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HEADER HORMONE/GROWTH FACTOR 30-OCT-04 1XWD TITLE CRYSTAL STRUCTURE OF HUMAN FOLLICLE STIMULATING HORMONE TITLE 2 COMPLEXED WITH ITS RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCOPROTEIN HORMONES ALPHA CHAIN; COMPND 3 CHAIN: A, D; COMPND 4 SYNONYM: FOLLITROPIN ALPHA CHAIN, FOLLICLE-STIMULATING COMPND 5 HORMONE ALPHA CHAIN, FSH-ALPHA, LUTROPIN ALPHA CHAIN, COMPND 6 LUTEINIZING HORMONE ALPHA CHAIN, LSH-ALPHA, THYROTROPIN COMPND 7 ALPHA CHAIN, THYROID-STIMULATING HORMONE ALPHA CHAIN, TSH- COMPND 8 ALPHA, CHORIOGONADOTROPIN ALPHA CHAIN, CHORIONIC COMPND 9 GONADOTROPHIN ALPHA SUBUNIT, CG-ALPHA; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: FOLLITROPIN BETA CHAIN; COMPND 13 CHAIN: B, E; COMPND 14 SYNONYM: FOLLICLE-STIMULATING HORMONE BETA SUBUNIT, FSH- COMPND 15 BETA, FSH-B; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: FOLLICLE STIMULATING HORMONE RECEPTOR; COMPND 19 CHAIN: C, F; COMPND 20 FRAGMENT: EXTRACELLULAR DOMAIN; COMPND 21 SYNONYM: FSH-R, FOLLITROPIN RECEPTOR; COMPND 22 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: CGA; SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIGH 5; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 GENE: FSHB; SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HIGH 5; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 GENE: FSHR; SOURCE 23 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 24 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: HIGH 5; SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL KEYWDS HORMONE-RECEPTOR COMPLEX, LEUCINE-RICH REPEATS, CYSTEINE- KEYWDS 2 KNOT MOTIF EXPDTA X-RAY DIFFRACTION AUTHOR Q.R.FAN,W.A.HENDRICKSON REVDAT 1 25-JAN-05 1XWD 0 JRNL AUTH Q.R.FAN,W.A.HENDRICKSON JRNL TITL STRUCTURE OF HUMAN FOLLICLE-STIMULATING HORMONE IN JRNL TITL 2 COMPLEX WITH ITS RECEPTOR. JRNL REF NATURE V. 433 269 2005 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.92 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0003 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.92 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 25282 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1262 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.92 REMARK 3 BIN RESOLUTION RANGE LOW : 3.08 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3271 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.2970 REMARK 3 BIN FREE R VALUE SET COUNT : 192 REMARK 3 BIN FREE R VALUE : 0.3560 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 7031 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.72000 REMARK 3 B22 (A**2) : -0.37000 REMARK 3 B33 (A**2) : -2.72000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.18000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.419 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.333 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.017 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7160 ; 0.010 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9737 ; 1.427 ; 1.976 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 856 ; 5.304 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 322 ;40.573 ;24.472 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1214 ;19.924 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;16.710 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1120 ; 0.089 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5292 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2955 ; 0.255 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4675 ; 0.323 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 214 ; 0.180 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 79 ; 0.255 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.064 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4405 ; 1.948 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7023 ; 2.884 ; 6.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3004 ; 2.901 ; 6.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2714 ; 4.234 ; 7.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : C F REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 11 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 C 18 C 27 6 REMARK 3 1 F 18 F 27 6 REMARK 3 2 C 28 C 66 1 REMARK 3 2 F 28 F 66 1 REMARK 3 3 C 67 C 68 6 REMARK 3 3 F 67 F 68 6 REMARK 3 4 C 69 C 91 1 REMARK 3 4 F 69 F 91 1 REMARK 3 5 C 92 C 93 6 REMARK 3 5 F 92 F 93 6 REMARK 3 6 C 94 C 166 1 REMARK 3 6 F 94 F 166 1 REMARK 3 7 C 167 C 168 6 REMARK 3 7 F 167 F 168 6 REMARK 3 8 C 169 C 215 1 REMARK 3 8 F 169 F 215 1 REMARK 3 9 C 216 C 217 6 REMARK 3 9 F 216 F 217 6 REMARK 3 10 C 218 C 244 1 REMARK 3 10 F 218 F 244 1 REMARK 3 11 C 245 C 250 6 REMARK 3 11 F 245 F 250 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 C (A): 1694 ; 0.37 ; 0.32 REMARK 3 LOOSE POSITIONAL 1 C (A): 178 ; 2.94 ; 10.00 REMARK 3 TIGHT THERMAL 1 C (A**2): 1694 ; 3.66 ; 3.16 REMARK 3 LOOSE THERMAL 1 C (A**2): 178 ; 16.04 ; 99.90 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 6 A 16 4 REMARK 3 1 D 6 D 16 4 REMARK 3 2 A 17 A 23 6 REMARK 3 2 D 17 D 23 6 REMARK 3 3 A 24 A 29 4 REMARK 3 3 D 24 D 29 4 REMARK 3 4 A 30 A 40 1 REMARK 3 4 D 30 D 40 1 REMARK 3 5 A 41 A 53 4 REMARK 3 5 D 41 D 53 4 REMARK 3 6 A 54 A 58 1 REMARK 3 6 D 54 D 58 1 REMARK 3 7 A 59 A 67 4 REMARK 3 7 D 59 D 67 4 REMARK 3 8 A 68 A 89 1 REMARK 3 8 D 68 D 89 1 REMARK 3 9 A 90 A 91 4 REMARK 3 9 D 90 D 91 4 REMARK 3 10 A 92 A 92 6 REMARK 3 10 D 92 D 92 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 2 A (A): 285 ; 0.40 ; 0.32 REMARK 3 MEDIUM POSITIONAL 2 A (A): 325 ; 0.57 ; 0.63 REMARK 3 LOOSE POSITIONAL 2 A (A): 60 ; 0.74 ; 10.00 REMARK 3 TIGHT THERMAL 2 A (A**2): 285 ; 6.64 ; 3.16 REMARK 3 MEDIUM THERMAL 2 A (A**2): 325 ; 5.23 ; 6.32 REMARK 3 LOOSE THERMAL 2 A (A**2): 60 ; 4.79 ; 99.90 REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : B E REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 14 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 3 B 4 4 REMARK 3 1 E 3 E 4 4 REMARK 3 2 B 5 B 12 1 REMARK 3 2 E 5 E 12 1 REMARK 3 3 B 13 B 15 4 REMARK 3 3 E 13 E 15 4 REMARK 3 4 B 16 B 35 1 REMARK 3 4 E 16 E 35 1 REMARK 3 5 B 36 B 37 4 REMARK 3 5 E 36 E 37 4 REMARK 3 6 B 38 B 42 6 REMARK 3 6 E 38 E 42 6 REMARK 3 7 B 43 B 47 4 REMARK 3 7 E 43 E 47 4 REMARK 3 8 B 48 B 55 1 REMARK 3 8 E 48 E 55 1 REMARK 3 9 B 56 B 75 4 REMARK 3 9 E 56 E 75 4 REMARK 3 10 B 76 B 93 1 REMARK 3 10 E 76 E 93 1 REMARK 3 11 B 94 B 99 4 REMARK 3 11 E 94 E 99 4 REMARK 3 12 B 100 B 101 6 REMARK 3 12 E 100 E 101 6 REMARK 3 13 B 102 B 106 1 REMARK 3 13 E 102 E 106 1 REMARK 3 14 B 107 B 107 6 REMARK 3 14 E 107 E 107 6 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 3 B (A): 462 ; 0.39 ; 0.32 REMARK 3 MEDIUM POSITIONAL 3 B (A): 297 ; 1.05 ; 0.63 REMARK 3 LOOSE POSITIONAL 3 B (A): 59 ; 1.11 ; 10.00 REMARK 3 TIGHT THERMAL 3 B (A**2): 462 ; 10.01 ; 3.16 REMARK 3 MEDIUM THERMAL 3 B (A**2): 297 ; 16.02 ; 6.32 REMARK 3 LOOSE THERMAL 3 B (A**2): 59 ; 9.41 ; 99.90 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 3 A 92 REMARK 3 RESIDUE RANGE : B 3 B 107 REMARK 3 RESIDUE RANGE : C 18 C 259 REMARK 3 ORIGIN FOR THE GROUP (A): 15.6897 -8.8262 51.2914 REMARK 3 T TENSOR REMARK 3 T11: -0.0210 T22: -0.0824 REMARK 3 T33: -0.0387 T12: -0.0261 REMARK 3 T13: -0.0480 T23: -0.0136 REMARK 3 L TENSOR REMARK 3 L11: 0.4631 L22: 0.8966 REMARK 3 L33: 1.8794 L12: -0.2297 REMARK 3 L13: 0.4158 L23: 0.0986 REMARK 3 S TENSOR REMARK 3 S11: 0.0367 S12: 0.0033 S13: -0.0242 REMARK 3 S21: 0.0644 S22: 0.0248 S23: -0.0550 REMARK 3 S31: 0.1184 S32: 0.1811 S33: -0.0615 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 6 D 92 REMARK 3 RESIDUE RANGE : E 3 E 107 REMARK 3 RESIDUE RANGE : F 18 F 250 REMARK 3 ORIGIN FOR THE GROUP (A): 19.4870 -43.3557 20.0938 REMARK 3 T TENSOR REMARK 3 T11: -0.1665 T22: -0.0380 REMARK 3 T33: -0.0448 T12: 0.0035 REMARK 3 T13: 0.0194 T23: -0.0058 REMARK 3 L TENSOR REMARK 3 L11: 1.0599 L22: 1.9714 REMARK 3 L33: 2.4145 L12: -0.1860 REMARK 3 L13: -0.4899 L23: 1.1100 REMARK 3 S TENSOR REMARK 3 S11: 0.0470 S12: 0.2397 S13: -0.0193 REMARK 3 S21: 0.1828 S22: -0.1388 S23: 0.1307 REMARK 3 S31: 0.0829 S32: -0.1850 S33: 0.0918 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XWD 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 RCSB030842. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-MAR-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.40 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 31-ID 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 : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25282 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.06900 REMARK 200 R SYM (I) : 0.06900 REMARK 200 FOR THE DATA SET : 12.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.38800 REMARK 200 R SYM FOR SHELL (I) : 0.38800 REMARK 200 FOR SHELL : 3.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1FL7 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM SULFATE, PH 6.4, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,Z REMARK 290 4555 1/2-X,1/2+Y,-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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.66500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.46900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.66500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.46900 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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 6 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, C, 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, K, L, M 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 ASN B 1 REMARK 465 SER B 2 REMARK 465 GLU B 108 REMARK 465 MET B 109 REMARK 465 LYS B 110 REMARK 465 GLU B 111 REMARK 465 GLY C 17 REMARK 465 LYS C 260 REMARK 465 LEU C 261 REMARK 465 VAL C 262 REMARK 465 ALA C 263 REMARK 465 LEU C 264 REMARK 465 MET C 265 REMARK 465 GLU C 266 REMARK 465 ALA C 267 REMARK 465 SER C 268 REMARK 465 ALA D 1 REMARK 465 PRO D 2 REMARK 465 ASP D 3 REMARK 465 VAL D 4 REMARK 465 GLN D 5 REMARK 465 ASN E 1 REMARK 465 SER E 2 REMARK 465 GLU E 108 REMARK 465 MET E 109 REMARK 465 LYS E 110 REMARK 465 GLU E 111 REMARK 465 GLY F 17 REMARK 465 ASN F 251 REMARK 465 LEU F 252 REMARK 465 LYS F 253 REMARK 465 LYS F 254 REMARK 465 LEU F 255 REMARK 465 PRO F 256 REMARK 465 THR F 257 REMARK 465 LEU F 258 REMARK 465 GLU F 259 REMARK 465 LYS F 260 REMARK 465 LEU F 261 REMARK 465 VAL F 262 REMARK 465 ALA F 263 REMARK 465 LEU F 264 REMARK 465 MET F 265 REMARK 465 GLU F 266 REMARK 465 ALA F 267 REMARK 465 SER F 268 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 ND2 ASN C 191 C2 NAG J 191 1.97 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 101 CB PRO B 101 CG -0.061 REMARK 500 THR C 56 CB THR C 56 CG2 -0.057 REMARK 500 PRO F 120 CB PRO F 120 CG -0.072 REMARK 500 PRO F 136 CB PRO F 136 CG -0.093 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 GLN A 5 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 ASP A 6 N - CA - C ANGL. DEV. = 10.2 DEGREES REMARK 500 MET A 71 N - CA - C ANGL. DEV. = 9.8 DEGREES REMARK 500 ASP B 41 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 LEU B 56 CA - CB - CG ANGL. DEV. = 9.2 DEGREES REMARK 500 HIS C 20 N - CA - C ANGL. DEV. =-14.8 DEGREES REMARK 500 LEU C 258 N - CA - C ANGL. DEV. =-10.1 DEGREES DBREF 1XWD A 1 92 UNP P01215 GLHA_HUMAN 25 116 DBREF 1XWD D 1 92 UNP P01215 GLHA_HUMAN 25 116 DBREF 1XWD B 1 111 UNP P01225 FSHB_HUMAN 19 129 DBREF 1XWD E 1 111 UNP P01225 FSHB_HUMAN 19 129 DBREF 1XWD C 17 268 UNP P23945 FSHR_HUMAN 17 268 DBREF 1XWD F 17 268 UNP P23945 FSHR_HUMAN 17 268 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 252 GLY CYS HIS HIS ARG ILE CYS HIS CYS SER ASN ARG VAL SEQRES 2 C 252 PHE LEU CYS GLN GLU SER LYS VAL THR GLU ILE PRO SER SEQRES 3 C 252 ASP LEU PRO ARG ASN ALA ILE GLU LEU ARG PHE VAL LEU SEQRES 4 C 252 THR LYS LEU ARG VAL ILE GLN LYS GLY ALA PHE SER GLY SEQRES 5 C 252 PHE GLY ASP LEU GLU LYS ILE GLU ILE SER GLN ASN ASP SEQRES 6 C 252 VAL LEU GLU VAL ILE GLU ALA ASP VAL PHE SER ASN LEU SEQRES 7 C 252 PRO LYS LEU HIS GLU ILE ARG ILE GLU LYS ALA ASN ASN SEQRES 8 C 252 LEU LEU TYR ILE ASN PRO GLU ALA PHE GLN ASN LEU PRO SEQRES 9 C 252 ASN LEU GLN TYR LEU LEU ILE SER ASN THR GLY ILE LYS SEQRES 10 C 252 HIS LEU PRO ASP VAL HIS LYS ILE HIS SER LEU GLN LYS SEQRES 11 C 252 VAL LEU LEU ASP ILE GLN ASP ASN ILE ASN ILE HIS THR SEQRES 12 C 252 ILE GLU ARG ASN SER PHE VAL GLY LEU SER PHE GLU SER SEQRES 13 C 252 VAL ILE LEU TRP LEU ASN LYS ASN GLY ILE GLN GLU ILE SEQRES 14 C 252 HIS ASN CYS ALA PHE ASN GLY THR GLN LEU ASP GLU LEU SEQRES 15 C 252 ASN LEU SER ASP ASN ASN ASN LEU GLU GLU LEU PRO ASN SEQRES 16 C 252 ASP VAL PHE HIS GLY ALA SER GLY PRO VAL ILE LEU ASP SEQRES 17 C 252 ILE SER ARG THR ARG ILE HIS SER LEU PRO SER TYR GLY SEQRES 18 C 252 LEU GLU ASN LEU LYS LYS LEU ARG ALA ARG SER THR TYR SEQRES 19 C 252 ASN LEU LYS LYS LEU PRO THR LEU GLU LYS LEU VAL ALA SEQRES 20 C 252 LEU MET GLU ALA SER SEQRES 1 D 92 ALA PRO ASP VAL GLN ASP CYS PRO GLU CYS THR LEU GLN SEQRES 2 D 92 GLU ASN PRO PHE PHE SER GLN PRO GLY ALA PRO ILE LEU SEQRES 3 D 92 GLN CYS MET GLY CYS CYS PHE SER ARG ALA TYR PRO THR SEQRES 4 D 92 PRO LEU ARG SER LYS LYS THR MET LEU VAL GLN LYS ASN SEQRES 5 D 92 VAL THR SER GLU SER THR CYS CYS VAL ALA LYS SER TYR SEQRES 6 D 92 ASN ARG VAL THR VAL MET GLY GLY PHE LYS VAL GLU ASN SEQRES 7 D 92 HIS THR ALA CYS HIS CYS SER THR CYS TYR TYR HIS LYS SEQRES 8 D 92 SER SEQRES 1 E 111 ASN SER CYS GLU LEU THR ASN ILE THR ILE ALA ILE GLU SEQRES 2 E 111 LYS GLU GLU CYS ARG PHE CYS ILE SER ILE ASN THR THR SEQRES 3 E 111 TRP CYS ALA GLY TYR CYS TYR THR ARG ASP LEU VAL TYR SEQRES 4 E 111 LYS ASP PRO ALA ARG PRO LYS ILE GLN LYS THR CYS THR SEQRES 5 E 111 PHE LYS GLU LEU VAL TYR GLU THR VAL ARG VAL PRO GLY SEQRES 6 E 111 CYS ALA HIS HIS ALA ASP SER LEU TYR THR TYR PRO VAL SEQRES 7 E 111 ALA THR GLN CYS HIS CYS GLY LYS CYS ASP SER ASP SER SEQRES 8 E 111 THR ASP CYS THR VAL ARG GLY LEU GLY PRO SER TYR CYS SEQRES 9 E 111 SER PHE GLY GLU MET LYS GLU SEQRES 1 F 252 GLY CYS HIS HIS ARG ILE CYS HIS CYS SER ASN ARG VAL SEQRES 2 F 252 PHE LEU CYS GLN GLU SER LYS VAL THR GLU ILE PRO SER SEQRES 3 F 252 ASP LEU PRO ARG ASN ALA ILE GLU LEU ARG PHE VAL LEU SEQRES 4 F 252 THR LYS LEU ARG VAL ILE GLN LYS GLY ALA PHE SER GLY SEQRES 5 F 252 PHE GLY ASP LEU GLU LYS ILE GLU ILE SER GLN ASN ASP SEQRES 6 F 252 VAL LEU GLU VAL ILE GLU ALA ASP VAL PHE SER ASN LEU SEQRES 7 F 252 PRO LYS LEU HIS GLU ILE ARG ILE GLU LYS ALA ASN ASN SEQRES 8 F 252 LEU LEU TYR ILE ASN PRO GLU ALA PHE GLN ASN LEU PRO SEQRES 9 F 252 ASN LEU GLN TYR LEU LEU ILE SER ASN THR GLY ILE LYS SEQRES 10 F 252 HIS LEU PRO ASP VAL HIS LYS ILE HIS SER LEU GLN LYS SEQRES 11 F 252 VAL LEU LEU ASP ILE GLN ASP ASN ILE ASN ILE HIS THR SEQRES 12 F 252 ILE GLU ARG ASN SER PHE VAL GLY LEU SER PHE GLU SER SEQRES 13 F 252 VAL ILE LEU TRP LEU ASN LYS ASN GLY ILE GLN GLU ILE SEQRES 14 F 252 HIS ASN CYS ALA PHE ASN GLY THR GLN LEU ASP GLU LEU SEQRES 15 F 252 ASN LEU SER ASP ASN ASN ASN LEU GLU GLU LEU PRO ASN SEQRES 16 F 252 ASP VAL PHE HIS GLY ALA SER GLY PRO VAL ILE LEU ASP SEQRES 17 F 252 ILE SER ARG THR ARG ILE HIS SER LEU PRO SER TYR GLY SEQRES 18 F 252 LEU GLU ASN LEU LYS LYS LEU ARG ALA ARG SER THR TYR SEQRES 19 F 252 ASN LEU LYS LYS LEU PRO THR LEU GLU LYS LEU VAL ALA SEQRES 20 F 252 LEU MET GLU ALA SER MODRES 1XWD ASN A 52 ASN GLYCOSYLATION SITE MODRES 1XWD ASN A 78 ASN GLYCOSYLATION SITE MODRES 1XWD ASN B 7 ASN GLYCOSYLATION SITE MODRES 1XWD ASN B 24 ASN GLYCOSYLATION SITE MODRES 1XWD ASN C 191 ASN GLYCOSYLATION SITE MODRES 1XWD ASN D 78 ASN GLYCOSYLATION SITE MODRES 1XWD ASN E 7 ASN GLYCOSYLATION SITE MODRES 1XWD ASN F 191 ASN GLYCOSYLATION SITE HET NAG H 52 14 HET NAG H 78 14 HET NAG I 7 14 HET NAG I 24 14 HET NAG J 191 14 HET NAG J 192 14 HET NAG K 78 14 HET NAG L 7 14 HET NAG M 191 14 HET NAG M 192 14 HET BMA M 193 11 HET SO4 401 5 HET SO4 402 5 HET SO4 403 5 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM SO4 SULFATE ION HETSYN NAG NAG FORMUL 7 NAG 10(C8 H15 N O6) FORMUL 14 BMA C6 H12 O6 FORMUL 15 SO4 3(O4 S 2-) FORMUL 18 HOH *50(H2 O) HELIX 1 1 PRO A 40 LYS A 45 1 6 HELIX 2 2 ARG D 42 THR D 46 5 5 HELIX 3 3 GLU E 15 ARG E 18 5 4 SHEET 1 A 4 THR A 11 GLU A 14 0 SHEET 2 A 4 LEU A 26 PRO A 38 -1 O GLN A 27 N GLN A 13 SHEET 3 A 4 PHE B 19 ARG B 35 -1 O THR B 34 N GLY A 30 SHEET 4 A 4 GLU B 4 LYS B 14 -1 N THR B 6 O TRP B 27 SHEET 1 B 4 THR A 11 GLU A 14 0 SHEET 2 B 4 LEU A 26 PRO A 38 -1 O GLN A 27 N GLN A 13 SHEET 3 B 4 VAL A 53 SER A 57 -1 O THR A 54 N TYR A 37 SHEET 4 B 4 THR B 92 THR B 95 1 O ASP B 93 N SER A 55 SHEET 1 C 2 CYS A 59 VAL A 70 0 SHEET 2 C 2 PHE A 74 SER A 85 -1 O SER A 85 N CYS A 59 SHEET 1 D 2 THR B 50 VAL B 63 0 SHEET 2 D 2 SER B 72 GLY B 85 -1 O GLY B 85 N THR B 50 SHEET 1 E12 CYS C 23 CYS C 25 0 SHEET 2 E12 VAL C 29 GLN C 33 -1 O LEU C 31 N HIS C 24 SHEET 3 E12 GLU C 50 VAL C 54 1 O ARG C 52 N PHE C 30 SHEET 4 E12 LYS C 74 SER C 78 1 O GLU C 76 N PHE C 53 SHEET 5 E12 GLU C 99 GLU C 103 1 O ARG C 101 N ILE C 77 SHEET 6 E12 TYR C 124 SER C 128 1 O LEU C 126 N ILE C 100 SHEET 7 E12 VAL C 147 GLN C 152 1 O ASP C 150 N LEU C 125 SHEET 8 E12 VAL C 173 TRP C 176 1 O TRP C 176 N LEU C 149 SHEET 9 E12 LEU C 195 ASN C 199 1 O GLU C 197 N LEU C 175 SHEET 10 E12 ILE C 222 ASP C 224 1 O ASP C 224 N LEU C 198 SHEET 11 E12 LYS C 243 ARG C 245 1 O LYS C 243 N LEU C 223 SHEET 12 E12 THR C 249 TYR C 250 -1 O TYR C 250 N LEU C 244 SHEET 1 F 3 VAL C 60 ILE C 61 0 SHEET 2 F 3 VAL C 85 ILE C 86 1 O VAL C 85 N ILE C 61 SHEET 3 F 3 TYR C 110 ILE C 111 1 O TYR C 110 N ILE C 86 SHEET 1 G 2 PHE C 91 SER C 92 0 SHEET 2 G 2 PHE C 116 GLN C 117 1 O GLN C 117 N PHE C 91 SHEET 1 H 2 THR C 159 ILE C 160 0 SHEET 2 H 2 GLU C 184 ILE C 185 1 O GLU C 184 N ILE C 160 SHEET 1 I 4 THR D 11 GLU D 14 0 SHEET 2 I 4 LEU D 26 PRO D 38 -1 O GLN D 27 N GLN D 13 SHEET 3 I 4 CYS E 20 ARG E 35 -1 O THR E 34 N GLY D 30 SHEET 4 I 4 GLU E 4 GLU E 13 -1 N THR E 6 O TRP E 27 SHEET 1 J 4 THR D 11 GLU D 14 0 SHEET 2 J 4 LEU D 26 PRO D 38 -1 O GLN D 27 N GLN D 13 SHEET 3 J 4 VAL D 53 SER D 57 -1 O THR D 54 N TYR D 37 SHEET 4 J 4 THR E 92 THR E 95 1 O THR E 95 N SER D 55 SHEET 1 K 2 CYS D 59 THR D 69 0 SHEET 2 K 2 LYS D 75 SER D 85 -1 O ASN D 78 N ASN D 66 SHEET 1 L 2 THR E 50 VAL E 63 0 SHEET 2 L 2 SER E 72 GLY E 85 -1 O GLN E 81 N LYS E 54 SHEET 1 M11 HIS F 24 CYS F 25 0 SHEET 2 M11 VAL F 29 GLN F 33 -1 O LEU F 31 N HIS F 24 SHEET 3 M11 GLU F 50 VAL F 54 1 O ARG F 52 N CYS F 32 SHEET 4 M11 LYS F 74 SER F 78 1 O GLU F 76 N LEU F 51 SHEET 5 M11 GLU F 99 ALA F 105 1 O ARG F 101 N ILE F 77 SHEET 6 M11 TYR F 124 THR F 130 1 O LEU F 126 N ILE F 100 SHEET 7 M11 VAL F 147 GLN F 152 1 O ASP F 150 N ILE F 127 SHEET 8 M11 SER F 172 TRP F 176 1 O ILE F 174 N VAL F 147 SHEET 9 M11 GLN F 194 ASN F 199 1 O GLU F 197 N LEU F 175 SHEET 10 M11 ILE F 222 ASP F 224 1 O ILE F 222 N LEU F 198 SHEET 11 M11 LYS F 243 ARG F 245 1 O LYS F 243 N LEU F 223 SHEET 1 N 3 VAL F 60 ILE F 61 0 SHEET 2 N 3 VAL F 85 ILE F 86 1 O VAL F 85 N ILE F 61 SHEET 3 N 3 TYR F 110 ILE F 111 1 O TYR F 110 N ILE F 86 SHEET 1 O 2 PHE F 91 SER F 92 0 SHEET 2 O 2 PHE F 116 GLN F 117 1 O GLN F 117 N PHE F 91 SHEET 1 P 2 THR F 159 ILE F 160 0 SHEET 2 P 2 GLU F 184 ILE F 185 1 O GLU F 184 N ILE F 160 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 18 CYS C 25 SSBOND 13 CYS C 23 CYS C 32 SSBOND 14 CYS D 7 CYS D 31 SSBOND 15 CYS D 10 CYS D 60 SSBOND 16 CYS D 28 CYS D 82 SSBOND 17 CYS D 32 CYS D 84 SSBOND 18 CYS D 59 CYS D 87 SSBOND 19 CYS E 3 CYS E 51 SSBOND 20 CYS E 17 CYS E 66 SSBOND 21 CYS E 20 CYS E 104 SSBOND 22 CYS E 28 CYS E 82 SSBOND 23 CYS E 32 CYS E 84 SSBOND 24 CYS E 87 CYS E 94 SSBOND 25 CYS F 18 CYS F 25 SSBOND 26 CYS F 23 CYS F 32 LINK C1 NAG H 52 ND2 ASN A 52 LINK C1 NAG H 78 ND2 ASN A 78 LINK C1 NAG I 7 ND2 ASN B 7 LINK C1 NAG I 24 ND2 ASN B 24 LINK C1 NAG J 191 ND2 ASN C 191 LINK C1 NAG K 78 ND2 ASN D 78 LINK C1 NAG L 7 ND2 ASN E 7 LINK C1 NAG M 191 ND2 ASN F 191 LINK O4 NAG J 191 C1 NAG J 192 LINK O4 NAG M 191 C1 NAG M 192 LINK O4 NAG M 192 C1 BMA M 193 CRYST1 121.330 66.938 148.629 90.00 99.13 90.00 C 1 2 1 8 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 0.008242 0.000000 0.001325 0.00000 SCALE2 0.000000 0.014939 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006814 0.00000