HEADER COMPLEMENT REGULATORY PROTEIN 01-JUN-94 1CDR
TITLE STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT
TITLE 2 REGULATORY PROTEIN CD59
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD59;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS COMPLEMENT REGULATORY PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.M.FLETCHER,R.A.HARRISON,P.J.LACHMANN,D.NEUHAUS
REVDAT 5 29-JUL-20 1CDR 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 13-JUL-11 1CDR 1 VERSN
REVDAT 3 25-AUG-09 1CDR 1 SOURCE
REVDAT 2 24-FEB-09 1CDR 1 VERSN
REVDAT 1 30-SEP-94 1CDR 0
JRNL AUTH C.M.FLETCHER,R.A.HARRISON,P.J.LACHMANN,D.NEUHAUS
JRNL TITL STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN
JRNL TITL 2 COMPLEMENT REGULATORY PROTEIN CD59.
JRNL REF STRUCTURE V. 2 185 1994
JRNL REFN ISSN 0969-2126
JRNL PMID 7520819
JRNL DOI 10.1016/S0969-2126(00)00020-4
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.M.FLETCHER,R.A.HARRISON,P.J.LACHMANN,D.NEUHAUS
REMARK 1 TITL SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS AND FOLDING TOPOLOGY OF
REMARK 1 TITL 2 HUMAN CD59
REMARK 1 REF PROTEIN SCI. V. 2 2015 1993
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.DAVIES,P.J.LACHMANN
REMARK 1 TITL MEMBRANE DEFENCE AGAINST COMPLEMENT LYSIS: THE STRUCTURE AND
REMARK 1 TITL 2 BIOLOGICAL PROPERTIES OF CD59
REMARK 1 REF IMMUNOL.RES. V. 12 258 1993
REMARK 1 REFN ISSN 0257-277X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CDR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172263.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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, 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 ASP A 12 42.84 -171.84
REMARK 500 1 LYS A 14 26.30 -140.52
REMARK 500 1 SER A 20 -177.33 -51.34
REMARK 500 1 ALA A 31 45.08 -85.93
REMARK 500 1 LEU A 33 -45.89 165.69
REMARK 500 1 PHE A 47 57.12 -90.89
REMARK 500 1 ASN A 48 -32.75 178.87
REMARK 500 1 GLU A 56 -157.66 -123.57
REMARK 500 1 ASN A 57 -75.40 -161.73
REMARK 500 1 GLU A 58 102.76 -59.65
REMARK 500 1 ASP A 67 97.95 -45.44
REMARK 500 1 LEU A 68 70.19 79.43
REMARK 500 1 PHE A 71 -179.82 -51.43
REMARK 500 1 GLU A 73 51.80 -157.12
REMARK 500 1 GLN A 74 26.15 -160.42
REMARK 500 1 LEU A 75 21.23 -147.00
REMARK 500 2 CYS A 6 92.34 172.25
REMARK 500 2 ASP A 12 34.40 -166.01
REMARK 500 2 VAL A 17 137.20 177.67
REMARK 500 2 CYS A 19 -75.01 -44.99
REMARK 500 2 SER A 20 157.15 64.01
REMARK 500 2 SER A 21 52.11 79.78
REMARK 500 2 ASP A 22 81.57 63.06
REMARK 500 2 ALA A 31 47.36 -106.98
REMARK 500 2 LEU A 33 -38.36 -171.79
REMARK 500 2 ASN A 48 -33.32 -178.09
REMARK 500 2 ASN A 57 -58.86 -140.61
REMARK 500 2 LEU A 59 126.80 -176.55
REMARK 500 2 LEU A 68 64.25 69.11
REMARK 500 2 ASN A 72 63.69 65.96
REMARK 500 2 GLU A 73 43.32 179.39
REMARK 500 2 GLN A 74 16.19 -149.30
REMARK 500 2 LEU A 75 21.27 -154.50
REMARK 500 3 ASP A 12 48.71 179.00
REMARK 500 3 SER A 20 -156.71 -105.89
REMARK 500 3 ASP A 24 -39.46 -157.07
REMARK 500 3 CYS A 45 73.92 -100.01
REMARK 500 3 ASN A 48 -35.82 178.56
REMARK 500 3 LEU A 68 63.55 67.74
REMARK 500 3 GLU A 73 34.51 -179.76
REMARK 500 3 GLN A 74 -74.51 -117.11
REMARK 500 3 GLU A 76 107.45 -44.21
REMARK 500 4 ASP A 12 35.62 -173.81
REMARK 500 4 ALA A 16 83.97 40.89
REMARK 500 4 ASN A 48 -34.07 178.81
REMARK 500 4 ASN A 57 -68.16 -121.82
REMARK 500 4 GLU A 58 90.20 -58.95
REMARK 500 4 LYS A 65 37.85 -146.54
REMARK 500 4 LEU A 68 69.44 72.79
REMARK 500 4 GLU A 73 38.82 177.11
REMARK 500
REMARK 500 THIS ENTRY HAS 155 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 53 0.30 SIDE CHAIN
REMARK 500 1 ARG A 55 0.28 SIDE CHAIN
REMARK 500 2 ARG A 53 0.24 SIDE CHAIN
REMARK 500 2 ARG A 55 0.15 SIDE CHAIN
REMARK 500 3 ARG A 53 0.23 SIDE CHAIN
REMARK 500 3 ARG A 55 0.31 SIDE CHAIN
REMARK 500 4 ARG A 53 0.21 SIDE CHAIN
REMARK 500 4 ARG A 55 0.21 SIDE CHAIN
REMARK 500 5 ARG A 53 0.22 SIDE CHAIN
REMARK 500 5 ARG A 55 0.32 SIDE CHAIN
REMARK 500 6 ARG A 53 0.29 SIDE CHAIN
REMARK 500 6 ARG A 55 0.30 SIDE CHAIN
REMARK 500 7 ARG A 53 0.27 SIDE CHAIN
REMARK 500 7 ARG A 55 0.28 SIDE CHAIN
REMARK 500 8 ARG A 53 0.12 SIDE CHAIN
REMARK 500 8 ARG A 55 0.31 SIDE CHAIN
REMARK 500 9 ARG A 53 0.31 SIDE CHAIN
REMARK 500 9 ARG A 55 0.31 SIDE CHAIN
REMARK 500 10 ARG A 53 0.17 SIDE CHAIN
REMARK 500 10 ARG A 55 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CDR A 1 77 UNP P13987 CD59_HUMAN 26 102
SEQRES 1 A 77 LEU GLN CYS TYR ASN CYS PRO ASN PRO THR ALA ASP CYS
SEQRES 2 A 77 LYS THR ALA VAL ASN CYS SER SER ASP PHE ASP ALA CYS
SEQRES 3 A 77 LEU ILE THR LYS ALA GLY LEU GLN VAL TYR ASN LYS CYS
SEQRES 4 A 77 TRP LYS PHE GLU HIS CYS ASN PHE ASN ASP VAL THR THR
SEQRES 5 A 77 ARG LEU ARG GLU ASN GLU LEU THR TYR TYR CYS CYS LYS
SEQRES 6 A 77 LYS ASP LEU CYS ASN PHE ASN GLU GLN LEU GLU ASN
MODRES 1CDR ASN A 18 ASN GLYCOSYLATION SITE
HET NAG B 1 26
HET NAG B 2 28
HET FUC B 3 21
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 FUC C6 H12 O5
HELIX 1 H1 PHE A 47 GLU A 56 1IRREGULAR H-BONDS AT C-T END 10
SHEET 1 S1 2 LEU A 1 CYS A 6 0
SHEET 2 S1 2 THR A 15 CYS A 19 -1 O VAL A 17 N CYS A 3
SHEET 1 S2 3 GLN A 34 TRP A 40 0
SHEET 2 S2 3 ALA A 25 ALA A 31 -1 N ALA A 25 O TRP A 40
SHEET 3 S2 3 LEU A 59 LYS A 65 -1 N CYS A 64 O CYS A 26
SSBOND 1 CYS A 3 CYS A 26 1555 1555 2.02
SSBOND 2 CYS A 6 CYS A 13 1555 1555 2.02
SSBOND 3 CYS A 19 CYS A 39 1555 1555 2.02
SSBOND 4 CYS A 45 CYS A 63 1555 1555 2.02
SSBOND 5 CYS A 64 CYS A 69 1555 1555 2.02
LINK ND2 ASN A 18 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39
LINK O6 NAG B 1 C1 FUC B 3 1555 1555 1.40
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
