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HEADER GLYCOPROTEIN 18-OCT-00 1E9J TITLE SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMAN CHORIONIC TITLE 2 GONADOTROPIN [INCLUDING A SINGLE GLCNAC RESIDUE AT ASN52 TITLE 3 AND ASN78] 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 OTHER_DETAILS: ISOLATED FROM URINE OF PREGNANT WOME KEYWDS GLYCOPROTEIN, CHORIONIC GONADOTROPIN, HCG, NMR, XPLOR EXPDTA NMR, 26 STRUCTURES AUTHOR P.J.A.ERBEL,Y.KARIMI-NEJAD,J.A.VANKUIK,R.BOELENS, AUTHOR 2 J.P.KAMERLING,J.F.G.VLIEGENTHART REVDAT 2 01-APR-03 1E9J 1 JRNL REVDAT 1 25-JUL-02 1E9J 0 JRNL AUTH P.J.ERBEL,Y.KARIMI-NEJAD,J.A.VAN KUIK,R.BOELENS, JRNL AUTH 2 J.P.KAMERLING,J.F.VLIEGENTHART JRNL TITL EFFECTS OF THE N-LINKED GLYCANS ON THE 3D JRNL TITL 2 STRUCTURE OF THE FREE ALPHA-SUBUNIT OF HUMAN JRNL TITL 3 CHORIONIC GONADOTROPIN. JRNL REF BIOCHEMISTRY V. 39 6012 2000 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR 3.851 REMARK 3 AUTHORS : BRUNGER NUMBER OF NON-HYDROGEN ATOMS USED IN REMARK 3 REFINEMENT. PROTEIN ATOMS : 1381 NUCLEIC ACID REMARK 3 ATOMS : 0 HETEROGEN ATOMS : 46 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1E9J COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI. REMARK 100 THE EBI ID CODE IS EBI-5454. 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 : 100MM REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL 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 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER, VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XPLOR REMARK 210 METHOD USED : DG/SA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: STRUCTURAL STATISTICS FOR THE FAMILY OF 27 AHCG REMARK 210 CONFORMERS EXCLUDE THE FLEXIBLE LOOP AND ENDS, SEGMENTS 1-10, REMARK 210 29-58 AND 85-92 (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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 LEU A 26 N - CA - CB ANGL. DEV. = -5.0 DEGREES REMARK 500 1 GLU A 77 N - CA - C ANGL. DEV. = -5.3 DEGREES REMARK 500 2 GLU A 77 N - CA - C ANGL. DEV. = -5.1 DEGREES REMARK 500 3 LEU A 26 N - CA - CB ANGL. DEV. = -5.1 DEGREES REMARK 500 4 GLU A 77 N - CA - C ANGL. DEV. = -5.4 DEGREES REMARK 500 5 GLU A 77 N - CA - C ANGL. DEV. = -5.1 DEGREES REMARK 500 6 GLU A 77 N - CA - C ANGL. DEV. = -5.5 DEGREES REMARK 500 7 GLU A 77 N - CA - C ANGL. DEV. = -5.3 DEGREES REMARK 500 8 GLU A 77 N - CA - C ANGL. DEV. = -5.3 DEGREES REMARK 500 9 GLU A 77 N - CA - C ANGL. DEV. = -5.4 DEGREES REMARK 500 10 GLU A 77 N - CA - C ANGL. DEV. = -5.5 DEGREES REMARK 500 11 GLU A 77 N - CA - C ANGL. DEV. = -5.3 DEGREES REMARK 500 12 GLU A 77 N - CA - C ANGL. DEV. = -5.2 DEGREES REMARK 500 14 GLU A 77 N - CA - C ANGL. DEV. = -5.5 DEGREES REMARK 500 15 LEU A 26 N - CA - CB ANGL. DEV. = -5.1 DEGREES REMARK 500 16 GLU A 77 N - CA - C ANGL. DEV. = -5.5 DEGREES REMARK 500 17 GLU A 77 N - CA - C ANGL. DEV. = -5.8 DEGREES REMARK 500 18 LEU A 26 N - CA - CB ANGL. DEV. = -5.1 DEGREES REMARK 500 18 GLU A 77 N - CA - C ANGL. DEV. = -5.3 DEGREES REMARK 500 19 GLU A 77 N - CA - C ANGL. DEV. = -5.3 DEGREES REMARK 500 20 GLU A 77 N - CA - C ANGL. DEV. = -5.6 DEGREES REMARK 500 21 GLU A 77 N - CA - C ANGL. DEV. = -5.9 DEGREES REMARK 500 22 GLU A 77 N - CA - C ANGL. DEV. = -5.5 DEGREES REMARK 500 23 GLU A 77 N - CA - C ANGL. DEV. = -5.1 DEGREES REMARK 500 24 GLU A 77 N - CA - C ANGL. DEV. = -5.5 DEGREES REMARK 500 25 GLU A 77 N - CA - C ANGL. DEV. = -5.1 DEGREES REMARK 500 26 LEU A 26 CA - CB - CG ANGL. DEV. = -5.4 DEGREES REMARK 500 26 GLU A 77 N - CA - C ANGL. DEV. = -5.6 DEGREES DBREF 1E9J 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 MODRES ASN A 52 ASN GLYCOSYLATION SITE MODRES ASN A 78 ASN GLYCOSYLATION SITE MODRES 1E9J ASN A 52 ASN GLYCOSYLATION SITE MODRES 1E9J ASN A 78 ASN GLYCOSYLATION SITE HET NAG A1052 23 HET NAG A1078 23 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETSYN NAG NAG FORMUL 2 NAG 2(C8 H15 N O6) HELIX 1 1 VAL A 70 PHE A 74 5 5 SSBOND 1 CYS A 7 CYS A 31 SSBOND 2 CYS A 10 CYS A 60 SSBOND 3 CYS A 28 CYS A 82 SSBOND 4 CYS A 32 CYS A 84 SSBOND 5 CYS A 59 CYS A 87 LINK ND2 ASN A 52 C1 NAG A1052 LINK ND2 ASN A 78 C1 NAG A1078 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