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HEADER HORMONE/GROWTH FACTOR 11-AUG-00 1FL7 TITLE HUMAN FOLLICLE STIMULATING HORMONE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FOLLICLE STIMULATING PROTEIN ALPHA CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: GLYCOPROTEIN HORMONES ALPHA CHAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FOLLICLE STIMULATING PROTEIN BETA CHAIN; COMPND 8 CHAIN: B, D; COMPND 9 SYNONYM: FOLLITROPHIN BETA CHAIN; COMPND 10 ENGINEERED: YES; COMPND 11 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGAN: PITUITARY GLAND; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 9 OTHER_DETAILS: HOMO SAPIENS, PITUITARY GLAND; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGAN: PITUITARY GLAND; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 18 OTHER_DETAILS: HOMO SAPIENS, PITUITARY GLAND KEYWDS CYSTEINE KNOT, HETERODIMER EXPDTA X-RAY DIFFRACTION AUTHOR K.M.FOX,J.A.DIAS,P.VAN ROEY REVDAT 2 21-MAR-01 1FL7 1 REMARK REVDAT 1 14-MAR-01 1FL7 0 JRNL AUTH K.M.FOX,J.A.DIAS,P.VAN ROEY JRNL TITL THREE-DIMENSIONAL STRUCTURE OF HUMAN JRNL TITL 2 FOLLICLE-STIMULATING HORMONE. JRNL REF MOL.ENDOCRINOL. V. 15 378 2001 JRNL REFN ASTM MOENEN US ISSN 0888-8809 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.9 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 26449 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 SET) : 0.259 REMARK 3 FREE R VALUE : 0.294 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2650 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2987 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 200 REMARK 3 SOLVENT ATOMS : 0 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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.50 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.00 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FL7 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 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB011683. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JAN-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 9.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26534 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.07400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.80 REMARK 200 R MERGE FOR SHELL (I) : 0.33000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 - 1.2 M AMMONIUM SULFATE, 0.1 REMARK 280 M GLYCINE, PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 10K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.61000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.15000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.15000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.80500 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.15000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.15000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 116.41500 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.15000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.15000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 38.80500 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.15000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.15000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 116.41500 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.61000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 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, E, F, G 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, I, J 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 LYS A 91 REMARK 465 SER A 92 REMARK 465 ASN B 1 REMARK 465 SER B 2 REMARK 465 LYS B 110 REMARK 465 GLU B 111 REMARK 465 ALA C 1 REMARK 465 PRO C 2 REMARK 465 ASP C 3 REMARK 465 VAL C 4 REMARK 465 ASN D 1 REMARK 465 SER D 2 REMARK 465 MET D 109 REMARK 465 LYS D 110 REMARK 465 GLU D 111 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 HIS A 90 O CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 91 CG CD CE NZ REMARK 470 SER C 92 OG 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 PRO B 45 CB PRO B 45 CG 0.060 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 CYS A 59 CA - CB - SG ANGL. DEV. =-20.3 DEGREES REMARK 500 TYR A 88 N - CA - C ANGL. DEV. =-15.0 DEGREES REMARK 500 LEU B 5 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 PRO B 45 C - N - CD ANGL. DEV. = -9.0 DEGREES REMARK 500 ASN C 15 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 ILE C 25 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 ILE D 21 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 ASP D 93 N - CA - C ANGL. DEV. =-10.7 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 LYS B 46 82.97 131.49 REMARK 500 GLN B 48 133.76 66.41 REMARK 500 TYR C 88 -37.46 87.43 REMARK 500 HIS C 90 -124.77 177.16 DBREF 1FL7 A 1 92 UNP P01215 GLHA_HUMAN 25 116 DBREF 1FL7 C 1 92 UNP P01215 GLHA_HUMAN 25 116 DBREF 1FL7 B 1 111 UNP P01225 FSHB_HUMAN 19 129 DBREF 1FL7 D 1 111 UNP P01225 FSHB_HUMAN 19 129 SEQADV 1FL7 ALA B 26 UNP P01225 THR 44 ENGINEERED SEQADV 1FL7 ALA D 26 UNP P01225 THR 44 ENGINEERED 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 111 ASN SER CYS GLU LEU THR ASN ILE THR ILE ALA ILE GLU SEQRES 2 B 111 LYS GLU GLU CYS ARG PHE CYS ILE SER ILE ASN THR ALA SEQRES 3 B 111 TRP CYS ALA GLY TYR CYS TYR THR ARG ASP LEU VAL TYR SEQRES 4 B 111 LYS ASP PRO ALA ARG PRO LYS ILE GLN LYS THR CYS THR SEQRES 5 B 111 PHE LYS GLU LEU VAL TYR GLU THR VAL ARG VAL PRO GLY SEQRES 6 B 111 CYS ALA HIS HIS ALA ASP SER LEU TYR THR TYR PRO VAL SEQRES 7 B 111 ALA THR GLN CYS HIS CYS GLY LYS CYS ASP SER ASP SER SEQRES 8 B 111 THR ASP CYS THR VAL ARG GLY LEU GLY PRO SER TYR CYS SEQRES 9 B 111 SER PHE GLY GLU MET LYS GLU SEQRES 1 C 92 ALA PRO ASP VAL GLN ASP CYS PRO GLU CYS THR LEU GLN SEQRES 2 C 92 GLU ASN PRO PHE PHE SER GLN PRO GLY ALA PRO ILE LEU SEQRES 3 C 92 GLN CYS MET GLY CYS CYS PHE SER ARG ALA TYR PRO THR SEQRES 4 C 92 PRO LEU ARG SER LYS LYS THR MET LEU VAL GLN LYS ASN SEQRES 5 C 92 VAL THR SER GLU SER THR CYS CYS VAL ALA LYS SER TYR SEQRES 6 C 92 ASN ARG VAL THR VAL MET GLY GLY PHE LYS VAL GLU ASN SEQRES 7 C 92 HIS THR ALA CYS HIS CYS SER THR CYS TYR TYR HIS LYS SEQRES 8 C 92 SER SEQRES 1 D 111 ASN SER CYS GLU LEU THR ASN ILE THR ILE ALA ILE GLU SEQRES 2 D 111 LYS GLU GLU CYS ARG PHE CYS ILE SER ILE ASN THR ALA SEQRES 3 D 111 TRP CYS ALA GLY TYR CYS TYR THR ARG ASP LEU VAL TYR SEQRES 4 D 111 LYS ASP PRO ALA ARG PRO LYS ILE GLN LYS THR CYS THR SEQRES 5 D 111 PHE LYS GLU LEU VAL TYR GLU THR VAL ARG VAL PRO GLY SEQRES 6 D 111 CYS ALA HIS HIS ALA ASP SER LEU TYR THR TYR PRO VAL SEQRES 7 D 111 ALA THR GLN CYS HIS CYS GLY LYS CYS ASP SER ASP SER SEQRES 8 D 111 THR ASP CYS THR VAL ARG GLY LEU GLY PRO SER TYR CYS SEQRES 9 D 111 SER PHE GLY GLU MET LYS GLU MODRES 1FL7 ASN C 78 ASN GLYCOSYLATION SITE MODRES 1FL7 ASN A 78 ASN GLYCOSYLATION SITE MODRES 1FL7 ASN C 52 ASN GLYCOSYLATION SITE MODRES 1FL7 ASN D 7 ASN GLYCOSYLATION SITE MODRES 1FL7 ASN B 7 ASN GLYCOSYLATION SITE MODRES 1FL7 ASN A 52 ASN GLYCOSYLATION SITE HET NAG E 152 14 HET NDG E 252 14 HET NAG F 178 14 HET NAG F 278 14 HET MAN F 378 11 HET NAG G 107 14 HET NAG G 207 14 HET NAG H 152 14 HET NDG H 252 14 HET NAG I 178 14 HET NDG I 278 14 HET MAN I 378 11 HET NAG J 107 14 HET NAG J 207 14 HET SO4 410 5 HET SO4 510 5 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM SO4 SULFATE ION HETSYN NAG NAG FORMUL 5 NAG 9(C8 H15 N O6) FORMUL 5 NDG 3(C8 H15 N O6) FORMUL 6 MAN 2(C6 H12 O6) FORMUL 11 SO4 2(O4 S 2-) HELIX 1 1 PRO A 40 MET A 47 1 8 HELIX 2 2 GLU B 15 ARG B 18 5 4 HELIX 3 3 PRO C 40 THR C 46 1 7 HELIX 4 4 MET C 71 GLY C 73 5 3 HELIX 5 5 GLU D 15 ARG D 18 5 4 SHEET 1 A 4 LEU B 5 ASN B 7 0 SHEET 2 A 4 ALA B 26 ARG B 35 -1 N TRP B 27 O THR B 6 SHEET 3 A 4 LEU A 26 PRO A 38 -1 O GLY A 30 N THR B 34 SHEET 4 A 4 THR A 11 GLU A 14 -1 N THR A 11 O MET A 29 SHEET 1 B 5 LEU B 5 ASN B 7 0 SHEET 2 B 5 ALA B 26 ARG B 35 -1 N TRP B 27 O THR B 6 SHEET 3 B 5 LEU A 26 PRO A 38 -1 O GLY A 30 N THR B 34 SHEET 4 B 5 VAL A 53 GLU A 56 -1 O THR A 54 N TYR A 37 SHEET 5 B 5 THR B 92 THR B 95 1 N ASP B 93 O VAL A 53 SHEET 1 C 2 CYS A 60 TYR A 65 0 SHEET 2 C 2 HIS A 79 CYS A 84 -1 N THR A 80 O SER A 64 SHEET 1 D 2 VAL A 68 VAL A 70 0 SHEET 2 D 2 PHE A 74 VAL A 76 -1 O PHE A 74 N VAL A 70 SHEET 1 E 2 ILE B 10 LYS B 14 0 SHEET 2 E 2 PHE B 19 ILE B 23 -1 O PHE B 19 N LYS B 14 SHEET 1 F 2 THR B 52 VAL B 63 0 SHEET 2 F 2 SER B 72 HIS B 83 -1 O SER B 72 N VAL B 63 SHEET 1 G 4 GLU D 4 LYS D 14 0 SHEET 2 G 4 PHE D 19 ARG D 35 -1 O PHE D 19 N LYS D 14 SHEET 3 G 4 LEU C 26 PRO C 38 -1 O GLY C 30 N THR D 34 SHEET 4 G 4 THR C 11 GLU C 14 -1 N THR C 11 O MET C 29 SHEET 1 H 5 GLU D 4 LYS D 14 0 SHEET 2 H 5 PHE D 19 ARG D 35 -1 O PHE D 19 N LYS D 14 SHEET 3 H 5 LEU C 26 PRO C 38 -1 O GLY C 30 N THR D 34 SHEET 4 H 5 VAL C 53 SER C 57 -1 N THR C 54 O TYR C 37 SHEET 5 H 5 THR D 92 THR D 95 1 N ASP D 93 O VAL C 53 SHEET 1 I 2 CYS C 59 THR C 69 0 SHEET 2 I 2 LYS C 75 SER C 85 -1 N VAL C 76 O VAL C 68 SHEET 1 J 2 THR D 50 VAL D 63 0 SHEET 2 J 2 SER D 72 GLY D 85 -1 O SER D 72 N VAL D 63 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 3 CYS B 51 SSBOND 7 CYS B 17 CYS B 66 SSBOND 8 CYS B 20 CYS B 104 SSBOND 9 CYS B 28 CYS B 82 SSBOND 10 CYS B 32 CYS B 84 SSBOND 11 CYS B 87 CYS B 94 SSBOND 12 CYS C 7 CYS C 31 SSBOND 13 CYS C 10 CYS C 60 SSBOND 14 CYS C 28 CYS C 82 SSBOND 15 CYS C 32 CYS C 84 SSBOND 16 CYS C 59 CYS C 87 SSBOND 17 CYS D 3 CYS D 51 SSBOND 18 CYS D 17 CYS D 66 SSBOND 19 CYS D 20 CYS D 104 SSBOND 20 CYS D 28 CYS D 82 SSBOND 21 CYS D 32 CYS D 84 SSBOND 22 CYS D 87 CYS D 94 LINK O4 NAG J 107 C1 NAG J 207 LINK O4 NAG I 178 C1 NDG I 278 LINK C1 NAG F 278 O4 NAG F 178 LINK C1 NDG H 252 O4 NAG H 152 LINK O4 NAG F 278 C1 MAN F 378 LINK O4 NAG G 107 C1 NAG G 207 LINK C1 NDG E 252 O4 NAG E 152 LINK C1 MAN I 378 O4 NDG I 278 LINK ND2 ASN C 78 C1 NAG I 178 LINK C1 NAG F 178 ND2 ASN A 78 LINK C1 NAG H 152 ND2 ASN C 52 LINK ND2 ASN D 7 C1 NAG J 107 LINK C1 NAG G 107 ND2 ASN B 7 LINK C1 NAG E 152 ND2 ASN A 52 CISPEP 1 ARG B 44 PRO B 45 0 -0.39 CRYST1 128.300 128.300 155.220 90.00 90.00 90.00 P 41 21 2 16 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 0.007794 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007794 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006442 0.00000