HEADER MEMBRANE PROTEIN 28-DEC-98 1B4R
TITLE PKD DOMAIN 1 FROM HUMAN POLYCYSTEIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PKD1_HUMAN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PKD DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
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_PLASMID: PRSETA
KEYWDS PKD DOMAIN 1 FROM HUMAN POLYCYSTEIN-1, POLYCYSTIN (PRECURSOR),
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.BYCROFT
REVDAT 4 16-FEB-22 1B4R 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1B4R 1 VERSN
REVDAT 2 29-DEC-99 1B4R 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 06-JAN-99 1B4R 0
JRNL AUTH M.BYCROFT,A.BATEMAN,J.CLARKE,S.J.HAMILL,R.SANDFORD,
JRNL AUTH 2 R.L.THOMAS,C.CHOTHIA
JRNL TITL THE STRUCTURE OF A PKD DOMAIN FROM POLYCYSTIN-1:
JRNL TITL 2 IMPLICATIONS FOR POLYCYSTIC KIDNEY DISEASE.
JRNL REF EMBO J. V. 18 297 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 9889186
JRNL DOI 10.1093/EMBOJ/18.2.297
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B4R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008305.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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: 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 HIS A 14 164.17 174.51
REMARK 500 1 ALA A 29 -62.26 176.56
REMARK 500 1 LEU A 31 -64.58 -13.13
REMARK 500 1 ASP A 42 35.70 -98.49
REMARK 500 1 ALA A 45 -90.70 -71.20
REMARK 500 1 PRO A 52 40.09 -88.43
REMARK 500 1 ALA A 54 -168.86 -165.88
REMARK 500 1 GLU A 86 -159.41 -110.59
REMARK 500 2 HIS A 14 -36.82 161.94
REMARK 500 2 HIS A 26 147.61 -172.47
REMARK 500 2 ALA A 29 -70.06 172.80
REMARK 500 2 ASP A 42 33.07 -97.04
REMARK 500 2 ALA A 45 -86.96 -75.30
REMARK 500 2 PRO A 52 38.91 -88.50
REMARK 500 2 ALA A 54 -169.64 -165.18
REMARK 500 2 GLU A 86 -160.98 -102.45
REMARK 500 3 HIS A 14 -38.87 168.90
REMARK 500 3 ALA A 29 -61.86 175.25
REMARK 500 3 LEU A 31 -64.03 -15.42
REMARK 500 3 ALA A 35 149.43 -178.60
REMARK 500 3 ALA A 45 -98.28 -71.38
REMARK 500 3 PRO A 52 42.63 -88.43
REMARK 500 4 HIS A 14 -35.63 159.11
REMARK 500 4 ALA A 29 -71.85 172.56
REMARK 500 4 ASP A 42 -104.71 -109.06
REMARK 500 4 ALA A 45 -85.01 -81.20
REMARK 500 4 PRO A 52 41.75 -88.45
REMARK 500 4 GLU A 86 -154.87 -126.58
REMARK 500 5 HIS A 14 175.28 152.25
REMARK 500 5 HIS A 26 149.52 -174.93
REMARK 500 5 ALA A 29 -72.36 170.88
REMARK 500 5 ASP A 42 -103.32 -105.42
REMARK 500 5 ALA A 45 -85.37 -81.49
REMARK 500 5 PRO A 52 40.79 -88.83
REMARK 500 5 ALA A 54 -167.67 -171.59
REMARK 500 6 HIS A 14 -37.50 163.16
REMARK 500 6 ALA A 29 -69.60 169.18
REMARK 500 6 ASP A 42 -104.48 -104.25
REMARK 500 6 ALA A 45 -85.40 -80.74
REMARK 500 6 PRO A 52 38.99 -88.96
REMARK 500 6 ALA A 54 -166.79 -163.61
REMARK 500 6 ALA A 74 -0.38 71.53
REMARK 500 6 GLU A 86 -157.32 -107.66
REMARK 500 7 HIS A 14 -33.98 158.87
REMARK 500 7 HIS A 26 148.51 -173.95
REMARK 500 7 ALA A 29 -71.54 172.31
REMARK 500 7 ASP A 42 35.60 -98.34
REMARK 500 7 ALA A 45 -89.99 -75.58
REMARK 500 7 PRO A 52 40.99 -88.97
REMARK 500 7 ALA A 54 -167.05 -171.55
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
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 1 ARG A 37 0.32 SIDE CHAIN
REMARK 500 1 ARG A 57 0.22 SIDE CHAIN
REMARK 500 1 ARG A 63 0.15 SIDE CHAIN
REMARK 500 2 ARG A 37 0.21 SIDE CHAIN
REMARK 500 2 ARG A 57 0.31 SIDE CHAIN
REMARK 500 2 ARG A 63 0.30 SIDE CHAIN
REMARK 500 3 ARG A 37 0.32 SIDE CHAIN
REMARK 500 3 ARG A 57 0.32 SIDE CHAIN
REMARK 500 3 ARG A 63 0.24 SIDE CHAIN
REMARK 500 4 ARG A 37 0.26 SIDE CHAIN
REMARK 500 4 ARG A 57 0.19 SIDE CHAIN
REMARK 500 4 ARG A 63 0.32 SIDE CHAIN
REMARK 500 5 ARG A 37 0.19 SIDE CHAIN
REMARK 500 5 ARG A 57 0.14 SIDE CHAIN
REMARK 500 5 ARG A 63 0.25 SIDE CHAIN
REMARK 500 6 ARG A 37 0.32 SIDE CHAIN
REMARK 500 6 ARG A 57 0.24 SIDE CHAIN
REMARK 500 6 ARG A 63 0.28 SIDE CHAIN
REMARK 500 7 ARG A 37 0.16 SIDE CHAIN
REMARK 500 7 ARG A 57 0.17 SIDE CHAIN
REMARK 500 7 ARG A 63 0.25 SIDE CHAIN
REMARK 500 8 ARG A 37 0.21 SIDE CHAIN
REMARK 500 8 ARG A 57 0.16 SIDE CHAIN
REMARK 500 8 ARG A 63 0.23 SIDE CHAIN
REMARK 500 9 ARG A 37 0.31 SIDE CHAIN
REMARK 500 9 ARG A 57 0.26 SIDE CHAIN
REMARK 500 9 ARG A 63 0.26 SIDE CHAIN
REMARK 500 10 ARG A 37 0.24 SIDE CHAIN
REMARK 500 10 ARG A 57 0.20 SIDE CHAIN
REMARK 500 10 ARG A 63 0.31 SIDE CHAIN
REMARK 500 11 ARG A 37 0.23 SIDE CHAIN
REMARK 500 11 ARG A 57 0.17 SIDE CHAIN
REMARK 500 11 ARG A 63 0.31 SIDE CHAIN
REMARK 500 12 ARG A 37 0.32 SIDE CHAIN
REMARK 500 12 ARG A 57 0.16 SIDE CHAIN
REMARK 500 12 ARG A 63 0.30 SIDE CHAIN
REMARK 500 13 ARG A 37 0.28 SIDE CHAIN
REMARK 500 13 ARG A 57 0.18 SIDE CHAIN
REMARK 500 13 ARG A 63 0.32 SIDE CHAIN
REMARK 500 14 ARG A 37 0.31 SIDE CHAIN
REMARK 500 14 ARG A 57 0.19 SIDE CHAIN
REMARK 500 14 ARG A 63 0.24 SIDE CHAIN
REMARK 500 15 ARG A 37 0.32 SIDE CHAIN
REMARK 500 15 ARG A 57 0.32 SIDE CHAIN
REMARK 500 15 ARG A 63 0.24 SIDE CHAIN
REMARK 500 16 ARG A 37 0.24 SIDE CHAIN
REMARK 500 16 ARG A 57 0.21 SIDE CHAIN
REMARK 500 16 ARG A 63 0.29 SIDE CHAIN
REMARK 500 17 ARG A 37 0.30 SIDE CHAIN
REMARK 500 17 ARG A 57 0.17 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 59 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1B4R A 8 87 UNP P98161 PKD1_HUMAN 275 354
SEQADV 1B4R ALA A 28 UNP P98161 ASP 302 CONFLICT
SEQRES 1 A 80 ALA THR LEU VAL GLY PRO HIS GLY PRO LEU ALA SER GLY
SEQRES 2 A 80 GLN LEU ALA ALA PHE HIS ILE ALA ALA PRO LEU PRO VAL
SEQRES 3 A 80 THR ALA THR ARG TRP ASP PHE GLY ASP GLY SER ALA GLU
SEQRES 4 A 80 VAL ASP ALA ALA GLY PRO ALA ALA SER HIS ARG TYR VAL
SEQRES 5 A 80 LEU PRO GLY ARG TYR HIS VAL THR ALA VAL LEU ALA LEU
SEQRES 6 A 80 GLY ALA GLY SER ALA LEU LEU GLY THR ASP VAL GLN VAL
SEQRES 7 A 80 GLU ALA
SHEET 1 A 3 THR A 9 VAL A 11 0
SHEET 2 A 3 GLN A 21 ALA A 28 -1 N ALA A 28 O THR A 9
SHEET 3 A 3 ALA A 53 TYR A 58 -1 N TYR A 58 O GLN A 21
SHEET 1 B 4 GLU A 46 ALA A 50 0
SHEET 2 B 4 ALA A 35 ASP A 39 -1 N TRP A 38 O VAL A 47
SHEET 3 B 4 GLY A 62 ALA A 71 -1 N ALA A 71 O ALA A 35
SHEET 4 B 4 SER A 76 VAL A 85 -1 N VAL A 85 O GLY A 62
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
(ATOM LINES ARE NOT SHOWN.)
END