Header list of 1i5h.pdb file
Complete list - b 23 2 Bytes
HEADER LIGASE 27-FEB-01 1I5H
TITLE SOLUTION STRUCTURE OF THE RNEDD4 WWIII DOMAIN-RENAL BP2 PEPTIDE
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN LIGASE NEDD4;
COMPND 3 CHAIN: W;
COMPND 4 FRAGMENT: WWIII DOMAIN;
COMPND 5 SYNONYM: RNEDD4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: AMILORIDE-SENSITIVE SODIUM CHANNEL BETA-SUBUNIT;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: RENAL BP2 PEPTIDE;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T2;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 12 ORGANISM_COMMON: NORWAY RAT;
SOURCE 13 ORGANISM_TAXID: 10116;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX4T2;
SOURCE 19 OTHER_DETAILS: AN IDENTICAL PEPTIDE WAS MADE SYNTHETICALLY USING
SOURCE 20 STANDARD F-MOC CHEMISTRY FOR NMR SAMPLES REQUIRING UNLABELED BP2
SOURCE 21 PEPTIDE.
KEYWDS NEDD4, WW DOMAINS, ENAC, PY MOTIF, LIDDLE SYNDROME, PROLINE-RICH,
KEYWDS 2 LIGASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR V.KANELIS,D.ROTIN,J.D.FORMAN-KAY
REVDAT 3 23-FEB-22 1I5H 1 REMARK
REVDAT 2 24-FEB-09 1I5H 1 VERSN
REVDAT 1 02-MAY-01 1I5H 0
JRNL AUTH V.KANELIS,D.ROTIN,J.D.FORMAN-KAY
JRNL TITL SOLUTION STRUCTURE OF A NEDD4 WW DOMAIN-ENAC PEPTIDE
JRNL TITL 2 COMPLEX.
JRNL REF NAT.STRUCT.BIOL. V. 8 407 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11323714
JRNL DOI 10.1038/87562
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.8, ARIA 1.0
REMARK 3 AUTHORS : DELAGLIO, F., GRZESIEK, S., VUISTER, G.W., ZHU,
REMARK 3 G., PFEIFER, J. AND BAX, A. (NMRPIPE), NILGES, M.
REMARK 3 (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PRELIMINARY STRUCTURES WERE CALCULATED
REMARK 3 USING CNS1.0. THESE STRUCTURES WERE THEN USED AS INPUT INTO THE
REMARK 3 PROGRAM ARIA1.0 FOR NOE ASSIGNMENT AND STRUCTURE REFINEMENT.
REMARK 3 THESE STRUCTURES WERE CALCULATED USING 1799 UNAMBIGUOUS AND 214
REMARK 3 AMBIGUOUS NOES, 14 HYDROGEN BOND RESTRAINTS, 44 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS AND DIRECTLY REFINED AGAINST 33 JHNHA COUPLING
REMARK 3 CONSTANTS.
REMARK 4
REMARK 4 1I5H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012928.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.01
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : SAMPLE 1:1MM RNEDD4 WWIII U
REMARK 210 -15N,13C; 3MM RENAC BP2 NA; 10
REMARK 210 MM NA+ PHOSPHATE, PH 6.5; 0.005
REMARK 210 MM EDTA; 0.01 MM APROTININ;
REMARK 210 0.005 MM LEUPEPTIN; 0.005 MM
REMARK 210 AEBSF; SAMPLE 2:1MM RENAC BP2 U-
REMARK 210 15N,13C; 3MM RNEDD4 WWIII NA; 10
REMARK 210 MM NA+ PHOSPHATE, PH 6.5; 0.005
REMARK 210 MM EDTA; 0.01 MM APROTININ;
REMARK 210 0.005 MM LEUPEPTIN; 0.005 MM
REMARK 210 AEBSF; MORE DETAILED DESCRIPTION
REMARK 210 GIVEN IN BMRB 4963; 1MM RENAC
REMARK 210 BP2 U-15N,13C; 3MM RNEDD4 WWIII
REMARK 210 NA; 10 MM NA+ PHOSPHATE, PH 6.5;
REMARK 210 0.005 MM EDTA; 0.01 MM APROTININ;
REMARK 210 0.005 MM LEUPEPTIN; 0.005 MM
REMARK 210 AEBSF;; 1MM RNEDD4 WWIII U-15N,
REMARK 210 13C; 3MM RENAC BP2 NA; 10 MM NA+
REMARK 210 PHOSPHATE, PH 6.5; 0.005 MM EDTA;
REMARK 210 0.01 MM APROTININ; 0.005 MM
REMARK 210 LEUPEPTIN; 0.005 MM AEBSF;; 1MM
REMARK 210 RENAC BP2 U-15N,13C; 3MM RNEDD4
REMARK 210 WWIII NA; 10 MM NA+ PHOSPHATE,
REMARK 210 PH 6.5; 0.005 MM EDTA; 0.01 MM
REMARK 210 APROTININ; 0.005 MM LEUPEPTIN;
REMARK 210 0.005 MM AEBSF;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N/13C-EDITED NOESY; 3D 13C
REMARK 210 F1-FILTERED, F3-EDITED NOESY;
REMARK 210 HNCOCA_COHACA_CROSS; HNCOCA_HNHA_
REMARK 210 CROSS; J-HNHA; HNCO-TROSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVEIW 4.1.2, CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 170
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, B
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: 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 SER W 451 67.79 65.87
REMARK 500 1 ASP W 454 42.92 -91.25
REMARK 500 1 LEU W 461 170.16 57.16
REMARK 500 1 LYS W 483 75.48 42.70
REMARK 500 1 VAL W 495 32.98 -159.65
REMARK 500 1 THR B 607 -71.94 69.09
REMARK 500 1 LEU B 608 107.78 -55.41
REMARK 500 1 PRO B 615 -175.41 -54.40
REMARK 500 2 PRO W 452 97.17 -51.02
REMARK 500 2 VAL W 453 66.95 -160.73
REMARK 500 2 LEU W 461 167.96 58.41
REMARK 500 2 LYS W 483 79.72 40.61
REMARK 500 2 GLU W 488 -177.68 -60.95
REMARK 500 2 ASN W 494 -72.27 -76.89
REMARK 500 2 VAL W 495 42.53 -158.75
REMARK 500 2 ILE W 497 -71.36 -157.41
REMARK 500 2 PRO B 615 175.07 -47.34
REMARK 500 3 ASP W 454 74.23 -155.66
REMARK 500 3 ASP W 457 88.12 175.17
REMARK 500 3 LEU W 461 171.55 55.86
REMARK 500 3 LYS W 483 80.60 42.77
REMARK 500 3 VAL W 495 78.12 -160.05
REMARK 500 3 ALA W 496 75.62 -168.52
REMARK 500 3 ILE W 497 52.57 -157.68
REMARK 500 3 SER B 606 -53.53 -161.59
REMARK 500 3 THR B 607 -66.45 68.09
REMARK 500 3 PRO B 615 -173.58 -52.43
REMARK 500 4 ASP W 454 132.95 -175.14
REMARK 500 4 SER W 455 -57.55 -166.18
REMARK 500 4 ASN W 456 -73.62 -155.44
REMARK 500 4 ASP W 457 91.92 50.39
REMARK 500 4 PRO W 460 71.01 -64.56
REMARK 500 4 LEU W 461 169.90 63.72
REMARK 500 4 LYS W 483 81.91 44.50
REMARK 500 4 ASN W 494 -79.52 -163.01
REMARK 500 4 VAL W 495 42.65 70.81
REMARK 500 4 ALA W 496 -160.90 38.96
REMARK 500 4 THR B 607 -68.65 76.77
REMARK 500 4 PRO B 615 -172.75 -55.33
REMARK 500 5 SER W 451 -53.72 173.80
REMARK 500 5 VAL W 453 -172.40 45.45
REMARK 500 5 SER W 455 -44.49 -166.51
REMARK 500 5 ASN W 456 142.25 65.76
REMARK 500 5 ASP W 457 74.83 -108.94
REMARK 500 5 LEU W 461 167.61 56.59
REMARK 500 5 LYS W 483 80.07 42.82
REMARK 500 5 GLU W 488 -173.66 -61.51
REMARK 500 5 GLN W 493 81.89 -63.17
REMARK 500 5 ASN W 494 -45.82 -164.77
REMARK 500 5 PRO B 614 160.24 -47.68
REMARK 500
REMARK 500 THIS ENTRY HAS 159 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4963 RELATED DB: BMRB
REMARK 900 4963 IS CHEMICAL SHIFTS FOR THE WW DOMAIN AND THE BP2 PEPTIDE.
REMARK 900 COUPLING CONSTANTS FOR THE WW DOMAIN (J-HNHA AND LONG RANGE J-CC)
REMARK 900 AND THE BP2 PEPTIDE (J-HNHA AND J-HAHB) ARE PROVIDED AS WELL.
DBREF 1I5H W 452 499 UNP Q62940 NEDD4_RAT 452 499
DBREF 1I5H B 607 621 UNP P37090 SCNNB_RAT 607 621
SEQADV 1I5H GLY W 450 UNP Q62940 SEE REMARK 999
SEQADV 1I5H SER W 451 UNP Q62940 SEE REMARK 999
SEQADV 1I5H GLY B 605 UNP P37090 SEE REMARK 999
SEQADV 1I5H SER B 606 UNP P37090 SEE REMARK 999
SEQRES 1 W 50 GLY SER PRO VAL ASP SER ASN ASP LEU GLY PRO LEU PRO
SEQRES 2 W 50 PRO GLY TRP GLU GLU ARG THR HIS THR ASP GLY ARG VAL
SEQRES 3 W 50 PHE PHE ILE ASN HIS ASN ILE LYS LYS THR GLN TRP GLU
SEQRES 4 W 50 ASP PRO ARG MET GLN ASN VAL ALA ILE THR GLY
SEQRES 1 B 17 GLY SER THR LEU PRO ILE PRO GLY THR PRO PRO PRO ASN
SEQRES 2 B 17 TYR ASP SER LEU
SHEET 1 A 3 TRP W 465 THR W 469 0
SHEET 2 A 3 VAL W 475 ASN W 479 -1 N PHE W 476 O ARG W 468
SHEET 3 A 3 LYS W 484 GLN W 486 -1 O LYS W 484 N ASN W 479
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