Header list of 1dz7.pdb file
Complete list - t 9 2 Bytes
HEADER GLYCOPROTEIN 18-FEB-00 1DZ7
TITLE SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMAN CHORIONIC GONADOTROPIN
TITLE 2 [MODELED WITHOUT CARBOHYDRATE RESIDUES]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHORIONIC GONADOTROPIN;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: GLYCOSYLATED AT ASN52 AND ASN78
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 OTHER_DETAILS: ISOLATED FROM URINE OF PREGNANT WOMEN
KEYWDS GLYCOPROTEIN, CHORIONIC GONADOTROPIN, CHORIONIC GONADOTROPIN FREE A
KEYWDS 2 SUBUNIT, GLYCOPROTEIN STRUCTURE, CYSTINE KNOT, XPLOR
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR P.J.A.ERBEL,Y.KARIMI-NEJAD,T.DE BEER,R.BOELENS,J.P.KAMERLING,
AUTHOR 2 J.F.G.VLIEGENTHART
REVDAT 5 09-OCT-19 1DZ7 1 JRNL REMARK
REVDAT 4 24-JAN-18 1DZ7 1 JRNL REMARK
REVDAT 3 24-FEB-09 1DZ7 1 VERSN
REVDAT 2 22-APR-00 1DZ7 1 ATOM DBREF SEQRES
REVDAT 1 29-FEB-00 1DZ7 0
JRNL AUTH P.J.ERBEL,Y.KARIMI-NEJAD,T.DE BEER,R.BOELENS,J.P.KAMERLING,
JRNL AUTH 2 J.F.VLIEGENTHART
JRNL TITL SOLUTION STRUCTURE OF THE ALPHA-SUBUNIT OF HUMAN CHORIONIC
JRNL TITL 2 GONADOTROPIN.
JRNL REF EUR.J.BIOCHEM. V. 260 490 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10095786
JRNL DOI 10.1046/J.1432-1327.1999.00188.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SPECIAL REFINEMENT PROCEDURE TO
REMARK 3 OPTIMIZE CONVERGENCE RATE OF THE CYSTINE KNOT FORMATION
REMARK 4
REMARK 4 1DZ7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1290004634.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 328
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DG/SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: STRUCTURAL STATISTICS FOR THE FAMILY OF 27 AHCG CONFORMERS
REMARK 210 EXCLUDE THE FLEXIBLE LOOP AND ENDS, SEGMENTS 1-10, 29-58 AND 85-
REMARK 210 92 (SEE REFERENCE)
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 H GLN A 20 O ALA A 23 1.32
REMARK 500 O CYS A 59 H SER A 85 1.45
REMARK 500 H ASN A 15 O ILE A 25 1.50
REMARK 500 O THR A 11 H MET A 29 1.59
REMARK 500 H CYS A 59 O SER A 85 1.59
REMARK 500 O GLU A 77 N HIS A 79 2.15
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 CYS A 7 170.17 -51.63
REMARK 500 1 PRO A 8 -167.37 -51.17
REMARK 500 1 CYS A 10 118.64 -39.05
REMARK 500 1 THR A 11 -168.59 169.97
REMARK 500 1 GLN A 13 44.76 -93.93
REMARK 500 1 GLU A 14 115.95 -2.53
REMARK 500 1 PHE A 17 -61.53 -92.36
REMARK 500 1 SER A 19 125.47 -22.40
REMARK 500 1 PRO A 21 68.84 -58.81
REMARK 500 1 ALA A 23 118.65 -172.66
REMARK 500 1 PRO A 24 31.63 -80.79
REMARK 500 1 ILE A 25 178.56 38.58
REMARK 500 1 GLN A 27 74.83 169.45
REMARK 500 1 CYS A 28 109.92 -21.66
REMARK 500 1 CYS A 31 87.63 -153.33
REMARK 500 1 CYS A 32 97.26 -50.07
REMARK 500 1 PHE A 33 99.75 -54.25
REMARK 500 1 TYR A 37 79.22 -165.51
REMARK 500 1 LEU A 41 -177.70 53.26
REMARK 500 1 ARG A 42 47.43 172.88
REMARK 500 1 SER A 43 -60.09 -152.31
REMARK 500 1 LYS A 44 144.05 -37.66
REMARK 500 1 LYS A 45 -33.75 -177.68
REMARK 500 1 THR A 46 -154.14 -60.53
REMARK 500 1 MET A 47 -108.99 -55.64
REMARK 500 1 LEU A 48 127.70 71.12
REMARK 500 1 LYS A 51 41.84 -163.20
REMARK 500 1 ASN A 52 175.89 -47.21
REMARK 500 1 SER A 55 116.54 53.39
REMARK 500 1 GLU A 56 116.53 61.36
REMARK 500 1 THR A 58 153.85 -37.11
REMARK 500 1 ALA A 62 108.21 -8.36
REMARK 500 1 ARG A 67 119.79 -0.34
REMARK 500 1 THR A 69 118.21 -20.38
REMARK 500 1 MET A 71 134.44 -13.49
REMARK 500 1 PHE A 74 -178.78 -59.72
REMARK 500 1 GLU A 77 38.76 27.82
REMARK 500 1 ASN A 78 56.76 5.19
REMARK 500 1 HIS A 79 106.06 -33.90
REMARK 500 1 SER A 85 -159.65 -174.54
REMARK 500 1 TYR A 89 29.73 175.99
REMARK 500 1 HIS A 90 143.92 178.95
REMARK 500 2 ASP A 3 -93.28 -72.73
REMARK 500 2 VAL A 4 89.90 37.95
REMARK 500 2 GLN A 5 -138.24 -92.14
REMARK 500 2 ASP A 6 144.18 -23.08
REMARK 500 2 CYS A 7 104.58 -34.15
REMARK 500 2 PRO A 8 -172.42 -69.52
REMARK 500 2 THR A 11 -166.75 163.44
REMARK 500 2 GLN A 13 50.78 -102.59
REMARK 500
REMARK 500 THIS ENTRY HAS 1172 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HCN RELATED DB: PDB
REMARK 900 RELATED ID: 1HRP RELATED DB: PDB
REMARK 900 RELATED ID: 1XUL RELATED DB: PDB
DBREF 1DZ7 A 1 92 UNP P01215 GLHA_HUMAN 25 116
SEQRES 1 A 92 ALA PRO ASP VAL GLN ASP CYS PRO GLU CYS THR LEU GLN
SEQRES 2 A 92 GLU ASN PRO PHE PHE SER GLN PRO GLY ALA PRO ILE LEU
SEQRES 3 A 92 GLN CYS MET GLY CYS CYS PHE SER ARG ALA TYR PRO THR
SEQRES 4 A 92 PRO LEU ARG SER LYS LYS THR MET LEU VAL GLN LYS ASN
SEQRES 5 A 92 VAL THR SER GLU SER THR CYS CYS VAL ALA LYS SER TYR
SEQRES 6 A 92 ASN ARG VAL THR VAL MET GLY GLY PHE LYS VAL GLU ASN
SEQRES 7 A 92 HIS THR ALA CYS HIS CYS SER THR CYS TYR TYR HIS LYS
SEQRES 8 A 92 SER
HELIX 1 1 VAL A 70 PHE A 74 5 5
SHEET 1 A 2 CYS A 59 CYS A 60 0
SHEET 2 A 2 CYS A 84 SER A 85 -1 O SER A 85 N CYS A 59
SSBOND 1 CYS A 7 CYS A 31 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 60 1555 1555 2.03
SSBOND 3 CYS A 28 CYS A 82 1555 1555 2.03
SSBOND 4 CYS A 32 CYS A 84 1555 1555 2.03
SSBOND 5 CYS A 59 CYS A 87 1555 1555 2.03
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 - t 9 2 Bytes