Header list of 2aiv.pdb file
Complete list - n 24 2 Bytes
HEADER TRANSPORT PROTEIN 01-AUG-05 2AIV
TITLE MULTIPLE CONFORMATIONS IN THE LIGAND-BINDING SITE OF THE YEAST NUCLEAR
TITLE 2 PORE TARGETING DOMAIN OF NUP116P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRAGMENT OF NUCLEOPORIN NUP116/NSP116;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 967-1113;
COMPND 5 SYNONYM: NUP116P; NUCLEAR PORE PROTEIN NUP116/NSP116;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: FRAGMENT INTERACTING WITH NUP82 NPC SUBCOMPLEX
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: NUP116, NSP116;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: GATEWAY;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST 15
KEYWDS BETA SANDWICH, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.A.ROBINSON,S.PARK,Z.-Y.J.SUN,P.SILVER,G.WAGNER,J.HOGLE
REVDAT 4 24-JAN-18 2AIV 1 AUTHOR JRNL REMARK
REVDAT 3 24-FEB-09 2AIV 1 VERSN
REVDAT 2 25-OCT-05 2AIV 1 JRNL
REVDAT 1 16-AUG-05 2AIV 0
JRNL AUTH M.A.ROBINSON,S.PARK,Z.-Y.J.SUN,P.A.SILVER,G.WAGNER,J.M.HOGLE
JRNL TITL MULTIPLE CONFORMATIONS IN THE LIGAND-BINDING SITE OF THE
JRNL TITL 2 YEAST NUCLEAR PORE-TARGETING DOMAIN OF NUP116P
JRNL REF J.BIOL.CHEM. V. 280 35723 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16105837
JRNL DOI 10.1074/JBC.M505068200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, DYANA 1.0
REMARK 3 AUTHORS : BRUNGER, A. (CNS), GUENTERT, P. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AIV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033945.
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 : 100MM SODIUM-POTASSIUM PHOSPHATE
REMARK 210 PH 6.5, 50MM NACL, 1MM DTT
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5-1MM NUP116P U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 400
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.0, NMRPIPE JULY 2004
REMARK 210 VERSION
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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: 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 HD12 ILE A 69 H LEU A 73 1.18
REMARK 500 HG2 PRO A 10 HG21 THR A 14 1.19
REMARK 500 HA PHE A 41 HB1 ALA A 87 1.25
REMARK 500 HG LEU A 21 HH21 ARG A 24 1.29
REMARK 500 HA LEU A 21 HE ARG A 24 1.29
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 26.36 -67.93
REMARK 500 1 SER A 11 161.05 131.16
REMARK 500 1 PRO A 27 -88.92 -46.30
REMARK 500 1 LYS A 34 -84.75 59.93
REMARK 500 1 ILE A 50 72.35 58.85
REMARK 500 1 PRO A 51 32.02 -94.24
REMARK 500 1 ILE A 59 -25.17 62.07
REMARK 500 1 LYS A 65 -29.68 171.60
REMARK 500 1 ALA A 71 70.74 160.57
REMARK 500 1 LEU A 73 92.72 -69.51
REMARK 500 1 PRO A 74 39.07 -70.22
REMARK 500 1 ARG A 76 94.16 -69.99
REMARK 500 1 TYR A 95 92.92 -69.06
REMARK 500 1 PRO A 96 36.38 -85.78
REMARK 500 1 VAL A 97 168.23 51.05
REMARK 500 1 LYS A 103 93.45 -69.54
REMARK 500 1 PRO A 104 92.75 -52.47
REMARK 500 1 LYS A 106 44.04 -140.58
REMARK 500 1 PRO A 108 34.33 -69.00
REMARK 500 1 ASN A 123 99.39 -66.13
REMARK 500 1 PRO A 124 33.23 -91.02
REMARK 500 1 GLU A 129 -79.75 -90.12
REMARK 500 2 PRO A 2 31.36 -87.51
REMARK 500 2 SER A 11 166.13 139.13
REMARK 500 2 PRO A 27 -85.91 -43.61
REMARK 500 2 TYR A 36 -73.79 -89.43
REMARK 500 2 VAL A 45 91.13 -67.99
REMARK 500 2 ALA A 48 77.76 49.29
REMARK 500 2 PRO A 51 24.94 -65.80
REMARK 500 2 ILE A 59 41.23 -71.24
REMARK 500 2 LYS A 65 -30.05 177.51
REMARK 500 2 ASN A 72 -1.67 64.86
REMARK 500 2 LEU A 73 92.90 -69.92
REMARK 500 2 PRO A 74 31.94 -93.28
REMARK 500 2 PRO A 96 21.55 -64.28
REMARK 500 2 LYS A 106 66.49 -109.69
REMARK 500 2 PRO A 108 45.87 -96.74
REMARK 500 2 ASN A 123 97.04 -68.16
REMARK 500 2 PRO A 124 31.87 -88.89
REMARK 500 2 GLU A 129 -79.81 -90.63
REMARK 500 3 PRO A 2 38.76 -70.42
REMARK 500 3 SER A 11 165.85 139.46
REMARK 500 3 PRO A 27 -84.14 -52.36
REMARK 500 3 LYS A 34 -68.25 66.80
REMARK 500 3 ASP A 46 92.54 -63.56
REMARK 500 3 ILE A 50 83.59 56.18
REMARK 500 3 ILE A 59 19.13 47.02
REMARK 500 3 LYS A 65 -31.14 179.10
REMARK 500 3 ALA A 71 84.95 67.91
REMARK 500 3 LEU A 73 93.01 -68.31
REMARK 500
REMARK 500 THIS ENTRY HAS 287 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2AIV A 3 149 UNP Q02630 NU116_YEAST 967 1113
SEQADV 2AIV GLY A 1 UNP Q02630 CLONING ARTIFACT
SEQADV 2AIV PRO A 2 UNP Q02630 CLONING ARTIFACT
SEQRES 1 A 149 GLY PRO ASN GLU ASN TYR TYR ILE SER PRO SER LEU ASP
SEQRES 2 A 149 THR LEU SER SER TYR SER LEU LEU GLN LEU ARG LYS VAL
SEQRES 3 A 149 PRO HIS LEU VAL VAL GLY HIS LYS SER TYR GLY LYS ILE
SEQRES 4 A 149 GLU PHE LEU GLU PRO VAL ASP LEU ALA GLY ILE PRO LEU
SEQRES 5 A 149 THR SER LEU GLY GLY VAL ILE ILE THR PHE GLU PRO LYS
SEQRES 6 A 149 THR CYS ILE ILE TYR ALA ASN LEU PRO ASN ARG PRO LYS
SEQRES 7 A 149 ARG GLY GLU GLY ILE ASN VAL ARG ALA ARG ILE THR CYS
SEQRES 8 A 149 PHE ASN CYS TYR PRO VAL ASP LYS SER THR ARG LYS PRO
SEQRES 9 A 149 ILE LYS ASP PRO ASN HIS GLN LEU VAL LYS ARG HIS ILE
SEQRES 10 A 149 GLU ARG LEU LYS LYS ASN PRO ASN SER LYS PHE GLU SER
SEQRES 11 A 149 TYR ASP ALA ASP SER GLY THR TYR VAL PHE ILE VAL ASN
SEQRES 12 A 149 HIS ALA ALA GLU GLN THR
HELIX 1 1 SER A 11 SER A 17 1 7
HELIX 2 2 SER A 19 LYS A 25 1 7
HELIX 3 3 PRO A 51 GLY A 56 1 6
HELIX 4 4 LEU A 112 ASN A 123 1 12
SHEET 1 A 5 LEU A 29 GLY A 32 0
SHEET 2 A 5 LYS A 38 PHE A 41 -1 O ILE A 39 N VAL A 31
SHEET 3 A 5 ALA A 87 CYS A 91 -1 O ARG A 88 N GLU A 40
SHEET 4 A 5 TYR A 138 ILE A 141 -1 O PHE A 140 N ILE A 89
SHEET 5 A 5 LYS A 127 TYR A 131 -1 N LYS A 127 O ILE A 141
SHEET 1 B 2 THR A 61 PHE A 62 0
SHEET 2 B 2 CYS A 67 ILE A 68 -1 O ILE A 68 N THR A 61
CISPEP 1 SER A 9 PRO A 10 1 5.34
CISPEP 2 SER A 9 PRO A 10 2 5.79
CISPEP 3 SER A 9 PRO A 10 3 4.65
CISPEP 4 SER A 9 PRO A 10 4 5.64
CISPEP 5 SER A 9 PRO A 10 5 5.75
CISPEP 6 SER A 9 PRO A 10 6 5.01
CISPEP 7 SER A 9 PRO A 10 7 4.80
CISPEP 8 SER A 9 PRO A 10 8 5.01
CISPEP 9 SER A 9 PRO A 10 9 6.82
CISPEP 10 SER A 9 PRO A 10 10 5.51
CISPEP 11 SER A 9 PRO A 10 11 6.96
CISPEP 12 SER A 9 PRO A 10 12 6.40
CISPEP 13 SER A 9 PRO A 10 13 7.19
CISPEP 14 SER A 9 PRO A 10 14 5.12
CISPEP 15 SER A 9 PRO A 10 15 7.04
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 - n 24 2 Bytes