HEADER IMMUNE SYSTEM 27-JAN-09 3G04
TITLE CRYSTAL STRUCTURE OF THE TSH RECEPTOR IN COMPLEX WITH A THYROID-
TITLE 2 STIMULATING AUTOANTIBODY
CAVEAT 3G04 NAG A 213 HAS WRONG CHIRALITY AT ATOM C1 NAG C 1 HAS WRONG
CAVEAT 2 3G04 CHIRALITY AT ATOM C1 NAG C 2 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 3 3G04 NAG C 3 HAS WRONG CHIRALITY AT ATOM C1 NAG C 5 HAS WRONG
CAVEAT 4 3G04 CHIRALITY AT ATOM C1 NAG C 6 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN THYROID STIMULATING AUTOANTIBODY M22 LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FAB FRAGMENT LIGHT CHAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HUMAN THYROID STIMULATING AUTOANTIBODY M22 HEAVY CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: FAB FRAGMENT HEAVY CHAIN;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: THYROTROPIN RECEPTOR;
COMPND 13 CHAIN: C;
COMPND 14 FRAGMENT: LEUCINE RICH REPEAT DOMAIN (SEGMENT 22-260);
COMPND 15 SYNONYM: THYROID-STIMULATING HORMONE RECEPTOR, TSH-R;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: MOUSE-HUMAN HETEROHYBRIDOMA CELL LINE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 37965;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: MOUSE-HUMAN HETEROHYBRIDOMA CELL LINE;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 37965;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: TSHR;
SOURCE 18 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS TSH RECEPTOR, GPCR, THYROID, GRAVES' DISEASE, AUTOIMMUNITY, RECEPTOR-
KEYWDS 2 AUTOANTIBODY COMPLEX, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SANDERS,D.Y.CHIRGADZE,P.SANDERS,S.BAKER,A.SULLIVAN,A.BHARDWAJA,
AUTHOR 2 J.BOLTON,M.REEVE,N.NAKATAKE,M.EVANS,T.RICHARDS,M.POWELL,R.N.MIGUEL,
AUTHOR 3 T.L.BLUNDELL,J.FURMANIAK,B.R.SMITH
REVDAT 4 01-NOV-23 3G04 1 HETSYN
REVDAT 3 29-JUL-20 3G04 1 CAVEAT COMPND REMARK HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 13-JUL-11 3G04 1 VERSN
REVDAT 1 04-AUG-09 3G04 0
JRNL AUTH J.SANDERS,D.Y.CHIRGADZE,P.SANDERS,S.BAKER,A.SULLIVAN,
JRNL AUTH 2 A.BHARDWAJA,J.BOLTON,M.REEVE,N.NAKATAKE,M.EVANS,T.RICHARDS,
JRNL AUTH 3 M.POWELL,R.N.MIGUEL,T.L.BLUNDELL,J.FURMANIAK,B.R.SMITH
JRNL TITL CRYSTAL STRUCTURE OF THE TSH RECEPTOR IN COMPLEX WITH A
JRNL TITL 2 THYROID-STIMULATING AUTOANTIBODY
JRNL REF THYROID V. 17 395 2007
JRNL REFN ISSN 1050-7256
JRNL PMID 17542669
JRNL DOI 10.1089/THY.2007.0034
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,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2175 ; 2.261 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1853 ; 3.392 ; 7.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 DEPOSITION ID IS D_1000051254.
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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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: A, B, C
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 A 245 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 235 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 294 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 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 HOH B 257 O
REMARK 620 2 HIS C 63 NE2 81.9
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XWD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN FOLLICLE STIMULATING HORMONE COMPLEXED
REMARK 900 WITH ITS RECEPTOR
DBREF 3G04 A 1 212 PDB 3G04 3G04 1 212
DBREF 3G04 B 1 220 PDB 3G04 3G04 1 220
DBREF 3G04 C 22 260 UNP P16473 TSHR_HUMAN 22 260
SEQRES 1 A 216 LEU THR VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA
SEQRES 2 A 216 PRO ARG GLN ARG VAL THR ILE SER CYS SER GLY ASN SER
SEQRES 3 A 216 SER ASN ILE GLY ASN ASN ALA VAL ASN TRP TYR GLN GLN
SEQRES 4 A 216 LEU PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TYR ASP
SEQRES 5 A 216 ASP GLN LEU PRO SER GLY VAL SER ASP ARG PHE SER GLY
SEQRES 6 A 216 SER ARG SER GLY THR SER ALA SER LEU ALA ILE ARG GLY
SEQRES 7 A 216 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS THR SER
SEQRES 8 A 216 TRP ASP ASP SER LEU ASP SER GLN LEU PHE GLY GLY GLY
SEQRES 9 A 216 THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO
SEQRES 10 A 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 A 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 A 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER
SEQRES 13 A 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER
SEQRES 14 A 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 A 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR
SEQRES 16 A 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 A 216 THR VAL ALA PRO THR GLU CYS SER
SEQRES 1 B 228 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 B 228 PRO GLY GLU SER LEU LYS ILE SER CYS ARG GLY SER GLY
SEQRES 3 B 228 TYR ARG PHE THR SER TYR TRP ILE ASN TRP VAL ARG GLN
SEQRES 4 B 228 LEU PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP
SEQRES 5 B 228 PRO THR ASP SER TYR THR ASN TYR SER PRO SER PHE LYS
SEQRES 6 B 228 GLY HIS VAL THR VAL SER ALA ASP LYS SER ILE ASN THR
SEQRES 7 B 228 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR
SEQRES 8 B 228 GLY MET TYR TYR CYS ALA ARG LEU GLU PRO GLY TYR SER
SEQRES 9 B 228 SER THR TRP SER VAL ASN TRP GLY GLN GLY THR LEU VAL
SEQRES 10 B 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE
SEQRES 11 B 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR
SEQRES 12 B 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU
SEQRES 13 B 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER
SEQRES 14 B 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY
SEQRES 15 B 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER
SEQRES 16 B 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS
SEQRES 17 B 228 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO
SEQRES 18 B 228 LYS SER CYS ASP LYS THR SER
SEQRES 1 C 239 MET GLY CYS SER SER PRO PRO CYS GLU CYS HIS GLN GLU
SEQRES 2 C 239 GLU ASP PHE ARG VAL THR CYS LYS ASP ILE GLN ARG ILE
SEQRES 3 C 239 PRO SER LEU PRO PRO SER THR GLN THR LEU LYS LEU ILE
SEQRES 4 C 239 GLU THR HIS LEU ARG THR ILE PRO SER HIS ALA PHE SER
SEQRES 5 C 239 ASN LEU PRO ASN ILE SER ARG ILE TYR VAL SER ILE ASP
SEQRES 6 C 239 VAL THR LEU GLN GLN LEU GLU SER HIS SER PHE TYR ASN
SEQRES 7 C 239 LEU SER LYS VAL THR HIS ILE GLU ILE ARG ASN THR ARG
SEQRES 8 C 239 ASN LEU THR TYR ILE ASP PRO ASP ALA LEU LYS GLU LEU
SEQRES 9 C 239 PRO LEU LEU LYS PHE LEU GLY ILE PHE ASN THR GLY LEU
SEQRES 10 C 239 LYS MET PHE PRO ASP LEU THR LYS VAL TYR SER THR ASP
SEQRES 11 C 239 ILE PHE PHE ILE LEU GLU ILE THR ASP ASN PRO TYR MET
SEQRES 12 C 239 THR SER ILE PRO VAL ASN ALA PHE GLN GLY LEU CYS ASN
SEQRES 13 C 239 GLU THR LEU THR LEU LYS LEU TYR ASN ASN GLY PHE THR
SEQRES 14 C 239 SER VAL GLN GLY TYR ALA PHE ASN GLY THR LYS LEU ASP
SEQRES 15 C 239 ALA VAL TYR LEU ASN LYS ASN LYS TYR LEU THR VAL ILE
SEQRES 16 C 239 ASP LYS ASP ALA PHE GLY GLY VAL TYR SER GLY PRO SER
SEQRES 17 C 239 LEU LEU ASP VAL SER GLN THR SER VAL THR ALA LEU PRO
SEQRES 18 C 239 SER LYS GLY LEU GLU HIS LEU LYS GLU LEU ILE ALA ARG
SEQRES 19 C 239 ASN THR TRP THR LEU
MODRES 3G04 ASN A 26 ASN GLYCOSYLATION SITE
MODRES 3G04 ASN C 77 ASN GLYCOSYLATION SITE
MODRES 3G04 ASN C 99 ASN GLYCOSYLATION SITE
MODRES 3G04 ASN C 113 ASN GLYCOSYLATION SITE
MODRES 3G04 ASN C 177 ASN GLYCOSYLATION SITE
MODRES 3G04 ASN C 198 ASN GLYCOSYLATION SITE
HET NAG A 213 14
HET ZN A 304 1
HET ZN A 305 1
HET NAG C 1 14
HET NAG C 2 14
HET NAG C 3 14
HET NAG C 5 14
HET NAG C 6 14
HET ZN C 301 1
HET ZN C 302 1
HET ZN C 303 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
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
FORMUL 4 NAG 6(C8 H15 N O6)
FORMUL 5 ZN 5(ZN 2+)
FORMUL 15 HOH *289(H2 O)
HELIX 1 1 GLN A 79 GLU A 83 5 5
HELIX 2 2 SER A 121 ALA A 127 1 7
HELIX 3 3 THR A 181 HIS A 188 1 8
HELIX 4 4 ARG B 28 TYR B 32 5 5
HELIX 5 5 LYS B 73 ILE B 75 5 3
HELIX 6 6 LYS B 83 THR B 87 5 5
HELIX 7 7 SER B 156 ALA B 158 5 3
HELIX 8 8 SER B 187 LEU B 189 5 3
HELIX 9 9 LYS B 201 ASN B 204 5 4
SHEET 1 A 5 SER A 9 GLY A 13 0
SHEET 2 A 5 THR A 102 VAL A 106 1 O THR A 105 N VAL A 11
SHEET 3 A 5 ASP A 85 ASP A 92 -1 N TYR A 86 O THR A 102
SHEET 4 A 5 ASN A 34 GLN A 38 -1 N GLN A 38 O ASP A 85
SHEET 5 A 5 LYS A 45 ILE A 48 -1 O ILE A 48 N TRP A 35
SHEET 1 B 4 SER A 9 GLY A 13 0
SHEET 2 B 4 THR A 102 VAL A 106 1 O THR A 105 N VAL A 11
SHEET 3 B 4 ASP A 85 ASP A 92 -1 N TYR A 86 O THR A 102
SHEET 4 B 4 SER A 95B PHE A 98 -1 O SER A 95B N ASP A 92
SHEET 1 C 3 VAL A 19 SER A 24 0
SHEET 2 C 3 SER A 70 ILE A 75 -1 O ILE A 75 N VAL A 19
SHEET 3 C 3 PHE A 62 SER A 67 -1 N SER A 63 O ALA A 74
SHEET 1 D 4 SER A 114 PHE A 118 0
SHEET 2 D 4 ALA A 130 PHE A 139 -1 O LEU A 135 N THR A 116
SHEET 3 D 4 TYR A 172 LEU A 180 -1 O ALA A 174 N ILE A 136
SHEET 4 D 4 VAL A 159 THR A 161 -1 N GLU A 160 O TYR A 177
SHEET 1 E 4 SER A 114 PHE A 118 0
SHEET 2 E 4 ALA A 130 PHE A 139 -1 O LEU A 135 N THR A 116
SHEET 3 E 4 TYR A 172 LEU A 180 -1 O ALA A 174 N ILE A 136
SHEET 4 E 4 SER A 165 LYS A 166 -1 N SER A 165 O ALA A 173
SHEET 1 F 4 SER A 153 VAL A 155 0
SHEET 2 F 4 THR A 145 ALA A 150 -1 N ALA A 150 O SER A 153
SHEET 3 F 4 TYR A 191 HIS A 197 -1 O GLN A 194 N ALA A 147
SHEET 4 F 4 SER A 200 VAL A 206 -1 O VAL A 202 N VAL A 195
SHEET 1 G 4 GLN B 3 GLN B 6 0
SHEET 2 G 4 LEU B 18 SER B 25 -1 O ARG B 23 N VAL B 5
SHEET 3 G 4 THR B 77 TRP B 82 -1 O ALA B 78 N CYS B 22
SHEET 4 G 4 THR B 68 ASP B 72 -1 N SER B 70 O TYR B 79
SHEET 1 H 6 GLU B 10 LYS B 12 0
SHEET 2 H 6 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10
SHEET 3 H 6 GLY B 88 LEU B 95 -1 N GLY B 88 O VAL B 109
SHEET 4 H 6 TRP B 33 GLN B 39 -1 N GLN B 39 O MET B 89
SHEET 5 H 6 LEU B 45 ILE B 51 -1 O GLU B 46 N ARG B 38
SHEET 6 H 6 THR B 57 TYR B 59 -1 O ASN B 58 N ARG B 50
SHEET 1 I 4 GLU B 10 LYS B 12 0
SHEET 2 I 4 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10
SHEET 3 I 4 GLY B 88 LEU B 95 -1 N GLY B 88 O VAL B 109
SHEET 4 I 4 SER B 100D TRP B 103 -1 O ASN B 102 N ARG B 94
SHEET 1 J 4 SER B 120 LEU B 124 0
SHEET 2 J 4 THR B 135 TYR B 145 -1 O LYS B 143 N SER B 120
SHEET 3 J 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136
SHEET 4 J 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181
SHEET 1 K 4 SER B 120 LEU B 124 0
SHEET 2 K 4 THR B 135 TYR B 145 -1 O LYS B 143 N SER B 120
SHEET 3 K 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136
SHEET 4 K 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177
SHEET 1 L 3 THR B 151 TRP B 154 0
SHEET 2 L 3 ILE B 195 HIS B 200 -1 O ASN B 199 N THR B 151
SHEET 3 L 3 THR B 205 LYS B 210 -1 O THR B 205 N HIS B 200
SHEET 1 M11 CYS C 31 GLU C 34 0
SHEET 2 M11 ARG C 38 CYS C 41 -1 O THR C 40 N HIS C 32
SHEET 3 M11 THR C 56 ILE C 60 1 O LYS C 58 N VAL C 39
SHEET 4 M11 ARG C 80 SER C 84 1 O TYR C 82 N LEU C 59
SHEET 5 M11 HIS C 105 THR C 111 1 O ARG C 109 N VAL C 83
SHEET 6 M11 PHE C 130 THR C 136 1 O GLY C 132 N ILE C 108
SHEET 7 M11 PHE C 153 THR C 159 1 O GLU C 157 N ILE C 133
SHEET 8 M11 THR C 179 LYS C 183 1 O LYS C 183 N LEU C 156
SHEET 9 M11 LEU C 202 TYR C 206 1 O TYR C 206 N LEU C 182
SHEET 10 M11 LEU C 230 ASP C 232 1 O LEU C 230 N VAL C 205
SHEET 11 M11 GLU C 251 ILE C 253 1 O ILE C 253 N LEU C 231
SHEET 1 N 3 THR C 66 ILE C 67 0
SHEET 2 N 3 GLN C 91 LEU C 92 1 O GLN C 91 N ILE C 67
SHEET 3 N 3 TYR C 116 ILE C 117 1 O TYR C 116 N LEU C 92
SHEET 1 O 2 PHE C 97 TYR C 98 0
SHEET 2 O 2 LEU C 122 LYS C 123 1 O LYS C 123 N PHE C 97
SHEET 1 P 3 SER C 166 ILE C 167 0
SHEET 2 P 3 SER C 191 VAL C 192 1 O SER C 191 N ILE C 167
SHEET 3 P 3 VAL C 215 ILE C 216 1 O VAL C 215 N VAL C 192
SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.04
SSBOND 2 CYS A 134 CYS A 193 1555 1555 2.03
SSBOND 3 CYS B 22 CYS B 92 1555 1555 2.04
SSBOND 4 CYS B 140 CYS B 196 1555 1555 2.04
SSBOND 5 CYS C 31 CYS C 41 1555 1555 2.03
LINK ND2 ASN A 26 C1 NAG A 213 1555 1555 1.45
LINK C1 NAG C 1 ND2 ASN C 198 1555 1555 1.45
LINK C1 NAG C 2 ND2 ASN C 177 1555 1555 1.45
LINK C1 NAG C 3 ND2 ASN C 99 1555 1555 1.45
LINK C1 NAG C 5 ND2 ASN C 113 1555 1555 1.45
LINK C1 NAG C 6 ND2 ASN C 77 1555 1555 1.45
LINK NE2 HIS A 188 ZN ZN A 304 1555 1555 1.86
LINK O HOH B 257 ZN ZN C 301 1555 1555 2.19
LINK NE2 HIS C 63 ZN ZN C 301 1555 1555 2.08
LINK OE2 GLU C 93 ZN ZN C 302 1555 1555 2.02
LINK OD2 ASP C 118 ZN ZN C 303 1555 1555 1.79
CISPEP 1 TYR A 140 PRO A 141 0 -1.00
CISPEP 2 PHE B 146 PRO B 147 0 -10.74
CISPEP 3 GLU B 148 PRO B 149 0 3.14
CISPEP 4 GLY C 227 PRO C 228 0 1.61
CRYST1 43.888 175.784 205.806 90.00 90.00 90.00 I 21 21 21 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 0.022785 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005689 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004859 0.00000
(ATOM LINES ARE NOT SHOWN.)
END