HEADER IMMUNE SYSTEM 18-JAN-25 9LME TITLE CHECKPOINT REGULATOR PROTEIN IN COMPLEX WITH A NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: CD276 ANTIGEN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: 4IG-B7-H3,B7 HOMOLOG 3,B7-H3,COSTIMULATORY MOLECULE; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: T3CL11; COMPND 8 CHAIN: C, F; COMPND 9 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: CD276, B7H3, PSEC0249, UNQ309/PRO352; 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: LAMA GLAMA; SOURCE 11 ORGANISM_TAXID: 9844; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, COMPLEX, CHECKPOINT REGULATOR, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR W.M.CHEN,A.SAHILI,W.N.YEW,J.LESCAR REVDAT 1 21-JAN-26 9LME 0 JRNL AUTH W.M.CHEN,A.SAHILI,S.KISHORE,W.N.YEW,J.LESCAR JRNL TITL CHECKPOINT REGULATOR IN COMPLEX WITH A NANOBODY. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.3 (18-SEP-2020) 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.16 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 70019 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) : 0.180 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.210 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3501 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 : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.42 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.98 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1331 REMARK 3 BIN R VALUE (WORKING SET) : 0.2406 REMARK 3 BIN FREE R VALUE : 0.2636 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL 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 : 5052 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 473 REMARK 3 SOLVENT ATOMS : 676 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.75920 REMARK 3 B22 (A**2) : -2.75920 REMARK 3 B33 (A**2) : 5.51840 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) : 0.290 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.170 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.156 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.158 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.150 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 : 0.945 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 5570 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 7484 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1918 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 910 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 5570 ; 10.000 ; 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 : 742 ; 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 : 4529 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.06 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.47 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.56 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 19.8880 -1.5763 33.6296 REMARK 3 T TENSOR REMARK 3 T11: -0.0096 T22: -0.0179 REMARK 3 T33: -0.0124 T12: -0.0313 REMARK 3 T13: -0.0380 T23: 0.0058 REMARK 3 L TENSOR REMARK 3 L11: 2.1048 L22: 0.2515 REMARK 3 L33: 0.5686 L12: 0.8215 REMARK 3 L13: -0.4888 L23: -0.2902 REMARK 3 S TENSOR REMARK 3 S11: 0.1747 S12: 0.0515 S13: -0.1636 REMARK 3 S21: 0.0824 S22: -0.1485 S23: 0.0072 REMARK 3 S31: 0.1527 S32: 0.1147 S33: -0.0262 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): 12.3429 34.5472 13.3977 REMARK 3 T TENSOR REMARK 3 T11: 0.0196 T22: -0.0380 REMARK 3 T33: -0.0203 T12: 0.0680 REMARK 3 T13: -0.0101 T23: -0.0351 REMARK 3 L TENSOR REMARK 3 L11: 0.5178 L22: 0.2886 REMARK 3 L33: 3.1368 L12: 0.1649 REMARK 3 L13: -1.3010 L23: 0.3882 REMARK 3 S TENSOR REMARK 3 S11: 0.0823 S12: 0.1580 S13: -0.0035 REMARK 3 S21: -0.0079 S22: -0.1829 S23: 0.1189 REMARK 3 S31: -0.1572 S32: -0.1896 S33: 0.1006 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): 15.8424 46.3733 46.8716 REMARK 3 T TENSOR REMARK 3 T11: 0.1458 T22: -0.1620 REMARK 3 T33: -0.0679 T12: -0.0472 REMARK 3 T13: -0.0039 T23: -0.0544 REMARK 3 L TENSOR REMARK 3 L11: 1.4054 L22: 2.8255 REMARK 3 L33: 3.4900 L12: 0.0097 REMARK 3 L13: -0.0855 L23: 2.9104 REMARK 3 S TENSOR REMARK 3 S11: 0.1273 S12: 0.0564 S13: 0.0335 REMARK 3 S21: 0.4598 S22: 0.2896 S23: -0.1337 REMARK 3 S31: 0.3600 S32: 0.2773 S33: -0.4169 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { F|* } REMARK 3 ORIGIN FOR THE GROUP (A): 48.4104 17.4489 43.8507 REMARK 3 T TENSOR REMARK 3 T11: -0.0693 T22: 0.0810 REMARK 3 T33: -0.0769 T12: -0.0412 REMARK 3 T13: -0.1151 T23: 0.0109 REMARK 3 L TENSOR REMARK 3 L11: 2.9255 L22: 0.0000 REMARK 3 L33: 3.7787 L12: 0.9817 REMARK 3 L13: 1.8849 L23: 1.3069 REMARK 3 S TENSOR REMARK 3 S11: -0.2491 S12: -0.1483 S13: 0.3680 REMARK 3 S21: -0.2158 S22: -0.0461 S23: 0.2275 REMARK 3 S31: -0.1936 S32: 0.2147 S33: 0.2952 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { G|* } REMARK 3 ORIGIN FOR THE GROUP (A): 18.1418 22.6372 27.9033 REMARK 3 T TENSOR REMARK 3 T11: 0.1764 T22: -0.1917 REMARK 3 T33: -0.0017 T12: 0.0750 REMARK 3 T13: -0.1271 T23: -0.1520 REMARK 3 L TENSOR REMARK 3 L11: 0.5707 L22: 0.2121 REMARK 3 L33: 0.0013 L12: -0.2029 REMARK 3 L13: -0.1541 L23: -0.3227 REMARK 3 S TENSOR REMARK 3 S11: 0.0929 S12: -0.0324 S13: 0.0209 REMARK 3 S21: 0.0293 S22: -0.0655 S23: 0.0559 REMARK 3 S31: 0.0037 S32: 0.0525 S33: -0.0275 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9LME COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300055444. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-SEP-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95373 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70019 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 49.160 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 24.67 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.1400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.150 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: ALPHAFOLD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 0.1 M MES MONOHYDRATE REMARK 280 (ACID), 12% V/V GLYCEROL, 6% W/V PEG 4000, 0.06 M MAGNESIUM REMARK 280 CHLORIDE HEXAHYDRATE, 0.06 M CALCIUM CHLORIDE DIHYDRATE, PH 6.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 3555 -Y,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X,Z+3/4 REMARK 290 5555 -X+1/2,Y,-Z+3/4 REMARK 290 6555 X,-Y+1/2,-Z+1/4 REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X,-Y,Z REMARK 290 11555 -Y+1/2,X,Z+3/4 REMARK 290 12555 Y,-X+1/2,Z+1/4 REMARK 290 13555 -X,Y+1/2,-Z+1/4 REMARK 290 14555 X+1/2,-Y,-Z+3/4 REMARK 290 15555 Y,X,-Z REMARK 290 16555 -Y+1/2,-X+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 109.92500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 109.92500 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.94500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 109.92500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.97250 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 109.92500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.91750 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 109.92500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 110.91750 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 109.92500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.97250 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 109.92500 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 109.92500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.94500 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 109.92500 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 109.92500 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 73.94500 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 109.92500 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 110.91750 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 109.92500 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 36.97250 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 109.92500 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 36.97250 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 109.92500 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 110.91750 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 109.92500 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 109.92500 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.94500 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 34970 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F, D, E, G, H 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 484 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 623 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 466 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 635 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 HIS A 16 REMARK 465 HIS A 17 REMARK 465 HIS A 18 REMARK 465 HIS A 19 REMARK 465 HIS A 20 REMARK 465 HIS A 21 REMARK 465 HIS B 16 REMARK 465 HIS B 17 REMARK 465 HIS B 18 REMARK 465 HIS B 19 REMARK 465 HIS B 20 REMARK 465 HIS B 21 REMARK 465 MET C -1 REMARK 465 ALA C 0 REMARK 465 GLY C 118 REMARK 465 ARG C 119 REMARK 465 TYR C 120 REMARK 465 PRO C 121 REMARK 465 TYR C 122 REMARK 465 ASP C 123 REMARK 465 VAL C 124 REMARK 465 PRO C 125 REMARK 465 ASP C 126 REMARK 465 TYR C 127 REMARK 465 GLY C 128 REMARK 465 SER C 129 REMARK 465 GLY C 130 REMARK 465 ARG C 131 REMARK 465 ALA C 132 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 GLY C 135 REMARK 465 SER C 136 REMARK 465 ASN C 137 REMARK 465 GLN C 138 REMARK 465 LEU C 139 REMARK 465 MET F 1 REMARK 465 ALA F 2 REMARK 465 GLY F 120 REMARK 465 ARG F 121 REMARK 465 TYR F 122 REMARK 465 PRO F 123 REMARK 465 TYR F 124 REMARK 465 ASP F 125 REMARK 465 VAL F 126 REMARK 465 PRO F 127 REMARK 465 ASP F 128 REMARK 465 TYR F 129 REMARK 465 GLY F 130 REMARK 465 SER F 131 REMARK 465 GLY F 132 REMARK 465 ARG F 133 REMARK 465 ALA F 134 REMARK 465 GLY F 135 REMARK 465 GLY F 136 REMARK 465 GLY F 137 REMARK 465 SER F 138 REMARK 465 ASN F 139 REMARK 465 GLN F 140 REMARK 465 LEU F 141 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 C4 NAG H 2 O1 MAN A 315 1.59 REMARK 500 C3 NAG H 2 O1 MAN A 315 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 TYR A 89 58.22 -118.36 REMARK 500 ILE A 126 -95.67 -121.24 REMARK 500 PRO A 172 -162.53 -77.12 REMARK 500 TYR B 89 58.52 -116.41 REMARK 500 ILE B 126 -95.38 -121.70 REMARK 500 PRO B 172 -164.69 -76.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 646 DISTANCE = 7.02 ANGSTROMS REMARK 525 HOH B 650 DISTANCE = 5.83 ANGSTROMS REMARK 525 HOH B 651 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH B 655 DISTANCE = 10.16 ANGSTROMS REMARK 525 HOH C 381 DISTANCE = 6.28 ANGSTROMS REMARK 525 HOH C 382 DISTANCE = 7.91 ANGSTROMS REMARK 525 HOH C 383 DISTANCE = 11.11 ANGSTROMS REMARK 525 HOH C 384 DISTANCE = 13.33 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG H 2 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 MG A 316 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PHE A 96 N REMARK 620 2 ASN A 104 O 130.1 REMARK 620 3 SER A 106 O 95.1 121.3 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 323 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 203 OD2 REMARK 620 2 HIS A 205 NE2 119.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B 305 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PHE B 96 N REMARK 620 2 ASN B 104 O 133.9 REMARK 620 3 SER B 106 O 94.0 118.7 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG C 201 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER C 35 OG REMARK 620 2 THR C 102 N 124.0 REMARK 620 3 THR C 102 O 137.4 60.8 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG C 202 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA C 40 N REMARK 620 2 GLY C 44 O 113.6 REMARK 620 N 1 DBREF 9LME A 29 240 UNP Q5ZPR3 CD276_HUMAN 29 240 DBREF 9LME B 29 240 UNP Q5ZPR3 CD276_HUMAN 29 240 DBREF 9LME C -1 139 PDB 9LME 9LME -1 139 DBREF 9LME F 1 141 PDB 9LME 9LME 1 141 SEQADV 9LME HIS A 16 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS A 17 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS A 18 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS A 19 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS A 20 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS A 21 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME GLU A 22 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME ASN A 23 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME LEU A 24 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME TYR A 25 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME PHE A 26 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME GLN A 27 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME GLY A 28 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS B 16 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS B 17 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS B 18 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS B 19 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS B 20 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME HIS B 21 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME GLU B 22 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME ASN B 23 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME LEU B 24 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME TYR B 25 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME PHE B 26 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME GLN B 27 UNP Q5ZPR3 EXPRESSION TAG SEQADV 9LME GLY B 28 UNP Q5ZPR3 EXPRESSION TAG SEQRES 1 A 225 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN GLY SEQRES 2 A 225 LEU GLU VAL GLN VAL PRO GLU ASP PRO VAL VAL ALA LEU SEQRES 3 A 225 VAL GLY THR ASP ALA THR LEU CYS CYS SER PHE SER PRO SEQRES 4 A 225 GLU PRO GLY PHE SER LEU ALA GLN LEU ASN LEU ILE TRP SEQRES 5 A 225 GLN LEU THR ASP THR LYS GLN LEU VAL HIS SER PHE ALA SEQRES 6 A 225 GLU GLY GLN ASP GLN GLY SER ALA TYR ALA ASN ARG THR SEQRES 7 A 225 ALA LEU PHE PRO ASP LEU LEU ALA GLN GLY ASN ALA SER SEQRES 8 A 225 LEU ARG LEU GLN ARG VAL ARG VAL ALA ASP GLU GLY SER SEQRES 9 A 225 PHE THR CYS PHE VAL SER ILE ARG ASP PHE GLY SER ALA SEQRES 10 A 225 ALA VAL SER LEU GLN VAL ALA ALA PRO TYR SER LYS PRO SEQRES 11 A 225 SER MET THR LEU GLU PRO ASN LYS ASP LEU ARG PRO GLY SEQRES 12 A 225 ASP THR VAL THR ILE THR CYS SER SER TYR GLN GLY TYR SEQRES 13 A 225 PRO GLU ALA GLU VAL PHE TRP GLN ASP GLY GLN GLY VAL SEQRES 14 A 225 PRO LEU THR GLY ASN VAL THR THR SER GLN MET ALA ASN SEQRES 15 A 225 GLU GLN GLY LEU PHE ASP VAL HIS SER ILE LEU ARG VAL SEQRES 16 A 225 VAL LEU GLY ALA ASN GLY THR TYR SER CYS LEU VAL ARG SEQRES 17 A 225 ASN PRO VAL LEU GLN GLN ASP ALA HIS SER SER VAL THR SEQRES 18 A 225 ILE THR PRO GLN SEQRES 1 B 225 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN GLY SEQRES 2 B 225 LEU GLU VAL GLN VAL PRO GLU ASP PRO VAL VAL ALA LEU SEQRES 3 B 225 VAL GLY THR ASP ALA THR LEU CYS CYS SER PHE SER PRO SEQRES 4 B 225 GLU PRO GLY PHE SER LEU ALA GLN LEU ASN LEU ILE TRP SEQRES 5 B 225 GLN LEU THR ASP THR LYS GLN LEU VAL HIS SER PHE ALA SEQRES 6 B 225 GLU GLY GLN ASP GLN GLY SER ALA TYR ALA ASN ARG THR SEQRES 7 B 225 ALA LEU PHE PRO ASP LEU LEU ALA GLN GLY ASN ALA SER SEQRES 8 B 225 LEU ARG LEU GLN ARG VAL ARG VAL ALA ASP GLU GLY SER SEQRES 9 B 225 PHE THR CYS PHE VAL SER ILE ARG ASP PHE GLY SER ALA SEQRES 10 B 225 ALA VAL SER LEU GLN VAL ALA ALA PRO TYR SER LYS PRO SEQRES 11 B 225 SER MET THR LEU GLU PRO ASN LYS ASP LEU ARG PRO GLY SEQRES 12 B 225 ASP THR VAL THR ILE THR CYS SER SER TYR GLN GLY TYR SEQRES 13 B 225 PRO GLU ALA GLU VAL PHE TRP GLN ASP GLY GLN GLY VAL SEQRES 14 B 225 PRO LEU THR GLY ASN VAL THR THR SER GLN MET ALA ASN SEQRES 15 B 225 GLU GLN GLY LEU PHE ASP VAL HIS SER ILE LEU ARG VAL SEQRES 16 B 225 VAL LEU GLY ALA ASN GLY THR TYR SER CYS LEU VAL ARG SEQRES 17 B 225 ASN PRO VAL LEU GLN GLN ASP ALA HIS SER SER VAL THR SEQRES 18 B 225 ILE THR PRO GLN SEQRES 1 C 141 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 C 141 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 C 141 SER GLY ASN THR PHE SER THR ALA HIS MET SER TRP VAL SEQRES 4 C 141 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 C 141 ILE LEU SER ASN GLY ALA GLY ALA SER TYR ALA ASP PHE SEQRES 6 C 141 VAL LYS GLY ARG PHE THR ILE SER ARG ASP SER ALA LYS SEQRES 7 C 141 ASN THR LEU TYR LEU GLN MET ASP SER LEU LYS PRO GLU SEQRES 8 C 141 ASP THR ALA VAL TYR TYR CYS ALA LEU GLY PHE ARG THR SEQRES 9 C 141 LEU THR GLY LEU ARG GLY GLN GLY THR GLN VAL THR VAL SEQRES 10 C 141 SER SER GLY ARG TYR PRO TYR ASP VAL PRO ASP TYR GLY SEQRES 11 C 141 SER GLY ARG ALA GLY GLY GLY SER ASN GLN LEU SEQRES 1 F 141 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 F 141 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 F 141 SER GLY ASN THR PHE SER THR ALA HIS MET SER TRP VAL SEQRES 4 F 141 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 F 141 ILE LEU SER ASN GLY ALA GLY ALA SER TYR ALA ASP PHE SEQRES 6 F 141 VAL LYS GLY ARG PHE THR ILE SER ARG ASP SER ALA LYS SEQRES 7 F 141 ASN THR LEU TYR LEU GLN MET ASP SER LEU LYS PRO GLU SEQRES 8 F 141 ASP THR ALA VAL TYR TYR CYS ALA LEU GLY PHE ARG THR SEQRES 9 F 141 LEU THR GLY LEU ARG GLY GLN GLY THR GLN VAL THR VAL SEQRES 10 F 141 SER SER GLY ARG TYR PRO TYR ASP VAL PRO ASP TYR GLY SEQRES 11 F 141 SER GLY ARG ALA GLY GLY GLY SER ASN GLN LEU HET NAG D 1 14 HET NAG D 2 14 HET MAN D 3 11 HET FUC D 4 10 HET NAG E 1 14 HET NAG E 2 14 HET MAN E 3 11 HET NAG G 1 14 HET NAG G 2 14 HET FUC G 3 10 HET NAG H 1 14 HET NAG H 2 13 HET FUC H 3 10 HET EDO A 301 4 HET EDO A 302 4 HET GOL A 303 6 HET EDO A 304 4 HET GOL A 305 6 HET PEG A 306 7 HET PEG A 307 7 HET PEG A 308 7 HET PEG A 309 7 HET PEG A 310 7 HET GOL A 311 6 HET PEG A 312 7 HET PEG A 313 7 HET PEG A 314 7 HET MAN A 315 12 HET MG A 316 1 HET MG A 317 1 HET MG A 318 1 HET MG A 319 1 HET MG A 320 1 HET MG A 321 1 HET MG A 322 1 HET MG A 323 1 HET EDO A 324 4 HET EDO A 325 4 HET EDO A 326 4 HET EDO A 327 4 HET EDO A 328 4 HET EDO A 329 4 HET EDO A 330 4 HET EDO A 331 4 HET EDO A 332 4 HET EDO A 333 4 HET EDO A 334 4 HET CA A 335 1 HET CA A 336 1 HET EDO B 301 4 HET GOL B 302 6 HET GOL B 303 6 HET PEG B 304 7 HET MG B 305 1 HET MG B 306 1 HET MG B 307 1 HET MG B 308 1 HET MG B 309 1 HET MG B 310 1 HET EDO B 311 4 HET EDO B 312 4 HET EDO B 313 4 HET EDO B 314 4 HET EDO B 315 4 HET EDO B 316 4 HET EDO B 317 4 HET EDO B 318 4 HET EDO B 319 4 HET EDO B 320 4 HET EDO B 321 4 HET EDO B 322 4 HET EDO B 323 4 HET EDO B 324 4 HET EDO B 325 4 HET EDO B 326 4 HET PO4 B 327 5 HET CA B 328 1 HET CA B 329 1 HET CA B 330 1 HET MG C 201 1 HET MG C 202 1 HET MG C 203 1 HET EDO C 204 4 HET EDO C 205 4 HET EDO C 206 4 HET PEG F 201 7 HET EDO F 202 4 HET EDO F 203 4 HET GOL F 204 6 HET PEG F 205 7 HET MG F 206 1 HET MG F 207 1 HET EDO F 208 4 HET EDO F 209 4 HET EDO F 210 4 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM MG MAGNESIUM ION HETNAM CA CALCIUM ION HETNAM PO4 PHOSPHATE 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 HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN EDO ETHYLENE GLYCOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 NAG 8(C8 H15 N O6) FORMUL 5 MAN 3(C6 H12 O6) FORMUL 5 FUC 3(C6 H12 O5) FORMUL 9 EDO 39(C2 H6 O2) FORMUL 11 GOL 6(C3 H8 O3) FORMUL 14 PEG 11(C4 H10 O3) FORMUL 24 MG 19(MG 2+) FORMUL 43 CA 5(CA 2+) FORMUL 71 PO4 O4 P 3- FORMUL 91 HOH *676(H2 O) HELIX 1 AA1 LEU A 99 GLY A 103 5 5 HELIX 2 AA2 ARG A 113 GLU A 117 5 5 HELIX 3 AA3 SER B 59 LEU B 63 5 5 HELIX 4 AA4 LEU B 99 GLY B 103 5 5 HELIX 5 AA5 ARG B 113 GLU B 117 5 5 HELIX 6 AA6 ASN C 27 ALA C 32 5 6 HELIX 7 AA7 ASP C 62 LYS C 65 5 4 HELIX 8 AA8 LYS C 87 THR C 91 5 5 HELIX 9 AA9 THR F 30 ALA F 34 5 5 HELIX 10 AB1 LYS F 89 THR F 93 5 5 SHEET 1 AA1 6 VAL A 38 LEU A 41 0 SHEET 2 AA1 6 PHE A 129 ALA A 139 1 O GLN A 137 N VAL A 38 SHEET 3 AA1 6 GLY A 118 SER A 125 -1 N GLY A 118 O LEU A 136 SHEET 4 AA1 6 ASN A 64 LEU A 69 -1 N GLN A 68 O THR A 121 SHEET 5 AA1 6 LEU A 75 ALA A 80 -1 O VAL A 76 N TRP A 67 SHEET 6 AA1 6 GLN A 83 SER A 87 -1 O GLN A 83 N ALA A 80 SHEET 1 AA2 3 ALA A 46 LEU A 48 0 SHEET 2 AA2 3 LEU A 107 LEU A 109 -1 O LEU A 109 N ALA A 46 SHEET 3 AA2 3 THR A 93 ALA A 94 -1 N ALA A 94 O ARG A 108 SHEET 1 AA3 4 SER A 146 GLU A 150 0 SHEET 2 AA3 4 THR A 160 GLY A 170 -1 O THR A 164 N THR A 148 SHEET 3 AA3 4 PHE A 202 VAL A 211 -1 O PHE A 202 N GLY A 170 SHEET 4 AA3 4 ASN A 189 ALA A 196 -1 N THR A 191 O ILE A 207 SHEET 1 AA4 3 GLU A 175 GLN A 179 0 SHEET 2 AA4 3 GLY A 216 ASN A 224 -1 O LEU A 221 N PHE A 177 SHEET 3 AA4 3 GLN A 229 ILE A 237 -1 O ALA A 231 N VAL A 222 SHEET 1 AA5 6 VAL B 38 LEU B 41 0 SHEET 2 AA5 6 PHE B 129 ALA B 139 1 O GLN B 137 N VAL B 38 SHEET 3 AA5 6 GLY B 118 SER B 125 -1 N GLY B 118 O LEU B 136 SHEET 4 AA5 6 ASN B 64 LEU B 69 -1 N ILE B 66 O PHE B 123 SHEET 5 AA5 6 LEU B 75 ALA B 80 -1 O HIS B 77 N TRP B 67 SHEET 6 AA5 6 GLN B 83 SER B 87 -1 O GLN B 83 N ALA B 80 SHEET 1 AA6 3 ALA B 46 LEU B 48 0 SHEET 2 AA6 3 LEU B 107 LEU B 109 -1 O LEU B 109 N ALA B 46 SHEET 3 AA6 3 THR B 93 ALA B 94 -1 N ALA B 94 O ARG B 108 SHEET 1 AA7 4 SER B 146 GLU B 150 0 SHEET 2 AA7 4 THR B 160 GLY B 170 -1 O THR B 164 N THR B 148 SHEET 3 AA7 4 PHE B 202 VAL B 211 -1 O PHE B 202 N GLY B 170 SHEET 4 AA7 4 ASN B 189 ALA B 196 -1 N THR B 191 O ILE B 207 SHEET 1 AA8 3 GLU B 175 GLN B 179 0 SHEET 2 AA8 3 GLY B 216 ASN B 224 -1 O SER B 219 N GLN B 179 SHEET 3 AA8 3 GLN B 229 ILE B 237 -1 O ALA B 231 N VAL B 222 SHEET 1 AA9 4 LEU C 4 SER C 7 0 SHEET 2 AA9 4 LEU C 18 ALA C 24 -1 O SER C 21 N SER C 7 SHEET 3 AA9 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA9 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AB1 6 GLY C 10 VAL C 12 0 SHEET 2 AB1 6 THR C 111 VAL C 115 1 O THR C 114 N GLY C 10 SHEET 3 AB1 6 ALA C 92 LEU C 98 -1 N TYR C 94 O THR C 111 SHEET 4 AB1 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AB1 6 LEU C 45 ILE C 51 -1 O VAL C 48 N TRP C 36 SHEET 6 AB1 6 SER C 59 TYR C 60 -1 O SER C 59 N GLY C 50 SHEET 1 AB2 4 LEU F 6 SER F 9 0 SHEET 2 AB2 4 LEU F 20 ALA F 26 -1 O SER F 23 N SER F 9 SHEET 3 AB2 4 THR F 80 MET F 85 -1 O MET F 85 N LEU F 20 SHEET 4 AB2 4 PHE F 70 ASP F 75 -1 N SER F 73 O TYR F 82 SHEET 1 AB3 6 GLY F 12 VAL F 14 0 SHEET 2 AB3 6 THR F 113 VAL F 117 1 O THR F 116 N GLY F 12 SHEET 3 AB3 6 ALA F 94 LEU F 100 -1 N TYR F 96 O THR F 113 SHEET 4 AB3 6 MET F 36 GLN F 41 -1 N VAL F 39 O TYR F 97 SHEET 5 AB3 6 LEU F 47 ILE F 53 -1 O ILE F 53 N MET F 36 SHEET 6 AB3 6 SER F 61 TYR F 62 -1 O SER F 61 N GLY F 52 SSBOND 1 CYS A 50 CYS A 122 1555 1555 2.02 SSBOND 2 CYS A 165 CYS A 220 1555 1555 2.03 SSBOND 3 CYS B 50 CYS B 122 1555 1555 2.03 SSBOND 4 CYS B 165 CYS B 220 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 96 1555 1555 2.05 SSBOND 6 CYS F 24 CYS F 98 1555 1555 2.04 LINK ND2 ASN A 104 C1 NAG H 1 1555 1555 1.43 LINK ND2 ASN A 189 C1 NAG D 1 1555 1555 1.43 LINK ND2 ASN B 104 C1 NAG E 1 1555 1555 1.43 LINK ND2 ASN B 189 C1 NAG G 1 1555 1555 1.43 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O6 NAG D 1 C1 FUC D 4 1555 1555 1.40 LINK O4 NAG D 2 C1 MAN D 3 1555 1555 1.42 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.43 LINK O4 NAG E 2 C1 MAN E 3 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.42 LINK O6 NAG G 1 C1 FUC G 3 1555 1555 1.40 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.41 LINK O6 NAG H 1 C1 FUC H 3 1555 1555 1.41 LINK N PHE A 96 MG MG A 316 1555 1555 2.79 LINK O ASN A 104 MG MG A 316 1555 1555 2.93 LINK O SER A 106 MG MG A 316 1555 1555 2.82 LINK OG SER A 135 MG MG A 322 1555 1555 2.38 LINK OD2 ASP A 203 MG MG A 323 1555 1555 2.89 LINK NE2 HIS A 205 MG MG A 323 1555 1555 2.83 LINK O3 GOL A 305 MG MG A 321 1555 1555 2.88 LINK MG MG A 317 NE2 GLN C 109 12555 1555 2.15 LINK MG MG A 318 O GLY C 108 12555 1555 2.84 LINK N PHE B 96 MG MG B 305 1555 1555 2.77 LINK O ASN B 104 MG MG B 305 1555 1555 2.85 LINK O SER B 106 MG MG B 305 1555 1555 2.91 LINK OG1 THR B 192 MG MG B 306 1555 1555 2.75 LINK O GLY B 200 CA CA B 329 1555 1555 3.08 LINK MG MG B 308 O LYS C 43 6555 1555 2.74 LINK MG MG B 310 O4 PO4 B 327 1555 1555 3.00 LINK O HOH B 483 MG MG C 203 1555 1555 2.99 LINK OG SER C 35 MG MG C 201 1555 1555 2.50 LINK N ALA C 40 MG MG C 202 1555 1555 2.79 LINK O GLY C 44 MG MG C 202 1555 1555 2.48 LINK N THR C 102 MG MG C 201 1555 1555 2.76 LINK O THR C 102 MG MG C 201 1555 1555 2.72 LINK OG1 THR F 104 MG MG F 206 1555 1555 2.89 CISPEP 1 GLU A 150 PRO A 151 0 -3.27 CISPEP 2 TYR A 171 PRO A 172 0 -5.13 CISPEP 3 GLU B 150 PRO B 151 0 -5.34 CISPEP 4 TYR B 171 PRO B 172 0 -5.00 CRYST1 219.850 219.850 147.890 90.00 90.00 90.00 I 41 2 2 32 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 0.004549 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004549 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006762 0.00000