HEADER PROTEIN BINDING 06-SEP-19 6SRX TITLE STRUCTURE OF THE ARGINASE-2-INHIBITORY HUMAN ANTIGEN-BINDING FRAGMENT TITLE 2 FAB C0021158 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB C0021158 HEAVY CHAIN (IGG1); COMPND 3 CHAIN: HHH, III; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 6 NUMBERING SCHEME.; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB C0021158 LIGHT CHAIN (IGG1); COMPND 9 CHAIN: LLL, MMM; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 12 NUMBERING SCHEME. RESIDUE 10 WOULD NOT BE PRESENT IN THE KABAT COMPND 13 SCHEME, BUT DUE TO PROBLEMS WITH NON-CONTINUOUS NUMBERING IN L- COMPND 14 PEPTIDES, WE INCLUDED IT. THEREFORE, RESIDUES 2-10 SHOULD BE READ AS COMPND 15 1-9, PER KABAT. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS GEN. SP.; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS GEN. SP.; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB KEYWDS ARGINASE-2 INHIBITOR, IGG, ANTIGEN-BINDING FRAGMENT, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR D.BURSCHOWSKY,A.ADDYMAN,S.FIEDLER,M.GROVES,S.HAYNES,C.SEEWOORUTHUN, AUTHOR 2 M.CARR JRNL AUTH M.AUSTIN,D.BURSCHOWSKY JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERISATION OF A JRNL TITL 2 HIGH-AFFINITY MONOCLONAL ANTIBODY C0021158 THAT INHIBITS JRNL TITL 3 ARGINASE 2 FUNCTION VIA A NOVEL NON-COMPETITIVE MECHANISM OF JRNL TITL 4 ACTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0253 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 67745 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.619 REMARK 3 FREE R VALUE TEST SET COUNT : 3129 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) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4766 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.47 REMARK 3 BIN R VALUE (WORKING SET) : 0.3510 REMARK 3 BIN FREE R VALUE SET COUNT : 269 REMARK 3 BIN FREE R VALUE : 0.3540 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6449 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 18 REMARK 3 SOLVENT ATOMS : 282 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.86 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.23700 REMARK 3 B22 (A**2) : -0.70500 REMARK 3 B33 (A**2) : -1.23100 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.32400 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.193 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.179 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.373 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6685 ; 0.005 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6028 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9133 ; 1.341 ; 1.644 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14077 ; 1.176 ; 1.568 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 877 ; 7.643 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 260 ;30.935 ;22.692 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1028 ;15.220 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;20.591 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 890 ; 0.047 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7531 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1323 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 895 ; 0.176 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 66 ; 0.151 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3141 ; 0.152 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 290 ; 0.146 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3503 ; 1.147 ; 3.201 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3498 ; 1.143 ; 3.197 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4379 ; 2.008 ; 4.787 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4380 ; 2.009 ; 4.788 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3182 ; 0.943 ; 3.243 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3183 ; 0.943 ; 3.244 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4754 ; 1.629 ; 4.818 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4755 ; 1.629 ; 4.819 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : Chains H I REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : Chains L M REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 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 : HH 1 HH 214 REMARK 3 ORIGIN FOR THE GROUP (A): 20.9358 -13.6668 -9.7537 REMARK 3 T TENSOR REMARK 3 T11: 0.0817 T22: 0.0482 REMARK 3 T33: 0.0705 T12: -0.0027 REMARK 3 T13: 0.0622 T23: -0.0306 REMARK 3 L TENSOR REMARK 3 L11: 0.7171 L22: 1.8409 REMARK 3 L33: 0.2676 L12: -0.9897 REMARK 3 L13: -0.0855 L23: 0.0884 REMARK 3 S TENSOR REMARK 3 S11: 0.0338 S12: 0.0992 S13: -0.0204 REMARK 3 S21: -0.0668 S22: -0.0389 S23: -0.0676 REMARK 3 S31: 0.0430 S32: 0.0288 S33: 0.0051 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 : LL 3 LL 211 REMARK 3 ORIGIN FOR THE GROUP (A): 8.6294 -26.4079 -13.3804 REMARK 3 T TENSOR REMARK 3 T11: 0.1183 T22: 0.0799 REMARK 3 T33: 0.1791 T12: -0.0261 REMARK 3 T13: 0.0643 T23: -0.0428 REMARK 3 L TENSOR REMARK 3 L11: 1.2629 L22: 2.5914 REMARK 3 L33: 0.2300 L12: -1.8033 REMARK 3 L13: 0.1286 L23: -0.1765 REMARK 3 S TENSOR REMARK 3 S11: 0.1363 S12: 0.0906 S13: -0.2545 REMARK 3 S21: -0.1869 S22: -0.1280 S23: 0.3455 REMARK 3 S31: 0.1003 S32: -0.0260 S33: -0.0083 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 : II 1 II 214 REMARK 3 ORIGIN FOR THE GROUP (A): -6.0088 37.7450 -22.8106 REMARK 3 T TENSOR REMARK 3 T11: 0.0805 T22: 0.0349 REMARK 3 T33: 0.0735 T12: -0.0279 REMARK 3 T13: 0.0603 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 0.3796 L22: 2.1522 REMARK 3 L33: 0.6185 L12: -0.6138 REMARK 3 L13: 0.2422 L23: -0.9208 REMARK 3 S TENSOR REMARK 3 S11: 0.0071 S12: 0.0788 S13: 0.0451 REMARK 3 S21: -0.0829 S22: -0.0820 S23: -0.0843 REMARK 3 S31: 0.0017 S32: 0.0819 S33: 0.0749 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 : MM 1 MM 210 REMARK 3 ORIGIN FOR THE GROUP (A): 5.0831 50.2570 -15.7058 REMARK 3 T TENSOR REMARK 3 T11: 0.1671 T22: 0.1061 REMARK 3 T33: 0.2384 T12: -0.0530 REMARK 3 T13: -0.0086 T23: 0.0085 REMARK 3 L TENSOR REMARK 3 L11: 0.5431 L22: 1.7549 REMARK 3 L33: 0.4401 L12: -0.7661 REMARK 3 L13: 0.3196 L23: -0.8564 REMARK 3 S TENSOR REMARK 3 S11: -0.0618 S12: 0.0057 S13: 0.2266 REMARK 3 S21: 0.2710 S22: -0.1686 S23: -0.5225 REMARK 3 S31: -0.1613 S32: 0.1167 S33: 0.2304 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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 THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 6SRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292104084. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-NOV-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97242 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67778 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 48.960 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.11000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 1.45000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 6SRV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.49 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NAACO PH 5.0 20% PEG6000 200 MM REMARK 280 LICL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 61.33500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3620 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: HHH, LLL REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20380 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: III, MMM 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 GLY H -3 REMARK 465 ALA H -2 REMARK 465 HIS H -1 REMARK 465 SER H 0 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 ALA H 221 REMARK 465 ALA H 222 REMARK 465 GLY L -2 REMARK 465 VAL L -1 REMARK 465 HIS L 0 REMARK 465 SER L 1 REMARK 465 GLN L 2 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 GLY I -3 REMARK 465 ALA I -2 REMARK 465 HIS I -1 REMARK 465 SER I 0 REMARK 465 SER I 215 REMARK 465 CYS I 216 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 THR I 219 REMARK 465 HIS I 220 REMARK 465 ALA I 221 REMARK 465 ALA I 222 REMARK 465 GLY M -2 REMARK 465 VAL M -1 REMARK 465 HIS M 0 REMARK 465 SER M 1 REMARK 465 GLN M 2 REMARK 465 GLU M 211 REMARK 465 CYS M 212 REMARK 465 SER M 213 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 HH12 ARGHH 66 OD1 ASPHH 86 1.44 REMARK 500 HH12 ARGII 66 OD1 ASPII 86 1.45 REMARK 500 O GLNMM 109 O HOHMM 301 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 HE21 GLNLL 79 OE1 GLNMM 79 2544 1.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARGHH 66 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARGHH 66 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARGII 66 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES 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 ARGHH 30 22.81 -142.21 REMARK 500 ALAHH 34 -3.11 -147.36 REMARK 500 ASNHH 76 62.68 26.52 REMARK 500 ASPHH 98 -101.21 -103.33 REMARK 500 THRHH 131 96.51 -54.10 REMARK 500 SERHH 132 68.93 -67.84 REMARK 500 ASPHH 144 63.33 65.09 REMARK 500 THRHH 191 -61.91 -95.74 REMARK 500 ASNLL 27B -98.18 -109.74 REMARK 500 ASNLL 51 -52.62 76.43 REMARK 500 ASPLL 152 -112.66 56.48 REMARK 500 ARGII 30 22.59 -141.93 REMARK 500 ALAII 34 -1.92 -147.51 REMARK 500 ASNII 76 62.22 27.03 REMARK 500 ASPII 98 -101.20 -101.47 REMARK 500 THRII 131 -79.94 -63.82 REMARK 500 ASPII 144 63.46 63.98 REMARK 500 THRII 191 -62.43 -95.32 REMARK 500 PROMM 15 150.50 -49.55 REMARK 500 ASNMM 27B -97.77 -110.59 REMARK 500 ASNMM 51 -53.53 76.74 REMARK 500 ASPMM 152 -112.45 56.78 REMARK 500 GLUMM 199 -110.90 55.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 VALII 33 ALAII 34 -149.84 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 H 488 DISTANCE = 5.91 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6SRV RELATED DB: PDB REMARK 900 RELATED ID: 6SS0 RELATED DB: PDB REMARK 900 RELATED ID: 6SS2 RELATED DB: PDB REMARK 900 RELATED ID: 6SS4 RELATED DB: PDB REMARK 900 RELATED ID: 6SS5 RELATED DB: PDB REMARK 900 RELATED ID: 6SS6 RELATED DB: PDB REMARK 900 RELATED ID: 6TUL RELATED DB: PDB DBREF 6SRXHH -3 222 PDB 6SRX 6SRX -3 222 DBREF 6SRXLL -2 213 PDB 6SRX 6SRX -2 213 DBREF 6SRXII -3 222 PDB 6SRX 6SRX -3 222 DBREF 6SRXMM -2 213 PDB 6SRX 6SRX -2 213 SEQRES 1HH 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2HH 233 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3HH 233 ALA ALA SER GLY PHE THR PHE ARG TYR GLU VAL ALA ALA SEQRES 4HH 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5HH 233 SER ALA ILE SER GLY PRO ILE PRO LYS GLY TYR TYR ALA SEQRES 6HH 233 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7HH 233 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG SEQRES 8HH 233 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LEU ARG SEQRES 9HH 233 ALA ASP LEU GLY LEU TYR MET ASP LEU TRP GLY ARG GLY SEQRES 10HH 233 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11HH 233 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12HH 233 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13HH 233 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14HH 233 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15HH 233 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16HH 233 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17HH 233 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18HH 233 VAL GLU PRO LYS SER CYS ASP LYS THR HIS ALA ALA SEQRES 1LL 220 GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO PRO SER SEQRES 2LL 220 VAL SER ALA ALA PRO GLY GLN LYS VAL THR ILE SER CYS SEQRES 3LL 220 SER GLY SER SER SER ASN ILE GLY ASN HIS TYR VAL SER SEQRES 4LL 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5LL 220 ILE TYR ASP ASN SER GLU ARG THR ALA GLY VAL PRO ASP SEQRES 6LL 220 ARG PHE SER GLY SER LYS SER GLY THR SER ALA THR LEU SEQRES 7LL 220 GLY ILE THR GLY LEU GLN THR GLY ASP GLU ALA ASP TYR SEQRES 8LL 220 TYR CYS GLY THR TRP ASP GLU LEU THR SER ASN LEU VAL SEQRES 9LL 220 PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO SEQRES 10LL 220 LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11LL 220 GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU SEQRES 12LL 220 ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP SEQRES 13LL 220 LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR SEQRES 14LL 220 THR THR PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SEQRES 15LL 220 SER SER TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER SEQRES 16LL 220 HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU GLY SER SEQRES 17LL 220 THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1II 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2II 233 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3II 233 ALA ALA SER GLY PHE THR PHE ARG TYR GLU VAL ALA ALA SEQRES 4II 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5II 233 SER ALA ILE SER GLY PRO ILE PRO LYS GLY TYR TYR ALA SEQRES 6II 233 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7II 233 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG SEQRES 8II 233 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LEU ARG SEQRES 9II 233 ALA ASP LEU GLY LEU TYR MET ASP LEU TRP GLY ARG GLY SEQRES 10II 233 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11II 233 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12II 233 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13II 233 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14II 233 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15II 233 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16II 233 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17II 233 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18II 233 VAL GLU PRO LYS SER CYS ASP LYS THR HIS ALA ALA SEQRES 1MM 220 GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO PRO SER SEQRES 2MM 220 VAL SER ALA ALA PRO GLY GLN LYS VAL THR ILE SER CYS SEQRES 3MM 220 SER GLY SER SER SER ASN ILE GLY ASN HIS TYR VAL SER SEQRES 4MM 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5MM 220 ILE TYR ASP ASN SER GLU ARG THR ALA GLY VAL PRO ASP SEQRES 6MM 220 ARG PHE SER GLY SER LYS SER GLY THR SER ALA THR LEU SEQRES 7MM 220 GLY ILE THR GLY LEU GLN THR GLY ASP GLU ALA ASP TYR SEQRES 8MM 220 TYR CYS GLY THR TRP ASP GLU LEU THR SER ASN LEU VAL SEQRES 9MM 220 PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO SEQRES 10MM 220 LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11MM 220 GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU SEQRES 12MM 220 ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP SEQRES 13MM 220 LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR SEQRES 14MM 220 THR THR PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SEQRES 15MM 220 SER SER TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER SEQRES 16MM 220 HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU GLY SER SEQRES 17MM 220 THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SER HET ACT HH 301 7 HET ACT HH 302 7 HET CL HH 303 1 HET ACT II 301 7 HET ACT II 302 7 HET CL II 303 1 HETNAM ACT ACETATE ION HETNAM CL CHLORIDE ION FORMUL 5 ACT 4(C2 H3 O2 1-) FORMUL 7 CL 2(CL 1-) FORMUL 11 HOH *282(H2 O) HELIX 1 AA1 ASNHH 73 LYSHH 75 5 3 HELIX 2 AA2 ARGHH 83 THRHH 87 5 5 HELIX 3 AA3 SERHH 156 ALAHH 158 5 3 HELIX 4 AA4 SERHH 187 GLYHH 190 5 4 HELIX 5 AA5 LYSHH 201 ASNHH 204 5 4 HELIX 6 AA6 GLNLL 79 GLULL 83 5 5 HELIX 7 AA7 SERLL 122 ALALL 128 1 7 HELIX 8 AA8 THRLL 182 HISLL 189 1 8 HELIX 9 AA9 ASNII 73 LYSII 75 5 3 HELIX 10 AB1 ARGII 83 THRII 87 5 5 HELIX 11 AB2 SERII 156 ALAII 158 5 3 HELIX 12 AB3 SERII 187 GLYII 190 5 4 HELIX 13 AB4 LYSII 201 ASNII 204 5 4 HELIX 14 AB5 GLNMM 79 GLUMM 83 5 5 HELIX 15 AB6 SERMM 122 ALAMM 128 1 7 HELIX 16 AB7 THRMM 182 HISMM 189 1 8 SHEET 1 AA1 4 GLNHH 3 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O ALAHH 23 N LEUHH 5 SHEET 3 AA1 4 THRHH 77 METHH 82 -1 O METHH 82 N LEUHH 18 SHEET 4 AA1 4 PHEHH 67 ASPHH 72 -1 N SERHH 70 O TYRHH 79 SHEET 1 AA2 6 GLYHH 10 VALHH 12 0 SHEET 2 AA2 6 THRHH 107 VALHH 111 1 O THRHH 110 N VALHH 12 SHEET 3 AA2 6 ALAHH 88 ALAHH 97 -1 N ALAHH 88 O VALHH 109 SHEET 4 AA2 6 VALHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 91 SHEET 5 AA2 6 GLUHH 46 SERHH 52 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AA2 6 LYSHH 56 TYRHH 59 -1 O TYRHH 58 N ALAHH 50 SHEET 1 AA3 4 GLYHH 10 VALHH 12 0 SHEET 2 AA3 4 THRHH 107 VALHH 111 1 O THRHH 110 N VALHH 12 SHEET 3 AA3 4 ALAHH 88 ALAHH 97 -1 N ALAHH 88 O VALHH 109 SHEET 4 AA3 4 LEUHH 100A TRPHH 103 -1 O TYRHH 100B N ARGHH 96 SHEET 1 AA4 4 SERHH 120 LEUHH 124 0 SHEET 2 AA4 4 THRHH 135 TYRHH 145 -1 O LYSHH 143 N SERHH 120 SHEET 3 AA4 4 TYRHH 176 PROHH 185 -1 O LEUHH 178 N VALHH 142 SHEET 4 AA4 4 VALHH 163 THRHH 165 -1 N HISHH 164 O VALHH 181 SHEET 1 AA5 4 SERHH 120 LEUHH 124 0 SHEET 2 AA5 4 THRHH 135 TYRHH 145 -1 O LYSHH 143 N SERHH 120 SHEET 3 AA5 4 TYRHH 176 PROHH 185 -1 O LEUHH 178 N VALHH 142 SHEET 4 AA5 4 VALHH 169 LEUHH 170 -1 N VALHH 169 O SERHH 177 SHEET 1 AA6 3 THRHH 151 TRPHH 154 0 SHEET 2 AA6 3 ILEHH 195 HISHH 200 -1 O ASNHH 197 N SERHH 153 SHEET 3 AA6 3 THRHH 205 ARGHH 210 -1 O VALHH 207 N VALHH 198 SHEET 1 AA7 6 SERLL 10 ALALL 13 0 SHEET 2 AA7 6 THRLL 102 VALLL 106 1 O THRLL 105 N VALLL 11 SHEET 3 AA7 6 ALALL 84 ASPLL 92 -1 N TYRLL 86 O THRLL 102 SHEET 4 AA7 6 SERLL 34 GLNLL 38 -1 N GLNLL 38 O ASPLL 85 SHEET 5 AA7 6 LYSLL 45 TYRLL 49 -1 O LYSLL 45 N GLNLL 37 SHEET 6 AA7 6 GLULL 53 ARGLL 54 -1 O GLULL 53 N TYRLL 49 SHEET 1 AA8 4 SERLL 10 ALALL 13 0 SHEET 2 AA8 4 THRLL 102 VALLL 106 1 O THRLL 105 N VALLL 11 SHEET 3 AA8 4 ALALL 84 ASPLL 92 -1 N TYRLL 86 O THRLL 102 SHEET 4 AA8 4 ASNLL 95B PHELL 98 -1 O VALLL 97 N THRLL 90 SHEET 1 AA9 3 VALLL 19 SERLL 24 0 SHEET 2 AA9 3 SERLL 70 ILELL 75 -1 O LEULL 73 N ILELL 21 SHEET 3 AA9 3 PHELL 62 SERLL 67 -1 N SERLL 63 O GLYLL 74 SHEET 1 AB1 4 SERLL 115 PHELL 119 0 SHEET 2 AB1 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB1 4 TYRLL 173 LEULL 181 -1 O SERLL 177 N CYSLL 135 SHEET 4 AB1 4 VALLL 160 THRLL 162 -1 N GLULL 161 O TYRLL 178 SHEET 1 AB2 4 SERLL 115 PHELL 119 0 SHEET 2 AB2 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB2 4 TYRLL 173 LEULL 181 -1 O SERLL 177 N CYSLL 135 SHEET 4 AB2 4 SERLL 166 LYSLL 167 -1 N SERLL 166 O ALALL 174 SHEET 1 AB3 4 SERLL 154 VALLL 156 0 SHEET 2 AB3 4 THRLL 146 ALALL 151 -1 N TRPLL 149 O VALLL 156 SHEET 3 AB3 4 TYRLL 192 HISLL 198 -1 O GLNLL 195 N ALALL 148 SHEET 4 AB3 4 SERLL 201 VALLL 207 -1 O VALLL 203 N VALLL 196 SHEET 1 AB4 4 GLNII 3 SERII 7 0 SHEET 2 AB4 4 LEUII 18 SERII 25 -1 O ALAII 23 N LEUII 5 SHEET 3 AB4 4 THRII 77 METII 82 -1 O METII 82 N LEUII 18 SHEET 4 AB4 4 PHEII 67 ASPII 72 -1 N SERII 70 O TYRII 79 SHEET 1 AB5 6 GLYII 10 VALII 12 0 SHEET 2 AB5 6 THRII 107 VALII 111 1 O THRII 110 N VALII 12 SHEET 3 AB5 6 ALAII 88 ALAII 97 -1 N ALAII 88 O VALII 109 SHEET 4 AB5 6 VALII 33 GLNII 39 -1 N VALII 37 O TYRII 91 SHEET 5 AB5 6 GLUII 46 SERII 52 -1 O GLUII 46 N ARGII 38 SHEET 6 AB5 6 LYSII 56 TYRII 59 -1 O TYRII 58 N ALAII 50 SHEET 1 AB6 4 GLYII 10 VALII 12 0 SHEET 2 AB6 4 THRII 107 VALII 111 1 O THRII 110 N VALII 12 SHEET 3 AB6 4 ALAII 88 ALAII 97 -1 N ALAII 88 O VALII 109 SHEET 4 AB6 4 LEUII 100A TRPII 103 -1 O TYRII 100B N ARGII 96 SHEET 1 AB7 4 SERII 120 LEUII 124 0 SHEET 2 AB7 4 THRII 135 TYRII 145 -1 O GLYII 139 N LEUII 124 SHEET 3 AB7 4 TYRII 176 PROII 185 -1 O LEUII 178 N VALII 142 SHEET 4 AB7 4 VALII 163 THRII 165 -1 N HISII 164 O VALII 181 SHEET 1 AB8 4 SERII 120 LEUII 124 0 SHEET 2 AB8 4 THRII 135 TYRII 145 -1 O GLYII 139 N LEUII 124 SHEET 3 AB8 4 TYRII 176 PROII 185 -1 O LEUII 178 N VALII 142 SHEET 4 AB8 4 VALII 169 LEUII 170 -1 N VALII 169 O SERII 177 SHEET 1 AB9 3 THRII 151 TRPII 154 0 SHEET 2 AB9 3 ILEII 195 HISII 200 -1 O ASNII 197 N SERII 153 SHEET 3 AB9 3 THRII 205 ARGII 210 -1 O VALII 207 N VALII 198 SHEET 1 AC1 6 SERMM 10 ALAMM 13 0 SHEET 2 AC1 6 THRMM 102 VALMM 106 1 O THRMM 105 N VALMM 11 SHEET 3 AC1 6 ALAMM 84 ASPMM 92 -1 N TYRMM 86 O THRMM 102 SHEET 4 AC1 6 SERMM 34 GLNMM 38 -1 N GLNMM 38 O ASPMM 85 SHEET 5 AC1 6 LYSMM 45 TYRMM 49 -1 O LYSMM 45 N GLNMM 37 SHEET 6 AC1 6 GLUMM 53 ARGMM 54 -1 O GLUMM 53 N TYRMM 49 SHEET 1 AC2 4 SERMM 10 ALAMM 13 0 SHEET 2 AC2 4 THRMM 102 VALMM 106 1 O THRMM 105 N VALMM 11 SHEET 3 AC2 4 ALAMM 84 ASPMM 92 -1 N TYRMM 86 O THRMM 102 SHEET 4 AC2 4 ASNMM 95B PHEMM 98 -1 O VALMM 97 N THRMM 90 SHEET 1 AC3 3 VALMM 19 SERMM 24 0 SHEET 2 AC3 3 SERMM 70 ILEMM 75 -1 O LEUMM 73 N ILEMM 21 SHEET 3 AC3 3 PHEMM 62 SERMM 67 -1 N SERMM 63 O GLYMM 74 SHEET 1 AC4 4 SERMM 115 PHEMM 119 0 SHEET 2 AC4 4 ALAMM 131 PHEMM 140 -1 O LEUMM 136 N THRMM 117 SHEET 3 AC4 4 TYRMM 173 LEUMM 181 -1 O SERMM 177 N CYSMM 135 SHEET 4 AC4 4 VALMM 160 THRMM 162 -1 N GLUMM 161 O TYRMM 178 SHEET 1 AC5 4 SERMM 115 PHEMM 119 0 SHEET 2 AC5 4 ALAMM 131 PHEMM 140 -1 O LEUMM 136 N THRMM 117 SHEET 3 AC5 4 TYRMM 173 LEUMM 181 -1 O SERMM 177 N CYSMM 135 SHEET 4 AC5 4 SERMM 166 LYSMM 167 -1 N SERMM 166 O ALAMM 174 SHEET 1 AC6 4 SERMM 154 VALMM 156 0 SHEET 2 AC6 4 THRMM 146 ALAMM 151 -1 N TRPMM 149 O VALMM 156 SHEET 3 AC6 4 TYRMM 192 HISMM 198 -1 O GLNMM 195 N ALAMM 148 SHEET 4 AC6 4 SERMM 201 VALMM 207 -1 O VALMM 203 N VALMM 196 SSBOND 1 CYSHH 22 CYSHH 92 1555 1555 2.06 SSBOND 2 CYSHH 140 CYSHH 196 1555 1555 2.01 SSBOND 3 CYSLL 23 CYSLL 88 1555 1555 2.02 SSBOND 4 CYSLL 135 CYSLL 194 1555 1555 2.04 SSBOND 5 CYSII 22 CYSII 92 1555 1555 2.05 SSBOND 6 CYSII 140 CYSII 196 1555 1555 2.01 SSBOND 7 CYSMM 23 CYSMM 88 1555 1555 2.02 SSBOND 8 CYSMM 135 CYSMM 194 1555 1555 2.05 CISPEP 1 GLYHH 52A PROHH 53 0 -3.22 CISPEP 2 PHEHH 146 PROHH 147 0 -10.38 CISPEP 3 GLUHH 148 PROHH 149 0 -1.36 CISPEP 4 TYRLL 141 PROLL 142 0 -2.07 CISPEP 5 GLYII 52A PROII 53 0 -4.13 CISPEP 6 PHEII 146 PROII 147 0 -10.49 CISPEP 7 GLUII 148 PROII 149 0 -0.62 CISPEP 8 TYRMM 141 PROMM 142 0 -2.12 CRYST1 62.732 122.670 63.985 90.00 114.89 90.00 P 1 21 1 4 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 0.015941 0.000000 0.007396 0.00000 SCALE2 0.000000 0.008152 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017229 0.00000