HEADER VIRUS 02-FEB-21 7LKI TITLE THE CRYSTAL STRUCTURE OF EPITOPE III OF HCV ENVELOP PROTEIN E2 IN TITLE 2 COMPLEX WITH ANTIBODY 1H8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY 1H8 HEAVY CHAIN; COMPND 3 CHAIN: AAA, DDD; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY 1H8 LIGHT CHAIN; COMPND 7 CHAIN: BBB, EEE; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: EPITOPE III PEPTIDE GLY-ALA-PRO-THR-TYR-SER-TRP-GLY; COMPND 11 CHAIN: CCC, FFF; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HEPACIVIRUS C; SOURCE 13 ORGANISM_TAXID: 11103; SOURCE 14 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 32630 KEYWDS HCV, ENVELOPE PROTEIN E2, VIRUS EXPDTA X-RAY DIFFRACTION AUTHOR L.DENG,P.ZHANG JRNL AUTH L.DENG,N.HERNANDEZ,L.ZHONG,D.D.HOLCOMB,H.YAN,M.L.VIRATA, JRNL AUTH 2 S.TARAFDAR,Y.XU,Y.HE,E.STRUBLE,H.J.ALTER,P.ZHANG JRNL TITL A CONSERVED EPITOPE III ON HEPATITIS C VIRUS E2 PROTEIN HAS JRNL TITL 2 ALTERNATE CONFORMATIONS FACILITATING CELL BINDING OR VIRUS JRNL TITL 3 NEUTRALIZATION. JRNL REF PROC.NATL.ACAD.SCI.USA V. 118 2021 JRNL REFN ESSN 1091-6490 JRNL PMID 34260404 JRNL DOI 10.1073/PNAS.2104242118 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.70 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 60144 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) : 0.245 REMARK 3 FREE R VALUE : 0.294 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.038 REMARK 3 FREE R VALUE TEST SET COUNT : 3030 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4161 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.26 REMARK 3 BIN R VALUE (WORKING SET) : 0.2980 REMARK 3 BIN FREE R VALUE SET COUNT : 208 REMARK 3 BIN FREE R VALUE : 0.3210 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6557 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 429 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.75 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.07800 REMARK 3 B22 (A**2) : 2.00500 REMARK 3 B33 (A**2) : -0.16200 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.38800 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.246 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.211 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.181 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.554 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.907 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.861 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6721 ; 0.006 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6036 ; 0.002 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9149 ; 1.513 ; 1.647 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14097 ; 1.210 ; 1.571 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 849 ;16.619 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 278 ;35.851 ;22.878 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1078 ;14.485 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;18.939 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 906 ; 0.060 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7427 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1360 ; 0.003 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1103 ; 0.195 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 98 ; 0.244 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3089 ; 0.161 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 384 ; 0.178 ; 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): 3425 ; 0.538 ; 1.023 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3423 ; 0.538 ; 1.023 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4264 ; 0.997 ; 1.530 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4264 ; 0.997 ; 1.530 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3295 ; 0.412 ; 1.059 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3296 ; 0.412 ; 1.059 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4884 ; 0.741 ; 1.566 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4885 ; 0.741 ; 1.566 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : AA 2 AA 118 REMARK 3 RESIDUE RANGE : BB 1 BB 112 REMARK 3 RESIDUE RANGE : CC 523 CC 530 REMARK 3 ORIGIN FOR THE GROUP (A): 11.0416 -10.0417 14.7998 REMARK 3 T TENSOR REMARK 3 T11: 0.2244 T22: 0.2909 REMARK 3 T33: 0.1073 T12: -0.0401 REMARK 3 T13: -0.0528 T23: -0.0054 REMARK 3 L TENSOR REMARK 3 L11: 2.3604 L22: 0.6217 REMARK 3 L33: 0.9500 L12: -0.5033 REMARK 3 L13: -1.1112 L23: 0.1754 REMARK 3 S TENSOR REMARK 3 S11: -0.0409 S12: 0.5404 S13: -0.0046 REMARK 3 S21: -0.0469 S22: -0.0278 S23: 0.0033 REMARK 3 S31: -0.0103 S32: -0.0278 S33: 0.0687 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : AA 120 AA 216 REMARK 3 RESIDUE RANGE : BB 115 BB 218 REMARK 3 ORIGIN FOR THE GROUP (A): 16.4654 -30.8201 43.9768 REMARK 3 T TENSOR REMARK 3 T11: 0.1894 T22: 0.0209 REMARK 3 T33: 0.1304 T12: 0.0038 REMARK 3 T13: -0.0414 T23: -0.0140 REMARK 3 L TENSOR REMARK 3 L11: 0.7463 L22: 1.7268 REMARK 3 L33: 0.8792 L12: 0.1050 REMARK 3 L13: -0.0160 L23: 0.5058 REMARK 3 S TENSOR REMARK 3 S11: 0.0146 S12: 0.0647 S13: -0.0577 REMARK 3 S21: 0.0865 S22: 0.0349 S23: -0.0474 REMARK 3 S31: 0.0614 S32: 0.1097 S33: -0.0495 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : DD 2 DD 118 REMARK 3 RESIDUE RANGE : EE 1 EE 112 REMARK 3 RESIDUE RANGE : FF 523 FF 530 REMARK 3 ORIGIN FOR THE GROUP (A): -46.7349 -12.1091 19.9448 REMARK 3 T TENSOR REMARK 3 T11: 0.2410 T22: 0.1804 REMARK 3 T33: 0.1559 T12: -0.0037 REMARK 3 T13: -0.0204 T23: 0.0516 REMARK 3 L TENSOR REMARK 3 L11: 1.0661 L22: 0.3621 REMARK 3 L33: 1.4443 L12: -0.3618 REMARK 3 L13: -0.4865 L23: 0.0277 REMARK 3 S TENSOR REMARK 3 S11: 0.0588 S12: 0.3574 S13: 0.1272 REMARK 3 S21: -0.0665 S22: -0.0828 S23: -0.0442 REMARK 3 S31: -0.0697 S32: 0.0521 S33: 0.0240 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : DD 120 DD 216 REMARK 3 RESIDUE RANGE : EE 115 EE 218 REMARK 3 ORIGIN FOR THE GROUP (A): -19.3048 -31.7084 32.4855 REMARK 3 T TENSOR REMARK 3 T11: 0.2944 T22: 0.1430 REMARK 3 T33: 0.1883 T12: 0.0736 REMARK 3 T13: -0.0258 T23: -0.0181 REMARK 3 L TENSOR REMARK 3 L11: 4.3775 L22: 0.6142 REMARK 3 L33: 1.1228 L12: -0.8258 REMARK 3 L13: -1.4795 L23: 0.3822 REMARK 3 S TENSOR REMARK 3 S11: -0.2876 S12: -0.4194 S13: -0.0479 REMARK 3 S21: 0.1110 S22: 0.1923 S23: -0.0253 REMARK 3 S31: 0.3208 S32: 0.1493 S33: 0.0953 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT 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 7LKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000254570. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-MAR-14 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 : NSLS REMARK 200 BEAMLINE : X29A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73746 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3 REMARK 200 DATA REDUNDANCY : 2.900 REMARK 200 R MERGE (I) : 0.09100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88 REMARK 200 COMPLETENESS FOR SHELL (%) : 70.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.51100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 1ZEA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350 0.1 M CITRATE PH 5.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 100.84150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.39650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 100.84150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.39650 REMARK 290 SMTRY3 4 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB, CCC 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4190 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: DDD, EEE, FFF 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 A 131 REMARK 465 SER A 132 REMARK 465 ALA A 133 REMARK 465 ALA A 134 REMARK 465 GLN A 135 REMARK 465 THR A 136 REMARK 465 ARG A 217 REMARK 465 ASP C 520 REMARK 465 ARG C 521 REMARK 465 SER C 522 REMARK 465 ALA C 531 REMARK 465 ASN C 532 REMARK 465 ASP C 533 REMARK 465 LYS C 534 REMARK 465 GLU D 1 REMARK 465 GLY D 131 REMARK 465 SER D 132 REMARK 465 ALA D 133 REMARK 465 ALA D 134 REMARK 465 GLN D 135 REMARK 465 THR D 136 REMARK 465 ASN D 137 REMARK 465 SER D 162 REMARK 465 LEU D 163 REMARK 465 ARG D 217 REMARK 465 ASP E 1 REMARK 465 GLN E 161 REMARK 465 ASN E 162 REMARK 465 GLY E 163 REMARK 465 VAL E 164 REMARK 465 ASN E 215 REMARK 465 ARG E 216 REMARK 465 ASN E 217 REMARK 465 GLU E 218 REMARK 465 ASP F 520 REMARK 465 ARG F 521 REMARK 465 SER F 522 REMARK 465 ALA F 531 REMARK 465 ASN F 532 REMARK 465 ASP F 533 REMARK 465 LYS F 534 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 OG1 THREE 131 O HOHEE 301 2.07 REMARK 500 O HOHAA 354 O HOHAA 378 2.10 REMARK 500 O SEREE 127 O HOHEE 301 2.11 REMARK 500 ND2 ASNDD 57 O HOHDD 301 2.12 REMARK 500 O ILEDD 214 O HOHDD 302 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 O THREE 131 O THREE 131 2556 1.80 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 ARGAA 69 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARGDD 69 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARGDD 69 NE - CZ - NH2 ANGL. DEV. = -4.7 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 THRAA 104 -176.78 -171.61 REMARK 500 PROAA 151 -178.28 -53.22 REMARK 500 ASPAA 177 -7.92 80.42 REMARK 500 PROBB 8 149.77 -26.57 REMARK 500 PHEBB 37 59.15 -94.12 REMARK 500 VALBB 56 -49.11 82.24 REMARK 500 PROBB 100 134.75 -28.95 REMARK 500 TYRBB 145 111.25 -165.76 REMARK 500 PRODD 151 -179.39 -49.74 REMARK 500 PROEE 8 154.16 -24.18 REMARK 500 PHEEE 37 59.44 -91.24 REMARK 500 VALEE 56 -49.89 83.89 REMARK 500 PROEE 100 137.00 -28.45 REMARK 500 TYREE 145 109.64 -167.48 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 PHEAA 150 PROAA 151 -50.19 REMARK 500 GLUAA 152 PROAA 153 -35.90 REMARK 500 TRPAA 192 PROAA 193 59.34 REMARK 500 THRBB 7 PROBB 8 -74.01 REMARK 500 PHEBB 99 PROBB 100 -70.18 REMARK 500 TYRBB 145 PROBB 146 51.55 REMARK 500 PHEDD 150 PRODD 151 -55.14 REMARK 500 GLUDD 152 PRODD 153 30.71 REMARK 500 TRPDD 192 PRODD 193 57.68 REMARK 500 THREE 7 PROEE 8 -76.34 REMARK 500 PHEEE 99 PROEE 100 -68.74 REMARK 500 TYREE 145 PROEE 146 52.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PHEAA 150 -12.40 REMARK 500 GLUAA 152 -13.35 REMARK 500 PHEBB 99 -10.96 REMARK 500 PHEDD 150 -10.76 REMARK 500 GLUDD 152 10.69 REMARK 500 TRPDD 192 10.68 REMARK 500 PHEEE 99 -11.65 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 414 DISTANCE = 6.70 ANGSTROMS REMARK 525 HOH A 415 DISTANCE = 6.73 ANGSTROMS DBREF 7LKIAA 1 217 PDB 7LKI 7LKI 1 217 DBREF 7LKIBB 1 218 PDB 7LKI 7LKI 1 218 DBREF 7LKICC 520 534 PDB 7LKI 7LKI 520 534 DBREF 7LKIDD 1 217 PDB 7LKI 7LKI 1 217 DBREF 7LKIEE 1 218 PDB 7LKI 7LKI 1 218 DBREF 7LKIFF 520 534 PDB 7LKI 7LKI 520 534 SEQRES 1AA 217 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2AA 217 PRO GLY GLY SER MET LYS LEU SER CYS ALA ALA SER GLY SEQRES 3AA 217 PHE THR PHE SER ASP ALA TYR MET ASP TRP VAL ARG GLN SEQRES 4AA 217 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE ARG SEQRES 5AA 217 ASN LYS ALA ASN ASN HIS ALA THR PHE TYR ALA GLU SER SEQRES 6AA 217 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7AA 217 SER SER VAL TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8AA 217 ASP THR GLY ILE TYR TYR CYS THR LEU GLN TYR GLY THR SEQRES 9AA 217 SER SER TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10AA 217 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO SEQRES 11AA 217 GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY SEQRES 12AA 217 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13AA 217 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR SEQRES 14AA 217 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SEQRES 15AA 217 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU SEQRES 16AA 217 THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR SEQRES 17AA 217 LYS VAL ASP LYS LYS ILE VAL PRO ARG SEQRES 1BB 218 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2BB 218 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3BB 218 GLN SER LEU LEU TYR SER ASN GLY LYS THR PHE LEU ASN SEQRES 4BB 218 TRP LEU PHE GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5BB 218 ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6BB 218 ARG PHE THR GLY SER GLY SER GLY THR ALA PHE THR LEU SEQRES 7BB 218 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8BB 218 TYR CYS VAL GLN GLY THR HIS PHE PRO LEU THR PHE GLY SEQRES 9BB 218 ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA SEQRES 10BB 218 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11BB 218 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12BB 218 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13BB 218 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14BB 218 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15BB 218 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16BB 218 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17BB 218 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU SEQRES 1CC 15 ASP ARG SER GLY ALA PRO THR TYR SER TRP GLY ALA ASN SEQRES 2CC 15 ASP LYS SEQRES 1DD 217 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2DD 217 PRO GLY GLY SER MET LYS LEU SER CYS ALA ALA SER GLY SEQRES 3DD 217 PHE THR PHE SER ASP ALA TYR MET ASP TRP VAL ARG GLN SEQRES 4DD 217 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE ARG SEQRES 5DD 217 ASN LYS ALA ASN ASN HIS ALA THR PHE TYR ALA GLU SER SEQRES 6DD 217 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7DD 217 SER SER VAL TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8DD 217 ASP THR GLY ILE TYR TYR CYS THR LEU GLN TYR GLY THR SEQRES 9DD 217 SER SER TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10DD 217 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO SEQRES 11DD 217 GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY SEQRES 12DD 217 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13DD 217 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR SEQRES 14DD 217 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SEQRES 15DD 217 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU SEQRES 16DD 217 THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR SEQRES 17DD 217 LYS VAL ASP LYS LYS ILE VAL PRO ARG SEQRES 1EE 218 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2EE 218 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3EE 218 GLN SER LEU LEU TYR SER ASN GLY LYS THR PHE LEU ASN SEQRES 4EE 218 TRP LEU PHE GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5EE 218 ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6EE 218 ARG PHE THR GLY SER GLY SER GLY THR ALA PHE THR LEU SEQRES 7EE 218 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8EE 218 TYR CYS VAL GLN GLY THR HIS PHE PRO LEU THR PHE GLY SEQRES 9EE 218 ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA SEQRES 10EE 218 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11EE 218 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12EE 218 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13EE 218 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14EE 218 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15EE 218 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16EE 218 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17EE 218 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU SEQRES 1FF 15 ASP ARG SER GLY ALA PRO THR TYR SER TRP GLY ALA ASN SEQRES 2FF 15 ASP LYS FORMUL 7 HOH *429(H2 O) HELIX 1 AA1 THRAA 28 ALAAA 32 5 5 HELIX 2 AA2 ASNAA 53 ASNAA 57 5 5 HELIX 3 AA3 ASPAA 76 LYSAA 78 5 3 HELIX 4 AA4 ARGAA 89 THRAA 93 5 5 HELIX 5 AA5 SERAA 160 SERAA 162 5 3 HELIX 6 AA6 PROAA 204 SERAA 207 5 4 HELIX 7 AA7 GLUBB 84 LEUBB 88 5 5 HELIX 8 AA8 SERBB 126 SERBB 132 1 7 HELIX 9 AA9 LYSBB 188 ARGBB 193 1 6 HELIX 10 AB1 THRDD 28 ALADD 32 5 5 HELIX 11 AB2 ASNDD 53 ASNDD 57 5 5 HELIX 12 AB3 ASPDD 76 LYSDD 78 5 3 HELIX 13 AB4 ARGDD 89 THRDD 93 5 5 HELIX 14 AB5 PRODD 204 SERDD 207 5 4 HELIX 15 AB6 GLUEE 84 LEUEE 88 5 5 HELIX 16 AB7 SEREE 126 SEREE 132 1 7 HELIX 17 AB8 LYSEE 188 ARGEE 193 1 6 SHEET 1 AA1 4 LYSAA 3 SERAA 7 0 SHEET 2 AA1 4 METAA 18 SERAA 25 -1 O SERAA 25 N LYSAA 3 SHEET 3 AA1 4 SERAA 80 METAA 85 -1 O METAA 85 N METAA 18 SHEET 4 AA1 4 PHEAA 70 ASPAA 75 -1 N ASPAA 75 O SERAA 80 SHEET 1 AA2 6 GLYAA 10 VALAA 12 0 SHEET 2 AA2 6 THRAA 111 VALAA 115 1 O THRAA 114 N VALAA 12 SHEET 3 AA2 6 GLYAA 94 LEUAA 100 -1 N TYRAA 96 O THRAA 111 SHEET 4 AA2 6 METAA 34 SERAA 40 -1 N VALAA 37 O TYRAA 97 SHEET 5 AA2 6 GLYAA 44 ILEAA 51 -1 O GLUAA 46 N ARGAA 38 SHEET 6 AA2 6 THRAA 60 TYRAA 62 -1 O PHEAA 61 N GLUAA 50 SHEET 1 AA3 4 GLYAA 10 VALAA 12 0 SHEET 2 AA3 4 THRAA 111 VALAA 115 1 O THRAA 114 N VALAA 12 SHEET 3 AA3 4 GLYAA 94 LEUAA 100 -1 N TYRAA 96 O THRAA 111 SHEET 4 AA3 4 SERAA 106 TRPAA 107 -1 O SERAA 106 N LEUAA 100 SHEET 1 AA4 4 SERAA 124 LEUAA 128 0 SHEET 2 AA4 4 METAA 139 TYRAA 149 -1 O LYSAA 147 N SERAA 124 SHEET 3 AA4 4 LEUAA 178 PROAA 188 -1 O LEUAA 181 N VALAA 146 SHEET 4 AA4 4 VALAA 167 THRAA 169 -1 N HISAA 168 O SERAA 184 SHEET 1 AA5 4 SERAA 124 LEUAA 128 0 SHEET 2 AA5 4 METAA 139 TYRAA 149 -1 O LYSAA 147 N SERAA 124 SHEET 3 AA5 4 LEUAA 178 PROAA 188 -1 O LEUAA 181 N VALAA 146 SHEET 4 AA5 4 VALAA 173 GLNAA 175 -1 N GLNAA 175 O LEUAA 178 SHEET 1 AA6 3 THRAA 155 TRPAA 158 0 SHEET 2 AA6 3 THRAA 198 HISAA 203 -1 O ASNAA 200 N THRAA 157 SHEET 3 AA6 3 THRAA 208 LYSAA 213 -1 O VALAA 210 N VALAA 201 SHEET 1 AA7 4 METBB 4 THRBB 7 0 SHEET 2 AA7 4 ALABB 19 SERBB 25 -1 O LYSBB 24 N THRBB 5 SHEET 3 AA7 4 ALABB 75 ILEBB 80 -1 O PHEBB 76 N CYSBB 23 SHEET 4 AA7 4 PHEBB 67 SERBB 72 -1 N THRBB 68 O LYSBB 79 SHEET 1 AA8 6 THRBB 10 VALBB 13 0 SHEET 2 AA8 6 THRBB 107 LEUBB 111 1 O GLUBB 110 N LEUBB 11 SHEET 3 AA8 6 GLYBB 89 GLNBB 95 -1 N GLYBB 89 O LEUBB 109 SHEET 4 AA8 6 LEUBB 38 GLNBB 43 -1 N LEUBB 41 O TYRBB 92 SHEET 5 AA8 6 LYSBB 50 TYRBB 54 -1 O LEUBB 52 N TRPBB 40 SHEET 6 AA8 6 LYSBB 58 LEUBB 59 -1 O LYSBB 58 N TYRBB 54 SHEET 1 AA9 4 THRBB 10 VALBB 13 0 SHEET 2 AA9 4 THRBB 107 LEUBB 111 1 O GLUBB 110 N LEUBB 11 SHEET 3 AA9 4 GLYBB 89 GLNBB 95 -1 N GLYBB 89 O LEUBB 109 SHEET 4 AA9 4 THRBB 102 PHEBB 103 -1 O THRBB 102 N GLNBB 95 SHEET 1 AB1 4 THRBB 119 PHEBB 123 0 SHEET 2 AB1 4 GLYBB 134 PHEBB 144 -1 O ASNBB 142 N THRBB 119 SHEET 3 AB1 4 TYRBB 178 THRBB 187 -1 O METBB 180 N LEUBB 141 SHEET 4 AB1 4 VALBB 164 TRPBB 168 -1 N SERBB 167 O SERBB 181 SHEET 1 AB2 4 SERBB 158 ARGBB 160 0 SHEET 2 AB2 4 ASNBB 150 ILEBB 155 -1 N ILEBB 155 O SERBB 158 SHEET 3 AB2 4 SERBB 196 HISBB 203 -1 O THRBB 202 N ASNBB 150 SHEET 4 AB2 4 SERBB 206 ASNBB 215 -1 O LYSBB 212 N CYSBB 199 SHEET 1 AB3 4 LYSDD 3 SERDD 7 0 SHEET 2 AB3 4 METDD 18 SERDD 25 -1 O SERDD 25 N LYSDD 3 SHEET 3 AB3 4 SERDD 80 METDD 85 -1 O METDD 85 N METDD 18 SHEET 4 AB3 4 PHEDD 70 ASPDD 75 -1 N SERDD 73 O TYRDD 82 SHEET 1 AB4 6 GLYDD 10 VALDD 12 0 SHEET 2 AB4 6 THRDD 111 VALDD 115 1 O THRDD 114 N VALDD 12 SHEET 3 AB4 6 GLYDD 94 LEUDD 100 -1 N GLYDD 94 O LEUDD 113 SHEET 4 AB4 6 METDD 34 SERDD 40 -1 N VALDD 37 O TYRDD 97 SHEET 5 AB4 6 GLYDD 44 ILEDD 51 -1 O VALDD 48 N TRPDD 36 SHEET 6 AB4 6 THRDD 60 TYRDD 62 -1 O PHEDD 61 N GLUDD 50 SHEET 1 AB5 4 GLYDD 10 VALDD 12 0 SHEET 2 AB5 4 THRDD 111 VALDD 115 1 O THRDD 114 N VALDD 12 SHEET 3 AB5 4 GLYDD 94 LEUDD 100 -1 N GLYDD 94 O LEUDD 113 SHEET 4 AB5 4 SERDD 106 TRPDD 107 -1 O SERDD 106 N LEUDD 100 SHEET 1 AB6 4 SERDD 124 LEUDD 128 0 SHEET 2 AB6 4 METDD 139 TYRDD 149 -1 O LYSDD 147 N SERDD 124 SHEET 3 AB6 4 LEUDD 178 PRODD 188 -1 O LEUDD 181 N VALDD 146 SHEET 4 AB6 4 VALDD 167 THRDD 169 -1 N HISDD 168 O SERDD 184 SHEET 1 AB7 4 SERDD 124 LEUDD 128 0 SHEET 2 AB7 4 METDD 139 TYRDD 149 -1 O LYSDD 147 N SERDD 124 SHEET 3 AB7 4 LEUDD 178 PRODD 188 -1 O LEUDD 181 N VALDD 146 SHEET 4 AB7 4 VALDD 173 GLNDD 175 -1 N VALDD 173 O THRDD 180 SHEET 1 AB8 3 THRDD 155 TRPDD 158 0 SHEET 2 AB8 3 THRDD 198 HISDD 203 -1 O ASNDD 200 N THRDD 157 SHEET 3 AB8 3 THRDD 208 LYSDD 213 -1 O VALDD 210 N VALDD 201 SHEET 1 AB9 4 METEE 4 THREE 7 0 SHEET 2 AB9 4 ALAEE 19 SEREE 25 -1 O LYSEE 24 N THREE 5 SHEET 3 AB9 4 ALAEE 75 ILEEE 80 -1 O PHEEE 76 N CYSEE 23 SHEET 4 AB9 4 PHEEE 67 SEREE 72 -1 N THREE 68 O LYSEE 79 SHEET 1 AC1 6 THREE 10 VALEE 13 0 SHEET 2 AC1 6 THREE 107 LEUEE 111 1 O GLUEE 110 N LEUEE 11 SHEET 3 AC1 6 GLYEE 89 GLNEE 95 -1 N GLYEE 89 O LEUEE 109 SHEET 4 AC1 6 LEUEE 38 GLNEE 43 -1 N LEUEE 41 O TYREE 92 SHEET 5 AC1 6 LYSEE 50 TYREE 54 -1 O LEUEE 52 N TRPEE 40 SHEET 6 AC1 6 LYSEE 58 LEUEE 59 -1 O LYSEE 58 N TYREE 54 SHEET 1 AC2 4 THREE 10 VALEE 13 0 SHEET 2 AC2 4 THREE 107 LEUEE 111 1 O GLUEE 110 N LEUEE 11 SHEET 3 AC2 4 GLYEE 89 GLNEE 95 -1 N GLYEE 89 O LEUEE 109 SHEET 4 AC2 4 THREE 102 PHEEE 103 -1 O THREE 102 N GLNEE 95 SHEET 1 AC3 4 THREE 119 PHEEE 123 0 SHEET 2 AC3 4 GLYEE 134 PHEEE 144 -1 O ASNEE 142 N THREE 119 SHEET 3 AC3 4 TYREE 178 THREE 187 -1 O LEUEE 184 N VALEE 137 SHEET 4 AC3 4 ASNEE 166 TRPEE 168 -1 N SEREE 167 O SEREE 181 SHEET 1 AC4 4 SEREE 158 ARGEE 160 0 SHEET 2 AC4 4 ASNEE 150 ILEEE 155 -1 N ILEEE 155 O SEREE 158 SHEET 3 AC4 4 TYREE 197 HISEE 203 -1 O THREE 198 N LYSEE 154 SHEET 4 AC4 4 SEREE 206 PHEEE 214 -1 O LYSEE 212 N CYSEE 199 SSBOND 1 CYSAA 22 CYSAA 98 1555 1555 2.08 SSBOND 2 CYSAA 144 CYSAA 199 1555 1555 2.05 SSBOND 3 CYSBB 23 CYSBB 93 1555 1555 2.09 SSBOND 4 CYSBB 139 CYSBB 199 1555 1555 2.04 SSBOND 5 CYSDD 22 CYSDD 98 1555 1555 2.03 SSBOND 6 CYSDD 144 CYSDD 199 1555 1555 2.01 SSBOND 7 CYSEE 23 CYSEE 93 1555 1555 2.08 SSBOND 8 CYSEE 139 CYSEE 199 1555 1555 2.02 CRYST1 201.683 42.793 110.824 90.00 109.53 90.00 C 1 2 1 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 0.004958 0.000000 0.001759 0.00000 SCALE2 0.000000 0.023368 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009574 0.00000