HEADER HORMONE 27-OCT-25 9YXD TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN FOLLICLE STIMULATING HORMONE IN TITLE 2 COMPLEX WITH AN ANTI-FSH ALPHA FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCOPROTEIN HORMONES ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ANTERIOR PITUITARY GLYCOPROTEIN HORMONES COMMON SUBUNIT COMPND 5 ALPHA,CHORIOGONADOTROPIN ALPHA CHAIN,CHORIONIC GONADOTROPHIN SUBUNIT COMPND 6 ALPHA,CG-ALPHA,FOLLICLE-STIMULATING HORMONE ALPHA CHAIN,FSH-ALPHA, COMPND 7 FOLLITROPIN ALPHA CHAIN,LUTEINIZING HORMONE ALPHA CHAIN,LSH-ALPHA, COMPND 8 LUTROPIN ALPHA CHAIN,THYROID-STIMULATING HORMONE ALPHA CHAIN,TSH- COMPND 9 ALPHA,THYROTROPIN ALPHA CHAIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: FOLLITROPIN SUBUNIT BETA; COMPND 13 CHAIN: B; COMPND 14 SYNONYM: FOLLICLE-STIMULATING HORMONE BETA SUBUNIT,FSH-B,FSH-BETA, COMPND 15 FOLLITROPIN BETA CHAIN; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: FAB LIGHT CHAIN; COMPND 19 CHAIN: C; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 4; COMPND 22 MOLECULE: FAB HEAVY CHAIN; COMPND 23 CHAIN: D; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 5; COMPND 26 MOLECULE: IG-LIKE DOMAIN-CONTAINING PROTEIN; COMPND 27 CHAIN: K; COMPND 28 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CGA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: PER.C6; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: FSHB; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: PER.C6; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 19 ORGANISM_TAXID: 10090; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 25 ORGANISM_TAXID: 10090; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 31 ORGANISM_TAXID: 9844; SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 33 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS GONADOTROPIN, GLYCOPROTEIN HORMONE, CYSTINE KNOT CYTOKINE, GPCR KEYWDS 2 SIGNALING, HORMONE EXPDTA X-RAY DIFFRACTION AUTHOR J.S.JOSEPH,D.KALSON,S.BAKSHI REVDAT 1 11-MAR-26 9YXD 0 JRNL AUTH D.KALSON,J.S.JOSEPH,S.BAKSHI JRNL TITL DISULFIDE BOND MAPPING OF RECOMBINANT HUMAN FSH ALPHA AT JRNL TITL 2 ATOMIC RESOLUTION BY X-RAY CRYSTALLOGRAPHY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.29 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5084 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.85 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 3 NUMBER OF REFLECTIONS : 55871 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 2814 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.8500 - 6.2000 1.00 2878 166 0.1974 0.2041 REMARK 3 2 6.2000 - 4.9300 1.00 2752 151 0.1686 0.1997 REMARK 3 3 4.9300 - 4.3100 1.00 2762 111 0.1430 0.1655 REMARK 3 4 4.3100 - 3.9100 1.00 2715 133 0.1638 0.1754 REMARK 3 5 3.9100 - 3.6300 1.00 2713 129 0.1920 0.2208 REMARK 3 6 3.6300 - 3.4200 1.00 2703 132 0.2082 0.2486 REMARK 3 7 3.4200 - 3.2500 1.00 2705 123 0.2228 0.2653 REMARK 3 8 3.2500 - 3.1100 1.00 2706 147 0.2480 0.2953 REMARK 3 9 3.1100 - 2.9900 1.00 2646 156 0.2381 0.2724 REMARK 3 10 2.9900 - 2.8900 1.00 2642 147 0.2377 0.2563 REMARK 3 11 2.8800 - 2.7900 1.00 2668 163 0.2381 0.2944 REMARK 3 12 2.7900 - 2.7100 1.00 2663 135 0.2468 0.3388 REMARK 3 13 2.7100 - 2.6400 1.00 2682 123 0.2620 0.3013 REMARK 3 14 2.6400 - 2.5800 1.00 2664 157 0.2433 0.2964 REMARK 3 15 2.5800 - 2.5200 1.00 2642 132 0.2379 0.2741 REMARK 3 16 2.5200 - 2.4700 1.00 2665 148 0.2301 0.2615 REMARK 3 17 2.4700 - 2.4200 1.00 2647 153 0.2247 0.2816 REMARK 3 18 2.4200 - 2.3700 0.98 2568 151 0.2367 0.2930 REMARK 3 19 2.3700 - 2.3300 0.91 2426 126 0.2452 0.2769 REMARK 3 20 2.3300 - 2.2900 0.84 2210 131 0.2685 0.3474 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.271 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.150 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 50.15 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.32 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 5929 REMARK 3 ANGLE : 0.952 8043 REMARK 3 CHIRALITY : 0.059 896 REMARK 3 PLANARITY : 0.008 1023 REMARK 3 DIHEDRAL : 15.395 2119 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9YXD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-25. REMARK 100 THE DEPOSITION ID IS D_1000301344. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-JUL-25 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56196 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290 REMARK 200 RESOLUTION RANGE LOW (A) : 29.850 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 33.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35 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 : 5.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.11 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M CALCIUM ACETATE, 0.1 M BIS-TRIS REMARK 280 PH 7, 30% V/V PEG 550 MME, PH 7.0, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+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 38.00500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.62000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.55150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.62000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.00500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.55150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, K, E 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 GLN A 5 REMARK 465 ASN B 1 REMARK 465 GLU B 108 REMARK 465 MET B 109 REMARK 465 LYS B 110 REMARK 465 GLU B 111 REMARK 465 ASP C 30 REMARK 465 SER C 31 REMARK 465 TYR C 32 REMARK 465 GLU C 219 REMARK 465 CYS C 220 REMARK 465 GLN D 1 REMARK 465 VAL D 2 REMARK 465 SER D 219 REMARK 465 CYS D 220 REMARK 465 ASP D 221 REMARK 465 LYS D 222 REMARK 465 THR D 223 REMARK 465 HIS D 224 REMARK 465 THR D 225 REMARK 465 HIS K -5 REMARK 465 HIS K -4 REMARK 465 HIS K -3 REMARK 465 HIS K -2 REMARK 465 HIS K -1 REMARK 465 HIS K 0 REMARK 465 GLN K 1 REMARK 465 SER K 121 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU C 181 CA - CB - CG ANGL. DEV. = 16.8 DEGREES 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 ALA A 23 59.23 -153.26 REMARK 500 CYS B 66 -156.29 -136.47 REMARK 500 HIS B 68 -4.26 88.14 REMARK 500 ALA C 55 -40.65 76.14 REMARK 500 SER C 56 6.46 -151.16 REMARK 500 SER C 71 -132.69 -132.25 REMARK 500 ASN C 80 116.01 -162.37 REMARK 500 ALA C 88 174.84 171.42 REMARK 500 ALA C 190 -71.81 -42.24 REMARK 500 SER D 85 71.62 30.99 REMARK 500 ASP D 148 62.34 63.54 REMARK 500 VAL K 48 -55.11 -120.47 REMARK 500 ARG K 53 155.59 -49.49 REMARK 500 ALA K 92 168.45 172.02 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 244 DISTANCE = 6.64 ANGSTROMS REMARK 525 HOH B 648 DISTANCE = 7.70 ANGSTROMS REMARK 525 HOH C 405 DISTANCE = 6.01 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG E 1 REMARK 610 NAG A 101 REMARK 610 NAG B 500 REMARK 610 NAG B 501 DBREF 9YXD A 1 92 UNP P01215 GLHA_HUMAN 25 116 DBREF 9YXD B 1 111 UNP P01225 FSHB_HUMAN 19 129 DBREF 9YXD C 1 220 PDB 9YXD 9YXD 1 220 DBREF 9YXD D 1 225 PDB 9YXD 9YXD 1 225 DBREF 9YXD K -5 121 PDB 9YXD 9YXD -5 121 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 THR 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 220 ASP ILE GLU LEU THR GLN SER PRO ASP SER LEU SER VAL SEQRES 2 C 220 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 C 220 GLU SER VAL ASP SER TYR GLY ASN SER PHE MET GLN TRP SEQRES 4 C 220 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 C 220 TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 C 220 PHE SER GLY THR GLY SER ARG THR ASP PHE THR LEU THR SEQRES 7 C 220 ILE ASN PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR SEQRES 8 C 220 CYS GLN GLN SER ASP GLU TYR PRO TYR MET TYR THR PHE SEQRES 9 C 220 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA SEQRES 10 C 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP SER GLN SEQRES 11 C 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 C 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 C 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 C 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 C 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 C 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 C 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 225 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 D 225 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER ASP SEQRES 3 D 225 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 D 225 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 D 225 PRO THR ASN GLY ARG THR TYR TYR ASN GLU LYS PHE LYS SEQRES 6 D 225 SER LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 D 225 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 D 225 ALA VAL TYR TYR CYS ALA ARG ARG TYR GLY ASN SER PHE SEQRES 9 D 225 ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 10 D 225 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 D 225 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 D 225 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 D 225 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 D 225 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 D 225 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 D 225 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 D 225 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 18 D 225 LYS THR HIS THR SEQRES 1 K 127 HIS HIS HIS HIS HIS HIS GLN VAL GLN LEU GLN GLU SER SEQRES 2 K 127 GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SEQRES 3 K 127 SER CYS ALA ALA SER GLY ARG THR ILE SER ARG TYR ALA SEQRES 4 K 127 MET SER TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 5 K 127 PHE VAL ALA VAL ALA ARG ARG SER GLY ASP GLY ALA PHE SEQRES 6 K 127 TYR ALA ASP SER VAL GLN GLY ARG PHE THR VAL SER ARG SEQRES 7 K 127 ASP ASP ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 8 K 127 LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ILE SEQRES 9 K 127 ASP SER ASP THR PHE TYR SER GLY SER TYR ASP TYR TRP SEQRES 10 K 127 GLY GLN GLY THR GLN VAL THR VAL SER SER HET NAG E 1 14 HET NAG E 2 14 HET NAG A 101 14 HET BTB A 102 33 HET NAG B 500 14 HET NAG B 501 14 HET GOL D 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL- HETNAM 2 BTB PROPANE-1,3-DIOL HETNAM GOL GLYCEROL HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BTB BIS-TRIS BUFFER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 6 NAG 5(C8 H15 N O6) FORMUL 8 BTB C8 H19 N O5 FORMUL 11 GOL C3 H8 O3 FORMUL 12 HOH *319(H2 O) HELIX 1 AA1 PRO A 16 SER A 19 5 4 HELIX 2 AA2 PRO A 40 LYS A 45 1 6 HELIX 3 AA3 GLU B 15 ARG B 18 5 4 HELIX 4 AA4 GLU C 83 VAL C 87 5 5 HELIX 5 AA5 SER C 127 SER C 133 1 7 HELIX 6 AA6 LYS C 189 LYS C 194 1 6 HELIX 7 AA7 THR D 28 TYR D 32 5 5 HELIX 8 AA8 GLU D 62 LYS D 65 5 4 HELIX 9 AA9 THR D 87 SER D 91 5 5 HELIX 10 AB1 SER D 131 LYS D 133 5 3 HELIX 11 AB2 SER D 160 ALA D 162 5 3 HELIX 12 AB3 SER D 191 LEU D 193 5 3 HELIX 13 AB4 LYS D 205 ASN D 208 5 4 HELIX 14 AB5 THR K 28 TYR K 32 5 5 HELIX 15 AB6 ASP K 62 GLN K 65 5 4 HELIX 16 AB7 ASP K 74 LYS K 76 5 3 HELIX 17 AB8 LYS K 87 THR K 91 5 5 SHEET 1 AA1 4 THR A 11 GLU A 14 0 SHEET 2 AA1 4 LEU A 26 PRO A 38 -1 O GLN A 27 N GLN A 13 SHEET 3 AA1 4 PHE B 19 ARG B 35 -1 O THR B 34 N GLY A 30 SHEET 4 AA1 4 GLU B 4 LYS B 14 -1 N THR B 6 O TRP B 27 SHEET 1 AA2 4 THR A 11 GLU A 14 0 SHEET 2 AA2 4 LEU A 26 PRO A 38 -1 O GLN A 27 N GLN A 13 SHEET 3 AA2 4 VAL A 53 SER A 57 -1 O THR A 54 N TYR A 37 SHEET 4 AA2 4 THR B 92 THR B 95 1 O ASP B 93 N SER A 55 SHEET 1 AA3 2 CYS A 59 VAL A 70 0 SHEET 2 AA3 2 PHE A 74 SER A 85 -1 O VAL A 76 N VAL A 68 SHEET 1 AA4 2 LYS B 49 VAL B 63 0 SHEET 2 AA4 2 SER B 72 LYS B 86 -1 O VAL B 78 N VAL B 57 SHEET 1 AA5 4 LEU C 4 SER C 7 0 SHEET 2 AA5 4 ALA C 19 ALA C 25 -1 O SER C 22 N SER C 7 SHEET 3 AA5 4 ASP C 74 ILE C 79 -1 O LEU C 77 N ILE C 21 SHEET 4 AA5 4 PHE C 66 GLY C 70 -1 N SER C 67 O THR C 78 SHEET 1 AA6 6 SER C 10 SER C 14 0 SHEET 2 AA6 6 THR C 108 LYS C 113 1 O LYS C 113 N VAL C 13 SHEET 3 AA6 6 ALA C 88 ASP C 96 -1 N ALA C 88 O LEU C 110 SHEET 4 AA6 6 SER C 35 GLN C 42 -1 N GLN C 38 O GLN C 93 SHEET 5 AA6 6 LYS C 49 TYR C 53 -1 O LEU C 51 N TRP C 39 SHEET 6 AA6 6 ASN C 57 LEU C 58 -1 O ASN C 57 N TYR C 53 SHEET 1 AA7 4 SER C 10 SER C 14 0 SHEET 2 AA7 4 THR C 108 LYS C 113 1 O LYS C 113 N VAL C 13 SHEET 3 AA7 4 ALA C 88 ASP C 96 -1 N ALA C 88 O LEU C 110 SHEET 4 AA7 4 MET C 101 PHE C 104 -1 O MET C 101 N ASP C 96 SHEET 1 AA8 4 SER C 120 PHE C 124 0 SHEET 2 AA8 4 THR C 135 PHE C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AA8 4 TYR C 179 SER C 188 -1 O LEU C 181 N LEU C 142 SHEET 4 AA8 4 SER C 165 VAL C 169 -1 N GLN C 166 O THR C 184 SHEET 1 AA9 4 ALA C 159 LEU C 160 0 SHEET 2 AA9 4 ALA C 150 VAL C 156 -1 N VAL C 156 O ALA C 159 SHEET 3 AA9 4 VAL C 197 HIS C 204 -1 O GLU C 201 N GLN C 153 SHEET 4 AA9 4 VAL C 211 ASN C 216 -1 O VAL C 211 N VAL C 202 SHEET 1 AB1 4 LEU D 4 GLN D 6 0 SHEET 2 AB1 4 VAL D 18 ALA D 24 -1 O LYS D 23 N GLN D 5 SHEET 3 AB1 4 THR D 78 LEU D 83 -1 O MET D 81 N LEU D 20 SHEET 4 AB1 4 ALA D 68 ASP D 73 -1 N ASP D 73 O THR D 78 SHEET 1 AB2 6 GLU D 10 VAL D 12 0 SHEET 2 AB2 6 THR D 111 VAL D 115 1 O THR D 114 N VAL D 12 SHEET 3 AB2 6 ALA D 92 TYR D 100 -1 N ALA D 92 O VAL D 113 SHEET 4 AB2 6 MET D 34 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AB2 6 LEU D 45 ILE D 51 -1 O GLU D 46 N LYS D 38 SHEET 6 AB2 6 THR D 58 TYR D 60 -1 O TYR D 59 N GLU D 50 SHEET 1 AB3 4 GLU D 10 VAL D 12 0 SHEET 2 AB3 4 THR D 111 VAL D 115 1 O THR D 114 N VAL D 12 SHEET 3 AB3 4 ALA D 92 TYR D 100 -1 N ALA D 92 O VAL D 113 SHEET 4 AB3 4 SER D 103 TRP D 107 -1 O SER D 103 N TYR D 100 SHEET 1 AB4 4 SER D 124 LEU D 128 0 SHEET 2 AB4 4 THR D 139 TYR D 149 -1 O LEU D 145 N PHE D 126 SHEET 3 AB4 4 TYR D 180 PRO D 189 -1 O VAL D 188 N ALA D 140 SHEET 4 AB4 4 VAL D 167 THR D 169 -1 N HIS D 168 O VAL D 185 SHEET 1 AB5 4 THR D 135 SER D 136 0 SHEET 2 AB5 4 THR D 139 TYR D 149 -1 O THR D 139 N SER D 136 SHEET 3 AB5 4 TYR D 180 PRO D 189 -1 O VAL D 188 N ALA D 140 SHEET 4 AB5 4 VAL D 173 LEU D 174 -1 N VAL D 173 O SER D 181 SHEET 1 AB6 3 THR D 155 TRP D 158 0 SHEET 2 AB6 3 ILE D 199 HIS D 204 -1 O ASN D 201 N SER D 157 SHEET 3 AB6 3 THR D 209 LYS D 214 -1 O VAL D 211 N VAL D 202 SHEET 1 AB7 4 GLN K 3 SER K 7 0 SHEET 2 AB7 4 LEU K 18 SER K 25 -1 O SER K 21 N SER K 7 SHEET 3 AB7 4 THR K 78 MET K 83 -1 O MET K 83 N LEU K 18 SHEET 4 AB7 4 PHE K 68 ASP K 73 -1 N ASP K 73 O THR K 78 SHEET 1 AB8 6 GLY K 10 VAL K 12 0 SHEET 2 AB8 6 THR K 115 VAL K 119 1 O THR K 118 N GLY K 10 SHEET 3 AB8 6 ALA K 92 ILE K 98 -1 N TYR K 94 O THR K 115 SHEET 4 AB8 6 MET K 34 GLN K 39 -1 N PHE K 37 O TYR K 95 SHEET 5 AB8 6 GLU K 46 ALA K 51 -1 O ALA K 49 N TRP K 36 SHEET 6 AB8 6 ALA K 58 TYR K 60 -1 O PHE K 59 N VAL K 50 SHEET 1 AB9 4 GLY K 10 VAL K 12 0 SHEET 2 AB9 4 THR K 115 VAL K 119 1 O THR K 118 N GLY K 10 SHEET 3 AB9 4 ALA K 92 ILE K 98 -1 N TYR K 94 O THR K 115 SHEET 4 AB9 4 TYR K 110 TRP K 111 -1 O TYR K 110 N ILE K 98 SSBOND 1 CYS A 7 CYS A 31 1555 1555 2.05 SSBOND 2 CYS A 10 CYS A 60 1555 1555 2.04 SSBOND 3 CYS A 28 CYS A 82 1555 1555 2.04 SSBOND 4 CYS A 32 CYS A 84 1555 1555 2.05 SSBOND 5 CYS A 59 CYS A 87 1555 1555 2.08 SSBOND 6 CYS B 3 CYS B 51 1555 1555 2.07 SSBOND 7 CYS B 17 CYS B 66 1555 1555 2.09 SSBOND 8 CYS B 20 CYS B 104 1555 1555 2.05 SSBOND 9 CYS B 28 CYS B 82 1555 1555 2.06 SSBOND 10 CYS B 32 CYS B 84 1555 1555 2.10 SSBOND 11 CYS B 87 CYS B 94 1555 1555 2.06 SSBOND 12 CYS C 23 CYS C 92 1555 1555 2.11 SSBOND 13 CYS C 140 CYS C 200 1555 1555 2.07 SSBOND 14 CYS D 22 CYS D 96 1555 1555 2.06 SSBOND 15 CYS D 144 CYS D 200 1555 1555 2.07 SSBOND 16 CYS K 22 CYS K 96 1555 1555 2.04 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 CISPEP 1 SER C 7 PRO C 8 0 -3.91 CISPEP 2 ASN C 80 PRO C 81 0 -3.32 CISPEP 3 TYR C 98 PRO C 99 0 -9.01 CISPEP 4 TYR C 146 PRO C 147 0 0.80 CISPEP 5 PHE D 150 PRO D 151 0 -7.36 CISPEP 6 GLU D 152 PRO D 153 0 -0.40 CRYST1 76.010 101.103 161.240 90.00 90.00 90.00 P 21 21 21 4 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 0.013156 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009891 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006202 0.00000