HEADER VIRAL PROTEIN/IMMUNE SYSTEM 18-JUN-21 7N9X TITLE CA-TARGETING NANOBODY IS A TOOL FOR STUDYING HIV-1 CAPSID LATTICE TITLE 2 INTERACTIONS COMPND MOL_ID: 1; COMPND 2 MOLECULE: CAPSID PROTEIN; COMPND 3 CHAIN: BBB, CCC, AAA; COMPND 4 FRAGMENT: UNP RESIDUES 133-354; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY; COMPND 8 CHAIN: FFF; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: NANOBODY; COMPND 12 CHAIN: EEE; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: NANOBODY; COMPND 16 CHAIN: DDD; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A; COMPND 20 CHAIN: GGG, HHH, III; COMPND 21 SYNONYM: PPIASE A,CYCLOPHILIN A,CYCLOSPORIN A-BINDING PROTEIN, COMPND 22 ROTAMASE A; COMPND 23 EC: 5.2.1.8; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_COMMON: HIV-1; SOURCE 4 ORGANISM_TAXID: 11676; SOURCE 5 GENE: GAG; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_COMMON: LLAMA; SOURCE 11 ORGANISM_TAXID: 9844; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 16 ORGANISM_COMMON: LLAMA; SOURCE 17 ORGANISM_TAXID: 9844; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 22 ORGANISM_COMMON: LLAMA; SOURCE 23 ORGANISM_TAXID: 9844; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 25 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 GENE: PPIA, CYPA; SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 32 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS HIV-1, HEXAMER, NANOBODY, CYPA, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR E.E.GERBER,K.M.DIGIANANTONIO,T.N.TRIPLER,S.S.SMAGA,B.J.SUMMERS, AUTHOR 2 Y.XIONG JRNL AUTH E.E.GERBER,K.M.DIGIANANTONIO,T.N.TRIPLER,S.S.SMAGA, JRNL AUTH 2 B.J.SUMMERS,Y.XIONG JRNL TITL CA-TARGETING NANOBODY IS A TOOL FOR STUDYING HIV-1 CAPSID JRNL TITL 2 LATTICE INTERACTIONS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.51 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 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) : 3.51 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.58 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4 REMARK 3 NUMBER OF REFLECTIONS : 33142 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 : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.033 REMARK 3 FREE R VALUE TEST SET COUNT : 1668 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) : 3.51 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.60 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1911 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.84 REMARK 3 BIN R VALUE (WORKING SET) : 0.3550 REMARK 3 BIN FREE R VALUE SET COUNT : 90 REMARK 3 BIN FREE R VALUE : 0.3590 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 11458 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 180.2 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.40000 REMARK 3 B22 (A**2) : 2.01400 REMARK 3 B33 (A**2) : -2.41400 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.593 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.616 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 97.604 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11689 ; 0.008 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15797 ; 1.602 ; 1.639 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1475 ; 5.008 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 588 ;31.926 ;22.687 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1984 ;14.578 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;15.919 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1526 ; 0.075 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8892 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5166 ; 0.232 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8133 ; 0.321 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 325 ; 0.190 ; 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): 5938 ; 7.218 ;10.227 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7401 ;11.904 ;15.324 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5750 ; 7.575 ;10.283 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8396 ;11.721 ;15.292 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 9 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : BBB CCC REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 BB 1 BB 218 NULL REMARK 3 2 CC 1 CC 218 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : BBB AAA REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 BB 1 BB 219 NULL REMARK 3 4 AA 1 AA 219 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : CCC AAA REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 5 CC 1 CC 218 NULL REMARK 3 6 AA 1 AA 218 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : FFF EEE REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 7 FF 1 FF 110 NULL REMARK 3 8 EE 1 EE 110 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : FFF DDD REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 9 FF 2 FF 111 NULL REMARK 3 10 DD 2 DD 111 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : EEE DDD REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 11 EE 2 EE 110 NULL REMARK 3 12 DD 2 DD 110 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : GGG HHH REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 14 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 13 GG 3 GG 164 NULL REMARK 3 14 HH 3 HH 164 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 8 REMARK 3 CHAIN NAMES : GGG III REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 16 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 15 GG 1 GG 165 NULL REMARK 3 16 II 1 II 165 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 9 REMARK 3 CHAIN NAMES : HHH III REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 18 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 17 HH 3 HH 164 NULL REMARK 3 18 II 3 II 164 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 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 : AA 1 AA 145 REMARK 3 ORIGIN FOR THE GROUP (A): 60.4320 43.3660 40.9131 REMARK 3 T TENSOR REMARK 3 T11: 0.9030 T22: 0.9536 REMARK 3 T33: 0.7936 T12: 0.0111 REMARK 3 T13: 0.1545 T23: 0.1276 REMARK 3 L TENSOR REMARK 3 L11: 1.4098 L22: 0.8341 REMARK 3 L33: 1.8346 L12: 0.3393 REMARK 3 L13: 0.1451 L23: -0.6304 REMARK 3 S TENSOR REMARK 3 S11: -0.0074 S12: -0.2698 S13: -0.0101 REMARK 3 S21: -0.1570 S22: -0.0435 S23: -0.1071 REMARK 3 S31: 0.2185 S32: -0.0337 S33: 0.0508 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 : AA 146 AA 219 REMARK 3 ORIGIN FOR THE GROUP (A): 32.4843 48.1463 64.1631 REMARK 3 T TENSOR REMARK 3 T11: 0.5118 T22: 1.0475 REMARK 3 T33: 0.7177 T12: -0.1969 REMARK 3 T13: 0.3364 T23: 0.2043 REMARK 3 L TENSOR REMARK 3 L11: 5.6617 L22: 6.2437 REMARK 3 L33: 5.3937 L12: -2.1672 REMARK 3 L13: -1.1706 L23: -0.4013 REMARK 3 S TENSOR REMARK 3 S11: 0.2974 S12: -0.5725 S13: -0.2704 REMARK 3 S21: 0.2240 S22: -0.0331 S23: 0.4526 REMARK 3 S31: -0.2357 S32: 0.1626 S33: -0.2642 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 : BB 1 BB 145 REMARK 3 ORIGIN FOR THE GROUP (A): 40.1297 59.2030 40.7232 REMARK 3 T TENSOR REMARK 3 T11: 0.7431 T22: 1.1193 REMARK 3 T33: 0.8033 T12: -0.0833 REMARK 3 T13: 0.1050 T23: -0.0193 REMARK 3 L TENSOR REMARK 3 L11: 1.8410 L22: 0.7290 REMARK 3 L33: 1.8666 L12: -0.6134 REMARK 3 L13: 0.0649 L23: 0.0388 REMARK 3 S TENSOR REMARK 3 S11: -0.1220 S12: -0.0986 S13: -0.1561 REMARK 3 S21: 0.0014 S22: -0.0701 S23: 0.0222 REMARK 3 S31: 0.2198 S32: -0.2256 S33: 0.1921 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 : BB 146 BB 219 REMARK 3 ORIGIN FOR THE GROUP (A): 29.8497 85.8785 63.7466 REMARK 3 T TENSOR REMARK 3 T11: 0.5978 T22: 1.2374 REMARK 3 T33: 0.6289 T12: 0.2369 REMARK 3 T13: 0.0699 T23: -0.1424 REMARK 3 L TENSOR REMARK 3 L11: 2.6273 L22: 6.1251 REMARK 3 L33: 1.4695 L12: -0.2054 REMARK 3 L13: -1.4432 L23: 1.5714 REMARK 3 S TENSOR REMARK 3 S11: -0.1617 S12: -0.0945 S13: -0.2665 REMARK 3 S21: 0.0143 S22: 0.1742 S23: -0.0268 REMARK 3 S31: -0.1322 S32: -0.4466 S33: -0.0126 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : CC 1 CC 145 REMARK 3 ORIGIN FOR THE GROUP (A): 43.6382 84.8106 40.8524 REMARK 3 T TENSOR REMARK 3 T11: 0.6628 T22: 1.0938 REMARK 3 T33: 0.7814 T12: 0.0594 REMARK 3 T13: 0.0002 T23: -0.1927 REMARK 3 L TENSOR REMARK 3 L11: 0.7386 L22: 2.2961 REMARK 3 L33: 3.6956 L12: -0.1799 REMARK 3 L13: 0.2806 L23: 0.3064 REMARK 3 S TENSOR REMARK 3 S11: -0.1131 S12: -0.1154 S13: -0.0342 REMARK 3 S21: -0.1018 S22: -0.1097 S23: -0.0400 REMARK 3 S31: -0.2559 S32: -0.2015 S33: 0.2228 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : CC 146 CC 219 REMARK 3 ORIGIN FOR THE GROUP (A): 62.2030 105.9532 65.3111 REMARK 3 T TENSOR REMARK 3 T11: 0.8365 T22: 0.9034 REMARK 3 T33: 0.7206 T12: 0.0304 REMARK 3 T13: -0.1556 T23: -0.2883 REMARK 3 L TENSOR REMARK 3 L11: 4.6239 L22: 2.9046 REMARK 3 L33: 2.1049 L12: 1.5236 REMARK 3 L13: 2.9599 L23: 1.3521 REMARK 3 S TENSOR REMARK 3 S11: -0.1291 S12: -0.1379 S13: -0.0106 REMARK 3 S21: 0.0602 S22: -0.1504 S23: 0.2852 REMARK 3 S31: -0.2236 S32: 0.0160 S33: 0.2796 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 1 FF 112 REMARK 3 ORIGIN FOR THE GROUP (A): 83.1609 122.4489 68.8116 REMARK 3 T TENSOR REMARK 3 T11: 1.1008 T22: 0.7812 REMARK 3 T33: 0.5447 T12: -0.3990 REMARK 3 T13: -0.3393 T23: -0.1821 REMARK 3 L TENSOR REMARK 3 L11: 3.9545 L22: 3.9301 REMARK 3 L33: 4.6786 L12: -0.0358 REMARK 3 L13: -1.6229 L23: -1.7157 REMARK 3 S TENSOR REMARK 3 S11: 0.4710 S12: -0.2270 S13: 0.2698 REMARK 3 S21: -0.1320 S22: -0.2764 S23: 0.4698 REMARK 3 S31: -0.7578 S32: 0.7475 S33: -0.1945 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 1 EE 111 REMARK 3 ORIGIN FOR THE GROUP (A): 21.8870 111.2147 62.6929 REMARK 3 T TENSOR REMARK 3 T11: 0.8612 T22: 0.9588 REMARK 3 T33: 0.6070 T12: 0.4630 REMARK 3 T13: 0.2873 T23: -0.1665 REMARK 3 L TENSOR REMARK 3 L11: 0.3638 L22: 7.9137 REMARK 3 L33: 1.5775 L12: -1.1898 REMARK 3 L13: 0.6918 L23: -2.1785 REMARK 3 S TENSOR REMARK 3 S11: -0.1173 S12: -0.0421 S13: -0.0116 REMARK 3 S21: 0.0230 S22: 0.4348 S23: 0.5758 REMARK 3 S31: -0.6496 S32: -0.1686 S33: -0.3175 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : DD 2 DD 112 REMARK 3 ORIGIN FOR THE GROUP (A): 6.8473 54.6685 64.7761 REMARK 3 T TENSOR REMARK 3 T11: 0.0837 T22: 1.0360 REMARK 3 T33: 1.9492 T12: 0.0267 REMARK 3 T13: 0.3711 T23: -0.2812 REMARK 3 L TENSOR REMARK 3 L11: 1.5557 L22: 0.9418 REMARK 3 L33: 3.8958 L12: 1.1853 REMARK 3 L13: 1.7414 L23: 1.1018 REMARK 3 S TENSOR REMARK 3 S11: 0.2134 S12: -0.6812 S13: 1.0244 REMARK 3 S21: 0.1959 S22: -0.4498 S23: 0.9800 REMARK 3 S31: 0.0020 S32: -0.6666 S33: 0.2364 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : GG 1 GG 165 REMARK 3 ORIGIN FOR THE GROUP (A): 70.8979 16.9916 16.6553 REMARK 3 T TENSOR REMARK 3 T11: 1.4895 T22: 0.5170 REMARK 3 T33: 0.6603 T12: 0.4144 REMARK 3 T13: 0.2596 T23: 0.1382 REMARK 3 L TENSOR REMARK 3 L11: 0.4065 L22: 0.4532 REMARK 3 L33: 6.5672 L12: 0.0682 REMARK 3 L13: -1.4085 L23: -0.3223 REMARK 3 S TENSOR REMARK 3 S11: -0.5694 S12: -0.2050 S13: 0.0631 REMARK 3 S21: 0.1221 S22: 0.1730 S23: 0.2610 REMARK 3 S31: 1.5978 S32: 0.8416 S33: 0.3964 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : HH 3 HH 165 REMARK 3 ORIGIN FOR THE GROUP (A): 23.3661 36.7977 16.4156 REMARK 3 T TENSOR REMARK 3 T11: 1.1923 T22: 1.1464 REMARK 3 T33: 0.3455 T12: -0.7679 REMARK 3 T13: 0.1468 T23: -0.2017 REMARK 3 L TENSOR REMARK 3 L11: 1.0471 L22: 0.7541 REMARK 3 L33: 7.7742 L12: -0.6267 REMARK 3 L13: 0.1381 L23: 1.2489 REMARK 3 S TENSOR REMARK 3 S11: -0.0611 S12: -0.2382 S13: 0.5632 REMARK 3 S21: 0.2240 S22: -0.2180 S23: -0.3258 REMARK 3 S31: 2.0937 S32: -1.5630 S33: 0.2790 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : II 1 II 165 REMARK 3 ORIGIN FOR THE GROUP (A): 15.6758 89.0308 16.6355 REMARK 3 T TENSOR REMARK 3 T11: 0.4196 T22: 1.9671 REMARK 3 T33: 0.3009 T12: 0.4145 REMARK 3 T13: -0.1486 T23: -0.2302 REMARK 3 L TENSOR REMARK 3 L11: 0.5410 L22: 2.4411 REMARK 3 L33: 7.1270 L12: 1.0530 REMARK 3 L13: -0.8460 L23: -0.5910 REMARK 3 S TENSOR REMARK 3 S11: -0.0211 S12: -0.0141 S13: -0.1553 REMARK 3 S21: 0.1261 S22: -0.1566 S23: -0.5305 REMARK 3 S31: -0.2159 S32: -1.9763 S33: 0.1777 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 NOT BEEN USED REMARK 4 REMARK 4 7N9X 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_1000257606. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-OCT-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0711 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 : DENZO REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33153 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 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 (%) : 95.9 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.18200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 1.17900 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: PDB ENTRIES 5O2U & 3H47 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS PROPANE, PH 6.8, 15% REMARK 280 PEG3350, 200 MM SODIUM, MICROBATCH, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 63.97500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.92500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 156.91600 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 63.97500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.92500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 156.91600 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 63.97500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 68.92500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 156.91600 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 63.97500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 68.92500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 156.91600 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: BBB, CCC, AAA, FFF, EEE, DDD, REMARK 350 AND CHAINS: GGG, HHH, III 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 APPLY THE FOLLOWING TO CHAINS: BBB, CCC, AAA, FFF, EEE, DDD, REMARK 350 AND CHAINS: GGG, HHH, III REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 127.95000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 137.85000 REMARK 350 BIOMT3 2 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 B 220 REMARK 465 VAL B 221 REMARK 465 GLY B 222 REMARK 465 GLY A 220 REMARK 465 VAL A 221 REMARK 465 GLY A 222 REMARK 465 UNK F 99 REMARK 465 UNK F 100 REMARK 465 UNK D 99 REMARK 465 UNK D 100 REMARK 465 MET H 1 REMARK 465 VAL H 2 REMARK 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY. REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 GLY H 80 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLU H 81 N CA C O REMARK 480 LYS H 155 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LYSBB 182 OG1 THRBB 186 2.05 REMARK 500 O GLYAA 208 NH2 ARGDD 50 2.18 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 GLUDD 75 CA - CB - CG ANGL. DEV. = 13.8 DEGREES REMARK 500 ARGGG 144 CB - CG - CD ANGL. DEV. = -25.1 DEGREES REMARK 500 PHEII 83 C - N - CA ANGL. DEV. = -17.4 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 ALABB 31 -123.07 51.58 REMARK 500 ALABB 177 165.87 53.82 REMARK 500 GLUBB 187 -3.68 -54.62 REMARK 500 THRBB 188 -74.21 -119.18 REMARK 500 ASNCC 5 -178.50 62.35 REMARK 500 ALACC 31 -123.19 51.90 REMARK 500 GLNCC 176 -66.31 55.21 REMARK 500 ALACC 177 -120.20 53.98 REMARK 500 GLUCC 187 -5.37 -52.44 REMARK 500 THRCC 188 -79.18 -121.41 REMARK 500 ALAAA 31 -122.75 51.96 REMARK 500 GLNAA 176 17.80 53.77 REMARK 500 SERAA 178 -130.87 66.23 REMARK 500 GLUAA 180 -163.21 -129.11 REMARK 500 ASNAA 183 -41.32 -133.08 REMARK 500 GLUAA 187 -5.25 -57.38 REMARK 500 THRAA 188 -77.19 -121.39 REMARK 500 ASPEE 97 -73.46 49.71 REMARK 500 ASPDD 97 74.73 -24.41 REMARK 500 LEUGG 17 -54.50 -121.41 REMARK 500 PHEGG 60 -79.25 -128.54 REMARK 500 GLUGG 81 -99.32 59.63 REMARK 500 PHEHH 60 -79.97 -129.06 REMARK 500 TYRHH 79 77.12 -104.62 REMARK 500 GLUHH 81 -42.19 -133.58 REMARK 500 LEUHH 164 110.17 -16.64 REMARK 500 PHEII 60 -79.10 -128.56 REMARK 500 THRII 73 -88.17 -67.30 REMARK 500 GLUII 81 -140.34 56.47 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 PHEII 46 -14.41 REMARK 500 REMARK 500 REMARK: NULL DBREF 7N9XBB 1 222 UNP B6DRA0 B6DRA0_9HIV1 133 354 DBREF 7N9XCC 1 222 UNP B6DRA0 B6DRA0_9HIV1 133 354 DBREF 7N9XAA 1 222 UNP B6DRA0 B6DRA0_9HIV1 133 354 DBREF 7N9XFF 1 112 PDB 7N9X 7N9X 1 112 DBREF 7N9XEE 1 111 PDB 7N9X 7N9X 1 111 DBREF 7N9XDD 2 112 PDB 7N9X 7N9X 2 112 DBREF 7N9XGG 1 165 UNP P62937 PPIA_HUMAN 1 165 DBREF 7N9XHH 1 165 UNP P62937 PPIA_HUMAN 1 165 DBREF 7N9XII 1 165 UNP P62937 PPIA_HUMAN 1 165 SEQADV 7N9X CYSBB 14 UNP B6DRA0 ALA 146 CONFLICT SEQADV 7N9X CYSBB 45 UNP B6DRA0 GLU 177 CONFLICT SEQADV 7N9X ALABB 184 UNP B6DRA0 TRP 316 CONFLICT SEQADV 7N9X ALABB 185 UNP B6DRA0 MET 317 CONFLICT SEQADV 7N9X CYSCC 14 UNP B6DRA0 ALA 146 CONFLICT SEQADV 7N9X CYSCC 45 UNP B6DRA0 GLU 177 CONFLICT SEQADV 7N9X ALACC 184 UNP B6DRA0 TRP 316 CONFLICT SEQADV 7N9X ALACC 185 UNP B6DRA0 MET 317 CONFLICT SEQADV 7N9X CYSAA 14 UNP B6DRA0 ALA 146 CONFLICT SEQADV 7N9X CYSAA 45 UNP B6DRA0 GLU 177 CONFLICT SEQADV 7N9X ALAAA 184 UNP B6DRA0 TRP 316 CONFLICT SEQADV 7N9X ALAAA 185 UNP B6DRA0 MET 317 CONFLICT SEQRES 1BB 222 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN SEQRES 2BB 222 CYS ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL SEQRES 3BB 222 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET SEQRES 4BB 222 PHE SER ALA LEU SER CYS GLY ALA THR PRO GLN ASP LEU SEQRES 5BB 222 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA SEQRES 6BB 222 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA SEQRES 7BB 222 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE SEQRES 8BB 222 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE SEQRES 9BB 222 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP SEQRES 10BB 222 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR SEQRES 11BB 222 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG SEQRES 12BB 222 MET TYR SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY SEQRES 13BB 222 PRO LYS GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR SEQRES 14BB 222 LYS THR LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS SEQRES 15BB 222 ASN ALA ALA THR GLU THR LEU LEU VAL GLN ASN ALA ASN SEQRES 16BB 222 PRO ASP CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY SEQRES 17BB 222 ALA THR LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL SEQRES 18BB 222 GLY SEQRES 1CC 222 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN SEQRES 2CC 222 CYS ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL SEQRES 3CC 222 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET SEQRES 4CC 222 PHE SER ALA LEU SER CYS GLY ALA THR PRO GLN ASP LEU SEQRES 5CC 222 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA SEQRES 6CC 222 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA SEQRES 7CC 222 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE SEQRES 8CC 222 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE SEQRES 9CC 222 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP SEQRES 10CC 222 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR SEQRES 11CC 222 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG SEQRES 12CC 222 MET TYR SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY SEQRES 13CC 222 PRO LYS GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR SEQRES 14CC 222 LYS THR LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS SEQRES 15CC 222 ASN ALA ALA THR GLU THR LEU LEU VAL GLN ASN ALA ASN SEQRES 16CC 222 PRO ASP CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY SEQRES 17CC 222 ALA THR LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL SEQRES 18CC 222 GLY SEQRES 1AA 222 PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN SEQRES 2AA 222 CYS ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL SEQRES 3AA 222 VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET SEQRES 4AA 222 PHE SER ALA LEU SER CYS GLY ALA THR PRO GLN ASP LEU SEQRES 5AA 222 ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA SEQRES 6AA 222 MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA SEQRES 7AA 222 GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE SEQRES 8AA 222 ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE SEQRES 9AA 222 ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP SEQRES 10AA 222 MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR SEQRES 11AA 222 LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG SEQRES 12AA 222 MET TYR SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY SEQRES 13AA 222 PRO LYS GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR SEQRES 14AA 222 LYS THR LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS SEQRES 15AA 222 ASN ALA ALA THR GLU THR LEU LEU VAL GLN ASN ALA ASN SEQRES 16AA 222 PRO ASP CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY SEQRES 17AA 222 ALA THR LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL SEQRES 18AA 222 GLY SEQRES 1FF 115 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2FF 115 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3FF 115 SER ILE SER ARG PHE ASN ALA MET GLY TRP TRP ARG GLN SEQRES 4FF 115 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ARG ILE VAL SEQRES 5FF 115 LYS GLY PHE ASP PRO VAL LEU ALA ASP SER VAL LYS GLY SEQRES 6FF 115 ARG PHE THR ILE SER ILE ASP SER ALA GLU ASN THR LEU SEQRES 7FF 115 ALA LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA SEQRES 8FF 115 VAL TYR TYR CYS PHE ALA ALA LEU ASP THR UNK UNK ALA SEQRES 9FF 115 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 1EE 112 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2EE 112 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3EE 112 SER ILE SER ARG PHE ASN ALA MET GLY TRP TRP ARG GLN SEQRES 4EE 112 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ARG ILE VAL SEQRES 5EE 112 LYS GLY PHE ASP PRO VAL LEU ALA ASP SER VAL LYS GLY SEQRES 6EE 112 ARG PHE THR ILE SER ILE ASP SER ALA GLU ASN THR LEU SEQRES 7EE 112 ALA LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR ALA SEQRES 8EE 112 VAL TYR TYR CYS PHE ALA ALA LEU ASP THR ALA TYR TRP SEQRES 9EE 112 GLY GLN GLY THR GLN VAL THR VAL SEQRES 1DD 114 VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN ALA SEQRES 2DD 114 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SER SEQRES 3DD 114 ILE SER ARG PHE ASN ALA MET GLY TRP TRP ARG GLN ALA SEQRES 4DD 114 PRO GLY LYS GLU ARG GLU PHE VAL ALA ARG ILE VAL LYS SEQRES 5DD 114 GLY PHE ASP PRO VAL LEU ALA ASP SER VAL LYS GLY ARG SEQRES 6DD 114 PHE THR ILE SER ILE ASP SER ALA GLU ASN THR LEU ALA SEQRES 7DD 114 LEU GLN ARG ASN ARG LEU LYS PRO GLU ASP THR ALA VAL SEQRES 8DD 114 TYR TYR CYS PHE ALA ALA LEU ASP THR UNK UNK ALA TYR SEQRES 9DD 114 TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 1GG 165 MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP SEQRES 2GG 165 GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA SEQRES 3GG 165 ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SEQRES 4GG 165 SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS SEQRES 5GG 165 PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY SEQRES 6GG 165 ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE SEQRES 7GG 165 TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS SEQRES 8GG 165 HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY SEQRES 9GG 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA SEQRES 10GG 165 LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY SEQRES 11GG 165 LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU SEQRES 12GG 165 ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE SEQRES 13GG 165 THR ILE ALA ASP CYS GLY GLN LEU GLU SEQRES 1HH 165 MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP SEQRES 2HH 165 GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA SEQRES 3HH 165 ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SEQRES 4HH 165 SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS SEQRES 5HH 165 PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY SEQRES 6HH 165 ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE SEQRES 7HH 165 TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS SEQRES 8HH 165 HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY SEQRES 9HH 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA SEQRES 10HH 165 LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY SEQRES 11HH 165 LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU SEQRES 12HH 165 ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE SEQRES 13HH 165 THR ILE ALA ASP CYS GLY GLN LEU GLU SEQRES 1II 165 MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP SEQRES 2II 165 GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA SEQRES 3II 165 ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SEQRES 4II 165 SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS SEQRES 5II 165 PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY SEQRES 6II 165 ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE SEQRES 7II 165 TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS SEQRES 8II 165 HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY SEQRES 9II 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA SEQRES 10II 165 LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY SEQRES 11II 165 LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU SEQRES 12II 165 ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE SEQRES 13II 165 THR ILE ALA ASP CYS GLY GLN LEU GLU HELIX 1 AA1 SERBB 16 ALABB 31 1 16 HELIX 2 AA2 GLUBB 35 SERBB 44 1 10 HELIX 3 AA3 THRBB 48 THRBB 58 1 11 HELIX 4 AA4 HISBB 62 HISBB 84 1 23 HELIX 5 AA5 ARGBB 100 ALABB 105 1 6 HELIX 6 AA6 THRBB 110 THRBB 119 1 10 HELIX 7 AA7 PROBB 125 TYRBB 145 1 21 HELIX 8 AA8 SERBB 149 ILEBB 153 5 5 HELIX 9 AA9 PROBB 160 GLUBB 175 1 16 HELIX 10 AB1 GLUBB 180 ALABB 185 1 6 HELIX 11 AB2 ALABB 185 ASNBB 193 1 9 HELIX 12 AB3 ASNBB 195 GLYBB 206 1 12 HELIX 13 AB4 THRBB 210 CYSBB 218 1 9 HELIX 14 AB5 SERCC 16 ALACC 31 1 16 HELIX 15 AB6 GLUCC 35 SERCC 44 1 10 HELIX 16 AB7 THRCC 48 THRCC 58 1 11 HELIX 17 AB8 HISCC 62 HISCC 84 1 23 HELIX 18 AB9 ARGCC 100 ALACC 105 1 6 HELIX 19 AC1 THRCC 110 THRCC 119 1 10 HELIX 20 AC2 PROCC 125 TYRCC 145 1 21 HELIX 21 AC3 SERCC 149 ILECC 153 5 5 HELIX 22 AC4 PROCC 160 GLNCC 176 1 17 HELIX 23 AC5 SERCC 178 ASNCC 193 1 16 HELIX 24 AC6 ASNCC 195 GLYCC 206 1 12 HELIX 25 AC7 THRCC 210 CYSCC 218 1 9 HELIX 26 AC8 SERAA 16 ALAAA 31 1 16 HELIX 27 AC9 GLUAA 35 SERAA 44 1 10 HELIX 28 AD1 THRAA 48 THRAA 58 1 11 HELIX 29 AD2 HISAA 62 HISAA 84 1 23 HELIX 30 AD3 ARGAA 100 ALAAA 105 1 6 HELIX 31 AD4 THRAA 110 THRAA 119 1 10 HELIX 32 AD5 PROAA 125 TYRAA 145 1 21 HELIX 33 AD6 SERAA 149 ILEAA 153 5 5 HELIX 34 AD7 PROAA 160 GLUAA 175 1 16 HELIX 35 AD8 GLNAA 176 SERAA 178 5 3 HELIX 36 AD9 ALAAA 185 ASNAA 193 1 9 HELIX 37 AE1 ASNAA 195 LEUAA 205 1 11 HELIX 38 AE2 THRAA 210 CYSAA 218 1 9 HELIX 39 AE3 SERFF 27 PHEFF 31 5 5 HELIX 40 AE4 LYSFF 83 THRFF 87 5 5 HELIX 41 AE5 SEREE 27 PHEEE 31 5 5 HELIX 42 AE6 ALAEE 60 GLYEE 65 1 6 HELIX 43 AE7 LYSEE 83 THREE 87 5 5 HELIX 44 AE8 SERDD 27 PHEDD 31 5 5 HELIX 45 AE9 LYSDD 83 THRDD 87 5 5 HELIX 46 AF1 VALGG 29 GLYGG 42 1 14 HELIX 47 AF2 THRGG 119 ASPGG 123 5 5 HELIX 48 AF3 GLYGG 135 ARGGG 144 1 10 HELIX 49 AF4 VALHH 29 GLYHH 42 1 14 HELIX 50 AF5 THRHH 119 ASPHH 123 5 5 HELIX 51 AF6 GLYHH 135 ARGHH 144 1 10 HELIX 52 AF7 VALII 29 GLYII 42 1 14 HELIX 53 AF8 THRII 119 ASPII 123 5 5 HELIX 54 AF9 GLYII 135 ARGII 144 1 10 SHEET 1 AA1 2 ILEBB 2 GLNBB 4 0 SHEET 2 AA1 2 METBB 10 HISBB 12 -1 O VALBB 11 N VALBB 3 SHEET 1 AA2 2 ILECC 2 VALCC 3 0 SHEET 2 AA2 2 VALCC 11 HISCC 12 -1 O VALCC 11 N VALCC 3 SHEET 1 AA3 2 ILEAA 2 GLNAA 4 0 SHEET 2 AA3 2 METAA 10 HISAA 12 -1 O VALAA 11 N VALAA 3 SHEET 1 AA4 4 LEUFF 4 SERFF 7 0 SHEET 2 AA4 4 LEUFF 18 ALAFF 24 -1 O SERFF 21 N SERFF 7 SHEET 3 AA4 4 THRFF 77 METFF 82 -1 O METFF 82 N LEUFF 18 SHEET 4 AA4 4 PHEFF 67 ASPFF 72 -1 N SERFF 70 O ALAFF 79 SHEET 1 AA5 6 LEUFF 11 GLNFF 13 0 SHEET 2 AA5 6 THRFF 107 SERFF 112 1 O THRFF 110 N VALFF 12 SHEET 3 AA5 6 ALAFF 88 ALAFF 95 -1 N ALAFF 88 O VALFF 109 SHEET 4 AA5 6 ALAFF 33 GLNFF 39 -1 N TRPFF 37 O TYRFF 91 SHEET 5 AA5 6 GLUFF 46 VALFF 52 -1 O ILEFF 51 N METFF 34 SHEET 6 AA5 6 VALFF 58 LEUFF 59 -1 O VALFF 58 N ARGFF 50 SHEET 1 AA6 4 LEUFF 11 GLNFF 13 0 SHEET 2 AA6 4 THRFF 107 SERFF 112 1 O THRFF 110 N VALFF 12 SHEET 3 AA6 4 ALAFF 88 ALAFF 95 -1 N ALAFF 88 O VALFF 109 SHEET 4 AA6 4 TYRFF 102 TRPFF 103 -1 O TYRFF 102 N ALAFF 94 SHEET 1 AA7 4 LEUEE 4 SEREE 7 0 SHEET 2 AA7 4 SEREE 17 ALAEE 24 -1 O ALAEE 23 N GLNEE 5 SHEET 3 AA7 4 THREE 77 ASNEE 82A-1 O METEE 82 N LEUEE 18 SHEET 4 AA7 4 PHEEE 67 ASPEE 72 -1 N THREE 68 O GLNEE 81 SHEET 1 AA8 5 VALEE 58 LEUEE 59 0 SHEET 2 AA8 5 GLUEE 46 VALEE 52 -1 N ARGEE 50 O VALEE 58 SHEET 3 AA8 5 ALAEE 33 GLNEE 39 -1 N ARGEE 38 O GLUEE 46 SHEET 4 AA8 5 ALAEE 88 ALAEE 95 -1 O TYREE 91 N TRPEE 37 SHEET 5 AA8 5 ALAEE 101 TRPEE 103 -1 O TYREE 102 N ALAEE 94 SHEET 1 AA9 5 VALEE 58 LEUEE 59 0 SHEET 2 AA9 5 GLUEE 46 VALEE 52 -1 N ARGEE 50 O VALEE 58 SHEET 3 AA9 5 ALAEE 33 GLNEE 39 -1 N ARGEE 38 O GLUEE 46 SHEET 4 AA9 5 ALAEE 88 ALAEE 95 -1 O TYREE 91 N TRPEE 37 SHEET 5 AA9 5 THREE 107 VALEE 109 -1 O THREE 107 N TYREE 90 SHEET 1 AB1 2 LEUDD 4 GLNDD 5 0 SHEET 2 AB1 2 ALADD 23 ALADD 24 -1 O ALADD 23 N GLNDD 5 SHEET 1 AB2 6 LEUDD 11 VALDD 12 0 SHEET 2 AB2 6 THRDD 107 VALDD 111 1 O THRDD 110 N VALDD 12 SHEET 3 AB2 6 ALADD 88 ALADD 95 -1 N ALADD 88 O VALDD 109 SHEET 4 AB2 6 ALADD 33 GLNDD 39 -1 N ALADD 33 O ALADD 95 SHEET 5 AB2 6 GLUDD 46 VALDD 52 -1 O VALDD 48 N TRPDD 36 SHEET 6 AB2 6 VALDD 58 LEUDD 59 -1 O VALDD 58 N ARGDD 50 SHEET 1 AB3 4 LEUDD 11 VALDD 12 0 SHEET 2 AB3 4 THRDD 107 VALDD 111 1 O THRDD 110 N VALDD 12 SHEET 3 AB3 4 ALADD 88 ALADD 95 -1 N ALADD 88 O VALDD 109 SHEET 4 AB3 4 TYRDD 102 TRPDD 103 -1 O TYRDD 102 N ALADD 94 SHEET 1 AB4 3 LEUDD 18 LEUDD 20 0 SHEET 2 AB4 3 THRDD 77 ARGDD 82 -1 O ARGDD 82 N LEUDD 18 SHEET 3 AB4 3 THRDD 68 ASPDD 72 -1 N THRDD 68 O GLNDD 81 SHEET 1 AB5 8 PHEGG 53 ILEGG 57 0 SHEET 2 AB5 8 METGG 61 GLYGG 64 -1 O GLNGG 63 N ARGGG 55 SHEET 3 AB5 8 ASNGG 108 CYSGG 115 -1 O ILEGG 114 N CYSGG 62 SHEET 4 AB5 8 ILEGG 97 ASNGG 102 -1 N SERGG 99 O PHEGG 113 SHEET 5 AB5 8 VALGG 128 VALGG 132 -1 O GLYGG 130 N LEUGG 98 SHEET 6 AB5 8 GLUGG 15 LEUGG 24 -1 N GLUGG 23 O LYSGG 131 SHEET 7 AB5 8 THRGG 5 VALGG 12 -1 N VALGG 6 O PHEGG 22 SHEET 8 AB5 8 ILEGG 156 LEUGG 164 -1 O ASPGG 160 N ASPGG 9 SHEET 1 AB6 8 PHEHH 53 ILEHH 57 0 SHEET 2 AB6 8 METHH 61 GLYHH 64 -1 O GLNHH 63 N ARGHH 55 SHEET 3 AB6 8 ASNHH 108 CYSHH 115 -1 O ILEHH 114 N CYSHH 62 SHEET 4 AB6 8 ILEHH 97 ASNHH 102 -1 N ALAHH 101 O GLNHH 111 SHEET 5 AB6 8 VALHH 128 GLUHH 134 -1 O GLYHH 130 N LEUHH 98 SHEET 6 AB6 8 GLUHH 15 LEUHH 24 -1 N SERHH 21 O LYSHH 133 SHEET 7 AB6 8 THRHH 5 VALHH 12 -1 N VALHH 6 O PHEHH 22 SHEET 8 AB6 8 ILEHH 156 GLNHH 163 -1 O THRHH 157 N ALAHH 11 SHEET 1 AB7 8 PHEII 53 ILEII 57 0 SHEET 2 AB7 8 METII 61 GLYII 64 -1 O GLNII 63 N ARGII 55 SHEET 3 AB7 8 ASNII 108 CYSII 115 -1 O ILEII 114 N CYSII 62 SHEET 4 AB7 8 ILEII 97 ASNII 102 -1 N ALAII 101 O GLNII 111 SHEET 5 AB7 8 VALII 128 GLUII 134 -1 O GLYII 130 N LEUII 98 SHEET 6 AB7 8 GLUII 15 LEUII 24 -1 N GLUII 23 O LYSII 131 SHEET 7 AB7 8 THRII 5 VALII 12 -1 N PHEII 8 O VALII 20 SHEET 8 AB7 8 ILEII 156 LEUII 164 -1 O THRII 157 N ALAII 11 SSBOND 1 CYSBB 14 CYSAA 45 1555 1555 2.05 SSBOND 2 CYSBB 45 CYSCC 14 1555 1555 2.04 SSBOND 3 CYSFF 22 CYSFF 92 1555 1555 2.04 SSBOND 4 CYSEE 22 CYSEE 92 1555 1555 2.03 SSBOND 5 CYSDD 22 CYSDD 92 1555 1555 2.02 CISPEP 1 ASNBB 121 PROBB 122 0 1.80 CISPEP 2 ASNCC 121 PROCC 122 0 1.51 CISPEP 3 ASNAA 121 PROAA 122 0 1.83 CRYST1 127.950 137.850 313.832 90.00 90.00 90.00 I 2 2 2 24 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 0.007816 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007254 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003186 0.00000