HEADER SIGNALING PROTEIN, IMMUNE SYSTEM 15-MAR-14 4P59 TITLE HER3 EXTRACELLULAR DOMAIN IN COMPLEX WITH FAB FRAGMENT OF MOR09825 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTO-ONCOGENE-LIKE PROTEIN C-ERBB-3,TYROSINE KINASE-TYPE COMPND 5 CELL SURFACE RECEPTOR HER3; COMPND 6 EC: 2.7.10.1; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: MOR09825 FAB FRAGMENT HEAVY CHAIN; COMPND 10 CHAIN: H; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: MOR09825 FAB FRAGMENT LIGHT CHAIN; COMPND 14 CHAIN: L; COMPND 15 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: ERBB3, HER3; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HER3 RECEPTOR, THERAPEUTIC ANTIBODY, FAB FRAGMENT, ANTI-HER3 EXPDTA X-RAY DIFFRACTION AUTHOR E.R.SPRAGUE REVDAT 1 16-APR-14 4P59 0 JRNL AUTH A.P.GARNER,C.U.BIALUCHA,E.R.SPRAGUE,J.T.GARRETT,Q.SHENG, JRNL AUTH 2 S.LI,O.SINESHCHEKOVA,P.SAXENA,C.R.SUTTON,D.CHEN,Y.CHEN, JRNL AUTH 3 H.WANG,J.LIANG,R.DAS,R.MOSHER,J.GU,A.HUANG,N.HAUBST, JRNL AUTH 4 C.ZEHETMEIER,M.HABERL,W.ELIS,C.KUNZ,A.B.HEIDT,K.HERLIHY, JRNL AUTH 5 J.MURTIE,A.SCHULLER,C.L.ARTEAGA,W.R.SELLERS,S.A.ETTENBERG JRNL TITL AN ANTIBODY THAT LOCKS HER3 IN THE INACTIVE CONFORMATION JRNL TITL 2 INHIBITS TUMOR GROWTH DRIVEN BY HER2 OR NEUREGULIN. JRNL REF CANCER RES. 6024 2013 JRNL PMID 23928993 JRNL DOI 10.1158/0008-5472.CAN-13-1198 REMARK 2 REMARK 2 RESOLUTION. 3.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.4 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 111.03 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 22111 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) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 1132 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 11 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.57 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2876 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1955 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2720 REMARK 3 BIN R VALUE (WORKING SET) : 0.1923 REMARK 3 BIN FREE R VALUE : 0.2498 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.42 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7733 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 98 REMARK 3 SOLVENT ATOMS : 3 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 74.13 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.29 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.86810 REMARK 3 B22 (A**2) : 25.53650 REMARK 3 B33 (A**2) : -29.40460 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.494 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.842 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 8050 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 10961 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2724 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 187 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 1181 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 8050 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1055 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 8811 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.24 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.71 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 25.59 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|26 - A|207 } REMARK 3 ORIGIN FOR THE GROUP (A): -49.5842 -84.9384 -31.9008 REMARK 3 T TENSOR REMARK 3 T11: -0.3540 T22: -0.2116 REMARK 3 T33: 0.4219 T12: -0.0910 REMARK 3 T13: 0.2367 T23: 0.0564 REMARK 3 L TENSOR REMARK 3 L11: 1.9062 L22: 6.4447 REMARK 3 L33: 2.5940 L12: -1.4869 REMARK 3 L13: -0.8084 L23: 0.5229 REMARK 3 S TENSOR REMARK 3 S11: -0.1135 S12: -0.5780 S13: -0.5890 REMARK 3 S21: 0.8058 S22: 0.0399 S23: 1.0885 REMARK 3 S31: 0.3578 S32: -0.3174 S33: 0.0736 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|208 - A|328 } REMARK 3 ORIGIN FOR THE GROUP (A): -39.9567 -56.1696 -34.6455 REMARK 3 T TENSOR REMARK 3 T11: -0.1447 T22: -0.3024 REMARK 3 T33: -0.0005 T12: 0.0140 REMARK 3 T13: 0.0159 T23: 0.0937 REMARK 3 L TENSOR REMARK 3 L11: 2.1944 L22: 7.9083 REMARK 3 L33: 0.0409 L12: -0.6531 REMARK 3 L13: 0.7843 L23: 0.9347 REMARK 3 S TENSOR REMARK 3 S11: 0.0162 S12: -0.3473 S13: -0.4329 REMARK 3 S21: 0.5865 S22: 0.0371 S23: -0.2407 REMARK 3 S31: 0.0764 S32: -0.3081 S33: -0.0532 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { A|329 - A|518 } REMARK 3 ORIGIN FOR THE GROUP (A): -26.5765 -33.7189 10.8075 REMARK 3 T TENSOR REMARK 3 T11: -0.0426 T22: 0.3209 REMARK 3 T33: -0.4508 T12: 0.2980 REMARK 3 T13: -0.1773 T23: 0.0044 REMARK 3 L TENSOR REMARK 3 L11: 4.5178 L22: 2.9514 REMARK 3 L33: 4.2372 L12: 0.5624 REMARK 3 L13: 0.6101 L23: 0.2974 REMARK 3 S TENSOR REMARK 3 S11: -0.2024 S12: -0.2153 S13: -0.0418 REMARK 3 S21: -0.2471 S22: 0.2529 S23: 0.4097 REMARK 3 S31: -0.5079 S32: -1.0885 S33: -0.0505 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { A|519 - A|631 } REMARK 3 ORIGIN FOR THE GROUP (A): -24.1172 -27.2704 -33.0000 REMARK 3 T TENSOR REMARK 3 T11: -0.2261 T22: -0.3083 REMARK 3 T33: 0.2444 T12: 0.0943 REMARK 3 T13: -0.2090 T23: 0.0581 REMARK 3 L TENSOR REMARK 3 L11: 1.5123 L22: 3.0236 REMARK 3 L33: 5.0016 L12: 0.1111 REMARK 3 L13: 0.6308 L23: -0.0815 REMARK 3 S TENSOR REMARK 3 S11: -0.1725 S12: -0.1714 S13: -0.0544 REMARK 3 S21: 0.5121 S22: -0.1149 S23: -0.8701 REMARK 3 S31: -0.5780 S32: 0.2589 S33: 0.2874 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { H|2 - H|117 } REMARK 3 ORIGIN FOR THE GROUP (A): -50.2437 -23.3191 -34.5204 REMARK 3 T TENSOR REMARK 3 T11: -0.0463 T22: -0.1443 REMARK 3 T33: 0.0399 T12: 0.0280 REMARK 3 T13: -0.0605 T23: 0.0070 REMARK 3 L TENSOR REMARK 3 L11: 4.4482 L22: 3.0659 REMARK 3 L33: 2.4780 L12: -2.0929 REMARK 3 L13: -0.3239 L23: 1.0988 REMARK 3 S TENSOR REMARK 3 S11: -0.1566 S12: -0.1142 S13: 0.1574 REMARK 3 S21: 0.6447 S22: 0.0237 S23: -0.1371 REMARK 3 S31: 0.2818 S32: 0.2250 S33: 0.1329 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { H|118 - H|217 } REMARK 3 ORIGIN FOR THE GROUP (A): -77.0941 -14.1345 -46.1947 REMARK 3 T TENSOR REMARK 3 T11: -0.1568 T22: -0.2043 REMARK 3 T33: 0.3709 T12: -0.0166 REMARK 3 T13: -0.1007 T23: 0.0896 REMARK 3 L TENSOR REMARK 3 L11: 4.6992 L22: 3.2254 REMARK 3 L33: 0.6418 L12: 2.7509 REMARK 3 L13: 1.7273 L23: 1.1638 REMARK 3 S TENSOR REMARK 3 S11: 0.0074 S12: -0.0656 S13: 0.2182 REMARK 3 S21: -0.1706 S22: 0.0128 S23: 0.4849 REMARK 3 S31: -0.1181 S32: -0.3372 S33: -0.0202 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: { L|1 - L|106 } REMARK 3 ORIGIN FOR THE GROUP (A): -47.1279 -27.5556 -56.4203 REMARK 3 T TENSOR REMARK 3 T11: -0.0619 T22: -0.0142 REMARK 3 T33: -0.0692 T12: 0.0887 REMARK 3 T13: 0.0140 T23: -0.0097 REMARK 3 L TENSOR REMARK 3 L11: 4.9862 L22: 3.2333 REMARK 3 L33: 0.6433 L12: -1.7386 REMARK 3 L13: 0.9175 L23: -0.2855 REMARK 3 S TENSOR REMARK 3 S11: 0.0814 S12: 0.7665 S13: -0.0008 REMARK 3 S21: -0.8017 S22: -0.2331 S23: -0.4294 REMARK 3 S31: 0.1008 S32: 0.2147 S33: 0.1516 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: { L|107 - L|211 } REMARK 3 ORIGIN FOR THE GROUP (A): -75.9494 -5.0488 -59.8187 REMARK 3 T TENSOR REMARK 3 T11: -0.2671 T22: -0.2220 REMARK 3 T33: 0.3758 T12: 0.0150 REMARK 3 T13: -0.1943 T23: 0.2040 REMARK 3 L TENSOR REMARK 3 L11: 4.0760 L22: 6.7155 REMARK 3 L33: 5.6855 L12: -3.3108 REMARK 3 L13: -0.3729 L23: 3.2522 REMARK 3 S TENSOR REMARK 3 S11: 0.0391 S12: 0.6490 S13: 0.7250 REMARK 3 S21: -0.6974 S22: -0.1822 S23: 0.6099 REMARK 3 S31: -0.5084 S32: -0.1146 S33: 0.1431 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4P59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-14. REMARK 100 THE DEPOSITION ID IS D_1000200714. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-JUN-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 17-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22112 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 REMARK 200 RESOLUTION RANGE LOW (A) : 111.030 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11800 REMARK 200 FOR THE DATA SET : 14.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 6.80 REMARK 200 R MERGE FOR SHELL (I) : 0.46100 REMARK 200 R SYM FOR SHELL (I) : 0.46100 REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: PDB ENTRY 1M6B REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.87 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS PH 6.5, 16% (W/V) PEG REMARK 280 10000 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 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 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-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 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 62.11300 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 70.46950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 90.12350 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 62.11300 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 70.46950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 90.12350 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 62.11300 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.46950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 90.12350 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 62.11300 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 70.46950 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 90.12350 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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM. 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: 7380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 48220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L 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 SER A 20 REMARK 465 GLU A 21 REMARK 465 VAL A 22 REMARK 465 GLY A 23 REMARK 465 ASN A 24 REMARK 465 SER A 25 REMARK 465 LEU A 36 REMARK 465 SER A 37 REMARK 465 VAL A 38 REMARK 465 THR A 39 REMARK 465 GLY A 40 REMARK 465 ASP A 41 REMARK 465 ALA A 42 REMARK 465 GLU A 43 REMARK 465 ASN A 44 REMARK 465 GLN A 45 REMARK 465 TYR A 46 REMARK 465 GLN A 47 REMARK 465 THR A 48 REMARK 465 LEU A 49 REMARK 465 GLN A 632 REMARK 465 THR A 633 REMARK 465 LEU A 634 REMARK 465 VAL A 635 REMARK 465 LEU A 636 REMARK 465 ILE A 637 REMARK 465 GLY A 638 REMARK 465 LYS A 639 REMARK 465 THR A 640 REMARK 465 GLU A 641 REMARK 465 PHE A 642 REMARK 465 ARG A 643 REMARK 465 HIS A 644 REMARK 465 ASP A 645 REMARK 465 SER A 646 REMARK 465 GLN H 1 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 GLY H 137 REMARK 465 GLY H 138 REMARK 465 LYS H 218 REMARK 465 SER H 219 REMARK 465 GLU H 220 REMARK 465 PHE H 221 REMARK 465 ASP H 222 REMARK 465 TYR H 223 REMARK 465 LYS H 224 REMARK 465 ASP H 225 REMARK 465 ASP H 226 REMARK 465 ASP H 227 REMARK 465 ASP H 228 REMARK 465 LYS H 229 REMARK 465 GLY H 230 REMARK 465 ALA H 231 REMARK 465 PRO H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 ALA L 214 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 55 45.95 -77.31 REMARK 500 GLU A 57 -52.90 -125.40 REMARK 500 ASN A 71 48.35 -106.01 REMARK 500 MET A 91 70.41 41.08 REMARK 500 ARG A 135 25.66 -77.33 REMARK 500 LEU A 136 44.62 -72.76 REMARK 500 LEU A 139 96.53 -59.06 REMARK 500 LYS A 151 35.92 38.73 REMARK 500 ILE A 166 -67.41 -103.18 REMARK 500 VAL A 167 99.84 -53.42 REMARK 500 ASN A 179 -142.08 -126.42 REMARK 500 PRO A 212 20.30 -68.16 REMARK 500 GLN A 225 25.61 -76.76 REMARK 500 ASP A 242 3.65 -58.48 REMARK 500 HIS A 248 -77.88 -112.08 REMARK 500 SER A 252 71.81 48.53 REMARK 500 PRO A 260 115.41 -38.54 REMARK 500 HIS A 292 108.57 -37.73 REMARK 500 GLN A 298 -83.43 59.54 REMARK 500 THR A 299 -6.60 -146.76 REMARK 500 GLU A 332 -74.09 -58.53 REMARK 500 THR A 334 -166.83 -113.33 REMARK 500 VAL A 343 94.61 -68.47 REMARK 500 LYS A 375 59.58 32.14 REMARK 500 PHE A 409 44.92 -92.77 REMARK 500 PHE A 412 38.98 -87.41 REMARK 500 ASN A 425 -107.30 58.70 REMARK 500 PHE A 443 43.44 -88.23 REMARK 500 ARG A 444 -51.54 -19.34 REMARK 500 ASN A 459 64.30 -105.38 REMARK 500 ARG A 460 -9.70 -49.60 REMARK 500 TYR A 464 -21.40 72.57 REMARK 500 GLU A 480 -29.93 66.01 REMARK 500 ARG A 481 36.81 -81.77 REMARK 500 GLN A 516 29.27 -75.63 REMARK 500 ASN A 522 -109.09 -97.19 REMARK 500 ARG A 525 -112.85 -92.89 REMARK 500 GLU A 539 -72.93 -63.19 REMARK 500 HIS A 578 -89.95 -125.99 REMARK 500 GLN A 607 31.14 -95.92 REMARK 500 ASN A 608 15.95 46.99 REMARK 500 CYS A 610 85.07 -66.32 REMARK 500 ASP H 148 92.37 39.10 REMARK 500 PRO H 151 -159.58 -82.74 REMARK 500 THR H 164 -39.47 -138.00 REMARK 500 SER H 192 27.23 -62.59 REMARK 500 THR H 195 -66.81 -136.14 REMARK 500 GLU H 216 -89.61 74.70 REMARK 500 SER L 30 -127.92 58.87 REMARK 500 ASN L 31 51.73 -116.50 REMARK 500 REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 703 through NAG A 704 bound to ASN A 250 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 705 through NAG A 706 bound to ASN A 353 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 701 bound REMARK 800 to ASN A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 707 bound REMARK 800 to ASN A 414 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 702 bound REMARK 800 to ASN A 437 DBREF 4P59 A 20 646 UNP P21860 ERBB3_HUMAN 20 646 DBREF 4P59 H 1 238 PDB PDB 4P59 1 238 DBREF 4P59 L 1 214 PDB PDB 4P59 1 214 SEQADV 4P59 GLU A 641 UNP P21860 HIS 641 CLONING ARTIFACT SEQADV 4P59 PHE A 642 UNP P21860 LEU 642 CLONING ARTIFACT SEQADV 4P59 ARG A 643 UNP P21860 THR 643 CLONING ARTIFACT SEQADV 4P59 HIS A 644 UNP P21860 MET 644 CLONING ARTIFACT SEQADV 4P59 ASP A 645 UNP P21860 ALA 645 CLONING ARTIFACT SEQADV 4P59 SER A 646 UNP P21860 LEU 646 CLONING ARTIFACT SEQRES 1 A 627 SER GLU VAL GLY ASN SER GLN ALA VAL CYS PRO GLY THR SEQRES 2 A 627 LEU ASN GLY LEU SER VAL THR GLY ASP ALA GLU ASN GLN SEQRES 3 A 627 TYR GLN THR LEU TYR LYS LEU TYR GLU ARG CYS GLU VAL SEQRES 4 A 627 VAL MET GLY ASN LEU GLU ILE VAL LEU THR GLY HIS ASN SEQRES 5 A 627 ALA ASP LEU SER PHE LEU GLN TRP ILE ARG GLU VAL THR SEQRES 6 A 627 GLY TYR VAL LEU VAL ALA MET ASN GLU PHE SER THR LEU SEQRES 7 A 627 PRO LEU PRO ASN LEU ARG VAL VAL ARG GLY THR GLN VAL SEQRES 8 A 627 TYR ASP GLY LYS PHE ALA ILE PHE VAL MET LEU ASN TYR SEQRES 9 A 627 ASN THR ASN SER SER HIS ALA LEU ARG GLN LEU ARG LEU SEQRES 10 A 627 THR GLN LEU THR GLU ILE LEU SER GLY GLY VAL TYR ILE SEQRES 11 A 627 GLU LYS ASN ASP LYS LEU CYS HIS MET ASP THR ILE ASP SEQRES 12 A 627 TRP ARG ASP ILE VAL ARG ASP ARG ASP ALA GLU ILE VAL SEQRES 13 A 627 VAL LYS ASP ASN GLY ARG SER CYS PRO PRO CYS HIS GLU SEQRES 14 A 627 VAL CYS LYS GLY ARG CYS TRP GLY PRO GLY SER GLU ASP SEQRES 15 A 627 CYS GLN THR LEU THR LYS THR ILE CYS ALA PRO GLN CYS SEQRES 16 A 627 ASN GLY HIS CYS PHE GLY PRO ASN PRO ASN GLN CYS CYS SEQRES 17 A 627 HIS ASP GLU CYS ALA GLY GLY CYS SER GLY PRO GLN ASP SEQRES 18 A 627 THR ASP CYS PHE ALA CYS ARG HIS PHE ASN ASP SER GLY SEQRES 19 A 627 ALA CYS VAL PRO ARG CYS PRO GLN PRO LEU VAL TYR ASN SEQRES 20 A 627 LYS LEU THR PHE GLN LEU GLU PRO ASN PRO HIS THR LYS SEQRES 21 A 627 TYR GLN TYR GLY GLY VAL CYS VAL ALA SER CYS PRO HIS SEQRES 22 A 627 ASN PHE VAL VAL ASP GLN THR SER CYS VAL ARG ALA CYS SEQRES 23 A 627 PRO PRO ASP LYS MET GLU VAL ASP LYS ASN GLY LEU LYS SEQRES 24 A 627 MET CYS GLU PRO CYS GLY GLY LEU CYS PRO LYS ALA CYS SEQRES 25 A 627 GLU GLY THR GLY SER GLY SER ARG PHE GLN THR VAL ASP SEQRES 26 A 627 SER SER ASN ILE ASP GLY PHE VAL ASN CYS THR LYS ILE SEQRES 27 A 627 LEU GLY ASN LEU ASP PHE LEU ILE THR GLY LEU ASN GLY SEQRES 28 A 627 ASP PRO TRP HIS LYS ILE PRO ALA LEU ASP PRO GLU LYS SEQRES 29 A 627 LEU ASN VAL PHE ARG THR VAL ARG GLU ILE THR GLY TYR SEQRES 30 A 627 LEU ASN ILE GLN SER TRP PRO PRO HIS MET HIS ASN PHE SEQRES 31 A 627 SER VAL PHE SER ASN LEU THR THR ILE GLY GLY ARG SER SEQRES 32 A 627 LEU TYR ASN ARG GLY PHE SER LEU LEU ILE MET LYS ASN SEQRES 33 A 627 LEU ASN VAL THR SER LEU GLY PHE ARG SER LEU LYS GLU SEQRES 34 A 627 ILE SER ALA GLY ARG ILE TYR ILE SER ALA ASN ARG GLN SEQRES 35 A 627 LEU CYS TYR HIS HIS SER LEU ASN TRP THR LYS VAL LEU SEQRES 36 A 627 ARG GLY PRO THR GLU GLU ARG LEU ASP ILE LYS HIS ASN SEQRES 37 A 627 ARG PRO ARG ARG ASP CYS VAL ALA GLU GLY LYS VAL CYS SEQRES 38 A 627 ASP PRO LEU CYS SER SER GLY GLY CYS TRP GLY PRO GLY SEQRES 39 A 627 PRO GLY GLN CYS LEU SER CYS ARG ASN TYR SER ARG GLY SEQRES 40 A 627 GLY VAL CYS VAL THR HIS CYS ASN PHE LEU ASN GLY GLU SEQRES 41 A 627 PRO ARG GLU PHE ALA HIS GLU ALA GLU CYS PHE SER CYS SEQRES 42 A 627 HIS PRO GLU CYS GLN PRO MET GLU GLY THR ALA THR CYS SEQRES 43 A 627 ASN GLY SER GLY SER ASP THR CYS ALA GLN CYS ALA HIS SEQRES 44 A 627 PHE ARG ASP GLY PRO HIS CYS VAL SER SER CYS PRO HIS SEQRES 45 A 627 GLY VAL LEU GLY ALA LYS GLY PRO ILE TYR LYS TYR PRO SEQRES 46 A 627 ASP VAL GLN ASN GLU CYS ARG PRO CYS HIS GLU ASN CYS SEQRES 47 A 627 THR GLN GLY CYS LYS GLY PRO GLU LEU GLN ASP CYS LEU SEQRES 48 A 627 GLY GLN THR LEU VAL LEU ILE GLY LYS THR GLU PHE ARG SEQRES 49 A 627 HIS ASP SER SEQRES 1 H 238 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 238 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 238 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE ASN SEQRES 5 H 238 SER GLN GLY LYS SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 238 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 238 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 238 ALA VAL TYR TYR CYS ALA ARG TRP GLY ASP GLU GLY PHE SEQRES 9 H 238 ASP ILE TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 H 238 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 H 238 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 H 238 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 H 238 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 H 238 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 H 238 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 H 238 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 H 238 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER GLU PHE SEQRES 18 H 238 ASP TYR LYS ASP ASP ASP ASP LYS GLY ALA PRO HIS HIS SEQRES 19 H 238 HIS HIS HIS HIS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN GLY ILE SER ASN TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 SER SER PHE PRO THR THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU ALA HET NAG A 701 14 HET NAG A 702 14 HET NAG A 703 14 HET NAG A 704 14 HET NAG A 705 14 HET NAG A 706 14 HET NAG A 707 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 7(C8 H15 N O6) FORMUL 9 HOH *3(H2 O) HELIX 1 AA1 SER A 75 ILE A 80 5 6 HELIX 2 AA2 VAL A 110 GLY A 113 5 4 HELIX 3 AA3 ASP A 162 ILE A 166 5 5 HELIX 4 AA4 ASN A 347 VAL A 352 5 6 HELIX 5 AA5 LEU A 364 ASN A 369 1 6 HELIX 6 AA6 ASP A 380 ARG A 388 5 9 HELIX 7 AA7 PHE A 409 ASN A 414 5 6 HELIX 8 AA8 ASN A 469 LEU A 474 1 6 HELIX 9 AA9 PRO A 489 GLY A 497 1 9 HELIX 10 AB1 THR H 28 TYR H 32 5 5 HELIX 11 AB2 ARG H 87 THR H 91 5 5 HELIX 12 AB3 SER H 160 ALA H 162 5 3 HELIX 13 AB4 PRO H 189 GLY H 194 5 6 HELIX 14 AB5 GLN L 79 PHE L 83 5 5 HELIX 15 AB6 SER L 121 SER L 127 1 7 HELIX 16 AB7 SER L 182 LYS L 188 1 7 SHEET 1 AA1 5 VAL A 28 PRO A 30 0 SHEET 2 AA1 5 VAL A 58 MET A 60 1 O MET A 60 N CYS A 29 SHEET 3 AA1 5 GLU A 82 VAL A 83 1 O GLU A 82 N VAL A 59 SHEET 4 AA1 5 VAL A 104 VAL A 105 1 O VAL A 104 N VAL A 83 SHEET 5 AA1 5 GLU A 141 ILE A 142 1 O GLU A 141 N VAL A 105 SHEET 1 AA2 5 LEU A 63 VAL A 66 0 SHEET 2 AA2 5 VAL A 87 ALA A 90 1 O LEU A 88 N ILE A 65 SHEET 3 AA2 5 PHE A 115 MET A 120 1 O ALA A 116 N VAL A 87 SHEET 4 AA2 5 GLY A 146 ILE A 149 1 O GLY A 146 N ALA A 116 SHEET 5 AA2 5 ILE A 174 VAL A 175 1 O VAL A 175 N ILE A 149 SHEET 1 AA3 2 THR A 96 LEU A 97 0 SHEET 2 AA3 2 GLN A 133 LEU A 134 1 O GLN A 133 N LEU A 97 SHEET 1 AA4 2 PHE A 249 ASP A 251 0 SHEET 2 AA4 2 ALA A 254 VAL A 256 -1 O VAL A 256 N PHE A 249 SHEET 1 AA5 2 LEU A 263 ASN A 266 0 SHEET 2 AA5 2 GLN A 271 PRO A 274 -1 O GLN A 271 N ASN A 266 SHEET 1 AA6 2 TYR A 280 TYR A 282 0 SHEET 2 AA6 2 VAL A 285 VAL A 287 -1 O VAL A 287 N TYR A 280 SHEET 1 AA7 2 VAL A 295 ASP A 297 0 SHEET 2 AA7 2 SER A 300 VAL A 302 -1 O SER A 300 N ASP A 297 SHEET 1 AA8 2 LYS A 309 LYS A 314 0 SHEET 2 AA8 2 LEU A 317 PRO A 322 -1 O MET A 319 N VAL A 312 SHEET 1 AA9 5 ALA A 330 CYS A 331 0 SHEET 2 AA9 5 LYS A 356 ILE A 357 1 O LYS A 356 N CYS A 331 SHEET 3 AA9 5 GLU A 392 ILE A 393 1 O GLU A 392 N ILE A 357 SHEET 4 AA9 5 THR A 417 ILE A 418 1 O THR A 417 N ILE A 393 SHEET 5 AA9 5 GLU A 448 ILE A 449 1 O GLU A 448 N ILE A 418 SHEET 1 AB1 5 LEU A 361 PHE A 363 0 SHEET 2 AB1 5 LEU A 397 ILE A 399 1 O ASN A 398 N PHE A 363 SHEET 3 AB1 5 LEU A 430 MET A 433 1 O LEU A 431 N ILE A 399 SHEET 4 AB1 5 ILE A 454 SER A 457 1 O TYR A 455 N ILE A 432 SHEET 5 AB1 5 LEU A 482 LYS A 485 1 O ASP A 483 N ILE A 456 SHEET 1 AB2 2 TYR A 523 SER A 524 0 SHEET 2 AB2 2 CYS A 529 VAL A 530 -1 O VAL A 530 N TYR A 523 SHEET 1 AB3 2 GLU A 542 ALA A 544 0 SHEET 2 AB3 2 CYS A 549 SER A 551 -1 O PHE A 550 N PHE A 543 SHEET 1 AB4 2 PHE A 579 ASP A 581 0 SHEET 2 AB4 2 HIS A 584 VAL A 586 -1 O VAL A 586 N PHE A 579 SHEET 1 AB5 3 HIS A 591 GLY A 595 0 SHEET 2 AB5 3 GLY A 598 PRO A 604 -1 O ILE A 600 N VAL A 593 SHEET 3 AB5 3 CYS A 610 PRO A 612 -1 O ARG A 611 N TYR A 603 SHEET 1 AB6 4 GLN H 3 SER H 7 0 SHEET 2 AB6 4 SER H 17 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB6 4 THR H 78 ASN H 84 -1 O LEU H 81 N LEU H 20 SHEET 4 AB6 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB7 6 LEU H 11 VAL H 12 0 SHEET 2 AB7 6 THR H 111 VAL H 115 1 O THR H 114 N VAL H 12 SHEET 3 AB7 6 ALA H 92 TRP H 99 -1 N TYR H 94 O THR H 111 SHEET 4 AB7 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB7 6 GLU H 46 ILE H 51 -1 O SER H 49 N TRP H 36 SHEET 6 AB7 6 THR H 58 TYR H 60 -1 O TYR H 59 N ALA H 50 SHEET 1 AB8 4 LEU H 11 VAL H 12 0 SHEET 2 AB8 4 THR H 111 VAL H 115 1 O THR H 114 N VAL H 12 SHEET 3 AB8 4 ALA H 92 TRP H 99 -1 N TYR H 94 O THR H 111 SHEET 4 AB8 4 PHE H 104 TRP H 107 -1 O ILE H 106 N ARG H 98 SHEET 1 AB9 4 SER H 124 LEU H 128 0 SHEET 2 AB9 4 ALA H 140 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 AB9 4 TYR H 180 VAL H 188 -1 O LEU H 182 N VAL H 146 SHEET 4 AB9 4 VAL H 167 THR H 169 -1 N HIS H 168 O VAL H 185 SHEET 1 AC1 4 SER H 124 LEU H 128 0 SHEET 2 AC1 4 ALA H 140 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 AC1 4 TYR H 180 VAL H 188 -1 O LEU H 182 N VAL H 146 SHEET 4 AC1 4 VAL H 173 LEU H 174 -1 N VAL H 173 O SER H 181 SHEET 1 AC2 3 VAL H 154 TRP H 158 0 SHEET 2 AC2 3 TYR H 198 HIS H 204 -1 O ASN H 201 N SER H 157 SHEET 3 AC2 3 THR H 209 VAL H 215 -1 O VAL H 211 N VAL H 202 SHEET 1 AC3 4 MET L 4 SER L 7 0 SHEET 2 AC3 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AC3 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AC3 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AC4 6 SER L 10 ALA L 13 0 SHEET 2 AC4 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AC4 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AC4 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AC4 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC4 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AC5 4 SER L 10 ALA L 13 0 SHEET 2 AC5 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AC5 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AC5 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AC6 4 SER L 114 PHE L 118 0 SHEET 2 AC6 4 ALA L 130 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AC6 4 TYR L 173 LEU L 181 -1 O LEU L 181 N ALA L 130 SHEET 4 AC6 4 SER L 159 GLN L 160 -1 N GLN L 160 O THR L 178 SHEET 1 AC7 4 ALA L 153 LEU L 154 0 SHEET 2 AC7 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AC7 4 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AC7 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS A 29 CYS A 56 1555 1555 2.04 SSBOND 2 CYS A 156 CYS A 183 1555 1555 2.02 SSBOND 3 CYS A 186 CYS A 194 1555 1555 2.04 SSBOND 4 CYS A 190 CYS A 202 1555 1555 2.04 SSBOND 5 CYS A 210 CYS A 218 1555 1555 2.04 SSBOND 6 CYS A 214 CYS A 226 1555 1555 2.04 SSBOND 7 CYS A 227 CYS A 235 1555 1555 2.03 SSBOND 8 CYS A 231 CYS A 243 1555 1555 2.04 SSBOND 9 CYS A 246 CYS A 255 1555 1555 2.04 SSBOND 10 CYS A 259 CYS A 286 1555 1555 2.04 SSBOND 11 CYS A 290 CYS A 301 1555 1555 2.05 SSBOND 12 CYS A 305 CYS A 320 1555 1555 2.05 SSBOND 13 CYS A 323 CYS A 327 1555 1555 2.03 SSBOND 14 CYS A 331 CYS A 354 1555 1555 2.04 SSBOND 15 CYS A 463 CYS A 493 1555 1555 2.04 SSBOND 16 CYS A 500 CYS A 509 1555 1555 2.03 SSBOND 17 CYS A 504 CYS A 517 1555 1555 2.04 SSBOND 18 CYS A 520 CYS A 529 1555 1555 2.04 SSBOND 19 CYS A 533 CYS A 549 1555 1555 2.04 SSBOND 20 CYS A 552 CYS A 565 1555 1555 2.03 SSBOND 21 CYS A 556 CYS A 573 1555 1555 2.03 SSBOND 22 CYS A 576 CYS A 585 1555 1555 2.04 SSBOND 23 CYS A 589 CYS A 610 1555 1555 2.06 SSBOND 24 CYS A 613 CYS A 621 1555 1555 2.04 SSBOND 25 CYS A 617 CYS A 629 1555 1555 2.04 SSBOND 26 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 27 CYS H 144 CYS H 200 1555 1555 2.03 SSBOND 28 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 29 CYS L 134 CYS L 194 1555 1555 2.04 LINK ND2 ASN A 250 C1 NAG A 703 1555 1555 1.44 LINK ND2 ASN A 353 C1 NAG A 705 1555 1555 1.44 LINK ND2 ASN A 408 C1 NAG A 701 1555 1555 1.44 LINK ND2 ASN A 414 C1 NAG A 707 1555 1555 1.43 LINK ND2 ASN A 437 C1 NAG A 702 1555 1555 1.43 LINK O4 NAG A 703 C1 NAG A 704 1555 1555 1.43 LINK O4 NAG A 705 C1 NAG A 706 1555 1555 1.44 CISPEP 1 PRO H 41 GLY H 42 0 -7.33 CISPEP 2 PRO H 130 SER H 131 0 0.63 CISPEP 3 PHE H 150 PRO H 151 0 -3.96 CISPEP 4 GLU H 152 PRO H 153 0 9.78 CISPEP 5 SER L 7 PRO L 8 0 -0.36 CISPEP 6 PHE L 94 PRO L 95 0 -1.03 CISPEP 7 TYR L 140 PRO L 141 0 -0.89 SITE 1 AC1 9 GLU A 57 ARG A 81 ARG A 103 CYS A 243 SITE 2 AC1 9 PHE A 244 ALA A 245 CYS A 246 ASN A 250 SITE 3 AC1 9 GLY A 253 SITE 1 AC2 1 ASN A 353 SITE 1 AC3 6 HIS A 405 MET A 406 HIS A 407 ASN A 408 SITE 2 AC3 6 SER A 440 PRO A 512 SITE 1 AC4 2 ARG A 388 ASN A 414 SITE 1 AC5 5 PRO A 404 LEU A 436 ASN A 437 GLN A 461 SITE 2 AC5 5 SER L 76 CRYST1 124.226 140.939 180.247 90.00 90.00 90.00 I 2 2 2 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 0.008050 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007095 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005548 0.00000