REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.SANDERS,M.EVANS,L.D.K.E.PREMAWARDHANA,H.DEPRAETERE, REMARK 1 AUTH 2 J.JEFFREYS,T.RICHARDS,J.FURMANIAK,B.R.SMITH REMARK 1 TITL HUMAN MONOCLONAL THYROID STIMULATING AUTOANTIBODY REMARK 1 REF LANCET V. 362 126 2003 REMARK 1 REFN ISSN 0140-6736 REMARK 1 PMID 12867115 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.SANDERS,J.JEFFREYS,H.DEPRAETERE,M.EVANS,T.RICHARDS, REMARK 1 AUTH 2 A.KIDDIE,K.BRERETON,L.D.K.E.PREMAWARDHANA,D.Y.CHIRGADZE, REMARK 1 AUTH 3 R.N.MIGUEL,T.L.BLUNDELL,J.FURMANIAK,B.R.SMITH REMARK 1 TITL CHARACTERISTICS OF A HUMAN MONOCLONAL AUTOANTIBODY TO THE REMARK 1 TITL 2 THYROTROPIN RECEPTOR: SEQUENCE STRUCTURE AND FUNCTION REMARK 1 REF THYROID V. 14 560 2004 REMARK 1 REFN ISSN 1050-7256 REMARK 1 PMID 15320966 REMARK 1 DOI 10.1089/1050725041692918 REMARK 1 REFERENCE 3 REMARK 1 AUTH R.N.MIGUEL,J.SANDERS,J.JEFFREYS,H.DEPRAETERE,M.EVANS, REMARK 1 AUTH 2 T.RICHARDS,T.L.BLUNDELL,B.REES SMITH,J.FURMANIAK REMARK 1 TITL ANALYSIS OF THE THYROTROPIN RECEPTOR-THYROTROPIN INTERACTION REMARK 1 TITL 2 BY COMPARATIVE MODELING REMARK 1 REF THYROID V. 14 991 2004 REMARK 1 REFN ISSN 1050-7256 REMARK 1 PMID 15650352 REMARK 1 DOI 10.1089/THY.2004.14.991 REMARK 1 REFERENCE 4 REMARK 1 AUTH R.N.MIGUEL,J.SANDERS,T.L.BLUNDELL,B.R.SMITH,J.FURMANIAK REMARK 1 TITL COMPARATIVE MODELLING OF THE THYROTROPIN RECEPTOR REMARK 1 REF THYROID V. 15 746 2005 REMARK 1 REFN ISSN 1050-7256 REMARK 1 REFERENCE 5 REMARK 1 AUTH J.SANDERS,J.BOLTON,P.SANDERS,J.JEFFREYS,N.NAKATAKE, REMARK 1 AUTH 2 T.RICHARDS,M.EVANS,A.KIDDIE,S.SUMMERHAYES,E.ROBERTS, REMARK 1 AUTH 3 R.N.MIGUEL,J.FURMANIAK,B.R.SMITH REMARK 1 TITL EFFECTS OF TSH RECEPTOR MUTATIONS ON BINDING AND BIOLOGICAL REMARK 1 TITL 2 ACTIVITY OF MONOCLONAL ANTIBODIES AND TSH REMARK 1 REF THYROID V. 16 1195 2006 REMARK 1 REFN ISSN 1050-7256 REMARK 1 PMID 17199429 REMARK 1 DOI 10.1089/THY.2006.16.1195 REMARK 1 REFERENCE 6 REMARK 1 AUTH J.SANDERS,R.N.MIGUEL,J.BOLTON,A.BHARDWAJA,P.SANDERS, REMARK 1 AUTH 2 N.NAKATAKE,M.EVANS,J.FURMANIAK,B.R.SMITH REMARK 1 TITL MOLECULAR INTERACTIONS BETWEEN THE TSH RECEPTOR AND A REMARK 1 TITL 2 THYROID-STIMULATING MONOCLONAL AUTOANTIBODY REMARK 1 REF THYROID V. 17 699 2007 REMARK 1 REFN ISSN 1050-7256 REMARK 1 PMID 17725428 REMARK 1 DOI 10.1089/THY.2007.0041 REMARK 1 REFERENCE 7 REMARK 1 AUTH R.N.MIGUEL,J.SANDERS,D.Y.CHIRGADZE,T.L.BLUNDELL,J.FURMANIAK, REMARK 1 AUTH 2 B.REES SMITH REMARK 1 TITL FSH AND TSH BINDING TO THEIR RESPECTIVE RECEPTORS: REMARK 1 TITL 2 SIMILARITIES, DIFFERENCES AND IMPLICATION FOR GLYCOPROTEIN REMARK 1 TITL 3 HORMONE SPECIFICITY REMARK 1 REF J.MOL.ENDOCRINOL. V. 41 145 2008 REMARK 1 REFN ISSN 0952-5041 REMARK 1 PMID 18606720 REMARK 1 DOI 10.1677/JME-08-0040 REMARK 1 REFERENCE 8 REMARK 1 AUTH R.N.MIGUEL,J.SANDERS,D.Y.CHIRGADZE,J.FURMANIAK,B.R.SMITH REMARK 1 TITL THYROID STIMULATING AUTOANTIBODY M22 MIMICS TSH IN ITS REMARK 1 TITL 2 BINDING TO THE TSH RECEPTOR: A COMPARATIVE STRUCTURAL STUDY REMARK 1 TITL 3 OF PROTEIN-PROTEIN INTERACTIONS REMARK 1 REF TO BE PUBLISHED 2009 REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. 2.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 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) : 2.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.72 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 3 NUMBER OF REFLECTIONS : 24426 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) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1301 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.55 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1803 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.99 REMARK 3 BIN R VALUE (WORKING SET) : 0.2240 REMARK 3 BIN FREE R VALUE SET COUNT : 95 REMARK 3 BIN FREE R VALUE : 0.3310 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5036 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 89 REMARK 3 SOLVENT ATOMS : 289 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 47.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.16000 REMARK 3 B22 (A**2) : -0.19000 REMARK 3 B33 (A**2) : 0.03000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.665 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.303 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.208 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.888 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5255 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7173 ; 1.236 ; 1.981 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 651 ; 6.528 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 202 ;39.599 ;24.604 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 834 ;16.207 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.934 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 831 ; 0.082 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3901 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2170 ; 0.201 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3515 ; 0.306 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 322 ; 0.146 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.177 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 51 ; 0.250 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.164 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.046 ; 0.200 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): 3363 ; 1.775 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5320 ; 2.673 ; 6.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2175 ; 2.261 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1853 ; 3.392 ; 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 : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 30 C 257 REMARK 3 ORIGIN FOR THE GROUP (A): 6.8220 74.0860 16.8290 REMARK 3 T TENSOR REMARK 3 T11: -0.0992 T22: -0.0050 REMARK 3 T33: -0.0796 T12: -0.0102 REMARK 3 T13: 0.0096 T23: 0.0087 REMARK 3 L TENSOR REMARK 3 L11: 0.1583 L22: 1.7188 REMARK 3 L33: 1.4269 L12: -0.2031 REMARK 3 L13: 0.0119 L23: 0.8203 REMARK 3 S TENSOR REMARK 3 S11: -0.0324 S12: 0.0579 S13: 0.0065 REMARK 3 S21: -0.0352 S22: -0.0012 S23: -0.0419 REMARK 3 S31: -0.0790 S32: -0.0457 S33: 0.0336 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1 B 114 REMARK 3 ORIGIN FOR THE GROUP (A): -5.7050 60.6090 38.7090 REMARK 3 T TENSOR REMARK 3 T11: -0.0899 T22: -0.0020 REMARK 3 T33: -0.0185 T12: -0.0633 REMARK 3 T13: 0.0330 T23: -0.0539 REMARK 3 L TENSOR REMARK 3 L11: 0.6876 L22: 0.2971 REMARK 3 L33: 3.0367 L12: 0.2497 REMARK 3 L13: -0.3280 L23: -0.2216 REMARK 3 S TENSOR REMARK 3 S11: 0.0225 S12: 0.0778 S13: -0.0143 REMARK 3 S21: 0.0199 S22: -0.0828 S23: -0.0021 REMARK 3 S31: 0.2942 S32: -0.2416 S33: 0.0603 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 115 B 213 REMARK 3 ORIGIN FOR THE GROUP (A): -16.4510 62.8160 73.8890 REMARK 3 T TENSOR REMARK 3 T11: -0.1106 T22: 0.0031 REMARK 3 T33: 0.0174 T12: 0.0620 REMARK 3 T13: -0.0154 T23: -0.0434 REMARK 3 L TENSOR REMARK 3 L11: 3.3868 L22: 3.6396 REMARK 3 L33: 4.7819 L12: 0.8695 REMARK 3 L13: -1.4842 L23: 1.2853 REMARK 3 S TENSOR REMARK 3 S11: -0.1155 S12: -0.2518 S13: 0.4632 REMARK 3 S21: 0.1353 S22: -0.0225 S23: 0.2909 REMARK 3 S31: -0.3013 S32: -0.3929 S33: 0.1380 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 108 REMARK 3 ORIGIN FOR THE GROUP (A): 12.2550 71.2810 45.0010 REMARK 3 T TENSOR REMARK 3 T11: -0.1118 T22: -0.0111 REMARK 3 T33: -0.0037 T12: 0.0125 REMARK 3 T13: 0.0205 T23: 0.0152 REMARK 3 L TENSOR REMARK 3 L11: 0.3322 L22: 1.1452 REMARK 3 L33: 1.9606 L12: 0.1726 REMARK 3 L13: 0.2609 L23: 0.7424 REMARK 3 S TENSOR REMARK 3 S11: 0.0079 S12: 0.0186 S13: -0.0030 REMARK 3 S21: 0.1340 S22: 0.0002 S23: -0.0481 REMARK 3 S31: 0.0447 S32: 0.0818 S33: -0.0081 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 109 A 208 REMARK 3 ORIGIN FOR THE GROUP (A): -1.0460 58.4750 79.4630 REMARK 3 T TENSOR REMARK 3 T11: -0.0636 T22: -0.0159 REMARK 3 T33: -0.0933 T12: -0.0312 REMARK 3 T13: 0.0285 T23: -0.0223 REMARK 3 L TENSOR REMARK 3 L11: 0.8201 L22: 3.2481 REMARK 3 L33: 1.0542 L12: 1.1967 REMARK 3 L13: -0.0249 L23: -0.4884 REMARK 3 S TENSOR REMARK 3 S11: -0.0206 S12: -0.1103 S13: -0.0105 REMARK 3 S21: 0.0996 S22: 0.0051 S23: 0.0388 REMARK 3 S31: -0.0492 S32: -0.0188 S33: 0.0154 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3G04 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-09. REMARK 100 THE RCSB ID CODE IS RCSB051254. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-NOV-06 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX14.2 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 CHANNEL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25731 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : 0.07100 REMARK 200 R SYM (I) : 0.07100 REMARK 200 FOR THE DATA SET : 10.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.61 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : 0.36100 REMARK 200 R SYM FOR SHELL (I) : 0.36100 REMARK 200 FOR SHELL : NULL 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 1XWD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 0.1M MES, 0.25M ZINC REMARK 280 ACETATE, PH 6.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y,-Z REMARK 290 8555 X,-Y,-Z+1/2 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 21.94400 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.90300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 87.89200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.90300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.94400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 87.89200 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 21.94400 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 87.89200 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 102.90300 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 87.89200 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.94400 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 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 102.90300 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7710 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH C 294 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 235 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 245 LIES ON A SPECIAL POSITION. 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 THR A 209 REMARK 465 GLU A 210 REMARK 465 CYS A 211 REMARK 465 SER A 212 REMARK 465 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 LYS B 214 REMARK 465 SER B 215 REMARK 465 CYS B 216 REMARK 465 ASP B 217 REMARK 465 LYS B 218 REMARK 465 THR B 219 REMARK 465 SER B 220 REMARK 465 MET C 22 REMARK 465 GLY C 23 REMARK 465 CYS C 24 REMARK 465 SER C 25 REMARK 465 SER C 26 REMARK 465 PRO C 27 REMARK 465 PRO C 28 REMARK 465 CYS C 29 REMARK 465 TRP C 258 REMARK 465 THR C 259 REMARK 465 LEU C 260 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 GLU C 35 CG CD OE1 OE2 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 DISTANCE REMARK 500 O HOH A 229 O HOH A 230 2.17 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 ARG A 16 -6.19 67.66 REMARK 500 ASN A 27B -93.82 -113.48 REMARK 500 ASP A 51 -46.06 78.53 REMARK 500 ASP A 52 13.41 -148.27 REMARK 500 LEU A 78 131.07 -39.40 REMARK 500 ASP A 151 -112.21 51.20 REMARK 500 ASP B 144 72.40 49.44 REMARK 500 THR B 191 -48.70 -136.64 REMARK 500 ASP C 36 62.19 -112.67 REMARK 500 ASP C 43 -22.17 70.17 REMARK 500 ILE C 85 64.35 60.52 REMARK 500 LEU C 125 77.40 -119.89 REMARK 500 ASN C 135 71.86 48.62 REMARK 500 GLU C 178 -144.88 -122.05 REMARK 500 LEU C 184 68.64 -118.98 REMARK 500 ASP C 203 -88.70 -99.60 REMARK 500 THR C 236 -163.95 -124.68 REMARK 500 ALA C 254 72.70 -150.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ASN C 77 21.9 L L OUTSIDE RANGE 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 B 255 DISTANCE = 5.20 ANGSTROMS REMARK 525 HOH C 375 DISTANCE = 5.18 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN C 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 63 NE2 REMARK 620 2 HOH B 257 O 81.9 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 5 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 6 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 303 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XWD RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN FOLLICLE STIMULATING HORMONE REMARK 900 COMPLEXED WITH ITS RECEPTOR