Header list of 1l2n.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 22-FEB-02 1L2N
TITLE SMT3 SOLUTION STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SMT3, UBIQUITIN-LIKE PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.SHENG,X.LIAO
REVDAT 4 23-FEB-22 1L2N 1 REMARK
REVDAT 3 24-FEB-09 1L2N 1 VERSN
REVDAT 2 05-JUN-02 1L2N 1 JRNL
REVDAT 1 06-MAR-02 1L2N 0
JRNL AUTH W.SHENG,X.LIAO
JRNL TITL SOLUTION STRUCTURE OF A YEAST UBIQUITIN-LIKE PROTEIN SMT3:
JRNL TITL 2 THE ROLE OF STRUCTURALLY LESS DEFINED SEQUENCES IN
JRNL TITL 3 PROTEIN-PROTEIN RECOGNITIONS.
JRNL REF PROTEIN SCI. V. 11 1482 2002
JRNL REFN ISSN 0961-8368
JRNL PMID 12021447
JRNL DOI 10.1110/PS.0201602
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTER, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L2N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015587.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM C13 AND 15N LABELLED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNCA-J; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 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 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 VAL A 6
REMARK 465 ASN A 7
REMARK 465 GLN A 8
REMARK 465 GLU A 9
REMARK 465 ALA A 10
REMARK 465 LYS A 11
REMARK 465 PRO A 12
REMARK 465 GLU A 13
REMARK 465 VAL A 14
REMARK 465 LYS A 15
REMARK 465 PRO A 16
REMARK 465 GLU A 17
REMARK 465 VAL A 18
REMARK 465 LYS A 19
REMARK 465 PRO A 20
REMARK 465 GLY A 97
REMARK 465 GLY A 98
REMARK 465 ALA A 99
REMARK 465 THR A 100
REMARK 465 TYR A 101
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 GLN A 56 H GLU A 59 1.57
REMARK 500 O ALA A 51 H LYS A 54 1.58
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 LYS A 40 58.13 -90.63
REMARK 500 1 LYS A 41 127.75 177.64
REMARK 500 1 THR A 43 94.68 -33.56
REMARK 500 1 ARG A 47 -77.92 -62.57
REMARK 500 1 ALA A 51 -70.72 -41.77
REMARK 500 1 MET A 60 29.79 37.99
REMARK 500 1 ILE A 70 42.34 -156.69
REMARK 500 1 MET A 83 -74.26 -100.62
REMARK 500 1 ASN A 86 94.65 -175.56
REMARK 500 1 GLU A 94 79.81 -161.23
REMARK 500 2 GLU A 34 108.08 -49.78
REMARK 500 2 LYS A 40 62.85 -106.40
REMARK 500 2 LYS A 41 140.65 178.88
REMARK 500 2 THR A 43 91.97 -30.19
REMARK 500 2 MET A 60 29.09 44.48
REMARK 500 2 ASP A 68 -75.10 -116.08
REMARK 500 2 ILE A 70 30.43 -160.37
REMARK 500 2 ALA A 74 -90.44 -82.04
REMARK 500 2 ASP A 75 46.71 -103.69
REMARK 500 2 MET A 83 -83.78 -100.30
REMARK 500 2 ASN A 86 86.57 -177.05
REMARK 500 2 GLU A 94 79.12 -160.78
REMARK 500 3 LYS A 40 63.96 -101.06
REMARK 500 3 LYS A 41 131.11 179.58
REMARK 500 3 THR A 43 94.78 -35.62
REMARK 500 3 ALA A 51 -70.04 -45.08
REMARK 500 3 MET A 60 29.83 37.79
REMARK 500 3 ASP A 68 -74.61 -109.53
REMARK 500 3 ILE A 70 32.91 -158.14
REMARK 500 3 ALA A 74 -87.68 -80.65
REMARK 500 3 ASP A 75 44.29 -107.89
REMARK 500 3 MET A 83 -70.40 -100.75
REMARK 500 3 ASN A 86 92.54 -176.33
REMARK 500 3 GLU A 94 79.41 -161.01
REMARK 500 3 GLN A 95 119.81 -160.33
REMARK 500 4 LYS A 40 59.49 -102.05
REMARK 500 4 LYS A 41 140.93 178.62
REMARK 500 4 THR A 43 93.08 -30.86
REMARK 500 4 ARG A 47 -76.15 -55.97
REMARK 500 4 MET A 60 31.58 36.28
REMARK 500 4 ILE A 70 34.84 -159.43
REMARK 500 4 ALA A 74 -72.54 -84.86
REMARK 500 4 MET A 83 -77.73 -98.77
REMARK 500 4 ASN A 86 99.70 -177.83
REMARK 500 4 GLU A 94 78.62 -160.34
REMARK 500 5 LYS A 40 58.86 -99.25
REMARK 500 5 LYS A 41 140.83 179.42
REMARK 500 5 THR A 43 93.07 -32.11
REMARK 500 5 MET A 60 29.07 45.90
REMARK 500 5 ASP A 68 -78.43 -110.59
REMARK 500
REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1L2N A 1 101 UNP Q12306 SMT3_YEAST 1 101
SEQRES 1 A 101 MET SER ASP SER GLU VAL ASN GLN GLU ALA LYS PRO GLU
SEQRES 2 A 101 VAL LYS PRO GLU VAL LYS PRO GLU THR HIS ILE ASN LEU
SEQRES 3 A 101 LYS VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE
SEQRES 4 A 101 LYS LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE
SEQRES 5 A 101 ALA LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE
SEQRES 6 A 101 LEU TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO
SEQRES 7 A 101 GLU ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA
SEQRES 8 A 101 HIS ARG GLU GLN ILE GLY GLY ALA THR TYR
HELIX 1 1 THR A 43 GLN A 56 1 14
SHEET 1 A 4 ILE A 35 ILE A 39 0
SHEET 2 A 4 ILE A 24 SER A 29 -1 N LEU A 26 O PHE A 37
SHEET 3 A 4 ASP A 87 HIS A 92 1 O ALA A 91 N SER A 29
SHEET 4 A 4 ARG A 64 LEU A 66 -1 N ARG A 64 O HIS A 92
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