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HEADER HORMONE 01-JUL-94 1HCN TITLE STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS TITLE 2 RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN CHORIONIC GONADOTROPIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HUMAN CHORIONIC GONADOTROPIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 MOL_ID: 2 KEYWDS HORMONE EXPDTA X-RAY DIFFRACTION AUTHOR H.WU,J.W.LUSTBADER,Y.LIU,R.E.CANFIELD,W.A.HENDRICKSON REVDAT 2 01-APR-03 1HCN 1 JRNL REVDAT 1 30-SEP-94 1HCN 0 JRNL AUTH H.WU,J.W.LUSTBADER,Y.LIU,R.E.CANFIELD, JRNL AUTH 2 W.A.HENDRICKSON JRNL TITL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 A JRNL TITL 2 RESOLUTION FROM MAD ANALYSIS OF THE JRNL TITL 3 SELENOMETHIONYL PROTEIN. JRNL REF STRUCTURE V. 2 545 1994 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.W.LUSTBADER,H.WU,S.BIRKEN,S.POLLAK,M.A.G.KOLKS, REMARK 1 AUTH 2 A.M.POUND,D.AUSTIN,W.A.HENDRICKSON,R.E.CANFIELD REMARK 1 TITL THE EXPRESSION, CHARACTERIZATION AND REMARK 1 TITL 2 CRYSTALLIZATION OF WILD-TYPE AND SELENOMETHIONYL REMARK 1 TITL 3 HCG REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ, X-PLOR REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 8876 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1462 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 63 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 4.498 ; 1.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.832 ; 1.500 REMARK 3 SIDE-CHAIN BOND (A**2) : 5.124 ; 1.500 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.713 ; 2.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HCN 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 3.100 (2007-03-17) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,2/3+Z REMARK 290 3555 -X+Y,-X,1/3+Z REMARK 290 4555 -X,-Y,1/2+Z REMARK 290 5555 Y,-X+Y,1/6+Z REMARK 290 6555 X-Y,X,5/6+Z REMARK 290 7555 Y,X,2/3-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,1/3-Z REMARK 290 10555 -Y,-X,1/6-Z REMARK 290 11555 -X+Y,Y,1/2-Z REMARK 290 12555 X,X-Y,5/6-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 118.46667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.23333 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 88.85000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 29.61667 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 148.08333 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 118.46667 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 59.23333 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 29.61667 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 88.85000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 148.08333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 1 REMARK 465 PRO A 2 REMARK 465 ASP A 3 REMARK 465 VAL A 4 REMARK 465 HIS A 90 REMARK 465 LYS A 91 REMARK 465 SER A 92 REMARK 465 SER B 1 REMARK 465 ASP B 112 REMARK 465 PRO B 113 REMARK 465 ARG B 114 REMARK 465 PHE B 115 REMARK 465 GLN B 116 REMARK 465 ASP B 117 REMARK 465 SER B 118 REMARK 465 SER B 119 REMARK 465 SER B 120 REMARK 465 SER B 121 REMARK 465 LYS B 122 REMARK 465 ALA B 123 REMARK 465 PRO B 124 REMARK 465 PRO B 125 REMARK 465 PRO B 126 REMARK 465 SER B 127 REMARK 465 LEU B 128 REMARK 465 PRO B 129 REMARK 465 SER B 130 REMARK 465 PRO B 131 REMARK 465 SER B 132 REMARK 465 ARG B 133 REMARK 465 LEU B 134 REMARK 465 PRO B 135 REMARK 465 GLY B 136 REMARK 465 PRO B 137 REMARK 465 SER B 138 REMARK 465 ASP B 139 REMARK 465 THR B 140 REMARK 465 PRO B 141 REMARK 465 ILE B 142 REMARK 465 LEU B 143 REMARK 465 PRO B 144 REMARK 465 GLN B 145 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 TYR A 89 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 2 CG CD CE NZ REMARK 470 ASP B 111 CG OD1 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 29 CG MET A 29 SD 0.144 REMARK 500 MET A 29 SD MET A 29 CE 0.118 REMARK 500 MET A 47 SD MET A 47 CE 0.108 REMARK 500 MET A 71 CG MET A 71 SD 0.105 REMARK 500 MET B 41 CG MET B 41 SD 0.145 REMARK 500 MET B 41 SD MET B 41 CE 0.120 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 MET A 29 CG - SD - CE ANGL. DEV. = 19.8 DEGREES REMARK 500 MET B 41 CG - SD - CE ANGL. DEV. =-15.0 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 TYR A 88 158.51 32.91 REMARK 500 LEU B 5 -50.54 88.85 DBREF 1HCN A 1 92 UNP P01215 GLHA_HUMAN 25 116 DBREF 1HCN B 1 145 UNP P01233 CGHB_HUMAN 21 165 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 SEQRES 1 B 145 SER LYS GLU PRO LEU ARG PRO ARG CYS ARG PRO ILE ASN SEQRES 2 B 145 ALA THR LEU ALA VAL GLU LYS GLU GLY CYS PRO VAL CYS SEQRES 3 B 145 ILE THR VAL ASN THR THR ILE CYS ALA GLY TYR CYS PRO SEQRES 4 B 145 THR MET THR ARG VAL LEU GLN GLY VAL LEU PRO ALA LEU SEQRES 5 B 145 PRO GLN VAL VAL CYS ASN TYR ARG ASP VAL ARG PHE GLU SEQRES 6 B 145 SER ILE ARG LEU PRO GLY CYS PRO ARG GLY VAL ASN PRO SEQRES 7 B 145 VAL VAL SER TYR ALA VAL ALA LEU SER CYS GLN CYS ALA SEQRES 8 B 145 LEU CYS ARG ARG SER THR THR ASP CYS GLY GLY PRO LYS SEQRES 9 B 145 ASP HIS PRO LEU THR CYS ASP ASP PRO ARG PHE GLN ASP SEQRES 10 B 145 SER SER SER SER LYS ALA PRO PRO PRO SER LEU PRO SER SEQRES 11 B 145 PRO SER ARG LEU PRO GLY PRO SER ASP THR PRO ILE LEU SEQRES 12 B 145 PRO GLN MODRES 1HCN ASN A 52 ASN GLYCOSYLATION SITE MODRES 1HCN ASN A 78 ASN GLYCOSYLATION SITE FTNOTE 1 CIS PROLINE - PRO B 50 HET NAG A 52 14 HET NAG A 78 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETSYN NAG NAG FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 5 HOH *63(H2 O) HELIX 1 A1 PRO A 40 MET A 47 1 8 SHEET 1 S1 3 PRO A 8 ASN A 15 0 SHEET 2 S1 3 ILE A 25 CYS A 32 -1 O ILE A 25 N ASN A 15 SHEET 3 S1 3 CYS B 38 THR B 40 -1 O THR B 40 N GLY A 30 SHEET 1 S2 5 PRO B 7 VAL B 18 0 SHEET 2 S2 5 ILE B 27 TYR B 37 -1 O ILE B 27 N VAL B 18 SHEET 3 S2 5 PHE A 33 THR A 39 -1 O SER A 34 N GLY B 36 SHEET 4 S2 5 ASN A 52 THR A 58 -1 O ASN A 52 N THR A 39 SHEET 5 S2 5 ASP B 99 GLY B 101 1 N ASP B 99 O VAL A 53 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 SSBOND 6 CYS B 9 CYS B 57 SSBOND 7 CYS B 23 CYS B 72 SSBOND 8 CYS B 26 CYS B 110 SSBOND 9 CYS B 34 CYS B 88 SSBOND 10 CYS B 38 CYS B 90 SSBOND 11 CYS B 93 CYS B 100 LINK ND2 ASN A 52 C1 NAG A 52 LINK ND2 ASN A 78 C1 NAG A 78 CISPEP 1 LEU B 49 PRO B 50 0 0.20 CRYST1 85.100 85.100 177.700 90.00 90.00 120.00 P 65 2 2 12 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 0.011751 0.006784 0.000000 0.00000 SCALE2 0.000000 0.013569 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005627 0.00000