Header list of 1n4c.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 30-OCT-02 1N4C
TITLE NMR STRUCTURE OF THE J-DOMAIN AND CLATHRIN SUBSTRATE BINDING DOMAIN OF
TITLE 2 BOVINE AUXILIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUXILIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES (737-845), J-DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FOUR HELIX BUNDLE, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.M.GRUSCHUS,C.J.HAN,T.GREENER,L.E.GREENE,J.A.FERRETTI,E.EISENBERG
REVDAT 4 23-FEB-22 1N4C 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1N4C 1 VERSN
REVDAT 2 25-JAN-05 1N4C 1 JRNL
REVDAT 1 11-NOV-03 1N4C 0
JRNL AUTH J.M.GRUSCHUS,C.J.HAN,T.GREENER,J.A.FERRETTI,L.E.GREENE,
JRNL AUTH 2 E.EISENBERG
JRNL TITL STRUCTURE OF THE FUNCTIONAL FRAGMENT OF AUXILIN REQUIRED FOR
JRNL TITL 2 CATALYTIC UNCOATING OF CLATHRIN-COATED VESICLES.
JRNL REF BIOCHEMISTRY V. 43 3111 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15023062
JRNL DOI 10.1021/BI0354740
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.HAN,J.M.GRUSCHUS,T.GREENER,L.E.GREENE,J.FERRETTI,
REMARK 1 AUTH 2 E.EISENBERG
REMARK 1 TITL H-1, 15N, AND 13C NMR BACKBONE ASSIGNMENTS AND SECONDARY
REMARK 1 TITL 2 STRUCTURE OF THE C-TERMINAL RECOMBINANT FRAGMENT OF AUXILIN
REMARK 1 TITL 3 INCLUDING THE J-DOMAIN
REMARK 1 REF J.BIOMOL.NMR V. 17 281 2000
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008353226591
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURE DETERMINED USING 2810 DISTANCE RESTRAINTS,
REMARK 3 144 PHI AND PSI DIHEDRAL RESTRAINTS
REMARK 4
REMARK 4 1N4C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017502.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 60MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM AUXILIN (20KD C-TERMINAL
REMARK 210 CONSTRUCT) U-15N; 1.5MM AUXILIN
REMARK 210 (20KD C-TERMINAL CONSTRUCT) U-
REMARK 210 15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TALOS 1, XWINNMR 2.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
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 TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 HD22 ASN A 101 HE ARG A 103 1.31
REMARK 500 O GLY A 124 H ASP A 127 1.41
REMARK 500 O ARG A 103 HG SER A 107 1.44
REMARK 500 O GLY A 177 H LYS A 179 1.46
REMARK 500 O GLU A 172 H GLN A 176 1.46
REMARK 500 OE1 GLU A 117 H LYS A 119 1.51
REMARK 500 OD1 ASP A 85 H GLU A 87 1.53
REMARK 500 O ALA A 159 H PHE A 163 1.54
REMARK 500 O PRO A 147 H ALA A 150 1.57
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 PRO A 2 -9.20 -45.93
REMARK 500 1 LEU A 3 -30.29 -161.45
REMARK 500 1 SER A 5 69.39 -167.75
REMARK 500 1 PRO A 6 153.96 -46.18
REMARK 500 1 HIS A 12 64.09 -169.86
REMARK 500 1 SER A 14 67.59 -169.37
REMARK 500 1 ASN A 17 -103.82 -79.09
REMARK 500 1 ARG A 18 68.04 -153.14
REMARK 500 1 SER A 26 67.92 -162.06
REMARK 500 1 GLU A 34 74.78 -63.13
REMARK 500 1 ALA A 38 86.80 -65.32
REMARK 500 1 LEU A 42 -58.72 -167.30
REMARK 500 1 GLU A 43 -177.82 -53.87
REMARK 500 1 ALA A 48 39.43 -78.88
REMARK 500 1 ALA A 49 9.68 -69.80
REMARK 500 1 PHE A 51 61.11 -153.98
REMARK 500 1 GLU A 52 -16.67 -161.09
REMARK 500 1 GLN A 58 -6.87 -54.53
REMARK 500 1 ASN A 61 -123.14 -79.94
REMARK 500 1 ALA A 62 98.67 -160.77
REMARK 500 1 LYS A 66 -124.64 -152.45
REMARK 500 1 PRO A 69 -177.92 -46.82
REMARK 500 1 ARG A 70 66.32 -151.11
REMARK 500 1 ARG A 76 -9.13 -52.36
REMARK 500 1 GLU A 83 84.06 -170.46
REMARK 500 1 MET A 84 39.73 -76.15
REMARK 500 1 PRO A 86 -4.16 -59.76
REMARK 500 1 LYS A 98 71.82 -171.10
REMARK 500 1 GLU A 99 28.96 -75.57
REMARK 500 1 ARG A 100 27.02 -140.36
REMARK 500 1 VAL A 112 29.02 -146.22
REMARK 500 1 PRO A 122 137.82 -36.57
REMARK 500 1 ASP A 127 31.98 -94.22
REMARK 500 1 LEU A 128 33.26 -141.96
REMARK 500 1 PRO A 154 -33.98 -35.83
REMARK 500 1 GLN A 178 50.31 -66.18
REMARK 500 1 PRO A 180 98.60 -42.74
REMARK 500 1 LEU A 181 68.88 -111.52
REMARK 500 2 SER A 5 60.13 -162.22
REMARK 500 2 GLU A 7 -126.69 -62.64
REMARK 500 2 SER A 14 68.90 -167.61
REMARK 500 2 PRO A 15 172.06 -46.16
REMARK 500 2 GLN A 16 96.69 -49.99
REMARK 500 2 ASN A 20 41.73 -159.98
REMARK 500 2 ASN A 22 -45.69 -165.96
REMARK 500 2 VAL A 23 97.76 -67.25
REMARK 500 2 SER A 24 90.44 -170.00
REMARK 500 2 SER A 26 -4.80 -165.91
REMARK 500 2 SER A 27 -116.68 -73.88
REMARK 500 2 MET A 28 67.53 -153.33
REMARK 500
REMARK 500 THIS ENTRY HAS 873 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1N4C A 9 182 UNP Q27974 AUXI_BOVIN 737 910
SEQADV 1N4C GLY A 1 UNP Q27974 CLONING ARTIFACT
SEQADV 1N4C PRO A 2 UNP Q27974 CLONING ARTIFACT
SEQADV 1N4C LEU A 3 UNP Q27974 CLONING ARTIFACT
SEQADV 1N4C GLY A 4 UNP Q27974 CLONING ARTIFACT
SEQADV 1N4C PRO A 6 UNP Q27974 CLONING ARTIFACT
SEQADV 1N4C GLU A 7 UNP Q27974 CLONING ARTIFACT
SEQADV 1N4C PHE A 8 UNP Q27974 CLONING ARTIFACT
SEQRES 1 A 182 GLY PRO LEU GLY SER PRO GLU PHE SER MET PRO HIS SER
SEQRES 2 A 182 SER PRO GLN ASN ARG PRO ASN TYR ASN VAL SER PHE SER
SEQRES 3 A 182 SER MET PRO GLY GLY GLN ASN GLU ARG GLY LYS ALA ALA
SEQRES 4 A 182 ALA ASN LEU GLU GLY LYS GLN LYS ALA ALA ASP PHE GLU
SEQRES 5 A 182 ASP LEU LEU SER GLY GLN GLY PHE ASN ALA HIS LYS ASP
SEQRES 6 A 182 LYS LYS GLY PRO ARG THR ILE ALA GLU MET ARG LYS GLU
SEQRES 7 A 182 GLU MET ALA LYS GLU MET ASP PRO GLU LYS LEU LYS ILE
SEQRES 8 A 182 LEU GLU TRP ILE GLU GLY LYS GLU ARG ASN ILE ARG ALA
SEQRES 9 A 182 LEU LEU SER THR MET HIS THR VAL LEU TRP ALA GLY GLU
SEQRES 10 A 182 THR LYS TRP LYS PRO VAL GLY MET ALA ASP LEU VAL THR
SEQRES 11 A 182 PRO GLU GLN VAL LYS LYS VAL TYR ARG LYS ALA VAL LEU
SEQRES 12 A 182 VAL VAL HIS PRO ASP LYS ALA THR GLY GLN PRO TYR GLU
SEQRES 13 A 182 GLN TYR ALA LYS MET ILE PHE MET GLU LEU ASN ASP ALA
SEQRES 14 A 182 TRP SER GLU PHE GLU ASN GLN GLY GLN LYS PRO LEU TYR
HELIX 1 1 GLU A 52 SER A 56 5 5
HELIX 2 2 ILE A 72 LYS A 82 1 11
HELIX 3 3 LYS A 88 GLU A 99 1 12
HELIX 4 4 ASN A 101 MET A 109 1 9
HELIX 5 5 HIS A 110 LEU A 113 5 4
HELIX 6 6 GLY A 124 VAL A 129 5 6
HELIX 7 7 THR A 130 VAL A 145 1 16
HELIX 8 8 HIS A 146 THR A 151 5 6
HELIX 9 9 TYR A 155 GLN A 178 1 24
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