 3 ERROR RANGE. FOR RESIDUES HAVING INTENSE INTRARESIDUE HN-HA NOES
REMARK 3 WITH POSITIVE PHI ANGLES SUGGESTED BY THE
REMARK 3 PROGRAM TALOS, PHI WAS RESTRAINED TO 40 DEGREES PLUS-MINUS 15
REMARK 3 DEGREES. ELECTROSTATIC SURFACES WERE
REMARK 3 CALCULATED USING GRASP. MOLECULAR MODELS WERE GENERATED WITH
REMARK 3 QUANTA (MSI),
REMARK 3 INSIGHT (MSI) AND MOLSCRIPT.
REMARK 4
REMARK 4 1D8V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009899.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313.00
REMARK 210 PH : 5.50
REMARK 210 IONIC STRENGTH : 10 MM NAPI
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : ~0.7 MM PROTEIN MAP30 (15N/13C)
REMARK 210 ENRICHED.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_ NOESY; 3D_
REMARK 210 13C-SEPARATED_ NOESY; 4D_13C-
REMARK 210 SEPARATED_ NOESY; HNHA; HNCA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MODIFIED X-PLOR 3.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THIS STRUCTURE WAS DETERMINED USING DIPOLAR COUPLING MEASURED IN
REMARK 210 LIQUID
REMARK 210 CRYSTAL MEDIA. IN ADDITION, WE ALSO MEASURED HYDROGEN BONDS
REMARK 210 DIRECTLY AND USED
REMARK 210 THEM IN STRUCTURE CALCULATIONS.
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 OG1 THR A 10 HG1 THR A 13 1.27
REMARK 500 O THR A 106 H ASN A 108 1.37
REMARK 500 O SER A 42 H ARG A 46 1.57
REMARK 500 O ASN A 141 H ALA A 145 1.58
REMARK 500 O THR A 10 H TYR A 14 1.60
REMARK 500 O LEU A 256 N GLY A 258 2.08
REMARK 500 O LEU A 152 OG1 THR A 156 2.18
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 PRO A 26 -169.22 -58.93
REMARK 500 PRO A 35 170.89 -59.27
REMARK 500 TYR A 38 -167.10 -65.86
REMARK 500 THR A 67 -85.35 -59.24
REMARK 500 ARG A 77 -123.60 46.26
REMARK 500 PHE A 83 -159.14 -86.71
REMARK 500 GLU A 85 -7.09 73.64
REMARK 500 SER A 86 -57.99 -163.22
REMARK 500 GLU A 89 -13.73 -47.30
REMARK 500 LEU A 94 -118.55 -49.77
REMARK 500 PRO A 104 -2.45 -58.20
REMARK 500 TYR A 139 49.26 -101.07
REMARK 500 TYR A 140 103.60 -29.54
REMARK 500 ALA A 145 -61.23 -29.96
REMARK 500 THR A 156 -60.40 -105.00
REMARK 500 ALA A 174 -40.92 -154.52
REMARK 500 PRO A 179 -148.68 -60.52
REMARK 500 LYS A 232 -155.93 -61.63
REMARK 500 LYS A 236 -89.02 -106.80
REMARK 500 ALA A 243 6.91 -170.53
REMARK 500 PHE A 250 -65.78 -129.73
REMARK 500 THR A 253 -13.98 70.57
REMARK 500 LEU A 256 109.16 11.05
REMARK 500 LEU A 257 -14.80 -33.04
REMARK 500 GLU A 259 166.02 -45.71
REMARK 500 VAL A 262 -89.96 -20.71
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 ARG A 22 0.31 SIDE CHAIN
REMARK 500 ARG A 45 0.15 SIDE CHAIN
REMARK 500 ARG A 75 0.19 SIDE CHAIN
REMARK 500 ARG A 77 0.14 SIDE CHAIN
REMARK 500 ARG A 99 0.30 SIDE CHAIN
REMARK 500 ARG A 120 0.30 SIDE CHAIN
REMARK 500 ARG A 161 0.32 SIDE CHAIN
REMARK 500 ARG A 208 0.22 SIDE CHAIN
REMARK 500 ARG A 220 0.30 SIDE CHAIN
REMARK 500 ARG A 242 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1D8V A 1 263 UNP P24817 RIP3_MOMCH 24 286
SEQADV 1D8V TYR A 14 UNP P24817 THR 37 CONFLICT
SEQRES 1 A 263 ASP VAL ASN PHE ASP LEU SER THR ALA THR ALA LYS THR
SEQRES 2 A 263 TYR THR LYS PHE ILE GLU ASP PHE ARG ALA THR LEU PRO
SEQRES 3 A 263 PHE SER HIS LYS VAL TYR ASP ILE PRO LEU LEU TYR SER
SEQRES 4 A 263 THR ILE SER ASP SER ARG ARG PHE ILE LEU LEU ASN LEU
SEQRES 5 A 263 THR SER TYR ALA TYR GLU THR ILE SER VAL ALA ILE ASP
SEQRES 6 A 263 VAL THR ASN VAL TYR VAL VAL ALA TYR ARG THR ARG ASP
SEQRES 7 A 263 VAL SER TYR PHE PHE LYS GLU SER PRO PRO GLU ALA TYR
SEQRES 8 A 263 ASN ILE LEU PHE LYS GLY THR ARG LYS ILE THR LEU PRO
SEQRES 9 A 263 TYR THR GLY ASN TYR GLU ASN LEU GLN THR ALA ALA HIS
SEQRES 10 A 263 LYS ILE ARG GLU ASN ILE ASP LEU GLY LEU PRO ALA LEU
SEQRES 11 A 263 SER SER ALA ILE THR THR LEU PHE TYR TYR ASN ALA GLN
SEQRES 12 A 263 SER ALA PRO SER ALA LEU LEU VAL LEU ILE GLN THR THR
SEQRES 13 A 263 ALA GLU ALA ALA ARG PHE LYS TYR ILE GLU ARG HIS VAL
SEQRES 14 A 263 ALA LYS TYR VAL ALA THR ASN PHE LYS PRO ASN LEU ALA
SEQRES 15 A 263 ILE ILE SER LEU GLU ASN GLN TRP SER ALA LEU SER LYS
SEQRES 16 A 263 GLN ILE PHE LEU ALA GLN ASN GLN GLY GLY LYS PHE ARG
SEQRES 17 A 263 ASN PRO VAL ASP LEU ILE LYS PRO THR GLY GLU ARG PHE
SEQRES 18 A 263 GLN VAL THR ASN VAL ASP SER ASP VAL VAL LYS GLY ASN
SEQRES 19 A 263 ILE LYS LEU LEU LEU ASN SER ARG ALA SER THR ALA ASP
SEQRES 20 A 263 GLU ASN PHE ILE THR THR MET THR LEU LEU GLY GLU SER
SEQRES 21 A 263 VAL VAL ASN
HELIX 1 1 THR A 10 LEU A 25 1 16
HELIX 2 2 SER A 42 ARG A 46 1 5
HELIX 3 3 PRO A 88 LEU A 94 1 7
HELIX 4 4 ASN A 108 HIS A 117 1 10
HELIX 5 5 ILE A 119 ILE A 123 5 5
HELIX 6 6 GLY A 126 TYR A 139 1 14
HELIX 7 7 GLN A 143 THR A 156 1 14
HELIX 8 8 THR A 156 PHE A 162 1 7
HELIX 9 9 PHE A 162 TYR A 172 1 11
HELIX 10 10 ASN A 180 GLY A 204 1 25
HELIX 11 11 ALA A 243 ASN A 249 5 7
SHEET 1 A 6 VAL A 2 ASP A 5 0
SHEET 2 A 6 PHE A 47 THR A 53 1 O LEU A 49 N VAL A 2
SHEET 3 A 6 THR A 59 ASP A 65 -1 N ILE A 60 O LEU A 52
SHEET 4 A 6 VAL A 71 THR A 76 -1 N VAL A 72 O ALA A 63
SHEET 5 A 6 VAL A 79 LYS A 84 -1 N VAL A 79 O THR A 76
SHEET 6 A 6 ARG A 99 THR A 106 1 O ARG A 99 N SER A 80
SHEET 1 B 2 LEU A 36 LEU A 37 0
SHEET 2 B 2 LEU A 238 LEU A 239 1 O LEU A 238 N LEU A 37
SHEET 1 C 2 LYS A 206 LYS A 215 0
SHEET 2 C 2 GLU A 219 ASN A 225 -1 O GLU A 219 N LYS A 215
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
Complete list - 16 20 Bytes