HEADER ANTIVIRAL PROTEIN 20-APR-21 7OAY TITLE NANOBODY F2 BOUND TO RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: AAA, CCC, EEE, GGG, III, KKK; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: F2 NANOBODY; COMPND 7 CHAIN: BBB, DDD, FFF, HHH, JJJ, LLL; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 12 ORGANISM_COMMON: LLAMA; SOURCE 13 ORGANISM_TAXID: 9844; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SPIKE, NANOBODY, HIGH AFFINITY, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.H.NAISMITH,H.MIKOLAJEK JRNL AUTH J.HUO,H.MIKOLAJEK,A.LE BAS,J.CLARK,P.SHARMA,A.KIPAR, JRNL AUTH 2 J.DORMON,C.NORMAN,M.WECKENER,D.CLARE,P.HARRISON,J.TREE, JRNL AUTH 3 K.BUTTIGIEG,F.SALGUERO,R.WATSON,D.KNOTT,O.CARNELL,D.NGABO, JRNL AUTH 4 M.ELMORE,S.FOTHERINGHAM,A.HARDING,P.WARD,L.MOYNIE,M.DUMOUX, JRNL AUTH 5 Y.HALL,J.HISCOX,A.OWEN,W.JAMES,M.CARROLL,J.STEWART, JRNL AUTH 6 J.NAISMITH,R.OWENS JRNL TITL A POTENT SARS-COV-2 NEUTRALISING NANOBODY SHOWS THERAPEUTIC JRNL TITL 2 EFFICACY IN THE SYRIAN GOLDEN HAMSTER MODEL OF COVID-19 JRNL REF RES SQ 2021 JRNL REFN ISSN 2693-5015 JRNL DOI 10.21203/RS.3.RS-548968/V1 REMARK 2 REMARK 2 RESOLUTION. 2.34 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) : 2.34 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 93.90 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 91817 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) : 0.192 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.057 REMARK 3 FREE R VALUE TEST SET COUNT : 4643 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) : 2.34 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6473 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3350 REMARK 3 BIN FREE R VALUE SET COUNT : 304 REMARK 3 BIN FREE R VALUE : 0.2990 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 15292 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 84 REMARK 3 SOLVENT ATOMS : 323 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.18 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.02400 REMARK 3 B22 (A**2) : 0.02400 REMARK 3 B33 (A**2) : -0.07700 REMARK 3 B12 (A**2) : 0.01200 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): 0.367 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.230 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.742 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15826 ; 0.009 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 14182 ; 0.001 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21530 ; 1.611 ; 1.660 REMARK 3 BOND ANGLES OTHERS (DEGREES): 32532 ; 1.287 ; 1.583 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1921 ; 7.729 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 879 ;32.378 ;21.604 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2358 ;15.259 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;18.137 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1986 ; 0.069 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18331 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 4154 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2459 ; 0.194 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 149 ; 0.257 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7669 ; 0.174 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 446 ; 0.137 ; 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): 7720 ; 1.883 ; 3.470 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7719 ; 1.882 ; 3.469 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9629 ; 3.086 ; 5.194 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 9630 ; 3.086 ; 5.195 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8106 ; 2.103 ; 3.678 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8106 ; 2.103 ; 3.678 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11901 ; 3.385 ; 5.435 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 11902 ; 3.385 ; 5.436 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 : 30 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : AAA CCC REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 AA 331 AA 528 NULL REMARK 3 1 CC 331 CC 528 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : AAA EEE REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 2 AA 332 AA 527 NULL REMARK 3 2 EE 332 EE 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : AAA GGG REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 AA 333 AA 527 NULL REMARK 3 3 GG 333 GG 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : AAA III REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 4 AA 331 AA 528 NULL REMARK 3 4 II 331 II 528 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : AAA KKK REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 5 AA 332 AA 527 NULL REMARK 3 5 KK 332 KK 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : BBB DDD REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 6 BB 1 BB 125 NULL REMARK 3 6 DD 1 DD 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : BBB FFF REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 7 BB 1 BB 123 NULL REMARK 3 7 FF 1 FF 123 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 8 REMARK 3 CHAIN NAMES : BBB HHH REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 8 BB 1 BB 125 NULL REMARK 3 8 HH 1 HH 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 9 REMARK 3 CHAIN NAMES : BBB JJJ REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 9 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 9 BB 1 BB 125 NULL REMARK 3 9 JJ 1 JJ 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 10 REMARK 3 CHAIN NAMES : BBB LLL REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 10 BB 1 BB 125 NULL REMARK 3 10 LL 1 LL 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 11 REMARK 3 CHAIN NAMES : CCC EEE REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 11 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 11 CC 332 CC 527 NULL REMARK 3 11 EE 332 EE 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 12 REMARK 3 CHAIN NAMES : CCC GGG REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 12 CC 333 CC 527 NULL REMARK 3 12 GG 333 GG 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 13 REMARK 3 CHAIN NAMES : CCC III REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 13 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 13 CC 331 CC 528 NULL REMARK 3 13 II 331 II 528 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 14 REMARK 3 CHAIN NAMES : CCC KKK REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 14 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 14 CC 332 CC 527 NULL REMARK 3 14 KK 332 KK 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 15 REMARK 3 CHAIN NAMES : DDD FFF REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 15 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 15 DD 1 DD 123 NULL REMARK 3 15 FF 1 FF 123 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 16 REMARK 3 CHAIN NAMES : DDD HHH REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 16 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 16 DD 1 DD 125 NULL REMARK 3 16 HH 1 HH 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 17 REMARK 3 CHAIN NAMES : DDD JJJ REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 17 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 17 DD 1 DD 125 NULL REMARK 3 17 JJ 1 JJ 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 18 REMARK 3 CHAIN NAMES : DDD LLL REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 18 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 18 DD 1 DD 125 NULL REMARK 3 18 LL 1 LL 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 19 REMARK 3 CHAIN NAMES : EEE GGG REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 19 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 19 EE 333 EE 527 NULL REMARK 3 19 GG 333 GG 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 20 REMARK 3 CHAIN NAMES : EEE III REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 20 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 20 EE 332 EE 527 NULL REMARK 3 20 II 332 II 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 21 REMARK 3 CHAIN NAMES : EEE KKK REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 21 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 21 EE 332 EE 528 NULL REMARK 3 21 KK 332 KK 528 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 22 REMARK 3 CHAIN NAMES : FFF HHH REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 22 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 22 FF 1 FF 123 NULL REMARK 3 22 HH 1 HH 123 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 23 REMARK 3 CHAIN NAMES : FFF JJJ REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 23 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 23 FF 1 FF 123 NULL REMARK 3 23 JJ 1 JJ 123 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 24 REMARK 3 CHAIN NAMES : FFF LLL REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 24 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 24 FF 1 FF 123 NULL REMARK 3 24 LL 1 LL 123 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 25 REMARK 3 CHAIN NAMES : GGG III REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 25 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 25 GG 333 GG 527 NULL REMARK 3 25 II 333 II 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 26 REMARK 3 CHAIN NAMES : GGG KKK REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 26 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 26 GG 333 GG 527 NULL REMARK 3 26 KK 333 KK 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 27 REMARK 3 CHAIN NAMES : HHH JJJ REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 27 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 27 HH 1 HH 125 NULL REMARK 3 27 JJ 1 JJ 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 28 REMARK 3 CHAIN NAMES : HHH LLL REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 28 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 28 HH 1 HH 125 NULL REMARK 3 28 LL 1 LL 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 29 REMARK 3 CHAIN NAMES : III KKK REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 29 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 29 II 332 II 527 NULL REMARK 3 29 KK 332 KK 527 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 30 REMARK 3 CHAIN NAMES : JJJ LLL REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 30 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 30 JJ 1 JJ 125 NULL REMARK 3 30 LL 1 LL 125 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 47 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 347 AA 368 REMARK 3 ORIGIN FOR THE GROUP (A): 21.8030 -15.1950 -9.2980 REMARK 3 T TENSOR REMARK 3 T11: 0.1651 T22: 0.1117 REMARK 3 T33: 0.1131 T12: -0.0818 REMARK 3 T13: 0.0324 T23: 0.0106 REMARK 3 L TENSOR REMARK 3 L11: 5.7589 L22: 0.9922 REMARK 3 L33: 3.4005 L12: -0.1554 REMARK 3 L13: -2.6976 L23: -1.2862 REMARK 3 S TENSOR REMARK 3 S11: 0.0344 S12: 0.1764 S13: -0.2863 REMARK 3 S21: -0.2131 S22: -0.0128 S23: 0.0313 REMARK 3 S31: 0.1945 S32: -0.0766 S33: -0.0216 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 369 AA 378 REMARK 3 ORIGIN FOR THE GROUP (A): 30.6680 -6.4940 -0.8750 REMARK 3 T TENSOR REMARK 3 T11: 0.0776 T22: 0.1006 REMARK 3 T33: 0.0647 T12: -0.0693 REMARK 3 T13: 0.0005 T23: -0.0085 REMARK 3 L TENSOR REMARK 3 L11: 3.6486 L22: 8.8785 REMARK 3 L33: 7.3282 L12: 0.3751 REMARK 3 L13: -0.9404 L23: -0.9922 REMARK 3 S TENSOR REMARK 3 S11: 0.1420 S12: 0.1363 S13: 0.0495 REMARK 3 S21: -0.1399 S22: -0.0386 S23: -0.0549 REMARK 3 S31: -0.4119 S32: 0.3818 S33: -0.1035 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 : AA 379 AA 527 REMARK 3 ORIGIN FOR THE GROUP (A): 15.7470 -16.1660 2.2420 REMARK 3 T TENSOR REMARK 3 T11: 0.0980 T22: 0.1240 REMARK 3 T33: 0.0630 T12: -0.0806 REMARK 3 T13: -0.0119 T23: 0.0462 REMARK 3 L TENSOR REMARK 3 L11: 2.0616 L22: 2.1222 REMARK 3 L33: 2.6050 L12: -0.2789 REMARK 3 L13: 0.0418 L23: -0.3470 REMARK 3 S TENSOR REMARK 3 S11: 0.0781 S12: -0.1731 S13: -0.0886 REMARK 3 S21: 0.0410 S22: 0.1132 S23: 0.3048 REMARK 3 S31: 0.1194 S32: -0.4398 S33: -0.1914 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 1 BB 63 REMARK 3 ORIGIN FOR THE GROUP (A): 42.9120 -12.8840 16.6320 REMARK 3 T TENSOR REMARK 3 T11: 0.0412 T22: 0.2020 REMARK 3 T33: 0.1133 T12: -0.0298 REMARK 3 T13: -0.0108 T23: -0.0789 REMARK 3 L TENSOR REMARK 3 L11: 3.3467 L22: 3.7894 REMARK 3 L33: 4.4657 L12: 1.0603 REMARK 3 L13: -0.2312 L23: -0.0838 REMARK 3 S TENSOR REMARK 3 S11: 0.0057 S12: -0.1308 S13: 0.2497 REMARK 3 S21: 0.1707 S22: 0.0280 S23: -0.2634 REMARK 3 S31: -0.2259 S32: 0.6423 S33: -0.0337 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 : BB 64 BB 69 REMARK 3 ORIGIN FOR THE GROUP (A): 52.9840 -7.2530 11.3660 REMARK 3 T TENSOR REMARK 3 T11: 0.1460 T22: 0.3918 REMARK 3 T33: 0.3531 T12: -0.0665 REMARK 3 T13: 0.0478 T23: -0.0463 REMARK 3 L TENSOR REMARK 3 L11: 8.0822 L22: 8.8855 REMARK 3 L33: 2.2656 L12: 3.3806 REMARK 3 L13: -1.5438 L23: 3.1720 REMARK 3 S TENSOR REMARK 3 S11: 0.2690 S12: -0.0048 S13: 0.1870 REMARK 3 S21: -0.6290 S22: -0.0860 S23: -0.3943 REMARK 3 S31: -0.4102 S32: -0.1029 S33: -0.1829 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 : BB 70 BB 104 REMARK 3 ORIGIN FOR THE GROUP (A): 45.6640 -12.8760 15.8850 REMARK 3 T TENSOR REMARK 3 T11: 0.0991 T22: 0.3143 REMARK 3 T33: 0.1665 T12: -0.0452 REMARK 3 T13: 0.0108 T23: -0.1095 REMARK 3 L TENSOR REMARK 3 L11: 1.8062 L22: 0.7345 REMARK 3 L33: 3.9140 L12: 0.0076 REMARK 3 L13: 0.3313 L23: -0.4613 REMARK 3 S TENSOR REMARK 3 S11: -0.0693 S12: -0.1789 S13: 0.2295 REMARK 3 S21: 0.0159 S22: 0.0729 S23: -0.2771 REMARK 3 S31: -0.1915 S32: 0.9282 S33: -0.0036 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 : BB 105 BB 124 REMARK 3 ORIGIN FOR THE GROUP (A): 38.2640 -7.8010 16.1760 REMARK 3 T TENSOR REMARK 3 T11: 0.0818 T22: 0.1315 REMARK 3 T33: 0.2638 T12: -0.0264 REMARK 3 T13: -0.0254 T23: -0.1588 REMARK 3 L TENSOR REMARK 3 L11: 1.8929 L22: 1.5187 REMARK 3 L33: 5.8035 L12: 1.2864 REMARK 3 L13: 0.5004 L23: -0.1138 REMARK 3 S TENSOR REMARK 3 S11: 0.1229 S12: -0.1212 S13: 0.2508 REMARK 3 S21: 0.2188 S22: 0.0933 S23: -0.1692 REMARK 3 S31: -0.3532 S32: 0.3552 S33: -0.2162 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 : CC 333 CC 346 REMARK 3 ORIGIN FOR THE GROUP (A): 20.4820 -68.0230 -11.6610 REMARK 3 T TENSOR REMARK 3 T11: 0.3285 T22: 0.2216 REMARK 3 T33: 0.1568 T12: 0.0678 REMARK 3 T13: -0.1027 T23: 0.0142 REMARK 3 L TENSOR REMARK 3 L11: 7.0600 L22: 3.8960 REMARK 3 L33: 14.7008 L12: 0.4973 REMARK 3 L13: -9.0441 L23: 2.4990 REMARK 3 S TENSOR REMARK 3 S11: 0.0674 S12: 0.6669 S13: -0.0765 REMARK 3 S21: -0.4098 S22: -0.4585 S23: 0.2791 REMARK 3 S31: -0.0948 S32: -1.2139 S33: 0.3911 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 : CC 347 CC 368 REMARK 3 ORIGIN FOR THE GROUP (A): 19.2250 -73.4970 -6.7660 REMARK 3 T TENSOR REMARK 3 T11: 0.1898 T22: 0.1762 REMARK 3 T33: 0.1009 T12: 0.0055 REMARK 3 T13: -0.0626 T23: 0.0194 REMARK 3 L TENSOR REMARK 3 L11: 5.2979 L22: 1.3973 REMARK 3 L33: 4.5975 L12: -1.4989 REMARK 3 L13: -4.1784 L23: 0.3555 REMARK 3 S TENSOR REMARK 3 S11: 0.1882 S12: 0.1895 S13: -0.0829 REMARK 3 S21: -0.3571 S22: -0.2920 S23: 0.0240 REMARK 3 S31: 0.0922 S32: -0.0847 S33: 0.1037 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 : CC 369 CC 378 REMARK 3 ORIGIN FOR THE GROUP (A): 29.5010 -65.9960 1.2370 REMARK 3 T TENSOR REMARK 3 T11: 0.1376 T22: 0.1859 REMARK 3 T33: 0.1781 T12: -0.0548 REMARK 3 T13: -0.0292 T23: -0.0238 REMARK 3 L TENSOR REMARK 3 L11: 5.1606 L22: 5.5037 REMARK 3 L33: 9.5154 L12: -1.3728 REMARK 3 L13: -2.1272 L23: 1.6197 REMARK 3 S TENSOR REMARK 3 S11: 0.4307 S12: 0.3789 S13: 0.1189 REMARK 3 S21: -0.3738 S22: -0.0351 S23: -0.4884 REMARK 3 S31: -0.5718 S32: 0.6382 S33: -0.3956 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 : CC 379 CC 527 REMARK 3 ORIGIN FOR THE GROUP (A): 13.9260 -73.9440 5.2360 REMARK 3 T TENSOR REMARK 3 T11: 0.1631 T22: 0.0747 REMARK 3 T33: 0.1014 T12: -0.0730 REMARK 3 T13: -0.0333 T23: -0.0126 REMARK 3 L TENSOR REMARK 3 L11: 2.1865 L22: 2.3963 REMARK 3 L33: 1.3969 L12: 0.4212 REMARK 3 L13: -0.2763 L23: -0.0386 REMARK 3 S TENSOR REMARK 3 S11: 0.1973 S12: -0.1646 S13: -0.0684 REMARK 3 S21: 0.3073 S22: -0.1995 S23: 0.3060 REMARK 3 S31: 0.0357 S32: -0.1693 S33: 0.0022 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 : DD 1 DD 23 REMARK 3 ORIGIN FOR THE GROUP (A): 46.7480 -75.8790 24.0150 REMARK 3 T TENSOR REMARK 3 T11: 0.1265 T22: 0.3665 REMARK 3 T33: 0.1812 T12: 0.0319 REMARK 3 T13: -0.1324 T23: -0.0644 REMARK 3 L TENSOR REMARK 3 L11: 1.7529 L22: 7.1595 REMARK 3 L33: 5.7888 L12: 3.4462 REMARK 3 L13: -1.1623 L23: -0.9015 REMARK 3 S TENSOR REMARK 3 S11: 0.0769 S12: -0.0267 S13: -0.0816 REMARK 3 S21: 0.1510 S22: 0.2235 S23: -0.2391 REMARK 3 S31: 0.0309 S32: 1.0226 S33: -0.3004 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : DD 24 DD 99 REMARK 3 ORIGIN FOR THE GROUP (A): 44.2160 -73.5800 15.2760 REMARK 3 T TENSOR REMARK 3 T11: 0.0729 T22: 0.2943 REMARK 3 T33: 0.1438 T12: -0.0307 REMARK 3 T13: -0.0478 T23: -0.0816 REMARK 3 L TENSOR REMARK 3 L11: 4.1130 L22: 3.5098 REMARK 3 L33: 5.2431 L12: 0.7146 REMARK 3 L13: 0.0661 L23: 0.0911 REMARK 3 S TENSOR REMARK 3 S11: 0.0648 S12: 0.0291 S13: 0.2691 REMARK 3 S21: -0.1049 S22: 0.1110 S23: -0.2249 REMARK 3 S31: -0.2460 S32: 0.8109 S33: -0.1758 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : DD 100 DD 106 REMARK 3 ORIGIN FOR THE GROUP (A): 33.5940 -72.3000 6.0430 REMARK 3 T TENSOR REMARK 3 T11: 0.0523 T22: 0.1571 REMARK 3 T33: 0.0664 T12: -0.0210 REMARK 3 T13: -0.0399 T23: -0.0381 REMARK 3 L TENSOR REMARK 3 L11: 9.0629 L22: 8.6961 REMARK 3 L33: 4.6529 L12: -1.8768 REMARK 3 L13: -0.7969 L23: -3.8267 REMARK 3 S TENSOR REMARK 3 S11: 0.2101 S12: 0.0042 S13: -0.1083 REMARK 3 S21: -0.2801 S22: -0.1529 S23: -0.0087 REMARK 3 S31: 0.0613 S32: 0.2466 S33: -0.0571 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : DD 107 DD 124 REMARK 3 ORIGIN FOR THE GROUP (A): 38.7410 -69.2180 19.4400 REMARK 3 T TENSOR REMARK 3 T11: 0.1469 T22: 0.1696 REMARK 3 T33: 0.3381 T12: -0.1004 REMARK 3 T13: 0.0730 T23: -0.1280 REMARK 3 L TENSOR REMARK 3 L11: 0.0990 L22: 1.9029 REMARK 3 L33: 5.1205 L12: 0.1582 REMARK 3 L13: -0.5545 L23: -0.0536 REMARK 3 S TENSOR REMARK 3 S11: 0.0808 S12: -0.0897 S13: 0.1074 REMARK 3 S21: 0.0176 S22: 0.1070 S23: 0.0616 REMARK 3 S31: -0.2529 S32: 0.5417 S33: -0.1878 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 333 EE 346 REMARK 3 ORIGIN FOR THE GROUP (A): 33.9190 -38.5870 13.1900 REMARK 3 T TENSOR REMARK 3 T11: 0.3447 T22: 0.2643 REMARK 3 T33: 0.1520 T12: -0.1048 REMARK 3 T13: -0.0020 T23: -0.0552 REMARK 3 L TENSOR REMARK 3 L11: 7.8389 L22: 2.6033 REMARK 3 L33: 6.8736 L12: 1.6539 REMARK 3 L13: -4.4028 L23: -0.6091 REMARK 3 S TENSOR REMARK 3 S11: 0.1589 S12: -1.2846 S13: 0.0454 REMARK 3 S21: 0.6930 S22: -0.3919 S23: 0.1180 REMARK 3 S31: 0.1095 S32: 0.4826 S33: 0.2329 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 347 EE 371 REMARK 3 ORIGIN FOR THE GROUP (A): 33.3530 -43.0990 8.2130 REMARK 3 T TENSOR REMARK 3 T11: 0.1726 T22: 0.0536 REMARK 3 T33: 0.1089 T12: 0.0085 REMARK 3 T13: 0.0071 T23: -0.0350 REMARK 3 L TENSOR REMARK 3 L11: 4.1449 L22: 1.3720 REMARK 3 L33: 1.8116 L12: 0.5582 REMARK 3 L13: -0.5813 L23: 0.3873 REMARK 3 S TENSOR REMARK 3 S11: 0.0551 S12: -0.2834 S13: -0.1046 REMARK 3 S21: 0.3548 S22: -0.0709 S23: 0.0830 REMARK 3 S31: -0.2117 S32: -0.0529 S33: 0.0158 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 372 EE 488 REMARK 3 ORIGIN FOR THE GROUP (A): 40.2790 -46.3720 -3.9480 REMARK 3 T TENSOR REMARK 3 T11: 0.1161 T22: 0.1131 REMARK 3 T33: 0.1157 T12: 0.0091 REMARK 3 T13: -0.0131 T23: -0.0519 REMARK 3 L TENSOR REMARK 3 L11: 4.2480 L22: 3.0188 REMARK 3 L33: 2.7012 L12: 0.2297 REMARK 3 L13: 0.0434 L23: -0.6177 REMARK 3 S TENSOR REMARK 3 S11: 0.0337 S12: 0.2520 S13: -0.3493 REMARK 3 S21: -0.1890 S22: -0.0765 S23: -0.3312 REMARK 3 S31: 0.0541 S32: 0.4267 S33: 0.0428 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : EE 489 EE 527 REMARK 3 ORIGIN FOR THE GROUP (A): 37.8700 -42.9850 -0.1720 REMARK 3 T TENSOR REMARK 3 T11: 0.1130 T22: 0.1811 REMARK 3 T33: 0.0619 T12: -0.0071 REMARK 3 T13: -0.0211 T23: -0.0808 REMARK 3 L TENSOR REMARK 3 L11: 1.9561 L22: 2.9891 REMARK 3 L33: 0.8666 L12: -0.5591 REMARK 3 L13: 0.8237 L23: 0.7018 REMARK 3 S TENSOR REMARK 3 S11: 0.0145 S12: -0.0167 S13: 0.0992 REMARK 3 S21: -0.1758 S22: 0.0374 S23: -0.1808 REMARK 3 S31: -0.0373 S32: 0.1384 S33: -0.0519 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 1 FF 24 REMARK 3 ORIGIN FOR THE GROUP (A): 8.3410 -44.4160 -23.0020 REMARK 3 T TENSOR REMARK 3 T11: 0.0912 T22: 0.1738 REMARK 3 T33: 0.1989 T12: 0.0179 REMARK 3 T13: -0.0968 T23: -0.0394 REMARK 3 L TENSOR REMARK 3 L11: 4.1014 L22: 7.3706 REMARK 3 L33: 3.4669 L12: -4.3987 REMARK 3 L13: -2.2206 L23: 1.3890 REMARK 3 S TENSOR REMARK 3 S11: 0.1117 S12: 0.0663 S13: 0.1168 REMARK 3 S21: -0.1137 S22: 0.0741 S23: 0.2134 REMARK 3 S31: -0.1464 S32: -0.2954 S33: -0.1858 REMARK 3 REMARK 3 TLS GROUP : 21 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 25 FF 32 REMARK 3 ORIGIN FOR THE GROUP (A): 19.9850 -56.2340 -14.3240 REMARK 3 T TENSOR REMARK 3 T11: 0.2107 T22: 0.2428 REMARK 3 T33: 0.2940 T12: -0.0556 REMARK 3 T13: 0.0957 T23: 0.0143 REMARK 3 L TENSOR REMARK 3 L11: 1.3442 L22: 2.2827 REMARK 3 L33: 14.7140 L12: -1.3557 REMARK 3 L13: 1.3484 L23: 2.1019 REMARK 3 S TENSOR REMARK 3 S11: -0.2235 S12: 0.4215 S13: -0.1059 REMARK 3 S21: 0.3404 S22: -0.3440 S23: 0.2369 REMARK 3 S31: 0.3958 S32: 0.8137 S33: 0.5676 REMARK 3 REMARK 3 TLS GROUP : 22 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 33 FF 103 REMARK 3 ORIGIN FOR THE GROUP (A): 10.0900 -40.6690 -13.8210 REMARK 3 T TENSOR REMARK 3 T11: 0.0828 T22: 0.1064 REMARK 3 T33: 0.1661 T12: 0.0760 REMARK 3 T13: 0.0108 T23: -0.0236 REMARK 3 L TENSOR REMARK 3 L11: 3.0871 L22: 2.3818 REMARK 3 L33: 2.7746 L12: -0.3992 REMARK 3 L13: 0.2631 L23: -0.5065 REMARK 3 S TENSOR REMARK 3 S11: -0.0013 S12: -0.0721 S13: 0.3716 REMARK 3 S21: 0.1261 S22: 0.0748 S23: 0.3055 REMARK 3 S31: -0.3190 S32: -0.4779 S33: -0.0735 REMARK 3 REMARK 3 TLS GROUP : 23 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : FF 104 FF 124 REMARK 3 ORIGIN FOR THE GROUP (A): 17.1300 -38.0740 -15.4640 REMARK 3 T TENSOR REMARK 3 T11: 0.0930 T22: 0.0851 REMARK 3 T33: 0.1451 T12: 0.0543 REMARK 3 T13: -0.0163 T23: 0.0538 REMARK 3 L TENSOR REMARK 3 L11: 1.3083 L22: 0.8225 REMARK 3 L33: 5.4284 L12: 0.3062 REMARK 3 L13: 1.0626 L23: 0.6118 REMARK 3 S TENSOR REMARK 3 S11: -0.1703 S12: -0.0141 S13: 0.0418 REMARK 3 S21: 0.0579 S22: 0.1915 S23: 0.2396 REMARK 3 S31: -0.2902 S32: -0.2739 S33: -0.0212 REMARK 3 REMARK 3 TLS GROUP : 24 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : GG 333 GG 346 REMARK 3 ORIGIN FOR THE GROUP (A): 14.4710 -14.9520 63.3700 REMARK 3 T TENSOR REMARK 3 T11: 0.1353 T22: 0.2611 REMARK 3 T33: 0.1477 T12: -0.0680 REMARK 3 T13: 0.0755 T23: 0.0355 REMARK 3 L TENSOR REMARK 3 L11: 9.8026 L22: 6.1018 REMARK 3 L33: 12.2269 L12: -2.2053 REMARK 3 L13: 7.3497 L23: -3.2923 REMARK 3 S TENSOR REMARK 3 S11: -0.2703 S12: -0.9420 S13: -0.0372 REMARK 3 S21: 0.5031 S22: 0.1636 S23: 0.1873 REMARK 3 S31: -0.3191 S32: -0.5578 S33: 0.1067 REMARK 3 REMARK 3 TLS GROUP : 25 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : GG 347 GG 373 REMARK 3 ORIGIN FOR THE GROUP (A): 18.4450 -12.7920 58.4340 REMARK 3 T TENSOR REMARK 3 T11: 0.1403 T22: 0.2035 REMARK 3 T33: 0.0878 T12: -0.0532 REMARK 3 T13: 0.0563 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 3.6258 L22: 2.6417 REMARK 3 L33: 4.4791 L12: -1.4686 REMARK 3 L13: 2.8644 L23: -3.2866 REMARK 3 S TENSOR REMARK 3 S11: 0.0399 S12: -0.4145 S13: -0.2123 REMARK 3 S21: -0.1464 S22: 0.0894 S23: 0.0504 REMARK 3 S31: 0.1920 S32: -0.2742 S33: -0.1292 REMARK 3 REMARK 3 TLS GROUP : 26 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : GG 374 GG 492 REMARK 3 ORIGIN FOR THE GROUP (A): 16.9190 -4.3190 45.7520 REMARK 3 T TENSOR REMARK 3 T11: 0.0490 T22: 0.1084 REMARK 3 T33: 0.0911 T12: -0.0299 REMARK 3 T13: 0.0032 T23: -0.0068 REMARK 3 L TENSOR REMARK 3 L11: 1.7628 L22: 3.3436 REMARK 3 L33: 1.9020 L12: 0.1329 REMARK 3 L13: 0.0616 L23: -0.7805 REMARK 3 S TENSOR REMARK 3 S11: -0.0283 S12: 0.0999 S13: 0.3320 REMARK 3 S21: -0.2867 S22: 0.0643 S23: 0.1853 REMARK 3 S31: 0.0338 S32: -0.1396 S33: -0.0359 REMARK 3 REMARK 3 TLS GROUP : 27 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : GG 493 GG 527 REMARK 3 ORIGIN FOR THE GROUP (A): 17.3300 -11.4870 51.4440 REMARK 3 T TENSOR REMARK 3 T11: 0.0669 T22: 0.0856 REMARK 3 T33: 0.0820 T12: -0.0086 REMARK 3 T13: 0.0499 T23: -0.0003 REMARK 3 L TENSOR REMARK 3 L11: 2.4370 L22: 2.0012 REMARK 3 L33: 3.3534 L12: 0.9608 REMARK 3 L13: 0.9762 L23: -0.3034 REMARK 3 S TENSOR REMARK 3 S11: -0.0905 S12: -0.0966 S13: 0.1131 REMARK 3 S21: -0.1005 S22: 0.1433 S23: 0.2015 REMARK 3 S31: -0.0712 S32: -0.0631 S33: -0.0528 REMARK 3 REMARK 3 TLS GROUP : 28 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : HH 1 HH 24 REMARK 3 ORIGIN FOR THE GROUP (A): 38.4170 -30.0980 28.9990 REMARK 3 T TENSOR REMARK 3 T11: 0.3173 T22: 0.2669 REMARK 3 T33: 0.1942 T12: 0.0845 REMARK 3 T13: 0.0638 T23: -0.0854 REMARK 3 L TENSOR REMARK 3 L11: 1.2767 L22: 10.0909 REMARK 3 L33: 3.1864 L12: 3.0396 REMARK 3 L13: -0.6067 L23: -4.1693 REMARK 3 S TENSOR REMARK 3 S11: 0.0073 S12: 0.1368 S13: -0.3049 REMARK 3 S21: -0.3505 S22: 0.0670 S23: -0.3766 REMARK 3 S31: 0.4467 S32: 0.1137 S33: -0.0744 REMARK 3 REMARK 3 TLS GROUP : 29 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : HH 25 HH 99 REMARK 3 ORIGIN FOR THE GROUP (A): 34.8180 -29.8990 37.5520 REMARK 3 T TENSOR REMARK 3 T11: 0.2799 T22: 0.1126 REMARK 3 T33: 0.1100 T12: 0.0969 REMARK 3 T13: -0.0310 T23: -0.0419 REMARK 3 L TENSOR REMARK 3 L11: 2.9261 L22: 5.3904 REMARK 3 L33: 4.4277 L12: 0.6736 REMARK 3 L13: -0.5139 L23: 1.1733 REMARK 3 S TENSOR REMARK 3 S11: -0.0983 S12: -0.0173 S13: -0.4054 REMARK 3 S21: 0.2067 S22: -0.0168 S23: 0.0036 REMARK 3 S31: 0.8329 S32: 0.2359 S33: 0.1151 REMARK 3 REMARK 3 TLS GROUP : 30 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : HH 100 HH 106 REMARK 3 ORIGIN FOR THE GROUP (A): 27.2620 -22.0680 46.5260 REMARK 3 T TENSOR REMARK 3 T11: 0.1757 T22: 0.0501 REMARK 3 T33: 0.0688 T12: 0.0155 REMARK 3 T13: 0.0098 T23: -0.0303 REMARK 3 L TENSOR REMARK 3 L11: 9.7736 L22: 10.9467 REMARK 3 L33: 4.4720 L12: 7.0247 REMARK 3 L13: -2.5626 L23: -2.6067 REMARK 3 S TENSOR REMARK 3 S11: -0.0008 S12: -0.0532 S13: 0.1180 REMARK 3 S21: -0.0498 S22: 0.1878 S23: 0.3560 REMARK 3 S31: 0.5185 S32: 0.2728 S33: -0.1870 REMARK 3 REMARK 3 TLS GROUP : 31 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : HH 107 HH 124 REMARK 3 ORIGIN FOR THE GROUP (A): 28.1930 -28.0570 33.1620 REMARK 3 T TENSOR REMARK 3 T11: 0.2069 T22: 0.0602 REMARK 3 T33: 0.1014 T12: -0.0092 REMARK 3 T13: -0.0175 T23: -0.0592 REMARK 3 L TENSOR REMARK 3 L11: 2.7179 L22: 1.9542 REMARK 3 L33: 4.1290 L12: 2.1830 REMARK 3 L13: -0.3071 L23: -1.1525 REMARK 3 S TENSOR REMARK 3 S11: 0.0572 S12: 0.1678 S13: -0.1224 REMARK 3 S21: -0.0484 S22: 0.1363 S23: -0.0557 REMARK 3 S31: 0.4524 S32: -0.0253 S33: -0.1935 REMARK 3 REMARK 3 TLS GROUP : 32 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : II 333 II 346 REMARK 3 ORIGIN FOR THE GROUP (A): 20.1290 -76.3750 66.6150 REMARK 3 T TENSOR REMARK 3 T11: 0.2206 T22: 0.5070 REMARK 3 T33: 0.3057 T12: -0.0574 REMARK 3 T13: 0.1469 T23: 0.0913 REMARK 3 L TENSOR REMARK 3 L11: 8.5286 L22: 8.7831 REMARK 3 L33: 1.5919 L12: -5.1940 REMARK 3 L13: 3.0659 L23: -2.9940 REMARK 3 S TENSOR REMARK 3 S11: -0.2503 S12: -0.8050 S13: 0.2062 REMARK 3 S21: 0.5316 S22: 0.2844 S23: -0.0721 REMARK 3 S31: -0.3626 S32: -0.2222 S33: -0.0342 REMARK 3 REMARK 3 TLS GROUP : 33 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : II 347 II 371 REMARK 3 ORIGIN FOR THE GROUP (A): 23.9620 -74.0500 61.6040 REMARK 3 T TENSOR REMARK 3 T11: 0.2593 T22: 0.3920 REMARK 3 T33: 0.1960 T12: -0.0439 REMARK 3 T13: 0.0894 T23: 0.0716 REMARK 3 L TENSOR REMARK 3 L11: 3.3057 L22: 3.7581 REMARK 3 L33: 2.8831 L12: -2.5137 REMARK 3 L13: 0.4747 L23: -1.1430 REMARK 3 S TENSOR REMARK 3 S11: 0.0038 S12: -0.3837 S13: -0.1329 REMARK 3 S21: 0.1373 S22: 0.0668 S23: 0.1206 REMARK 3 S31: 0.2796 S32: -0.5921 S33: -0.0707 REMARK 3 REMARK 3 TLS GROUP : 34 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : II 372 II 487 REMARK 3 ORIGIN FOR THE GROUP (A): 22.2130 -66.3600 49.5730 REMARK 3 T TENSOR REMARK 3 T11: 0.0824 T22: 0.3128 REMARK 3 T33: 0.1446 T12: 0.0284 REMARK 3 T13: 0.0136 T23: 0.0215 REMARK 3 L TENSOR REMARK 3 L11: 3.1008 L22: 3.1599 REMARK 3 L33: 2.7105 L12: -1.5478 REMARK 3 L13: -0.0478 L23: 0.5253 REMARK 3 S TENSOR REMARK 3 S11: 0.1817 S12: 0.0493 S13: 0.0300 REMARK 3 S21: -0.2496 S22: -0.1102 S23: 0.3306 REMARK 3 S31: -0.2563 S32: -0.5993 S33: -0.0715 REMARK 3 REMARK 3 TLS GROUP : 35 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : II 488 II 527 REMARK 3 ORIGIN FOR THE GROUP (A): 20.8970 -69.8390 53.1090 REMARK 3 T TENSOR REMARK 3 T11: 0.1455 T22: 0.6724 REMARK 3 T33: 0.2675 T12: 0.0080 REMARK 3 T13: 0.0469 T23: 0.1157 REMARK 3 L TENSOR REMARK 3 L11: 0.9079 L22: 2.3554 REMARK 3 L33: 0.9331 L12: -0.1242 REMARK 3 L13: -0.7320 L23: 0.6756 REMARK 3 S TENSOR REMARK 3 S11: 0.0607 S12: 0.0065 S13: -0.0642 REMARK 3 S21: -0.1245 S22: -0.1447 S23: 0.5353 REMARK 3 S31: -0.0824 S32: -0.4036 S33: 0.0840 REMARK 3 REMARK 3 TLS GROUP : 36 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : JJ 1 JJ 32 REMARK 3 ORIGIN FOR THE GROUP (A): 38.4590 -87.7490 31.1620 REMARK 3 T TENSOR REMARK 3 T11: 0.1192 T22: 0.1993 REMARK 3 T33: 0.1770 T12: 0.0317 REMARK 3 T13: -0.1116 T23: -0.0467 REMARK 3 L TENSOR REMARK 3 L11: 2.5955 L22: 0.2738 REMARK 3 L33: 4.8739 L12: 0.7427 REMARK 3 L13: 0.9087 L23: -0.2672 REMARK 3 S TENSOR REMARK 3 S11: 0.0037 S12: 0.2250 S13: -0.3035 REMARK 3 S21: -0.0376 S22: 0.0691 S23: -0.0922 REMARK 3 S31: 0.3491 S32: 0.1007 S33: -0.0727 REMARK 3 REMARK 3 TLS GROUP : 37 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : JJ 33 JJ 99 REMARK 3 ORIGIN FOR THE GROUP (A): 34.1720 -94.2080 37.4840 REMARK 3 T TENSOR REMARK 3 T11: 0.3212 T22: 0.1577 REMARK 3 T33: 0.2014 T12: -0.0204 REMARK 3 T13: -0.1488 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 2.7425 L22: 4.0617 REMARK 3 L33: 3.6178 L12: 0.3047 REMARK 3 L13: -1.0226 L23: 1.0741 REMARK 3 S TENSOR REMARK 3 S11: 0.1026 S12: -0.0466 S13: -0.4554 REMARK 3 S21: 0.2940 S22: -0.0043 S23: 0.1064 REMARK 3 S31: 0.9177 S32: -0.1710 S33: -0.0983 REMARK 3 REMARK 3 TLS GROUP : 38 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : JJ 100 JJ 106 REMARK 3 ORIGIN FOR THE GROUP (A): 29.4560 -84.4570 48.0420 REMARK 3 T TENSOR REMARK 3 T11: 0.1614 T22: 0.2343 REMARK 3 T33: 0.2229 T12: -0.1071 REMARK 3 T13: -0.0840 T23: 0.0383 REMARK 3 L TENSOR REMARK 3 L11: 3.4271 L22: 7.3059 REMARK 3 L33: 5.4350 L12: -2.6595 REMARK 3 L13: -1.7003 L23: 0.2212 REMARK 3 S TENSOR REMARK 3 S11: -0.0200 S12: 0.0449 S13: -0.1281 REMARK 3 S21: -0.0815 S22: -0.1603 S23: 0.1108 REMARK 3 S31: 0.6554 S32: -0.1317 S33: 0.1804 REMARK 3 REMARK 3 TLS GROUP : 39 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : JJ 107 JJ 124 REMARK 3 ORIGIN FOR THE GROUP (A): 28.1080 -89.2770 34.1620 REMARK 3 T TENSOR REMARK 3 T11: 0.1555 T22: 0.1920 REMARK 3 T33: 0.2969 T12: -0.0523 REMARK 3 T13: -0.1343 T23: -0.0577 REMARK 3 L TENSOR REMARK 3 L11: 2.5755 L22: 2.7318 REMARK 3 L33: 3.2424 L12: 2.4950 REMARK 3 L13: 0.9025 L23: 0.3035 REMARK 3 S TENSOR REMARK 3 S11: 0.1258 S12: 0.0088 S13: -0.0638 REMARK 3 S21: 0.0005 S22: -0.0629 S23: 0.1804 REMARK 3 S31: 0.2285 S32: -0.1511 S33: -0.0630 REMARK 3 REMARK 3 TLS GROUP : 40 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : KK 333 KK 346 REMARK 3 ORIGIN FOR THE GROUP (A): -31.2030 -37.8420 -9.0360 REMARK 3 T TENSOR REMARK 3 T11: 0.5526 T22: 0.3495 REMARK 3 T33: 0.1266 T12: 0.0983 REMARK 3 T13: -0.0357 T23: 0.0448 REMARK 3 L TENSOR REMARK 3 L11: 12.9191 L22: 6.0180 REMARK 3 L33: 11.3570 L12: -0.5378 REMARK 3 L13: -9.7659 L23: 5.2622 REMARK 3 S TENSOR REMARK 3 S11: 0.0233 S12: 0.6429 S13: -0.0534 REMARK 3 S21: -0.7897 S22: -0.2262 S23: 0.1738 REMARK 3 S31: -0.5267 S32: -0.5996 S33: 0.2029 REMARK 3 REMARK 3 TLS GROUP : 41 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : KK 347 KK 368 REMARK 3 ORIGIN FOR THE GROUP (A): -33.3790 -43.4560 -4.6870 REMARK 3 T TENSOR REMARK 3 T11: 0.2485 T22: 0.2277 REMARK 3 T33: 0.1535 T12: -0.0697 REMARK 3 T13: 0.0034 T23: 0.0266 REMARK 3 L TENSOR REMARK 3 L11: 4.4366 L22: 2.5866 REMARK 3 L33: 3.6250 L12: -2.2453 REMARK 3 L13: -2.3522 L23: 1.2802 REMARK 3 S TENSOR REMARK 3 S11: 0.2489 S12: 0.5990 S13: -0.0204 REMARK 3 S21: -0.6035 S22: -0.2504 S23: -0.1931 REMARK 3 S31: -0.2205 S32: 0.0354 S33: 0.0015 REMARK 3 REMARK 3 TLS GROUP : 42 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : KK 369 KK 378 REMARK 3 ORIGIN FOR THE GROUP (A): -22.5270 -37.9030 3.8200 REMARK 3 T TENSOR REMARK 3 T11: 0.3972 T22: 0.2126 REMARK 3 T33: 0.2672 T12: -0.0468 REMARK 3 T13: 0.1035 T23: -0.0294 REMARK 3 L TENSOR REMARK 3 L11: 3.3380 L22: 0.9184 REMARK 3 L33: 10.5795 L12: -1.6878 REMARK 3 L13: -3.8117 L23: 2.3217 REMARK 3 S TENSOR REMARK 3 S11: 0.4846 S12: 0.1310 S13: 0.2573 REMARK 3 S21: -0.3513 S22: -0.0481 S23: -0.1618 REMARK 3 S31: -0.5518 S32: 0.3897 S33: -0.4365 REMARK 3 REMARK 3 TLS GROUP : 43 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : KK 379 KK 527 REMARK 3 ORIGIN FOR THE GROUP (A): -38.9540 -43.8610 7.3170 REMARK 3 T TENSOR REMARK 3 T11: 0.1304 T22: 0.0900 REMARK 3 T33: 0.0687 T12: -0.0679 REMARK 3 T13: -0.0329 T23: -0.0068 REMARK 3 L TENSOR REMARK 3 L11: 3.1065 L22: 2.1208 REMARK 3 L33: 1.6901 L12: 0.8631 REMARK 3 L13: 0.3081 L23: -0.2182 REMARK 3 S TENSOR REMARK 3 S11: 0.0238 S12: -0.0419 S13: -0.0432 REMARK 3 S21: 0.0186 S22: -0.0419 S23: 0.2086 REMARK 3 S31: 0.0611 S32: -0.1959 S33: 0.0181 REMARK 3 REMARK 3 TLS GROUP : 44 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : LL 1 LL 23 REMARK 3 ORIGIN FOR THE GROUP (A): -8.4000 -50.0110 27.5060 REMARK 3 T TENSOR REMARK 3 T11: 0.1282 T22: 0.1653 REMARK 3 T33: 0.1218 T12: 0.0287 REMARK 3 T13: -0.0331 T23: 0.0295 REMARK 3 L TENSOR REMARK 3 L11: 3.4714 L22: 5.0836 REMARK 3 L33: 3.5793 L12: 3.7501 REMARK 3 L13: -2.1351 L23: -0.7805 REMARK 3 S TENSOR REMARK 3 S11: -0.1291 S12: -0.0469 S13: -0.1883 REMARK 3 S21: -0.0342 S22: 0.1732 S23: -0.3123 REMARK 3 S31: 0.2184 S32: 0.3938 S33: -0.0441 REMARK 3 REMARK 3 TLS GROUP : 45 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : LL 24 LL 99 REMARK 3 ORIGIN FOR THE GROUP (A): -9.9610 -47.5860 18.6080 REMARK 3 T TENSOR REMARK 3 T11: 0.0448 T22: 0.1351 REMARK 3 T33: 0.0850 T12: 0.0016 REMARK 3 T13: 0.0390 T23: -0.0279 REMARK 3 L TENSOR REMARK 3 L11: 3.9255 L22: 3.5025 REMARK 3 L33: 4.4373 L12: 1.0933 REMARK 3 L13: 1.1303 L23: -0.1467 REMARK 3 S TENSOR REMARK 3 S11: -0.1332 S12: 0.2871 S13: 0.0638 REMARK 3 S21: -0.1429 S22: 0.0728 S23: -0.2200 REMARK 3 S31: -0.0653 S32: 0.4988 S33: 0.0603 REMARK 3 REMARK 3 TLS GROUP : 46 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : LL 100 LL 106 REMARK 3 ORIGIN FOR THE GROUP (A): -19.5340 -45.1040 8.5080 REMARK 3 T TENSOR REMARK 3 T11: 0.1599 T22: 0.1344 REMARK 3 T33: 0.0871 T12: 0.0311 REMARK 3 T13: -0.0199 T23: -0.0810 REMARK 3 L TENSOR REMARK 3 L11: 7.6169 L22: 9.8921 REMARK 3 L33: 1.1885 L12: 1.5622 REMARK 3 L13: 2.6393 L23: -1.0402 REMARK 3 S TENSOR REMARK 3 S11: 0.3045 S12: 0.4074 S13: 0.0740 REMARK 3 S21: -0.4180 S22: -0.3104 S23: -0.0313 REMARK 3 S31: 0.2174 S32: 0.2254 S33: 0.0059 REMARK 3 REMARK 3 TLS GROUP : 47 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : LL 107 LL 124 REMARK 3 ORIGIN FOR THE GROUP (A): -14.9420 -42.3380 22.2440 REMARK 3 T TENSOR REMARK 3 T11: 0.0342 T22: 0.0241 REMARK 3 T33: 0.0422 T12: -0.0045 REMARK 3 T13: 0.0129 T23: -0.0304 REMARK 3 L TENSOR REMARK 3 L11: 1.6661 L22: 2.7522 REMARK 3 L33: 3.3448 L12: 1.3216 REMARK 3 L13: -0.6673 L23: -1.0036 REMARK 3 S TENSOR REMARK 3 S11: 0.0402 S12: -0.1166 S13: 0.1528 REMARK 3 S21: -0.0267 S22: 0.0240 S23: -0.0735 REMARK 3 S31: 0.0306 S32: 0.1058 S33: -0.0641 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 : 1.00 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 7OAY 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_1292115389. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-JUL-20 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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91842 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340 REMARK 200 RESOLUTION RANGE LOW (A) : 94.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 10.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.800 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: 6ZBP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.18 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SPG, PH 8, 25 % PEG 1500,, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.17933 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 110.35867 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 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 APPLY THE FOLLOWING TO CHAINS: AAA, BBB 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 APPLY THE FOLLOWING TO CHAINS: CCC, DDD 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: GGG, HHH 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: III, JJJ 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: KKK, 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 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 PRO A 330 REMARK 465 LYS A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LYS A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 HIS A 536 REMARK 465 HIS A 537 REMARK 465 HIS A 538 REMARK 465 HIS A 539 REMARK 465 LYS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 REMARK 465 PRO C 330 REMARK 465 LYS C 529 REMARK 465 SER C 530 REMARK 465 THR C 531 REMARK 465 ASN C 532 REMARK 465 LYS C 533 REMARK 465 HIS C 534 REMARK 465 HIS C 535 REMARK 465 HIS C 536 REMARK 465 HIS C 537 REMARK 465 HIS C 538 REMARK 465 HIS C 539 REMARK 465 LYS D 126 REMARK 465 HIS D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 PRO E 330 REMARK 465 ASN E 331 REMARK 465 LYS E 529 REMARK 465 SER E 530 REMARK 465 THR E 531 REMARK 465 ASN E 532 REMARK 465 LYS E 533 REMARK 465 HIS E 534 REMARK 465 HIS E 535 REMARK 465 HIS E 536 REMARK 465 HIS E 537 REMARK 465 HIS E 538 REMARK 465 HIS E 539 REMARK 465 SER F 125 REMARK 465 LYS F 126 REMARK 465 HIS F 127 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 PRO G 330 REMARK 465 ASN G 331 REMARK 465 ILE G 332 REMARK 465 LYS G 529 REMARK 465 SER G 530 REMARK 465 THR G 531 REMARK 465 ASN G 532 REMARK 465 LYS G 533 REMARK 465 HIS G 534 REMARK 465 HIS G 535 REMARK 465 HIS G 536 REMARK 465 HIS G 537 REMARK 465 HIS G 538 REMARK 465 HIS G 539 REMARK 465 LYS H 126 REMARK 465 HIS H 127 REMARK 465 HIS H 128 REMARK 465 HIS H 129 REMARK 465 HIS H 130 REMARK 465 HIS H 131 REMARK 465 HIS H 132 REMARK 465 PRO I 330 REMARK 465 LYS I 529 REMARK 465 SER I 530 REMARK 465 THR I 531 REMARK 465 ASN I 532 REMARK 465 LYS I 533 REMARK 465 HIS I 534 REMARK 465 HIS I 535 REMARK 465 HIS I 536 REMARK 465 HIS I 537 REMARK 465 HIS I 538 REMARK 465 HIS I 539 REMARK 465 LYS J 126 REMARK 465 HIS J 127 REMARK 465 HIS J 128 REMARK 465 HIS J 129 REMARK 465 HIS J 130 REMARK 465 HIS J 131 REMARK 465 HIS J 132 REMARK 465 PRO K 330 REMARK 465 ASN K 331 REMARK 465 LYS K 529 REMARK 465 SER K 530 REMARK 465 THR K 531 REMARK 465 ASN K 532 REMARK 465 LYS K 533 REMARK 465 HIS K 534 REMARK 465 HIS K 535 REMARK 465 HIS K 536 REMARK 465 HIS K 537 REMARK 465 HIS K 538 REMARK 465 HIS K 539 REMARK 465 LYS L 126 REMARK 465 HIS L 127 REMARK 465 HIS L 128 REMARK 465 HIS L 129 REMARK 465 HIS L 130 REMARK 465 HIS L 131 REMARK 465 HIS L 132 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 ASNEE 481 O HOHEE 701 1.99 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 355 CB - CA - C ANGL. DEV. = -15.7 DEGREES REMARK 500 ARGAA 355 CG - CD - NE ANGL. DEV. = -13.7 DEGREES REMARK 500 ARGAA 357 CG - CD - NE ANGL. DEV. = -12.9 DEGREES REMARK 500 ARGCC 355 CB - CA - C ANGL. DEV. = -16.9 DEGREES REMARK 500 ARGCC 355 CG - CD - NE ANGL. DEV. = -15.7 DEGREES REMARK 500 ARGEE 355 CB - CA - C ANGL. DEV. = -15.8 DEGREES REMARK 500 ARGEE 355 CG - CD - NE ANGL. DEV. = -13.8 DEGREES REMARK 500 ARGGG 355 CB - CA - C ANGL. DEV. = -15.3 DEGREES REMARK 500 ARGGG 355 CG - CD - NE ANGL. DEV. = -16.2 DEGREES REMARK 500 ARGII 355 CB - CA - C ANGL. DEV. = -15.4 DEGREES REMARK 500 ARGII 355 CG - CD - NE ANGL. DEV. = -12.7 DEGREES REMARK 500 ARGKK 355 CB - CA - C ANGL. DEV. = -15.8 DEGREES REMARK 500 ARGKK 355 CG - CD - NE ANGL. DEV. = -16.1 DEGREES REMARK 500 ARGKK 408 CG - CD - NE ANGL. DEV. = -13.1 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 333 -30.73 -141.11 REMARK 500 ASNAA 422 -57.37 -126.53 REMARK 500 SERBB 55 -2.41 82.30 REMARK 500 TYRBB 105 57.93 -97.65 REMARK 500 ASNCC 422 -57.80 -127.24 REMARK 500 SERDD 55 -0.80 81.57 REMARK 500 TYRDD 105 59.09 -97.41 REMARK 500 THREE 333 -44.16 174.24 REMARK 500 ASNEE 422 -57.92 -126.13 REMARK 500 SERFF 55 -1.35 81.57 REMARK 500 TYRFF 105 59.53 -98.45 REMARK 500 PHEGG 377 89.96 -157.53 REMARK 500 ASNGG 422 -57.82 -126.70 REMARK 500 SERHH 55 -2.21 81.87 REMARK 500 ALAHH 92 172.79 178.71 REMARK 500 TYRHH 105 59.82 -98.31 REMARK 500 ASNII 422 -59.57 -127.35 REMARK 500 SERJJ 55 -1.48 81.69 REMARK 500 TYRJJ 105 58.38 -95.73 REMARK 500 THRKK 333 -46.21 162.24 REMARK 500 ASNKK 422 -57.61 -126.38 REMARK 500 SERLL 55 -1.05 81.70 REMARK 500 TYRLL 105 59.04 -97.21 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 SERBB 55 THRBB 56 -147.38 REMARK 500 SERFF 55 THRFF 56 -149.32 REMARK 500 SERHH 55 THRHH 56 -147.84 REMARK 500 SERJJ 55 THRJJ 56 -148.89 REMARK 500 SERLL 55 THRLL 56 -148.04 REMARK 500 REMARK 500 REMARK: NULL DBREF 7OAYAA 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAYBB 1 132 PDB 7OAY 7OAY 1 132 DBREF 7OAYCC 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAYDD 1 132 PDB 7OAY 7OAY 1 132 DBREF 7OAYEE 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAYFF 1 132 PDB 7OAY 7OAY 1 132 DBREF 7OAYGG 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAYHH 1 132 PDB 7OAY 7OAY 1 132 DBREF 7OAYII 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAYJJ 1 132 PDB 7OAY 7OAY 1 132 DBREF 7OAYKK 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7OAYLL 1 132 PDB 7OAY 7OAY 1 132 SEQADV 7OAY LYSAA 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISAA 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISAA 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISAA 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISAA 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISAA 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISAA 539 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY LYSCC 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISCC 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISCC 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISCC 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISCC 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISCC 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISCC 539 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY LYSEE 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISEE 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISEE 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISEE 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISEE 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISEE 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISEE 539 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY LYSGG 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISGG 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISGG 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISGG 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISGG 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISGG 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISGG 539 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY LYSII 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISII 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISII 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISII 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISII 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISII 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISII 539 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY LYSKK 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISKK 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISKK 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISKK 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISKK 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISKK 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7OAY HISKK 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1AA 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2AA 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3AA 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4AA 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5AA 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6AA 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7AA 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8AA 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9AA 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10AA 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11AA 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12AA 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13AA 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14AA 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15AA 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16AA 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17AA 210 HIS HIS SEQRES 1BB 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2BB 132 ALA GLY GLY SER LEU ARG LEU ALA CYS ILE ALA SER GLY SEQRES 3BB 132 ARG THR PHE HIS SER TYR VAL MET ALA TRP PHE ARG GLN SEQRES 4BB 132 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5BB 132 TRP SER SER THR PRO THR TYR TYR GLY GLU SER VAL LYS SEQRES 6BB 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7BB 132 VAL TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR SEQRES 8BB 132 ALA VAL TYR PHE CYS ALA ALA ASP ARG GLY GLU SER TYR SEQRES 9BB 132 TYR TYR THR ARG PRO THR GLU TYR GLU PHE TRP GLY GLN SEQRES 10BB 132 GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11BB 132 HIS HIS SEQRES 1CC 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2CC 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3CC 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4CC 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5CC 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6CC 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7CC 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8CC 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9CC 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10CC 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11CC 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12CC 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13CC 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14CC 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15CC 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16CC 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17CC 210 HIS HIS SEQRES 1DD 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2DD 132 ALA GLY GLY SER LEU ARG LEU ALA CYS ILE ALA SER GLY SEQRES 3DD 132 ARG THR PHE HIS SER TYR VAL MET ALA TRP PHE ARG GLN SEQRES 4DD 132 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5DD 132 TRP SER SER THR PRO THR TYR TYR GLY GLU SER VAL LYS SEQRES 6DD 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7DD 132 VAL TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR SEQRES 8DD 132 ALA VAL TYR PHE CYS ALA ALA ASP ARG GLY GLU SER TYR SEQRES 9DD 132 TYR TYR THR ARG PRO THR GLU TYR GLU PHE TRP GLY GLN SEQRES 10DD 132 GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11DD 132 HIS HIS SEQRES 1EE 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2EE 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3EE 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4EE 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5EE 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6EE 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7EE 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8EE 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9EE 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10EE 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11EE 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12EE 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13EE 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14EE 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15EE 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16EE 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17EE 210 HIS HIS SEQRES 1FF 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2FF 132 ALA GLY GLY SER LEU ARG LEU ALA CYS ILE ALA SER GLY SEQRES 3FF 132 ARG THR PHE HIS SER TYR VAL MET ALA TRP PHE ARG GLN SEQRES 4FF 132 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5FF 132 TRP SER SER THR PRO THR TYR TYR GLY GLU SER VAL LYS SEQRES 6FF 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7FF 132 VAL TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR SEQRES 8FF 132 ALA VAL TYR PHE CYS ALA ALA ASP ARG GLY GLU SER TYR SEQRES 9FF 132 TYR TYR THR ARG PRO THR GLU TYR GLU PHE TRP GLY GLN SEQRES 10FF 132 GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11FF 132 HIS HIS SEQRES 1GG 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2GG 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3GG 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4GG 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5GG 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6GG 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7GG 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8GG 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9GG 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10GG 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11GG 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12GG 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13GG 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14GG 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15GG 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16GG 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17GG 210 HIS HIS SEQRES 1HH 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2HH 132 ALA GLY GLY SER LEU ARG LEU ALA CYS ILE ALA SER GLY SEQRES 3HH 132 ARG THR PHE HIS SER TYR VAL MET ALA TRP PHE ARG GLN SEQRES 4HH 132 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5HH 132 TRP SER SER THR PRO THR TYR TYR GLY GLU SER VAL LYS SEQRES 6HH 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7HH 132 VAL TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR SEQRES 8HH 132 ALA VAL TYR PHE CYS ALA ALA ASP ARG GLY GLU SER TYR SEQRES 9HH 132 TYR TYR THR ARG PRO THR GLU TYR GLU PHE TRP GLY GLN SEQRES 10HH 132 GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11HH 132 HIS HIS SEQRES 1II 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2II 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3II 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4II 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5II 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6II 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7II 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8II 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9II 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10II 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11II 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12II 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13II 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14II 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15II 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16II 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17II 210 HIS HIS SEQRES 1JJ 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2JJ 132 ALA GLY GLY SER LEU ARG LEU ALA CYS ILE ALA SER GLY SEQRES 3JJ 132 ARG THR PHE HIS SER TYR VAL MET ALA TRP PHE ARG GLN SEQRES 4JJ 132 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5JJ 132 TRP SER SER THR PRO THR TYR TYR GLY GLU SER VAL LYS SEQRES 6JJ 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7JJ 132 VAL TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR SEQRES 8JJ 132 ALA VAL TYR PHE CYS ALA ALA ASP ARG GLY GLU SER TYR SEQRES 9JJ 132 TYR TYR THR ARG PRO THR GLU TYR GLU PHE TRP GLY GLN SEQRES 10JJ 132 GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11JJ 132 HIS HIS SEQRES 1KK 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2KK 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3KK 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4KK 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5KK 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6KK 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7KK 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8KK 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9KK 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10KK 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11KK 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12KK 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13KK 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14KK 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15KK 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16KK 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17KK 210 HIS HIS SEQRES 1LL 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2LL 132 ALA GLY GLY SER LEU ARG LEU ALA CYS ILE ALA SER GLY SEQRES 3LL 132 ARG THR PHE HIS SER TYR VAL MET ALA TRP PHE ARG GLN SEQRES 4LL 132 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5LL 132 TRP SER SER THR PRO THR TYR TYR GLY GLU SER VAL LYS SEQRES 6LL 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7LL 132 VAL TYR LEU GLN MET ASN ARG LEU LYS PRO GLU ASP THR SEQRES 8LL 132 ALA VAL TYR PHE CYS ALA ALA ASP ARG GLY GLU SER TYR SEQRES 9LL 132 TYR TYR THR ARG PRO THR GLU TYR GLU PHE TRP GLY GLN SEQRES 10LL 132 GLY THR GLN VAL THR VAL SER SER LYS HIS HIS HIS HIS SEQRES 11LL 132 HIS HIS HET NAG AA 601 14 HET NAG CC 601 14 HET NAG EE 601 14 HET NAG GG 601 14 HET NAG II 601 14 HET NAG KK 601 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 13 NAG 6(C8 H15 N O6) FORMUL 19 HOH *323(H2 O) HELIX 1 AA1 PROAA 337 ASNAA 343 1 7 HELIX 2 AA2 SERAA 349 TRPAA 353 5 5 HELIX 3 AA3 TYRAA 365 ASNAA 370 1 6 HELIX 4 AA4 SERAA 383 ASPAA 389 5 7 HELIX 5 AA5 ASPAA 405 ILEAA 410 5 6 HELIX 6 AA6 GLYAA 416 ASNAA 422 1 7 HELIX 7 AA7 SERAA 438 SERAA 443 1 6 HELIX 8 AA8 GLYAA 502 TYRAA 505 5 4 HELIX 9 AA9 THRBB 28 TYRBB 32 5 5 HELIX 10 AB1 ASNBB 74 LYSBB 76 5 3 HELIX 11 AB2 LYSBB 87 THRBB 91 5 5 HELIX 12 AB3 ARGBB 108 TYRBB 112 5 5 HELIX 13 AB4 PHECC 338 ASNCC 343 1 6 HELIX 14 AB5 SERCC 349 TRPCC 353 5 5 HELIX 15 AB6 TYRCC 365 ASNCC 370 1 6 HELIX 16 AB7 SERCC 383 ASPCC 389 5 7 HELIX 17 AB8 ASPCC 405 ILECC 410 5 6 HELIX 18 AB9 GLYCC 416 ASNCC 422 1 7 HELIX 19 AC1 SERCC 438 SERCC 443 1 6 HELIX 20 AC2 GLYCC 502 TYRCC 505 5 4 HELIX 21 AC3 THRDD 28 TYRDD 32 5 5 HELIX 22 AC4 ASNDD 74 LYSDD 76 5 3 HELIX 23 AC5 LYSDD 87 THRDD 91 5 5 HELIX 24 AC6 ARGDD 108 TYRDD 112 5 5 HELIX 25 AC7 PHEEE 338 ASNEE 343 1 6 HELIX 26 AC8 SEREE 349 TRPEE 353 5 5 HELIX 27 AC9 TYREE 365 ASNEE 370 1 6 HELIX 28 AD1 SEREE 383 ASPEE 389 5 7 HELIX 29 AD2 ASPEE 405 ILEEE 410 5 6 HELIX 30 AD3 GLYEE 416 ASNEE 422 1 7 HELIX 31 AD4 SEREE 438 SEREE 443 1 6 HELIX 32 AD5 GLYEE 502 TYREE 505 5 4 HELIX 33 AD6 THRFF 28 TYRFF 32 5 5 HELIX 34 AD7 ASNFF 74 LYSFF 76 5 3 HELIX 35 AD8 LYSFF 87 THRFF 91 5 5 HELIX 36 AD9 ARGFF 108 TYRFF 112 5 5 HELIX 37 AE1 PROGG 337 ASNGG 343 1 7 HELIX 38 AE2 SERGG 349 TRPGG 353 5 5 HELIX 39 AE3 TYRGG 365 ASNGG 370 1 6 HELIX 40 AE4 SERGG 383 ASPGG 389 5 7 HELIX 41 AE5 ASPGG 405 ILEGG 410 5 6 HELIX 42 AE6 GLYGG 416 ASNGG 422 1 7 HELIX 43 AE7 SERGG 438 SERGG 443 1 6 HELIX 44 AE8 GLYGG 502 TYRGG 505 5 4 HELIX 45 AE9 THRHH 28 TYRHH 32 5 5 HELIX 46 AF1 ASNHH 74 LYSHH 76 5 3 HELIX 47 AF2 LYSHH 87 THRHH 91 5 5 HELIX 48 AF3 ARGHH 108 TYRHH 112 5 5 HELIX 49 AF4 PROII 337 ASNII 343 1 7 HELIX 50 AF5 SERII 349 TRPII 353 5 5 HELIX 51 AF6 TYRII 365 ASNII 370 1 6 HELIX 52 AF7 SERII 383 ASPII 389 5 7 HELIX 53 AF8 ASPII 405 ILEII 410 5 6 HELIX 54 AF9 GLYII 416 ASNII 422 1 7 HELIX 55 AG1 SERII 438 SERII 443 1 6 HELIX 56 AG2 GLYII 502 TYRII 505 5 4 HELIX 57 AG3 THRJJ 28 TYRJJ 32 5 5 HELIX 58 AG4 ASNJJ 74 LYSJJ 76 5 3 HELIX 59 AG5 LYSJJ 87 THRJJ 91 5 5 HELIX 60 AG6 ARGJJ 108 TYRJJ 112 5 5 HELIX 61 AG7 PROKK 337 ASNKK 343 1 7 HELIX 62 AG8 SERKK 349 TRPKK 353 5 5 HELIX 63 AG9 TYRKK 365 ASNKK 370 1 6 HELIX 64 AH1 SERKK 383 ASPKK 389 5 7 HELIX 65 AH2 ASPKK 405 ILEKK 410 5 6 HELIX 66 AH3 GLYKK 416 ASNKK 422 1 7 HELIX 67 AH4 SERKK 438 SERKK 443 1 6 HELIX 68 AH5 GLYKK 502 TYRKK 505 5 4 HELIX 69 AH6 THRLL 28 TYRLL 32 5 5 HELIX 70 AH7 ASNLL 74 LYSLL 76 5 3 HELIX 71 AH8 LYSLL 87 THRLL 91 5 5 HELIX 72 AH9 ARGLL 108 TYRLL 112 5 5 SHEET 1 AA1 6 ASNAA 354 ILEAA 358 0 SHEET 2 AA1 6 ASNAA 394 ARGAA 403 -1 O VALAA 395 N ILEAA 358 SHEET 3 AA1 6 PROAA 507 GLUAA 516 -1 O TYRAA 508 N ILEAA 402 SHEET 4 AA1 6 GLYAA 431 ASNAA 437 -1 N ILEAA 434 O VALAA 511 SHEET 5 AA1 6 THRAA 376 TYRAA 380 -1 N LYSAA 378 O VALAA 433 SHEET 6 AA1 6 GLUBB 102 SERBB 103 -1 O GLUBB 102 N CYSAA 379 SHEET 1 AA2 3 CYSAA 361 VALAA 362 0 SHEET 2 AA2 3 VALAA 524 CYSAA 525 1 O CYSAA 525 N CYSAA 361 SHEET 3 AA2 3 CYSAA 391 PHEAA 392 -1 N PHEAA 392 O VALAA 524 SHEET 1 AA3 2 LEUAA 452 ARGAA 454 0 SHEET 2 AA3 2 LEUAA 492 SERAA 494 -1 O GLNAA 493 N TYRAA 453 SHEET 1 AA4 2 TYRAA 473 GLNAA 474 0 SHEET 2 AA4 2 CYSAA 488 TYRAA 489 -1 O TYRAA 489 N TYRAA 473 SHEET 1 AA5 4 LEUBB 4 SERBB 7 0 SHEET 2 AA5 4 LEUBB 18 ALABB 24 -1 O ALABB 21 N SERBB 7 SHEET 3 AA5 4 THRBB 78 METBB 83 -1 O METBB 83 N LEUBB 18 SHEET 4 AA5 4 PHEBB 68 ASPBB 73 -1 N ASPBB 73 O THRBB 78 SHEET 1 AA6 6 GLYBB 10 GLNBB 13 0 SHEET 2 AA6 6 THRBB 119 SERBB 124 1 O THRBB 122 N GLYBB 10 SHEET 3 AA6 6 ALABB 92 ASPBB 99 -1 N TYRBB 94 O THRBB 119 SHEET 4 AA6 6 VALBB 33 GLNBB 39 -1 N VALBB 33 O ASPBB 99 SHEET 5 AA6 6 GLUBB 46 ILEBB 51 -1 O GLUBB 46 N ARGBB 38 SHEET 6 AA6 6 THRBB 58 TYRBB 60 -1 O TYRBB 59 N ALABB 50 SHEET 1 AA7 4 GLYBB 10 GLNBB 13 0 SHEET 2 AA7 4 THRBB 119 SERBB 124 1 O THRBB 122 N GLYBB 10 SHEET 3 AA7 4 ALABB 92 ASPBB 99 -1 N TYRBB 94 O THRBB 119 SHEET 4 AA7 4 PHEBB 114 TRPBB 115 -1 O PHEBB 114 N ALABB 98 SHEET 1 AA8 6 ASNCC 354 ILECC 358 0 SHEET 2 AA8 6 ASNCC 394 ARGCC 403 -1 O VALCC 395 N ILECC 358 SHEET 3 AA8 6 PROCC 507 GLUCC 516 -1 O TYRCC 508 N ILECC 402 SHEET 4 AA8 6 GLYCC 431 ASNCC 437 -1 N CYSCC 432 O LEUCC 513 SHEET 5 AA8 6 THRCC 376 TYRCC 380 -1 N TYRCC 380 O GLYCC 431 SHEET 6 AA8 6 GLUDD 102 SERDD 103 -1 O GLUDD 102 N CYSCC 379 SHEET 1 AA9 3 CYSCC 361 VALCC 362 0 SHEET 2 AA9 3 VALCC 524 CYSCC 525 1 O CYSCC 525 N CYSCC 361 SHEET 3 AA9 3 CYSCC 391 PHECC 392 -1 N PHECC 392 O VALCC 524 SHEET 1 AB1 2 LEUCC 452 ARGCC 454 0 SHEET 2 AB1 2 LEUCC 492 SERCC 494 -1 O GLNCC 493 N TYRCC 453 SHEET 1 AB2 2 TYRCC 473 GLNCC 474 0 SHEET 2 AB2 2 CYSCC 488 TYRCC 489 -1 O TYRCC 489 N TYRCC 473 SHEET 1 AB3 4 LEUDD 4 SERDD 7 0 SHEET 2 AB3 4 LEUDD 18 ALADD 24 -1 O ALADD 21 N SERDD 7 SHEET 3 AB3 4 THRDD 78 METDD 83 -1 O METDD 83 N LEUDD 18 SHEET 4 AB3 4 PHEDD 68 ASPDD 73 -1 N SERDD 71 O TYRDD 80 SHEET 1 AB4 6 GLYDD 10 GLNDD 13 0 SHEET 2 AB4 6 THRDD 119 SERDD 124 1 O THRDD 122 N GLYDD 10 SHEET 3 AB4 6 ALADD 92 ASPDD 99 -1 N TYRDD 94 O THRDD 119 SHEET 4 AB4 6 VALDD 33 GLNDD 39 -1 N VALDD 33 O ASPDD 99 SHEET 5 AB4 6 GLUDD 46 ILEDD 51 -1 O GLUDD 46 N ARGDD 38 SHEET 6 AB4 6 THRDD 58 TYRDD 60 -1 O TYRDD 59 N ALADD 50 SHEET 1 AB5 4 GLYDD 10 GLNDD 13 0 SHEET 2 AB5 4 THRDD 119 SERDD 124 1 O THRDD 122 N GLYDD 10 SHEET 3 AB5 4 ALADD 92 ASPDD 99 -1 N TYRDD 94 O THRDD 119 SHEET 4 AB5 4 PHEDD 114 TRPDD 115 -1 O PHEDD 114 N ALADD 98 SHEET 1 AB6 6 ASNEE 354 ILEEE 358 0 SHEET 2 AB6 6 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AB6 6 PROEE 507 GLUEE 516 -1 O TYREE 508 N ILEEE 402 SHEET 4 AB6 6 GLYEE 431 ASNEE 437 -1 N ILEEE 434 O VALEE 511 SHEET 5 AB6 6 THREE 376 TYREE 380 -1 N TYREE 380 O GLYEE 431 SHEET 6 AB6 6 GLUFF 102 SERFF 103 -1 O GLUFF 102 N CYSEE 379 SHEET 1 AB7 3 CYSEE 361 VALEE 362 0 SHEET 2 AB7 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AB7 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AB8 2 LEUEE 452 ARGEE 454 0 SHEET 2 AB8 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AB9 2 TYREE 473 GLNEE 474 0 SHEET 2 AB9 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AC1 4 LEUFF 4 SERFF 7 0 SHEET 2 AC1 4 LEUFF 18 ALAFF 24 -1 O ALAFF 21 N SERFF 7 SHEET 3 AC1 4 THRFF 78 METFF 83 -1 O METFF 83 N LEUFF 18 SHEET 4 AC1 4 PHEFF 68 ASPFF 73 -1 N ASPFF 73 O THRFF 78 SHEET 1 AC2 6 GLYFF 10 VALFF 12 0 SHEET 2 AC2 6 THRFF 119 VALFF 123 1 O THRFF 122 N GLYFF 10 SHEET 3 AC2 6 ALAFF 92 ASPFF 99 -1 N TYRFF 94 O THRFF 119 SHEET 4 AC2 6 VALFF 33 GLNFF 39 -1 N VALFF 33 O ASPFF 99 SHEET 5 AC2 6 GLUFF 46 ILEFF 51 -1 O GLUFF 46 N ARGFF 38 SHEET 6 AC2 6 THRFF 58 TYRFF 60 -1 O TYRFF 59 N ALAFF 50 SHEET 1 AC3 4 GLYFF 10 VALFF 12 0 SHEET 2 AC3 4 THRFF 119 VALFF 123 1 O THRFF 122 N GLYFF 10 SHEET 3 AC3 4 ALAFF 92 ASPFF 99 -1 N TYRFF 94 O THRFF 119 SHEET 4 AC3 4 PHEFF 114 TRPFF 115 -1 O PHEFF 114 N ALAFF 98 SHEET 1 AC4 6 ASNGG 354 ILEGG 358 0 SHEET 2 AC4 6 ASNGG 394 ARGGG 403 -1 O VALGG 395 N ILEGG 358 SHEET 3 AC4 6 PROGG 507 GLUGG 516 -1 O TYRGG 508 N ILEGG 402 SHEET 4 AC4 6 GLYGG 431 ASNGG 437 -1 N ILEGG 434 O VALGG 511 SHEET 5 AC4 6 THRGG 376 TYRGG 380 -1 N LYSGG 378 O VALGG 433 SHEET 6 AC4 6 GLUHH 102 SERHH 103 -1 O GLUHH 102 N CYSGG 379 SHEET 1 AC5 3 CYSGG 361 VALGG 362 0 SHEET 2 AC5 3 VALGG 524 CYSGG 525 1 O CYSGG 525 N CYSGG 361 SHEET 3 AC5 3 CYSGG 391 PHEGG 392 -1 N PHEGG 392 O VALGG 524 SHEET 1 AC6 2 LEUGG 452 ARGGG 454 0 SHEET 2 AC6 2 LEUGG 492 SERGG 494 -1 O GLNGG 493 N TYRGG 453 SHEET 1 AC7 2 TYRGG 473 GLNGG 474 0 SHEET 2 AC7 2 CYSGG 488 TYRGG 489 -1 O TYRGG 489 N TYRGG 473 SHEET 1 AC8 4 LEUHH 4 SERHH 7 0 SHEET 2 AC8 4 LEUHH 18 ALAHH 24 -1 O ALAHH 21 N SERHH 7 SHEET 3 AC8 4 THRHH 78 METHH 83 -1 O METHH 83 N LEUHH 18 SHEET 4 AC8 4 PHEHH 68 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AC9 6 GLYHH 10 GLNHH 13 0 SHEET 2 AC9 6 THRHH 119 SERHH 124 1 O THRHH 122 N GLYHH 10 SHEET 3 AC9 6 ALAHH 92 ASPHH 99 -1 N TYRHH 94 O THRHH 119 SHEET 4 AC9 6 VALHH 33 GLNHH 39 -1 N VALHH 33 O ASPHH 99 SHEET 5 AC9 6 GLUHH 46 ILEHH 51 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AC9 6 THRHH 58 TYRHH 60 -1 O TYRHH 59 N ALAHH 50 SHEET 1 AD1 4 GLYHH 10 GLNHH 13 0 SHEET 2 AD1 4 THRHH 119 SERHH 124 1 O THRHH 122 N GLYHH 10 SHEET 3 AD1 4 ALAHH 92 ASPHH 99 -1 N TYRHH 94 O THRHH 119 SHEET 4 AD1 4 PHEHH 114 TRPHH 115 -1 O PHEHH 114 N ALAHH 98 SHEET 1 AD2 6 ASNII 354 ILEII 358 0 SHEET 2 AD2 6 ASNII 394 ARGII 403 -1 O VALII 395 N ILEII 358 SHEET 3 AD2 6 PROII 507 GLUII 516 -1 O TYRII 508 N ILEII 402 SHEET 4 AD2 6 GLYII 431 ASNII 437 -1 N CYSII 432 O LEUII 513 SHEET 5 AD2 6 THRII 376 TYRII 380 -1 N LYSII 378 O VALII 433 SHEET 6 AD2 6 GLUJJ 102 SERJJ 103 -1 O GLUJJ 102 N CYSII 379 SHEET 1 AD3 3 CYSII 361 VALII 362 0 SHEET 2 AD3 3 VALII 524 CYSII 525 1 O CYSII 525 N CYSII 361 SHEET 3 AD3 3 CYSII 391 PHEII 392 -1 N PHEII 392 O VALII 524 SHEET 1 AD4 2 LEUII 452 ARGII 454 0 SHEET 2 AD4 2 LEUII 492 SERII 494 -1 O GLNII 493 N TYRII 453 SHEET 1 AD5 2 TYRII 473 GLNII 474 0 SHEET 2 AD5 2 CYSII 488 TYRII 489 -1 O TYRII 489 N TYRII 473 SHEET 1 AD6 4 LEUJJ 4 SERJJ 7 0 SHEET 2 AD6 4 LEUJJ 18 ALAJJ 24 -1 O ALAJJ 21 N SERJJ 7 SHEET 3 AD6 4 THRJJ 78 METJJ 83 -1 O METJJ 83 N LEUJJ 18 SHEET 4 AD6 4 PHEJJ 68 ASPJJ 73 -1 N SERJJ 71 O TYRJJ 80 SHEET 1 AD7 6 GLYJJ 10 GLNJJ 13 0 SHEET 2 AD7 6 THRJJ 119 SERJJ 124 1 O THRJJ 122 N GLYJJ 10 SHEET 3 AD7 6 ALAJJ 92 ASPJJ 99 -1 N TYRJJ 94 O THRJJ 119 SHEET 4 AD7 6 VALJJ 33 GLNJJ 39 -1 N VALJJ 33 O ASPJJ 99 SHEET 5 AD7 6 GLUJJ 46 ILEJJ 51 -1 O GLUJJ 46 N ARGJJ 38 SHEET 6 AD7 6 THRJJ 58 TYRJJ 60 -1 O TYRJJ 59 N ALAJJ 50 SHEET 1 AD8 4 GLYJJ 10 GLNJJ 13 0 SHEET 2 AD8 4 THRJJ 119 SERJJ 124 1 O THRJJ 122 N GLYJJ 10 SHEET 3 AD8 4 ALAJJ 92 ASPJJ 99 -1 N TYRJJ 94 O THRJJ 119 SHEET 4 AD8 4 PHEJJ 114 TRPJJ 115 -1 O PHEJJ 114 N ALAJJ 98 SHEET 1 AD9 6 ASNKK 354 ILEKK 358 0 SHEET 2 AD9 6 ASNKK 394 ARGKK 403 -1 O VALKK 395 N ILEKK 358 SHEET 3 AD9 6 PROKK 507 GLUKK 516 -1 O TYRKK 508 N ILEKK 402 SHEET 4 AD9 6 GLYKK 431 ASNKK 437 -1 N CYSKK 432 O LEUKK 513 SHEET 5 AD9 6 THRKK 376 TYRKK 380 -1 N LYSKK 378 O VALKK 433 SHEET 6 AD9 6 GLULL 102 SERLL 103 -1 O GLULL 102 N CYSKK 379 SHEET 1 AE1 3 CYSKK 361 VALKK 362 0 SHEET 2 AE1 3 VALKK 524 CYSKK 525 1 O CYSKK 525 N CYSKK 361 SHEET 3 AE1 3 CYSKK 391 PHEKK 392 -1 N PHEKK 392 O VALKK 524 SHEET 1 AE2 2 LEUKK 452 ARGKK 454 0 SHEET 2 AE2 2 LEUKK 492 SERKK 494 -1 O GLNKK 493 N TYRKK 453 SHEET 1 AE3 2 TYRKK 473 GLNKK 474 0 SHEET 2 AE3 2 CYSKK 488 TYRKK 489 -1 O TYRKK 489 N TYRKK 473 SHEET 1 AE4 4 LEULL 4 SERLL 7 0 SHEET 2 AE4 4 LEULL 18 ALALL 24 -1 O ALALL 21 N SERLL 7 SHEET 3 AE4 4 THRLL 78 METLL 83 -1 O METLL 83 N LEULL 18 SHEET 4 AE4 4 PHELL 68 ASPLL 73 -1 N SERLL 71 O TYRLL 80 SHEET 1 AE5 6 GLYLL 10 GLNLL 13 0 SHEET 2 AE5 6 THRLL 119 SERLL 124 1 O THRLL 122 N GLYLL 10 SHEET 3 AE5 6 ALALL 92 ASPLL 99 -1 N TYRLL 94 O THRLL 119 SHEET 4 AE5 6 VALLL 33 GLNLL 39 -1 N VALLL 33 O ASPLL 99 SHEET 5 AE5 6 GLULL 46 ILELL 51 -1 O GLULL 46 N ARGLL 38 SHEET 6 AE5 6 THRLL 58 TYRLL 60 -1 O TYRLL 59 N ALALL 50 SHEET 1 AE6 4 GLYLL 10 GLNLL 13 0 SHEET 2 AE6 4 THRLL 119 SERLL 124 1 O THRLL 122 N GLYLL 10 SHEET 3 AE6 4 ALALL 92 ASPLL 99 -1 N TYRLL 94 O THRLL 119 SHEET 4 AE6 4 PHELL 114 TRPLL 115 -1 O PHELL 114 N ALALL 98 SSBOND 1 CYSAA 336 CYSAA 361 1555 1555 2.08 SSBOND 2 CYSAA 379 CYSAA 432 1555 1555 2.11 SSBOND 3 CYSAA 391 CYSAA 525 1555 1555 2.15 SSBOND 4 CYSAA 480 CYSAA 488 1555 1555 2.07 SSBOND 5 CYSBB 22 CYSBB 96 1555 1555 2.03 SSBOND 6 CYSCC 336 CYSCC 361 1555 1555 2.07 SSBOND 7 CYSCC 379 CYSCC 432 1555 1555 2.10 SSBOND 8 CYSCC 391 CYSCC 525 1555 1555 2.14 SSBOND 9 CYSCC 480 CYSCC 488 1555 1555 2.09 SSBOND 10 CYSDD 22 CYSDD 96 1555 1555 2.05 SSBOND 11 CYSEE 336 CYSEE 361 1555 1555 2.08 SSBOND 12 CYSEE 379 CYSEE 432 1555 1555 2.07 SSBOND 13 CYSEE 391 CYSEE 525 1555 1555 2.10 SSBOND 14 CYSEE 480 CYSEE 488 1555 1555 2.05 SSBOND 15 CYSFF 22 CYSFF 96 1555 1555 2.02 SSBOND 16 CYSGG 336 CYSGG 361 1555 1555 2.06 SSBOND 17 CYSGG 379 CYSGG 432 1555 1555 2.02 SSBOND 18 CYSGG 391 CYSGG 525 1555 1555 2.16 SSBOND 19 CYSGG 480 CYSGG 488 1555 1555 2.08 SSBOND 20 CYSHH 22 CYSHH 96 1555 1555 2.02 SSBOND 21 CYSII 336 CYSII 361 1555 1555 2.07 SSBOND 22 CYSII 379 CYSII 432 1555 1555 2.07 SSBOND 23 CYSII 391 CYSII 525 1555 1555 2.11 SSBOND 24 CYSII 480 CYSII 488 1555 1555 2.09 SSBOND 25 CYSJJ 22 CYSJJ 96 1555 1555 2.03 SSBOND 26 CYSKK 336 CYSKK 361 1555 1555 2.04 SSBOND 27 CYSKK 379 CYSKK 432 1555 1555 2.07 SSBOND 28 CYSKK 391 CYSKK 525 1555 1555 2.12 SSBOND 29 CYSKK 480 CYSKK 488 1555 1555 2.09 SSBOND 30 CYSLL 22 CYSLL 96 1555 1555 2.06 LINK ND2 ASNAA 343 C1 NAGAA 601 1555 1555 1.44 LINK ND2 ASNCC 343 C1 NAGCC 601 1555 1555 1.44 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.44 LINK ND2 ASNGG 343 C1 NAGGG 601 1555 1555 1.43 LINK ND2 ASNII 343 C1 NAGII 601 1555 1555 1.43 LINK ND2 ASNKK 343 C1 NAGKK 601 1555 1555 1.44 CRYST1 108.420 108.420 165.538 90.00 90.00 120.00 P 31 18 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 0.009223 0.005325 0.000000 0.00000 SCALE2 0.000000 0.010650 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006041 0.00000