HEADER OXIDOREDUCTASE 10-APR-18 6G94
TITLE STRUCTURE OF E. COLI HYDROGENASE-1 C19G VARIANT IN COMPLEX WITH
TITLE 2 CYTOCHROME B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROGENASE-1 SMALL CHAIN;
COMPND 3 CHAIN: S, T, Q, R;
COMPND 4 SYNONYM: HYD1,MEMBRANE-BOUND HYDROGENASE 1 SMALL SUBUNIT,NIFE
COMPND 5 HYDROGENASE;
COMPND 6 EC: 1.12.99.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: C19G VARIANT;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: HYDROGENASE-1 LARGE CHAIN;
COMPND 11 CHAIN: L, M, J, K;
COMPND 12 SYNONYM: HYD1,MEMBRANE-BOUND HYDROGENASE 1 LARGE SUBUNIT,NIFE
COMPND 13 HYDROGENASE;
COMPND 14 EC: 1.12.99.6;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: PROBABLE NI/FE-HYDROGENASE 1 B-TYPE CYTOCHROME SUBUNIT;
COMPND 18 CHAIN: A, B;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: HYAA, B0972, JW0954;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 9 ORGANISM_TAXID: 83333;
SOURCE 10 STRAIN: K12;
SOURCE 11 GENE: HYAB, B0973, JW0955;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 16 ORGANISM_TAXID: 83333;
SOURCE 17 GENE: HYAC, B0974, JW0956;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NEW [4FE-4S] CLUSTER, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VOLBEDA,J.C.FONTECILLA-CAMPS
REVDAT 6 17-JAN-24 6G94 1 LINK
REVDAT 5 05-FEB-20 6G94 1 SOURCE DBREF SEQADV
REVDAT 4 21-AUG-19 6G94 1 SEQADV
REVDAT 3 04-JUL-18 6G94 1 JRNL
REVDAT 2 20-JUN-18 6G94 1 JRNL
REVDAT 1 13-JUN-18 6G94 0
JRNL AUTH A.VOLBEDA,J.M.MOUESCA,C.DARNAULT,M.M.ROESSLER,A.PARKIN,
JRNL AUTH 2 F.A.ARMSTRONG,J.C.FONTECILLA-CAMPS
JRNL TITL X-RAY STRUCTURAL, FUNCTIONAL AND COMPUTATIONAL STUDIES OF
JRNL TITL 2 THE O2-SENSITIVE E. COLI HYDROGENASE-1 C19G VARIANT REVEAL
JRNL TITL 3 AN UNUSUAL [4FE-4S] CLUSTER.
JRNL REF CHEM. COMMUN. (CAMB.) V. 54 7175 2018
JRNL REFN ESSN 1364-548X
JRNL PMID 29888350
JRNL DOI 10.1039/C8CC02896F
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.VOLBEDA,C.DARNAULT,A.PARKIN,F.SARGENT,F.A.ARMSTRONG,
REMARK 1 AUTH 2 J.C.FONTECILLA-CAMPS
REMARK 1 TITL CRYSTAL STRUCTURE OF THE O(2)-TOLERANT MEMBRANE-BOUND
REMARK 1 TITL 2 HYDROGENASE 1 FROM ESCHERICHIA COLI IN COMPLEX WITH ITS
REMARK 1 TITL 3 COGNATE CYTOCHROME B.
REMARK 1 REF STRUCTURE V. 21 184 2013
REMARK 1 REFN ISSN 1878-4186
REMARK 1 PMID 23260654
REMARK 1 DOI 10.1016/J.STR.2012.11.010
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.M.EVANS,A.PARKIN,M.M.ROESSLER,B.J.MURPHY,H.ADAMSON,
REMARK 1 AUTH 2 M.J.LUKEY,F.SARGENT,A.VOLBEDA,J.C.FONTECILLA-CAMPS,
REMARK 1 AUTH 3 F.A.ARMSTRONG
REMARK 1 TITL PRINCIPLES OF SUSTAINED ENZYMATIC HYDROGEN OXIDATION IN THE
REMARK 1 TITL 2 PRESENCE OF OXYGEN--THE CRUCIAL INFLUENCE OF HIGH POTENTIAL
REMARK 1 TITL 3 FE-S CLUSTERS IN THE ELECTRON RELAY OF [NIFE]-HYDROGENASES.
REMARK 1 REF J. AM. CHEM. SOC. V. 135 2694 2013
REMARK 1 REFN ESSN 1520-5126
REMARK 1 PMID 23398301
REMARK 1 DOI 10.1021/JA311055D
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.VOLBEDA,P.AMARA,C.DARNAULT,J.M.MOUESCA,A.PARKIN,
REMARK 1 AUTH 2 M.M.ROESSLER,F.A.ARMSTRONG,J.C.FONTECILLA-CAMPS
REMARK 1 TITL X-RAY CRYSTALLOGRAPHIC AND COMPUTATIONAL STUDIES OF THE
REMARK 1 TITL 2 O2-TOLERANT [NIFE]-HYDROGENASE 1 FROM ESCHERICHIA COLI.
REMARK 1 REF PROC. NATL. ACAD. SCI. V. 109 5305 2012
REMARK 1 REF 2 U.S.A.
REMARK 1 REFN ESSN 1091-6490
REMARK 1 PMID 22431599
REMARK 1 DOI 10.1073/PNAS.1119806109
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 136263
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 7064
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8577
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.3780
REMARK 3 BIN FREE R VALUE SET COUNT : 439
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 29537
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 218
REMARK 3 SOLVENT ATOMS : 702
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.92000
REMARK 3 B22 (A**2) : 0.40000
REMARK 3 B33 (A**2) : 0.52000
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): 0.827
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.307
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.358
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.343
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 30675 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 41735 ; 1.195 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3822 ; 4.966 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1338 ;35.659 ;23.752
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4632 ;14.582 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 173 ;17.800 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4502 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 23604 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 13
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : S T Q R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 S 6 S 15 1
REMARK 3 1 T 6 T 15 1
REMARK 3 1 Q 6 Q 15 1
REMARK 3 1 R 6 R 15 1
REMARK 3 2 S 17 S 36 1
REMARK 3 2 T 17 T 36 1
REMARK 3 2 Q 17 Q 36 1
REMARK 3 2 R 17 R 36 1
REMARK 3 3 S 40 S 57 1
REMARK 3 3 T 40 T 57 1
REMARK 3 3 Q 40 Q 57 1
REMARK 3 3 R 40 R 57 1
REMARK 3 4 S 59 S 60 1
REMARK 3 4 T 59 T 60 1
REMARK 3 4 Q 59 Q 60 1
REMARK 3 4 R 59 R 60 1
REMARK 3 5 S 62 S 65 1
REMARK 3 5 T 62 T 65 1
REMARK 3 5 Q 62 Q 65 1
REMARK 3 5 R 62 R 65 1
REMARK 3 6 S 67 S 93 1
REMARK 3 6 T 67 T 93 1
REMARK 3 6 Q 67 Q 93 1
REMARK 3 6 R 67 R 93 1
REMARK 3 7 S 95 S 102 1
REMARK 3 7 T 95 T 102 1
REMARK 3 7 Q 95 Q 102 1
REMARK 3 7 R 95 R 102 1
REMARK 3 8 S 104 S 106 1
REMARK 3 8 T 104 T 106 1
REMARK 3 8 Q 104 Q 106 1
REMARK 3 8 R 104 R 106 1
REMARK 3 9 S 112 S 124 1
REMARK 3 9 T 112 T 124 1
REMARK 3 9 Q 112 Q 124 1
REMARK 3 9 R 112 R 124 1
REMARK 3 10 S 343 S 350 1
REMARK 3 10 T 343 T 350 1
REMARK 3 10 Q 343 Q 350 1
REMARK 3 10 R 343 R 350 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 S (A): 56 ; 0.070 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 S (A): 52 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 S (A): 911 ; 0.070 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 S (A): 163 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 T (A): 163 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 Q (A): 163 ; 0.050 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 R (A): 163 ; 0.050 ; 0.050
REMARK 3 TIGHT THERMAL 1 S (A**2): 781 ; 4.410 ; 4.000
REMARK 3 TIGHT THERMAL 1 T (A**2): 781 ; 3.720 ; 4.000
REMARK 3 TIGHT THERMAL 1 Q (A**2): 781 ; 3.200 ; 4.000
REMARK 3 TIGHT THERMAL 1 R (A**2): 781 ; 4.060 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : S T Q R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 S 126 S 135 1
REMARK 3 1 T 126 T 135 1
REMARK 3 1 Q 126 Q 135 1
REMARK 3 1 R 126 R 135 1
REMARK 3 2 S 137 S 138 1
REMARK 3 2 T 137 T 138 1
REMARK 3 2 Q 137 Q 138 1
REMARK 3 2 R 137 R 138 1
REMARK 3 3 S 140 S 167 1
REMARK 3 3 T 140 T 167 1
REMARK 3 3 Q 140 Q 167 1
REMARK 3 3 R 140 R 167 1
REMARK 3 4 S 169 S 172 1
REMARK 3 4 T 169 T 172 1
REMARK 3 4 Q 169 Q 172 1
REMARK 3 4 R 169 R 172 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 2 S (A**2): 330 ; 4.970 ; 4.000
REMARK 3 TIGHT THERMAL 2 T (A**2): 330 ; 3.570 ; 4.000
REMARK 3 TIGHT THERMAL 2 Q (A**2): 330 ; 3.100 ; 4.000
REMARK 3 TIGHT THERMAL 2 R (A**2): 330 ; 4.750 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : S T Q R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 S 176 S 184 1
REMARK 3 1 T 176 T 184 1
REMARK 3 1 Q 176 Q 184 1
REMARK 3 1 R 176 R 184 1
REMARK 3 2 S 186 S 187 1
REMARK 3 2 T 186 T 187 1
REMARK 3 2 Q 186 Q 187 1
REMARK 3 2 R 186 R 187 1
REMARK 3 3 S 189 S 192 1
REMARK 3 3 T 189 T 192 1
REMARK 3 3 Q 189 Q 192 1
REMARK 3 3 R 189 R 192 1
REMARK 3 4 S 194 S 196 1
REMARK 3 4 T 194 T 196 1
REMARK 3 4 Q 194 Q 196 1
REMARK 3 4 R 194 R 196 1
REMARK 3 5 S 198 S 216 1
REMARK 3 5 T 198 T 216 1
REMARK 3 5 Q 198 Q 216 1
REMARK 3 5 R 198 R 216 1
REMARK 3 6 S 219 S 255 1
REMARK 3 6 T 219 T 255 1
REMARK 3 6 Q 219 Q 255 1
REMARK 3 6 R 219 R 255 1
REMARK 3 7 S 257 S 259 1
REMARK 3 7 T 257 T 259 1
REMARK 3 7 Q 257 Q 259 1
REMARK 3 7 R 257 R 259 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 3 S (A**2): 603 ; 3.410 ; 4.000
REMARK 3 TIGHT THERMAL 3 T (A**2): 603 ; 2.920 ; 4.000
REMARK 3 TIGHT THERMAL 3 Q (A**2): 603 ; 3.110 ; 4.000
REMARK 3 TIGHT THERMAL 3 R (A**2): 603 ; 2.850 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : S Q
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 S 261 S 265 2
REMARK 3 1 Q 261 Q 265 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 S (A): 19 ; 0.080 ; 0.500
REMARK 3 TIGHT THERMAL 4 S (A**2): 20 ; 2.260 ; 4.000
REMARK 3 MEDIUM THERMAL 4 S (A**2): 19 ; 2.150 ; 8.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : S Q
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 S 278 S 286 2
REMARK 3 1 Q 278 Q 286 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 5 S (A): 22 ; 0.070 ; 0.500
REMARK 3 TIGHT THERMAL 5 S (A**2): 36 ; 2.590 ; 4.000
REMARK 3 MEDIUM THERMAL 5 S (A**2): 22 ; 4.020 ; 8.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : L M J K
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 7 L 10 1
REMARK 3 1 M 7 M 10 1
REMARK 3 1 J 7 J 10 1
REMARK 3 1 K 7 K 10 1
REMARK 3 2 L 12 L 15 1
REMARK 3 2 M 12 M 15 1
REMARK 3 2 J 12 J 15 1
REMARK 3 2 K 12 K 15 1
REMARK 3 3 L 19 L 38 1
REMARK 3 3 M 19 M 38 1
REMARK 3 3 J 19 J 38 1
REMARK 3 3 K 19 K 38 1
REMARK 3 4 L 41 L 60 1
REMARK 3 4 M 41 M 60 1
REMARK 3 4 J 41 J 60 1
REMARK 3 4 K 41 K 60 1
REMARK 3 5 L 64 L 138 1
REMARK 3 5 M 64 M 138 1
REMARK 3 5 J 64 J 138 1
REMARK 3 5 K 64 K 138 1
REMARK 3 6 L 145 L 146 1
REMARK 3 6 M 145 M 146 1
REMARK 3 6 J 145 J 146 1
REMARK 3 6 K 145 K 146 1
REMARK 3 7 L 148 L 149 1
REMARK 3 7 M 148 M 149 1
REMARK 3 7 J 148 J 149 1
REMARK 3 7 K 148 K 149 1
REMARK 3 8 L 151 L 153 1
REMARK 3 8 M 151 M 153 1
REMARK 3 8 J 151 J 153 1
REMARK 3 8 K 151 K 153 1
REMARK 3 9 L 155 L 168 1
REMARK 3 9 M 155 M 168 1
REMARK 3 9 J 155 J 168 1
REMARK 3 9 K 155 K 168 1
REMARK 3 10 L 173 L 174 1
REMARK 3 10 M 173 M 174 1
REMARK 3 10 J 173 J 174 1
REMARK 3 10 K 173 K 174 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 6 L (A**2): 1139 ; 3.570 ; 4.000
REMARK 3 TIGHT THERMAL 6 M (A**2): 1139 ; 3.470 ; 4.000
REMARK 3 TIGHT THERMAL 6 J (A**2): 1139 ; 2.700 ; 4.000
REMARK 3 TIGHT THERMAL 6 K (A**2): 1139 ; 3.030 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : L M J K
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 176 L 182 1
REMARK 3 1 M 176 M 182 1
REMARK 3 1 J 176 J 182 1
REMARK 3 1 K 176 K 182 1
REMARK 3 2 L 185 L 244 1
REMARK 3 2 M 185 M 244 1
REMARK 3 2 J 185 J 244 1
REMARK 3 2 K 185 K 244 1
REMARK 3 3 L 247 L 255 1
REMARK 3 3 M 247 M 255 1
REMARK 3 3 J 247 J 255 1
REMARK 3 3 K 247 K 255 1
REMARK 3 4 L 257 L 268 1
REMARK 3 4 M 257 M 268 1
REMARK 3 4 J 257 J 268 1
REMARK 3 4 K 257 K 268 1
REMARK 3 5 L 270 L 279 1
REMARK 3 5 M 270 M 279 1
REMARK 3 5 J 270 J 279 1
REMARK 3 5 K 270 K 279 1
REMARK 3 6 L 281 L 283 1
REMARK 3 6 M 281 M 283 1
REMARK 3 6 J 281 J 283 1
REMARK 3 6 K 281 K 283 1
REMARK 3 7 L 288 L 290 1
REMARK 3 7 M 288 M 290 1
REMARK 3 7 J 288 J 290 1
REMARK 3 7 K 288 K 290 1
REMARK 3 8 L 292 L 315 1
REMARK 3 8 M 292 M 315 1
REMARK 3 8 J 292 J 315 1
REMARK 3 8 K 292 K 315 1
REMARK 3 9 L 318 L 331 1
REMARK 3 9 M 318 M 331 1
REMARK 3 9 J 318 J 331 1
REMARK 3 9 K 318 K 331 1
REMARK 3 10 L 334 L 342 1
REMARK 3 10 M 334 M 342 1
REMARK 3 10 J 334 J 342 1
REMARK 3 10 K 334 K 342 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 7 L (A**2): 1132 ; 3.240 ; 4.000
REMARK 3 TIGHT THERMAL 7 M (A**2): 1132 ; 3.040 ; 4.000
REMARK 3 TIGHT THERMAL 7 J (A**2): 1132 ; 3.350 ; 4.000
REMARK 3 TIGHT THERMAL 7 K (A**2): 1132 ; 3.100 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : L M J K
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 344 L 354 1
REMARK 3 1 M 344 M 354 1
REMARK 3 1 J 344 J 354 1
REMARK 3 1 K 344 K 354 1
REMARK 3 2 L 356 L 371 1
REMARK 3 2 M 356 M 371 1
REMARK 3 2 J 356 J 371 1
REMARK 3 2 K 356 K 371 1
REMARK 3 3 L 395 L 428 1
REMARK 3 3 M 395 M 428 1
REMARK 3 3 J 395 J 428 1
REMARK 3 3 K 395 K 428 1
REMARK 3 4 L 443 L 471 1
REMARK 3 4 M 443 M 471 1
REMARK 3 4 J 443 J 471 1
REMARK 3 4 K 443 K 471 1
REMARK 3 5 L 473 L 486 1
REMARK 3 5 M 473 M 486 1
REMARK 3 5 J 473 J 486 1
REMARK 3 5 K 473 K 486 1
REMARK 3 6 L 490 L 497 1
REMARK 3 6 M 490 M 497 1
REMARK 3 6 J 490 J 497 1
REMARK 3 6 K 490 K 497 1
REMARK 3 7 L 499 L 499 1
REMARK 3 7 M 499 M 499 1
REMARK 3 7 J 499 J 499 1
REMARK 3 7 K 499 K 499 1
REMARK 3 8 L 501 L 518 1
REMARK 3 8 M 501 M 518 1
REMARK 3 8 J 501 J 518 1
REMARK 3 8 K 501 K 518 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 8 L (A**2): 1031 ; 3.170 ; 4.000
REMARK 3 TIGHT THERMAL 8 M (A**2): 1031 ; 3.500 ; 4.000
REMARK 3 TIGHT THERMAL 8 J (A**2): 1031 ; 3.420 ; 4.000
REMARK 3 TIGHT THERMAL 8 K (A**2): 1031 ; 3.240 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : L M J K
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 521 L 522 1
REMARK 3 1 M 521 M 522 1
REMARK 3 1 J 521 J 522 1
REMARK 3 1 K 521 K 522 1
REMARK 3 2 L 526 L 541 1
REMARK 3 2 M 526 M 541 1
REMARK 3 2 J 526 J 541 1
REMARK 3 2 K 526 K 541 1
REMARK 3 3 L 543 L 558 1
REMARK 3 3 M 543 M 558 1
REMARK 3 3 J 543 J 558 1
REMARK 3 3 K 543 K 558 1
REMARK 3 4 L 563 L 590 1
REMARK 3 4 M 563 M 590 1
REMARK 3 4 J 563 J 590 1
REMARK 3 4 K 563 K 590 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 9 L (A**2): 425 ; 3.790 ; 4.000
REMARK 3 TIGHT THERMAL 9 M (A**2): 425 ; 3.550 ; 4.000
REMARK 3 TIGHT THERMAL 9 J (A**2): 425 ; 3.040 ; 4.000
REMARK 3 TIGHT THERMAL 9 K (A**2): 425 ; 2.850 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : T R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 T 261 T 272 2
REMARK 3 1 R 261 R 272 2
REMARK 3 2 T 274 T 275 2
REMARK 3 2 R 274 R 275 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 10 T (A): 51 ; 0.100 ; 0.500
REMARK 3 TIGHT THERMAL 10 T (A**2): 56 ; 2.680 ; 4.000
REMARK 3 MEDIUM THERMAL 10 T (A**2): 51 ; 3.200 ; 8.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : T R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 T 278 T 283 2
REMARK 3 1 R 278 R 283 2
REMARK 3 2 T 285 T 286 2
REMARK 3 2 R 285 R 286 2
REMARK 3 3 T 288 T 288 2
REMARK 3 3 R 288 R 288 2
REMARK 3 4 T 290 T 293 2
REMARK 3 4 R 290 R 293 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 11 T (A): 24 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 11 T (A**2): 52 ; 1.910 ; 4.000
REMARK 3 MEDIUM THERMAL 11 T (A**2): 24 ; 1.800 ; 8.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 23 A 73 1
REMARK 3 1 B 23 B 73 1
REMARK 3 2 A 131 A 132 1
REMARK 3 2 B 131 B 132 1
REMARK 3 3 A 134 A 151 1
REMARK 3 3 B 134 B 151 1
REMARK 3 4 A 159 A 163 1
REMARK 3 4 B 159 B 163 1
REMARK 3 5 A 165 A 187 1
REMARK 3 5 B 165 B 187 1
REMARK 3 6 A 189 A 195 1
REMARK 3 6 B 189 B 195 1
REMARK 3 7 A 301 A 317 1
REMARK 3 7 B 301 B 317 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 12 Q (A**2): 911 ; 3.010 ; 4.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 1 E 49 1
REMARK 3 1 F 1 F 49 1
REMARK 3 1 G 1 G 49 1
REMARK 3 1 H 1 H 49 1
REMARK 3 2 E 51 E 56 1
REMARK 3 2 F 51 F 56 1
REMARK 3 2 G 51 G 56 1
REMARK 3 2 H 51 H 56 1
REMARK 3 3 E 58 E 88 1
REMARK 3 3 F 58 F 88 1
REMARK 3 3 G 58 G 88 1
REMARK 3 3 H 58 H 88 1
REMARK 3 4 E 90 E 120 1
REMARK 3 4 F 90 F 120 1
REMARK 3 4 G 90 G 120 1
REMARK 3 4 H 90 H 120 1
REMARK 3 5 E 122 E 161 1
REMARK 3 5 F 122 F 161 1
REMARK 3 5 G 122 G 161 1
REMARK 3 5 H 122 H 161 1
REMARK 3 6 E 163 E 164 1
REMARK 3 6 F 163 F 164 1
REMARK 3 6 G 163 G 164 1
REMARK 3 6 H 163 H 164 1
REMARK 3 7 E 167 E 171 1
REMARK 3 7 F 167 F 171 1
REMARK 3 7 G 167 G 171 1
REMARK 3 7 H 167 H 171 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 13 Q (A**2): 163 ; 2.190 ; 4.000
REMARK 3 TIGHT THERMAL 13 S (A**2): 163 ; 2.250 ; 4.000
REMARK 3 TIGHT THERMAL 13 T (A**2): 163 ; 2.460 ; 4.000
REMARK 3 TIGHT THERMAL 13 R (A**2): 163 ; 2.370 ; 4.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 3 S 172
REMARK 3 RESIDUE RANGE : S 343 S 343
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7890 24.5190 -11.5840
REMARK 3 T TENSOR
REMARK 3 T11: 0.5572 T22: 0.1773
REMARK 3 T33: 0.0246 T12: 0.0363
REMARK 3 T13: -0.0033 T23: -0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 0.9040 L22: 1.0690
REMARK 3 L33: 1.0699 L12: 0.2423
REMARK 3 L13: -0.0670 L23: -0.2740
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: -0.0381 S13: -0.0302
REMARK 3 S21: 0.1275 S22: 0.0546 S23: -0.0666
REMARK 3 S31: -0.0095 S32: 0.1684 S33: -0.0737
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 173 S 266
REMARK 3 RESIDUE RANGE : S 341 S 342
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8680 22.2080 -32.5000
REMARK 3 T TENSOR
REMARK 3 T11: 0.5420 T22: 0.1493
REMARK 3 T33: 0.0617 T12: 0.0085
REMARK 3 T13: 0.0033 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 1.0395 L22: 0.6916
REMARK 3 L33: 1.4660 L12: -0.1291
REMARK 3 L13: 0.8026 L23: -0.2107
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: 0.0926 S13: -0.0232
REMARK 3 S21: -0.0468 S22: 0.0183 S23: 0.0555
REMARK 3 S31: -0.0560 S32: -0.0225 S33: -0.0343
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 2 L 582
REMARK 3 RESIDUE RANGE : L 583 L 590
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8300 35.0570 -3.6330
REMARK 3 T TENSOR
REMARK 3 T11: 0.5774 T22: 0.1433
REMARK 3 T33: 0.0323 T12: 0.0346
REMARK 3 T13: 0.0191 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.1023 L22: 0.7384
REMARK 3 L33: 0.6548 L12: 0.0523
REMARK 3 L13: 0.1383 L23: 0.1326
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: -0.0524 S13: 0.0033
REMARK 3 S21: 0.0284 S22: -0.0123 S23: 0.0359
REMARK 3 S31: -0.1140 S32: -0.0868 S33: 0.0241
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 4 T 172
REMARK 3 RESIDUE RANGE : T 343 T 343
REMARK 3 ORIGIN FOR THE GROUP (A): -39.5030 -6.2870 -22.5170
REMARK 3 T TENSOR
REMARK 3 T11: 0.5450 T22: 0.2586
REMARK 3 T33: 0.1441 T12: -0.0454
REMARK 3 T13: -0.0396 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.7095 L22: 1.4579
REMARK 3 L33: 0.9238 L12: 0.4648
REMARK 3 L13: -0.2274 L23: 0.1847
REMARK 3 S TENSOR
REMARK 3 S11: 0.0465 S12: -0.0283 S13: 0.0368
REMARK 3 S21: -0.0024 S22: 0.0151 S23: 0.2127
REMARK 3 S31: 0.0982 S32: -0.2686 S33: -0.0616
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 173 T 266
REMARK 3 RESIDUE RANGE : T 341 T 342
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8450 1.8680 -36.4650
REMARK 3 T TENSOR
REMARK 3 T11: 0.5457 T22: 0.1564
REMARK 3 T33: 0.1000 T12: -0.0140
REMARK 3 T13: -0.0048 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.9206 L22: 0.8217
REMARK 3 L33: 0.9569 L12: 0.5620
REMARK 3 L13: -0.7807 L23: -0.1033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0625 S12: 0.0676 S13: 0.0045
REMARK 3 S21: -0.0299 S22: 0.0252 S23: 0.0565
REMARK 3 S31: 0.0333 S32: -0.0887 S33: 0.0373
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 2 M 582
REMARK 3 RESIDUE RANGE : M 583 M 590
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1180 -19.4800 -13.2970
REMARK 3 T TENSOR
REMARK 3 T11: 0.6419 T22: 0.1182
REMARK 3 T33: 0.0559 T12: -0.0467
REMARK 3 T13: -0.0184 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.2727 L22: 0.6490
REMARK 3 L33: 0.6379 L12: 0.2141
REMARK 3 L13: -0.0787 L23: 0.0880
REMARK 3 S TENSOR
REMARK 3 S11: 0.0350 S12: -0.0488 S13: -0.0208
REMARK 3 S21: 0.0717 S22: -0.0126 S23: 0.0055
REMARK 3 S31: 0.2099 S32: -0.0751 S33: -0.0225
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 4 Q 172
REMARK 3 RESIDUE RANGE : Q 343 Q 343
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7420 -14.4330 -20.0570
REMARK 3 T TENSOR
REMARK 3 T11: 0.6659 T22: 0.1396
REMARK 3 T33: 0.0372 T12: 0.0074
REMARK 3 T13: -0.0111 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 0.5055 L22: 0.6587
REMARK 3 L33: 0.7176 L12: -0.0512
REMARK 3 L13: 0.2097 L23: 0.2176
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -0.1038 S13: -0.0855
REMARK 3 S21: 0.1875 S22: -0.0080 S23: 0.0364
REMARK 3 S31: 0.0097 S32: 0.0254 S33: 0.0061
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 173 Q 266
REMARK 3 RESIDUE RANGE : Q 341 Q 342
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8100 -12.2650 -47.0790
REMARK 3 T TENSOR
REMARK 3 T11: 0.6040 T22: 0.1328
REMARK 3 T33: 0.0409 T12: -0.0056
REMARK 3 T13: 0.0137 T23: -0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 0.8983 L22: 1.2375
REMARK 3 L33: 1.0311 L12: 0.0068
REMARK 3 L13: 0.1984 L23: 0.0155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: 0.0155 S13: -0.0147
REMARK 3 S21: -0.1701 S22: 0.0025 S23: 0.1459
REMARK 3 S31: 0.0108 S32: 0.0808 S33: -0.0209
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 2 J 582
REMARK 3 RESIDUE RANGE : J 583 J 590
REMARK 3 ORIGIN FOR THE GROUP (A): 44.6380 -24.6630 -30.0430
REMARK 3 T TENSOR
REMARK 3 T11: 0.6261 T22: 0.1627
REMARK 3 T33: 0.0729 T12: 0.0536
REMARK 3 T13: -0.0128 T23: -0.0740
REMARK 3 L TENSOR
REMARK 3 L11: 0.3270 L22: 0.4814
REMARK 3 L33: 0.5126 L12: -0.1001
REMARK 3 L13: 0.1814 L23: -0.1475
REMARK 3 S TENSOR
REMARK 3 S11: 0.0492 S12: 0.0459 S13: -0.0606
REMARK 3 S21: 0.0119 S22: -0.0329 S23: -0.0814
REMARK 3 S31: 0.0967 S32: 0.1445 S33: -0.0163
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 4 R 172
REMARK 3 RESIDUE RANGE : R 343 R 343
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6170 16.3180 -61.4590
REMARK 3 T TENSOR
REMARK 3 T11: 0.6616 T22: 0.2834
REMARK 3 T33: 0.0274 T12: -0.0223
REMARK 3 T13: 0.0924 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.9124 L22: 1.0581
REMARK 3 L33: 0.7962 L12: 0.3504
REMARK 3 L13: 0.1473 L23: -0.3543
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: 0.1974 S13: -0.1144
REMARK 3 S21: -0.1984 S22: 0.0680 S23: -0.0885
REMARK 3 S31: 0.0045 S32: 0.2123 S33: -0.0203
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 173 R 266
REMARK 3 RESIDUE RANGE : R 341 R 342
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7040 7.9790 -54.4020
REMARK 3 T TENSOR
REMARK 3 T11: 0.6122 T22: 0.1572
REMARK 3 T33: 0.0282 T12: -0.0036
REMARK 3 T13: 0.0295 T23: -0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 1.5226 L22: 0.5288
REMARK 3 L33: 0.9023 L12: 0.3121
REMARK 3 L13: -0.4926 L23: 0.1271
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: 0.0795 S13: 0.0111
REMARK 3 S21: -0.1066 S22: -0.0091 S23: 0.0855
REMARK 3 S31: -0.0100 S32: 0.0546 S33: -0.0267
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 2 K 582
REMARK 3 RESIDUE RANGE : K 583 K 590
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0820 29.5160 -41.6030
REMARK 3 T TENSOR
REMARK 3 T11: 0.6331 T22: 0.1804
REMARK 3 T33: 0.0124 T12: -0.0313
REMARK 3 T13: 0.0219 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.3641 L22: 0.6865
REMARK 3 L33: 0.2975 L12: 0.1457
REMARK 3 L13: 0.1002 L23: -0.1760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0112 S12: 0.0509 S13: 0.0035
REMARK 3 S21: -0.0017 S22: -0.0422 S23: -0.0492
REMARK 3 S31: -0.0731 S32: 0.1157 S33: 0.0534
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 267 S 297
REMARK 3 RESIDUE RANGE : T 267 T 299
REMARK 3 RESIDUE RANGE : A 14 A 89
REMARK 3 RESIDUE RANGE : A 100 A 113
REMARK 3 RESIDUE RANGE : A 126 A 207
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9040 3.6460 -61.5890
REMARK 3 T TENSOR
REMARK 3 T11: 0.6772 T22: 0.2505
REMARK 3 T33: 0.0928 T12: 0.0129
REMARK 3 T13: -0.0231 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.1402 L22: 1.0184
REMARK 3 L33: 0.7702 L12: 0.4603
REMARK 3 L13: 0.2173 L23: -0.0022
REMARK 3 S TENSOR
REMARK 3 S11: -0.0170 S12: 0.1724 S13: -0.0086
REMARK 3 S21: -0.2500 S22: -0.0038 S23: 0.1674
REMARK 3 S31: 0.0592 S32: -0.1237 S33: 0.0208
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 267 Q 298
REMARK 3 RESIDUE RANGE : R 267 R 294
REMARK 3 RESIDUE RANGE : B 14 B 83
REMARK 3 RESIDUE RANGE : B 101 B 114
REMARK 3 RESIDUE RANGE : B 127 B 202
REMARK 3 RESIDUE RANGE : B 301 B 301
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9150 4.9450 -75.4450
REMARK 3 T TENSOR
REMARK 3 T11: 0.6781 T22: 0.2538
REMARK 3 T33: 0.0818 T12: 0.0045
REMARK 3 T13: -0.0448 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.5145 L22: 1.4136
REMARK 3 L33: 1.5606 L12: 0.6991
REMARK 3 L13: -0.4526 L23: -0.2116
REMARK 3 S TENSOR
REMARK 3 S11: -0.0547 S12: 0.1767 S13: 0.0814
REMARK 3 S21: -0.1824 S22: 0.0912 S23: 0.2374
REMARK 3 S31: -0.0292 S32: 0.0540 S33: -0.0366
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6G94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.32
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146009
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 49.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.30500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 2.19400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: 4GD3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, NAAC, NH4AC, DTT, DMM, PH
REMARK 280 5.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 62.20500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.11000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.51500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.11000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.20500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 82.51500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, L, T, M, Q, J, R, K, A, B
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 LEU S 1
REMARK 465 GLU S 2
REMARK 465 VAL S 299
REMARK 465 ALA S 300
REMARK 465 SER S 301
REMARK 465 ALA S 302
REMARK 465 VAL S 303
REMARK 465 ASP S 304
REMARK 465 GLN S 305
REMARK 465 ARG S 306
REMARK 465 ARG S 307
REMARK 465 ARG S 308
REMARK 465 HIS S 309
REMARK 465 ASN S 310
REMARK 465 GLN S 311
REMARK 465 GLN S 312
REMARK 465 PRO S 313
REMARK 465 THR S 314
REMARK 465 GLU S 315
REMARK 465 THR S 316
REMARK 465 GLU S 317
REMARK 465 HIS S 318
REMARK 465 GLN S 319
REMARK 465 PRO S 320
REMARK 465 GLY S 321
REMARK 465 ASN S 322
REMARK 465 GLU S 323
REMARK 465 ASP S 324
REMARK 465 LYS S 325
REMARK 465 GLN S 326
REMARK 465 ALA S 327
REMARK 465 ARG S 328
REMARK 465 SER S 329
REMARK 465 HIS S 330
REMARK 465 HIS S 331
REMARK 465 HIS S 332
REMARK 465 HIS S 333
REMARK 465 HIS S 334
REMARK 465 HIS S 335
REMARK 465 MET L 1
REMARK 465 LEU T 1
REMARK 465 GLU T 2
REMARK 465 ASN T 3
REMARK 465 ALA T 300
REMARK 465 SER T 301
REMARK 465 ALA T 302
REMARK 465 VAL T 303
REMARK 465 ASP T 304
REMARK 465 GLN T 305
REMARK 465 ARG T 306
REMARK 465 ARG T 307
REMARK 465 ARG T 308
REMARK 465 HIS T 309
REMARK 465 ASN T 310
REMARK 465 GLN T 311
REMARK 465 GLN T 312
REMARK 465 PRO T 313
REMARK 465 THR T 314
REMARK 465 GLU T 315
REMARK 465 THR T 316
REMARK 465 GLU T 317
REMARK 465 HIS T 318
REMARK 465 GLN T 319
REMARK 465 PRO T 320
REMARK 465 GLY T 321
REMARK 465 ASN T 322
REMARK 465 GLU T 323
REMARK 465 ASP T 324
REMARK 465 LYS T 325
REMARK 465 GLN T 326
REMARK 465 ALA T 327
REMARK 465 ARG T 328
REMARK 465 SER T 329
REMARK 465 HIS T 330
REMARK 465 HIS T 331
REMARK 465 HIS T 332
REMARK 465 HIS T 333
REMARK 465 HIS T 334
REMARK 465 HIS T 335
REMARK 465 MET M 1
REMARK 465 LEU Q 1
REMARK 465 GLU Q 2
REMARK 465 ASN Q 3
REMARK 465 VAL Q 299
REMARK 465 ALA Q 300
REMARK 465 SER Q 301
REMARK 465 ALA Q 302
REMARK 465 VAL Q 303
REMARK 465 ASP Q 304
REMARK 465 GLN Q 305
REMARK 465 ARG Q 306
REMARK 465 ARG Q 307
REMARK 465 ARG Q 308
REMARK 465 HIS Q 309
REMARK 465 ASN Q 310
REMARK 465 GLN Q 311
REMARK 465 GLN Q 312
REMARK 465 PRO Q 313
REMARK 465 THR Q 314
REMARK 465 GLU Q 315
REMARK 465 THR Q 316
REMARK 465 GLU Q 317
REMARK 465 HIS Q 318
REMARK 465 GLN Q 319
REMARK 465 PRO Q 320
REMARK 465 GLY Q 321
REMARK 465 ASN Q 322
REMARK 465 GLU Q 323
REMARK 465 ASP Q 324
REMARK 465 LYS Q 325
REMARK 465 GLN Q 326
REMARK 465 ALA Q 327
REMARK 465 ARG Q 328
REMARK 465 SER Q 329
REMARK 465 HIS Q 330
REMARK 465 HIS Q 331
REMARK 465 HIS Q 332
REMARK 465 HIS Q 333
REMARK 465 HIS Q 334
REMARK 465 HIS Q 335
REMARK 465 MET J 1
REMARK 465 LEU R 1
REMARK 465 GLU R 2
REMARK 465 ASN R 3
REMARK 465 GLY R 295
REMARK 465 VAL R 296
REMARK 465 HIS R 297
REMARK 465 ALA R 298
REMARK 465 VAL R 299
REMARK 465 ALA R 300
REMARK 465 SER R 301
REMARK 465 ALA R 302
REMARK 465 VAL R 303
REMARK 465 ASP R 304
REMARK 465 GLN R 305
REMARK 465 ARG R 306
REMARK 465 ARG R 307
REMARK 465 ARG R 308
REMARK 465 HIS R 309
REMARK 465 ASN R 310
REMARK 465 GLN R 311
REMARK 465 GLN R 312
REMARK 465 PRO R 313
REMARK 465 THR R 314
REMARK 465 GLU R 315
REMARK 465 THR R 316
REMARK 465 GLU R 317
REMARK 465 HIS R 318
REMARK 465 GLN R 319
REMARK 465 PRO R 320
REMARK 465 GLY R 321
REMARK 465 ASN R 322
REMARK 465 GLU R 323
REMARK 465 ASP R 324
REMARK 465 LYS R 325
REMARK 465 GLN R 326
REMARK 465 ALA R 327
REMARK 465 ARG R 328
REMARK 465 SER R 329
REMARK 465 HIS R 330
REMARK 465 HIS R 331
REMARK 465 HIS R 332
REMARK 465 HIS R 333
REMARK 465 HIS R 334
REMARK 465 HIS R 335
REMARK 465 MET K 1
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 4
REMARK 465 SER A 5
REMARK 465 ASP A 6
REMARK 465 ASN A 7
REMARK 465 VAL A 8
REMARK 465 VAL A 9
REMARK 465 SER A 10
REMARK 465 HIS A 11
REMARK 465 TYR A 12
REMARK 465 VAL A 13
REMARK 465 GLU A 90
REMARK 465 LEU A 91
REMARK 465 PHE A 92
REMARK 465 ILE A 93
REMARK 465 VAL A 94
REMARK 465 PRO A 95
REMARK 465 VAL A 96
REMARK 465 TRP A 97
REMARK 465 ARG A 98
REMARK 465 LYS A 99
REMARK 465 PHE A 114
REMARK 465 LEU A 115
REMARK 465 ALA A 116
REMARK 465 LYS A 117
REMARK 465 ARG A 118
REMARK 465 PRO A 119
REMARK 465 SER A 120
REMARK 465 ALA A 121
REMARK 465 ASP A 122
REMARK 465 ILE A 123
REMARK 465 GLY A 124
REMARK 465 HIS A 125
REMARK 465 MET A 208
REMARK 465 SER A 209
REMARK 465 ASP A 210
REMARK 465 ASP A 211
REMARK 465 THR A 212
REMARK 465 VAL A 213
REMARK 465 ILE A 214
REMARK 465 SER A 215
REMARK 465 THR A 216
REMARK 465 MET A 217
REMARK 465 VAL A 218
REMARK 465 ASN A 219
REMARK 465 GLY A 220
REMARK 465 TYR A 221
REMARK 465 ARG A 222
REMARK 465 SER A 223
REMARK 465 HIS A 224
REMARK 465 LYS A 225
REMARK 465 PHE A 226
REMARK 465 GLY A 227
REMARK 465 LYS A 228
REMARK 465 ILE A 229
REMARK 465 SER A 230
REMARK 465 ASN A 231
REMARK 465 LYS A 232
REMARK 465 GLU A 233
REMARK 465 ARG A 234
REMARK 465 SER A 235
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 GLN B 3
REMARK 465 LYS B 4
REMARK 465 SER B 5
REMARK 465 ASP B 6
REMARK 465 ASN B 7
REMARK 465 VAL B 8
REMARK 465 VAL B 9
REMARK 465 SER B 10
REMARK 465 HIS B 11
REMARK 465 TYR B 12
REMARK 465 VAL B 13
REMARK 465 GLY B 84
REMARK 465 ASN B 85
REMARK 465 ARG B 86
REMARK 465 TYR B 87
REMARK 465 SER B 88
REMARK 465 ARG B 89
REMARK 465 GLU B 90
REMARK 465 LEU B 91
REMARK 465 PHE B 92
REMARK 465 ILE B 93
REMARK 465 VAL B 94
REMARK 465 PRO B 95
REMARK 465 VAL B 96
REMARK 465 TRP B 97
REMARK 465 ARG B 98
REMARK 465 LYS B 99
REMARK 465 SER B 100
REMARK 465 LEU B 115
REMARK 465 ALA B 116
REMARK 465 LYS B 117
REMARK 465 ARG B 118
REMARK 465 PRO B 119
REMARK 465 SER B 120
REMARK 465 ALA B 121
REMARK 465 ASP B 122
REMARK 465 ILE B 123
REMARK 465 GLY B 124
REMARK 465 HIS B 125
REMARK 465 ASN B 126
REMARK 465 LEU B 203
REMARK 465 ARG B 204
REMARK 465 GLU B 205
REMARK 465 ASP B 206
REMARK 465 ILE B 207
REMARK 465 MET B 208
REMARK 465 SER B 209
REMARK 465 ASP B 210
REMARK 465 ASP B 211
REMARK 465 THR B 212
REMARK 465 VAL B 213
REMARK 465 ILE B 214
REMARK 465 SER B 215
REMARK 465 THR B 216
REMARK 465 MET B 217
REMARK 465 VAL B 218
REMARK 465 ASN B 219
REMARK 465 GLY B 220
REMARK 465 TYR B 221
REMARK 465 ARG B 222
REMARK 465 SER B 223
REMARK 465 HIS B 224
REMARK 465 LYS B 225
REMARK 465 PHE B 226
REMARK 465 GLY B 227
REMARK 465 LYS B 228
REMARK 465 ILE B 229
REMARK 465 SER B 230
REMARK 465 ASN B 231
REMARK 465 LYS B 232
REMARK 465 GLU B 233
REMARK 465 ARG B 234
REMARK 465 SER B 235
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS S 4 CG CD CE NZ
REMARK 470 ARG S 125 NE CZ NH1 NH2
REMARK 470 ARG L 143 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 169 CG CD NE CZ NH1 NH2
REMARK 470 GLU L 175 CG CD OE1 OE2
REMARK 470 LYS L 317 CG CD CE NZ
REMARK 470 ARG L 433 NE CZ NH1 NH2
REMARK 470 LYS L 542 CE NZ
REMARK 470 LYS T 4 CG CD CE NZ
REMARK 470 GLU T 61 CG CD OE1 OE2
REMARK 470 GLN T 66 CG CD OE1 NE2
REMARK 470 LYS T 70 CG CD CE NZ
REMARK 470 ARG T 93 NE CZ NH1 NH2
REMARK 470 ARG T 101 CD NE CZ NH1 NH2
REMARK 470 VAL T 296 CG1 CG2
REMARK 470 VAL T 299 CG1 CG2
REMARK 470 ASP M 39 OD1 OD2
REMARK 470 ARG M 143 CD NE CZ NH1 NH2
REMARK 470 LYS M 144 CD CE NZ
REMARK 470 GLU M 147 CG CD OE1 OE2
REMARK 470 ARG M 169 CG CD NE CZ NH1 NH2
REMARK 470 GLU M 175 CD OE1 OE2
REMARK 470 GLN M 392 CD OE1 NE2
REMARK 470 ARG M 519 CD NE CZ NH1 NH2
REMARK 470 GLU M 561 CD OE1 OE2
REMARK 470 LYS Q 4 CG CD CE NZ
REMARK 470 ARG Q 125 NE CZ NH1 NH2
REMARK 470 LYS J 172 CG CD CE NZ
REMARK 470 ASN J 332 OD1 ND2
REMARK 470 ASP J 378 OD1 OD2
REMARK 470 LYS J 380 CD CE NZ
REMARK 470 GLU J 488 CD OE1 OE2
REMARK 470 ARG J 519 NE CZ NH1 NH2
REMARK 470 LYS R 4 CB CG CD CE NZ
REMARK 470 LYS R 70 CD CE NZ
REMARK 470 LYS R 98 CD CE NZ
REMARK 470 VAL R 294 CG1 CG2
REMARK 470 ARG K 143 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 172 CD CE NZ
REMARK 470 LYS K 287 CE NZ
REMARK 470 LYS K 380 CD CE NZ
REMARK 470 GLN K 392 CD OE1 NE2
REMARK 470 GLU K 393 CD OE1 OE2
REMARK 470 PHE A 14 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 18 CG1 CG2
REMARK 470 ARG A 19 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 86 CB CG CD NE CZ NH1 NH2
REMARK 470 SER A 88 CB OG
REMARK 470 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 470 SER A 100 OG
REMARK 470 TRP A 101 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 101 CZ3 CH2
REMARK 470 TRP A 102 CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP A 102 CH2
REMARK 470 GLN A 103 CG CD OE1 NE2
REMARK 470 VAL A 105 CG1 CG2
REMARK 470 ILE A 109 CG1 CG2 CD1
REMARK 470 ARG A 110 NE CZ NH1 NH2
REMARK 470 TRP A 111 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 111 CZ3 CH2
REMARK 470 TYR A 112 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 113 CG CD1 CD2
REMARK 470 ASN A 126 CG OD1 ND2
REMARK 470 PRO A 127 CG CD
REMARK 470 ILE A 128 CG1 CG2 CD1
REMARK 470 GLN A 130 CG CD OE1 NE2
REMARK 470 MET A 133 CG SD CE
REMARK 470 SER A 152 OG
REMARK 470 GLU A 153 CG CD OE1 OE2
REMARK 470 HIS A 154 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 155 OG
REMARK 470 GLN A 156 CG CD OE1 NE2
REMARK 470 TYR A 157 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A 200 OH
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 205 CG CD OE1 OE2
REMARK 470 ASP A 206 CG OD1 OD2
REMARK 470 ILE A 207 CG1 CG2 CD1
REMARK 470 PHE B 14 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL B 18 CG1 CG2
REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 74 CD1 CD2
REMARK 470 LEU B 75 CG CD1 CD2
REMARK 470 TYR B 79 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP B 80 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP B 80 CZ2 CZ3 CH2
REMARK 470 ALA B 81 CB
REMARK 470 PHE B 82 CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP B 101 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 101 CZ3 CH2
REMARK 470 PRO B 127 CB CG CD
REMARK 470 ILE B 128 CG1 CG2 CD1
REMARK 470 GLN B 130 CG CD OE1 NE2
REMARK 470 MET B 133 CG SD CE
REMARK 470 SER B 152 OG
REMARK 470 GLU B 153 CG CD OE1 OE2
REMARK 470 HIS B 154 CB CG ND1 CD2 CE1 NE2
REMARK 470 SER B 155 OG
REMARK 470 GLN B 156 CG CD OE1 NE2
REMARK 470 TYR B 157 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 196 CB CG1 CG2 CD1
REMARK 470 VAL B 199 CG1 CG2
REMARK 470 TYR B 200 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET B 201 SD CE
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 HIS S 29 107.34 -164.66
REMARK 500 ASP S 45 102.58 -171.12
REMARK 500 TYR S 67 30.96 -89.87
REMARK 500 CYS S 120 -151.47 54.91
REMARK 500 VAL S 146 76.39 -118.07
REMARK 500 SER S 232 -63.33 -109.16
REMARK 500 ARG S 234 178.53 71.26
REMARK 500 ARG S 260 38.52 -97.84
REMARK 500 HIS S 297 172.54 -58.47
REMARK 500 CYS L 79 45.20 -87.57
REMARK 500 LEU L 126 -64.93 -103.44
REMARK 500 SER L 158 13.83 -150.23
REMARK 500 HIS L 229 61.83 67.17
REMARK 500 LYS L 299 -62.58 -123.77
REMARK 500 GLN L 344 -82.78 -92.43
REMARK 500 GLU L 393 -128.81 -116.29
REMARK 500 PRO L 563 42.92 -79.99
REMARK 500 HIS T 29 108.08 -163.66
REMARK 500 ASP T 45 104.47 -168.09
REMARK 500 CYS T 120 -154.72 55.63
REMARK 500 VAL T 146 78.98 -116.14
REMARK 500 ARG T 234 -176.14 68.12
REMARK 500 GLN T 272 8.96 -69.91
REMARK 500 ALA T 298 28.61 -71.72
REMARK 500 ASN M 38 -163.47 -75.57
REMARK 500 LEU M 126 -65.25 -102.81
REMARK 500 SER M 158 11.92 -151.35
REMARK 500 GLU M 175 -9.67 -54.48
REMARK 500 HIS M 229 66.10 67.64
REMARK 500 LYS M 299 -62.59 -125.18
REMARK 500 GLN M 344 -82.85 -87.49
REMARK 500 SER M 382 -158.23 -137.60
REMARK 500 GLU M 393 -132.89 -101.41
REMARK 500 TYR M 395 17.01 -144.11
REMARK 500 GLU M 488 -37.34 -29.85
REMARK 500 PRO M 563 47.24 -74.11
REMARK 500 ASP M 574 63.80 61.68
REMARK 500 HIS Q 29 109.48 -161.45
REMARK 500 ASP Q 45 106.19 -168.44
REMARK 500 CYS Q 120 -152.75 57.22
REMARK 500 VAL Q 146 72.79 -117.47
REMARK 500 LYS Q 189 27.34 -140.58
REMARK 500 ARG Q 234 -174.53 69.36
REMARK 500 ARG Q 260 38.11 -94.44
REMARK 500 VAL Q 296 44.69 -105.13
REMARK 500 ASN J 38 -156.74 -80.36
REMARK 500 CYS J 79 46.61 -83.93
REMARK 500 LEU J 126 -63.63 -103.18
REMARK 500 SER J 158 16.50 -150.45
REMARK 500 HIS J 229 63.91 66.58
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 S 403 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 17 SG
REMARK 620 2 ER2 S 403 S4 100.6
REMARK 620 3 ER2 S 403 S1 125.0 106.1
REMARK 620 4 ER2 S 403 S2 109.8 107.9 106.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 S 403 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 20 SG
REMARK 620 2 ER2 S 403 S3 104.2
REMARK 620 3 ER2 S 403 S4 131.3 105.0
REMARK 620 4 ER2 S 403 S1 104.8 103.8 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 S 403 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 115 SG
REMARK 620 2 ER2 S 403 S3 109.3
REMARK 620 3 ER2 S 403 S1 123.4 105.6
REMARK 620 4 ER2 S 403 S2 105.6 103.9 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 S 403 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 120 SG
REMARK 620 2 ER2 S 403 S3 119.8
REMARK 620 3 ER2 S 403 S2 110.6 102.7
REMARK 620 4 CYS S 149 SG 99.6 119.5 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 187 ND1
REMARK 620 2 SF4 S 401 S1 113.4
REMARK 620 3 SF4 S 401 S2 113.2 103.5
REMARK 620 4 SF4 S 401 S4 114.0 105.5 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 190 SG
REMARK 620 2 SF4 S 401 S1 109.9
REMARK 620 3 SF4 S 401 S3 120.3 108.7
REMARK 620 4 SF4 S 401 S4 107.3 104.7 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 215 SG
REMARK 620 2 SF4 S 401 S2 105.6
REMARK 620 3 SF4 S 401 S3 114.2 106.0
REMARK 620 4 SF4 S 401 S4 119.3 104.9 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 221 SG
REMARK 620 2 SF4 S 401 S1 106.7
REMARK 620 3 SF4 S 401 S2 112.0 102.4
REMARK 620 4 SF4 S 401 S3 119.5 109.0 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S 402 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 230 SG
REMARK 620 2 F3S S 402 S1 107.3
REMARK 620 3 F3S S 402 S3 115.5 104.7
REMARK 620 4 F3S S 402 S4 120.6 101.0 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S 402 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 249 SG
REMARK 620 2 F3S S 402 S2 106.4
REMARK 620 3 F3S S 402 S3 115.6 102.7
REMARK 620 4 F3S S 402 S4 117.4 108.3 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S 402 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 252 SG
REMARK 620 2 F3S S 402 S1 112.8
REMARK 620 3 F3S S 402 S2 113.2 102.2
REMARK 620 4 F3S S 402 S3 119.1 104.1 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 57 OE1
REMARK 620 2 CYS L 528 O 100.4
REMARK 620 3 HIS L 582 NE2 93.6 98.3
REMARK 620 4 HOH L 745 O 88.5 87.9 173.0
REMARK 620 5 HOH L 770 O 93.3 163.7 89.6 83.6
REMARK 620 6 HOH L 799 O 166.8 91.5 90.2 86.3 74.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI L 602 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 76 SG
REMARK 620 2 CYS L 79 SG 96.4
REMARK 620 3 CYS L 576 SG 84.9 175.7
REMARK 620 4 CYS L 579 SG 113.8 76.3 99.4
REMARK 620 5 HOH L 808 O 155.7 91.1 89.3 90.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO L 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 79 SG
REMARK 620 2 FCO L 601 C1 165.6
REMARK 620 3 FCO L 601 C2 98.5 91.0
REMARK 620 4 FCO L 601 C3 102.0 89.2 87.0
REMARK 620 5 CYS L 579 SG 83.4 87.4 177.4 90.9
REMARK 620 6 HOH L 808 O 84.1 85.8 86.6 171.8 95.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 T 403 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 17 SG
REMARK 620 2 ER2 T 403 S4 107.6
REMARK 620 3 ER2 T 403 S1 119.6 105.4
REMARK 620 4 ER2 T 403 S2 109.6 108.0 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 T 403 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 20 SG
REMARK 620 2 ER2 T 403 S3 103.6
REMARK 620 3 ER2 T 403 S4 131.0 104.9
REMARK 620 4 ER2 T 403 S1 104.9 103.7 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 T 403 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 115 SG
REMARK 620 2 ER2 T 403 S3 109.3
REMARK 620 3 ER2 T 403 S1 120.8 104.3
REMARK 620 4 ER2 T 403 S2 109.5 104.6 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 T 403 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 120 SG
REMARK 620 2 ER2 T 403 S3 118.6
REMARK 620 3 ER2 T 403 S2 106.1 104.0
REMARK 620 4 CYS T 149 SG 102.3 122.4 101.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS T 187 ND1
REMARK 620 2 SF4 T 401 S1 114.6
REMARK 620 3 SF4 T 401 S2 105.3 103.2
REMARK 620 4 SF4 T 401 S4 119.3 108.0 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 190 SG
REMARK 620 2 SF4 T 401 S1 98.9
REMARK 620 3 SF4 T 401 S3 125.7 108.9
REMARK 620 4 SF4 T 401 S4 111.7 106.1 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 215 SG
REMARK 620 2 SF4 T 401 S2 108.9
REMARK 620 3 SF4 T 401 S3 115.6 104.5
REMARK 620 4 SF4 T 401 S4 116.4 104.9 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 221 SG
REMARK 620 2 SF4 T 401 S1 109.3
REMARK 620 3 SF4 T 401 S2 112.7 103.7
REMARK 620 4 SF4 T 401 S3 117.0 109.1 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S T 402 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 230 SG
REMARK 620 2 F3S T 402 S1 107.1
REMARK 620 3 F3S T 402 S3 120.0 101.7
REMARK 620 4 F3S T 402 S4 116.6 101.3 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S T 402 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 249 SG
REMARK 620 2 F3S T 402 S2 108.0
REMARK 620 3 F3S T 402 S3 115.7 103.8
REMARK 620 4 F3S T 402 S4 113.7 110.0 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S T 402 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 252 SG
REMARK 620 2 F3S T 402 S1 114.9
REMARK 620 3 F3S T 402 S2 113.2 102.6
REMARK 620 4 F3S T 402 S3 117.8 101.4 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG M 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU M 57 OE1
REMARK 620 2 CYS M 528 O 93.4
REMARK 620 3 HIS M 582 NE2 90.5 95.5
REMARK 620 4 HOH M 755 O 81.8 84.8 172.3
REMARK 620 5 HOH M 770 O 88.1 170.2 94.1 85.9
REMARK 620 6 HOH M 784 O 160.9 101.8 99.3 88.1 75.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI M 602 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 76 SG
REMARK 620 2 CYS M 79 SG 94.3
REMARK 620 3 CYS M 576 SG 85.7 172.0
REMARK 620 4 CYS M 579 SG 108.8 75.9 96.5
REMARK 620 5 HOH M 812 O 158.3 94.9 87.8 92.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO M 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 79 SG
REMARK 620 2 FCO M 601 C1 165.9
REMARK 620 3 FCO M 601 C2 97.6 91.8
REMARK 620 4 FCO M 601 C3 102.1 88.5 89.1
REMARK 620 5 CYS M 579 SG 82.0 87.9 176.2 94.7
REMARK 620 6 HOH M 812 O 86.0 85.1 81.1 168.0 95.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 Q 403 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 17 SG
REMARK 620 2 ER2 Q 403 S4 102.9
REMARK 620 3 ER2 Q 403 S1 118.0 106.2
REMARK 620 4 ER2 Q 403 S2 114.7 106.3 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 Q 403 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 20 SG
REMARK 620 2 ER2 Q 403 S3 104.2
REMARK 620 3 ER2 Q 403 S4 131.4 103.2
REMARK 620 4 ER2 Q 403 S1 105.5 104.7 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 Q 403 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 115 SG
REMARK 620 2 ER2 Q 403 S3 108.3
REMARK 620 3 ER2 Q 403 S1 129.7 105.7
REMARK 620 4 ER2 Q 403 S2 100.4 103.7 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 Q 403 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 120 SG
REMARK 620 2 ER2 Q 403 S3 128.0
REMARK 620 3 ER2 Q 403 S2 108.0 104.8
REMARK 620 4 CYS Q 149 SG 96.2 116.7 99.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 Q 401 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 187 ND1
REMARK 620 2 SF4 Q 401 S1 115.5
REMARK 620 3 SF4 Q 401 S2 111.9 103.3
REMARK 620 4 SF4 Q 401 S4 112.5 105.2 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 Q 401 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 190 SG
REMARK 620 2 SF4 Q 401 S1 107.4
REMARK 620 3 SF4 Q 401 S3 119.8 106.3
REMARK 620 4 SF4 Q 401 S4 112.2 105.0 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 Q 401 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 215 SG
REMARK 620 2 SF4 Q 401 S2 105.6
REMARK 620 3 SF4 Q 401 S3 114.0 106.6
REMARK 620 4 SF4 Q 401 S4 118.5 105.1 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 Q 401 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 221 SG
REMARK 620 2 SF4 Q 401 S1 107.5
REMARK 620 3 SF4 Q 401 S2 115.4 102.9
REMARK 620 4 SF4 Q 401 S3 116.7 105.8 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S Q 402 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 230 SG
REMARK 620 2 F3S Q 402 S1 102.9
REMARK 620 3 F3S Q 402 S3 121.3 105.4
REMARK 620 4 F3S Q 402 S4 115.8 103.9 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S Q 402 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 249 SG
REMARK 620 2 F3S Q 402 S2 112.6
REMARK 620 3 F3S Q 402 S3 115.3 106.3
REMARK 620 4 F3S Q 402 S4 115.9 102.1 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S Q 402 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 252 SG
REMARK 620 2 F3S Q 402 S1 111.5
REMARK 620 3 F3S Q 402 S2 111.9 101.5
REMARK 620 4 F3S Q 402 S3 118.9 105.6 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU J 57 OE1
REMARK 620 2 CYS J 528 O 96.6
REMARK 620 3 HIS J 582 NE2 86.3 95.8
REMARK 620 4 HOH J 707 O 164.6 78.8 108.6
REMARK 620 5 HOH J 738 O 94.6 102.8 161.1 72.5
REMARK 620 6 HOH J 788 O 105.2 158.2 85.4 80.3 76.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI J 602 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 76 SG
REMARK 620 2 CYS J 79 SG 92.0
REMARK 620 3 CYS J 576 SG 89.1 173.0
REMARK 620 4 CYS J 579 SG 111.2 74.6 98.5
REMARK 620 5 HOH J 806 O 153.3 93.7 88.4 95.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO J 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 79 SG
REMARK 620 2 FCO J 601 C1 161.1
REMARK 620 3 FCO J 601 C2 100.3 90.1
REMARK 620 4 FCO J 601 C3 102.5 93.3 89.3
REMARK 620 5 CYS J 579 SG 78.9 89.5 175.9 94.9
REMARK 620 6 HOH J 806 O 82.8 83.6 79.5 168.3 96.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 R 403 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 17 SG
REMARK 620 2 ER2 R 403 S4 104.3
REMARK 620 3 ER2 R 403 S1 120.7 106.7
REMARK 620 4 ER2 R 403 S2 108.9 103.0 111.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 R 403 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 20 SG
REMARK 620 2 ER2 R 403 S3 106.7
REMARK 620 3 ER2 R 403 S4 134.6 99.6
REMARK 620 4 ER2 R 403 S1 101.2 105.5 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 R 403 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 115 SG
REMARK 620 2 ER2 R 403 S3 110.9
REMARK 620 3 ER2 R 403 S1 121.8 104.4
REMARK 620 4 ER2 R 403 S2 105.5 103.6 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ER2 R 403 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 120 SG
REMARK 620 2 ER2 R 403 S3 122.5
REMARK 620 3 ER2 R 403 S2 105.6 105.1
REMARK 620 4 CYS R 149 SG 100.8 113.9 108.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 R 401 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS R 187 ND1
REMARK 620 2 SF4 R 401 S1 108.9
REMARK 620 3 SF4 R 401 S2 114.7 106.6
REMARK 620 4 SF4 R 401 S4 115.6 106.7 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 R 401 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 190 SG
REMARK 620 2 SF4 R 401 S1 106.8
REMARK 620 3 SF4 R 401 S3 115.0 105.2
REMARK 620 4 SF4 R 401 S4 118.6 107.5 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 R 401 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 215 SG
REMARK 620 2 SF4 R 401 S2 95.7
REMARK 620 3 SF4 R 401 S3 124.0 105.6
REMARK 620 4 SF4 R 401 S4 120.7 105.2 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 R 401 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 221 SG
REMARK 620 2 SF4 R 401 S1 107.9
REMARK 620 3 SF4 R 401 S2 114.6 107.5
REMARK 620 4 SF4 R 401 S3 117.5 104.9 103.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S R 402 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 230 SG
REMARK 620 2 F3S R 402 S1 101.0
REMARK 620 3 F3S R 402 S3 123.0 101.8
REMARK 620 4 F3S R 402 S4 118.8 108.6 101.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S R 402 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 249 SG
REMARK 620 2 F3S R 402 S2 105.8
REMARK 620 3 F3S R 402 S3 116.6 100.6
REMARK 620 4 F3S R 402 S4 111.5 119.7 102.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S R 402 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 252 SG
REMARK 620 2 F3S R 402 S1 112.7
REMARK 620 3 F3S R 402 S2 110.4 116.0
REMARK 620 4 F3S R 402 S3 113.2 102.8 101.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 57 OE1
REMARK 620 2 CYS K 528 O 93.2
REMARK 620 3 HIS K 582 NE2 89.8 88.8
REMARK 620 4 HOH K 731 O 91.2 88.0 176.7
REMARK 620 5 HOH K 769 O 170.3 88.2 99.8 79.3
REMARK 620 6 HOH K 802 O 110.4 156.3 92.5 90.0 68.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI K 602 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 76 SG
REMARK 620 2 CYS K 79 SG 94.3
REMARK 620 3 CYS K 576 SG 86.8 171.9
REMARK 620 4 HOH K 805 O 154.5 95.0 87.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO K 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 79 SG
REMARK 620 2 FCO K 601 C1 165.4
REMARK 620 3 FCO K 601 C2 101.6 89.6
REMARK 620 4 FCO K 601 C3 99.2 89.8 90.9
REMARK 620 5 CYS K 579 SG 78.7 89.9 178.9 90.1
REMARK 620 6 HOH K 805 O 87.4 85.8 78.0 168.0 101.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 NE2
REMARK 620 2 HEM A 301 NA 77.5
REMARK 620 3 HEM A 301 NB 92.9 88.0
REMARK 620 4 HEM A 301 NC 101.2 174.4 86.6
REMARK 620 5 HEM A 301 ND 89.2 93.6 177.7 91.8
REMARK 620 6 HIS A 184 NE2 164.5 87.3 83.9 93.7 94.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 NE2
REMARK 620 2 HEM B 301 NA 86.2
REMARK 620 3 HEM B 301 NB 94.9 87.8
REMARK 620 4 HEM B 301 NC 93.5 173.9 86.2
REMARK 620 5 HEM B 301 ND 86.9 94.0 177.6 92.0
REMARK 620 6 HIS B 184 NE2 174.4 88.3 83.6 91.8 94.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 S 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F3S S 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER2 S 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FCO L 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI L 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL L 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 T 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F3S T 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER2 T 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FCO M 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI M 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG M 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 Q 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F3S Q 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER2 Q 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FCO J 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI J 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL J 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 R 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F3S R 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER2 R 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FCO K 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI K 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL K 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GD3 RELATED DB: PDB
REMARK 900 RELATED ID: 3UQY RELATED DB: PDB
REMARK 900 RELATED ID: 3USC RELATED DB: PDB
REMARK 900 RELATED ID: 3USE RELATED DB: PDB
DBREF 6G94 S 1 327 UNP P69739 MBHS_ECOLI 46 372
DBREF 6G94 L 1 582 UNP P0ACD8 MBHL_ECOLI 1 582
DBREF 6G94 T 1 327 UNP P69739 MBHS_ECOLI 46 372
DBREF 6G94 M 1 582 UNP P0ACD8 MBHL_ECOLI 1 582
DBREF 6G94 Q 1 327 UNP P69739 MBHS_ECOLI 46 372
DBREF 6G94 J 1 582 UNP P0ACD8 MBHL_ECOLI 1 582
DBREF 6G94 R 1 327 UNP P69739 MBHS_ECOLI 46 372
DBREF 6G94 K 1 582 UNP P0ACD8 MBHL_ECOLI 1 582
DBREF 6G94 A 1 235 UNP P0AAM1 CYBH_ECOLI 1 235
DBREF 6G94 B 1 235 UNP P0AAM1 CYBH_ECOLI 1 235
SEQADV 6G94 GLY S 19 UNP P69739 CYS 64 CONFLICT
SEQADV 6G94 ARG S 328 UNP P69739 EXPRESSION TAG
SEQADV 6G94 SER S 329 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS S 330 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS S 331 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS S 332 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS S 333 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS S 334 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS S 335 UNP P69739 EXPRESSION TAG
SEQADV 6G94 GLY T 19 UNP P69739 CYS 64 CONFLICT
SEQADV 6G94 ARG T 328 UNP P69739 EXPRESSION TAG
SEQADV 6G94 SER T 329 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS T 330 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS T 331 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS T 332 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS T 333 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS T 334 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS T 335 UNP P69739 EXPRESSION TAG
SEQADV 6G94 GLY Q 19 UNP P69739 CYS 64 CONFLICT
SEQADV 6G94 ARG Q 328 UNP P69739 EXPRESSION TAG
SEQADV 6G94 SER Q 329 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS Q 330 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS Q 331 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS Q 332 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS Q 333 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS Q 334 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS Q 335 UNP P69739 EXPRESSION TAG
SEQADV 6G94 GLY R 19 UNP P69739 CYS 64 CONFLICT
SEQADV 6G94 ARG R 328 UNP P69739 EXPRESSION TAG
SEQADV 6G94 SER R 329 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS R 330 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS R 331 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS R 332 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS R 333 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS R 334 UNP P69739 EXPRESSION TAG
SEQADV 6G94 HIS R 335 UNP P69739 EXPRESSION TAG
SEQRES 1 S 335 LEU GLU ASN LYS PRO ARG ILE PRO VAL VAL TRP ILE HIS
SEQRES 2 S 335 GLY LEU GLU CYS THR GLY CYS THR GLU SER PHE ILE ARG
SEQRES 3 S 335 SER ALA HIS PRO LEU ALA LYS ASP VAL ILE LEU SER LEU
SEQRES 4 S 335 ILE SER LEU ASP TYR ASP ASP THR LEU MET ALA ALA ALA
SEQRES 5 S 335 GLY THR GLN ALA GLU GLU VAL PHE GLU ASP ILE ILE THR
SEQRES 6 S 335 GLN TYR ASN GLY LYS TYR ILE LEU ALA VAL GLU GLY ASN
SEQRES 7 S 335 PRO PRO LEU GLY GLU GLN GLY MET PHE CYS ILE SER SER
SEQRES 8 S 335 GLY ARG PRO PHE ILE GLU LYS LEU LYS ARG ALA ALA ALA
SEQRES 9 S 335 GLY ALA SER ALA ILE ILE ALA TRP GLY THR CYS ALA SER
SEQRES 10 S 335 TRP GLY CYS VAL GLN ALA ALA ARG PRO ASN PRO THR GLN
SEQRES 11 S 335 ALA THR PRO ILE ASP LYS VAL ILE THR ASP LYS PRO ILE
SEQRES 12 S 335 ILE LYS VAL PRO GLY CYS PRO PRO ILE PRO ASP VAL MET
SEQRES 13 S 335 SER ALA ILE ILE THR TYR MET VAL THR PHE ASP ARG LEU
SEQRES 14 S 335 PRO ASP VAL ASP ARG MET GLY ARG PRO LEU MET PHE TYR
SEQRES 15 S 335 GLY GLN ARG ILE HIS ASP LYS CYS TYR ARG ARG ALA HIS
SEQRES 16 S 335 PHE ASP ALA GLY GLU PHE VAL GLN SER TRP ASP ASP ASP
SEQRES 17 S 335 ALA ALA ARG LYS GLY TYR CYS LEU TYR LYS MET GLY CYS
SEQRES 18 S 335 LYS GLY PRO THR THR TYR ASN ALA CYS SER SER THR ARG
SEQRES 19 S 335 TRP ASN ASP GLY VAL SER PHE PRO ILE GLN SER GLY HIS
SEQRES 20 S 335 GLY CYS LEU GLY CYS ALA GLU ASN GLY PHE TRP ASP ARG
SEQRES 21 S 335 GLY SER PHE TYR SER ARG VAL VAL ASP ILE PRO GLN MET
SEQRES 22 S 335 GLY THR HIS SER THR ALA ASP THR VAL GLY LEU THR ALA
SEQRES 23 S 335 LEU GLY VAL VAL ALA ALA ALA VAL GLY VAL HIS ALA VAL
SEQRES 24 S 335 ALA SER ALA VAL ASP GLN ARG ARG ARG HIS ASN GLN GLN
SEQRES 25 S 335 PRO THR GLU THR GLU HIS GLN PRO GLY ASN GLU ASP LYS
SEQRES 26 S 335 GLN ALA ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 L 582 MET SER THR GLN TYR GLU THR GLN GLY TYR THR ILE ASN
SEQRES 2 L 582 ASN ALA GLY ARG ARG LEU VAL VAL ASP PRO ILE THR ARG
SEQRES 3 L 582 ILE GLU GLY HIS MET ARG CYS GLU VAL ASN ILE ASN ASP
SEQRES 4 L 582 GLN ASN VAL ILE THR ASN ALA VAL SER CYS GLY THR MET
SEQRES 5 L 582 PHE ARG GLY LEU GLU ILE ILE LEU GLN GLY ARG ASP PRO
SEQRES 6 L 582 ARG ASP ALA TRP ALA PHE VAL GLU ARG ILE CYS GLY VAL
SEQRES 7 L 582 CYS THR GLY VAL HIS ALA LEU ALA SER VAL TYR ALA ILE
SEQRES 8 L 582 GLU ASP ALA ILE GLY ILE LYS VAL PRO ASP ASN ALA ASN
SEQRES 9 L 582 ILE ILE ARG ASN ILE MET LEU ALA THR LEU TRP CYS HIS
SEQRES 10 L 582 ASP HIS LEU VAL HIS PHE TYR GLN LEU ALA GLY MET ASP
SEQRES 11 L 582 TRP ILE ASP VAL LEU ASP ALA LEU LYS ALA ASP PRO ARG
SEQRES 12 L 582 LYS THR SER GLU LEU ALA GLN SER LEU SER SER TRP PRO
SEQRES 13 L 582 LYS SER SER PRO GLY TYR PHE PHE ASP VAL GLN ASN ARG
SEQRES 14 L 582 LEU LYS LYS PHE VAL GLU GLY GLY GLN LEU GLY ILE PHE
SEQRES 15 L 582 ARG ASN GLY TYR TRP GLY HIS PRO GLN TYR LYS LEU PRO
SEQRES 16 L 582 PRO GLU ALA ASN LEU MET GLY PHE ALA HIS TYR LEU GLU
SEQRES 17 L 582 ALA LEU ASP PHE GLN ARG GLU ILE VAL LYS ILE HIS ALA
SEQRES 18 L 582 VAL PHE GLY GLY LYS ASN PRO HIS PRO ASN TRP ILE VAL
SEQRES 19 L 582 GLY GLY MET PRO CYS ALA ILE ASN ILE ASP GLU SER GLY
SEQRES 20 L 582 ALA VAL GLY ALA VAL ASN MET GLU ARG LEU ASN LEU VAL
SEQRES 21 L 582 GLN SER ILE ILE THR ARG THR ALA ASP PHE ILE ASN ASN
SEQRES 22 L 582 VAL MET ILE PRO ASP ALA LEU ALA ILE GLY GLN PHE ASN
SEQRES 23 L 582 LYS PRO TRP SER GLU ILE GLY THR GLY LEU SER ASP LYS
SEQRES 24 L 582 CYS VAL LEU SER TYR GLY ALA PHE PRO ASP ILE ALA ASN
SEQRES 25 L 582 ASP PHE GLY GLU LYS SER LEU LEU MET PRO GLY GLY ALA
SEQRES 26 L 582 VAL ILE ASN GLY ASP PHE ASN ASN VAL LEU PRO VAL ASP
SEQRES 27 L 582 LEU VAL ASP PRO GLN GLN VAL GLN GLU PHE VAL ASP HIS
SEQRES 28 L 582 ALA TRP TYR ARG TYR PRO ASN ASP GLN VAL GLY ARG HIS
SEQRES 29 L 582 PRO PHE ASP GLY ILE THR ASP PRO TRP TYR ASN PRO GLY
SEQRES 30 L 582 ASP VAL LYS GLY SER ASP THR ASN ILE GLN GLN LEU ASN
SEQRES 31 L 582 GLU GLN GLU ARG TYR SER TRP ILE LYS ALA PRO ARG TRP
SEQRES 32 L 582 ARG GLY ASN ALA MET GLU VAL GLY PRO LEU ALA ARG THR
SEQRES 33 L 582 LEU ILE ALA TYR HIS LYS GLY ASP ALA ALA THR VAL GLU
SEQRES 34 L 582 SER VAL ASP ARG MET MET SER ALA LEU ASN LEU PRO LEU
SEQRES 35 L 582 SER GLY ILE GLN SER THR LEU GLY ARG ILE LEU CYS ARG
SEQRES 36 L 582 ALA HIS GLU ALA GLN TRP ALA ALA GLY LYS LEU GLN TYR
SEQRES 37 L 582 PHE PHE ASP LYS LEU MET THR ASN LEU LYS ASN GLY ASN
SEQRES 38 L 582 LEU ALA THR ALA SER THR GLU LYS TRP GLU PRO ALA THR
SEQRES 39 L 582 TRP PRO THR GLU CYS ARG GLY VAL GLY PHE THR GLU ALA
SEQRES 40 L 582 PRO ARG GLY ALA LEU GLY HIS TRP ALA ALA ILE ARG ASP
SEQRES 41 L 582 GLY LYS ILE ASP LEU TYR GLN CYS VAL VAL PRO THR THR
SEQRES 42 L 582 TRP ASN ALA SER PRO ARG ASP PRO LYS GLY GLN ILE GLY
SEQRES 43 L 582 ALA TYR GLU ALA ALA LEU MET ASN THR LYS MET ALA ILE
SEQRES 44 L 582 PRO GLU GLN PRO LEU GLU ILE LEU ARG THR LEU HIS SER
SEQRES 45 L 582 PHE ASP PRO CYS LEU ALA CYS SER THR HIS
SEQRES 1 T 335 LEU GLU ASN LYS PRO ARG ILE PRO VAL VAL TRP ILE HIS
SEQRES 2 T 335 GLY LEU GLU CYS THR GLY CYS THR GLU SER PHE ILE ARG
SEQRES 3 T 335 SER ALA HIS PRO LEU ALA LYS ASP VAL ILE LEU SER LEU
SEQRES 4 T 335 ILE SER LEU ASP TYR ASP ASP THR LEU MET ALA ALA ALA
SEQRES 5 T 335 GLY THR GLN ALA GLU GLU VAL PHE GLU ASP ILE ILE THR
SEQRES 6 T 335 GLN TYR ASN GLY LYS TYR ILE LEU ALA VAL GLU GLY ASN
SEQRES 7 T 335 PRO PRO LEU GLY GLU GLN GLY MET PHE CYS ILE SER SER
SEQRES 8 T 335 GLY ARG PRO PHE ILE GLU LYS LEU LYS ARG ALA ALA ALA
SEQRES 9 T 335 GLY ALA SER ALA ILE ILE ALA TRP GLY THR CYS ALA SER
SEQRES 10 T 335 TRP GLY CYS VAL GLN ALA ALA ARG PRO ASN PRO THR GLN
SEQRES 11 T 335 ALA THR PRO ILE ASP LYS VAL ILE THR ASP LYS PRO ILE
SEQRES 12 T 335 ILE LYS VAL PRO GLY CYS PRO PRO ILE PRO ASP VAL MET
SEQRES 13 T 335 SER ALA ILE ILE THR TYR MET VAL THR PHE ASP ARG LEU
SEQRES 14 T 335 PRO ASP VAL ASP ARG MET GLY ARG PRO LEU MET PHE TYR
SEQRES 15 T 335 GLY GLN ARG ILE HIS ASP LYS CYS TYR ARG ARG ALA HIS
SEQRES 16 T 335 PHE ASP ALA GLY GLU PHE VAL GLN SER TRP ASP ASP ASP
SEQRES 17 T 335 ALA ALA ARG LYS GLY TYR CYS LEU TYR LYS MET GLY CYS
SEQRES 18 T 335 LYS GLY PRO THR THR TYR ASN ALA CYS SER SER THR ARG
SEQRES 19 T 335 TRP ASN ASP GLY VAL SER PHE PRO ILE GLN SER GLY HIS
SEQRES 20 T 335 GLY CYS LEU GLY CYS ALA GLU ASN GLY PHE TRP ASP ARG
SEQRES 21 T 335 GLY SER PHE TYR SER ARG VAL VAL ASP ILE PRO GLN MET
SEQRES 22 T 335 GLY THR HIS SER THR ALA ASP THR VAL GLY LEU THR ALA
SEQRES 23 T 335 LEU GLY VAL VAL ALA ALA ALA VAL GLY VAL HIS ALA VAL
SEQRES 24 T 335 ALA SER ALA VAL ASP GLN ARG ARG ARG HIS ASN GLN GLN
SEQRES 25 T 335 PRO THR GLU THR GLU HIS GLN PRO GLY ASN GLU ASP LYS
SEQRES 26 T 335 GLN ALA ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 M 582 MET SER THR GLN TYR GLU THR GLN GLY TYR THR ILE ASN
SEQRES 2 M 582 ASN ALA GLY ARG ARG LEU VAL VAL ASP PRO ILE THR ARG
SEQRES 3 M 582 ILE GLU GLY HIS MET ARG CYS GLU VAL ASN ILE ASN ASP
SEQRES 4 M 582 GLN ASN VAL ILE THR ASN ALA VAL SER CYS GLY THR MET
SEQRES 5 M 582 PHE ARG GLY LEU GLU ILE ILE LEU GLN GLY ARG ASP PRO
SEQRES 6 M 582 ARG ASP ALA TRP ALA PHE VAL GLU ARG ILE CYS GLY VAL
SEQRES 7 M 582 CYS THR GLY VAL HIS ALA LEU ALA SER VAL TYR ALA ILE
SEQRES 8 M 582 GLU ASP ALA ILE GLY ILE LYS VAL PRO ASP ASN ALA ASN
SEQRES 9 M 582 ILE ILE ARG ASN ILE MET LEU ALA THR LEU TRP CYS HIS
SEQRES 10 M 582 ASP HIS LEU VAL HIS PHE TYR GLN LEU ALA GLY MET ASP
SEQRES 11 M 582 TRP ILE ASP VAL LEU ASP ALA LEU LYS ALA ASP PRO ARG
SEQRES 12 M 582 LYS THR SER GLU LEU ALA GLN SER LEU SER SER TRP PRO
SEQRES 13 M 582 LYS SER SER PRO GLY TYR PHE PHE ASP VAL GLN ASN ARG
SEQRES 14 M 582 LEU LYS LYS PHE VAL GLU GLY GLY GLN LEU GLY ILE PHE
SEQRES 15 M 582 ARG ASN GLY TYR TRP GLY HIS PRO GLN TYR LYS LEU PRO
SEQRES 16 M 582 PRO GLU ALA ASN LEU MET GLY PHE ALA HIS TYR LEU GLU
SEQRES 17 M 582 ALA LEU ASP PHE GLN ARG GLU ILE VAL LYS ILE HIS ALA
SEQRES 18 M 582 VAL PHE GLY GLY LYS ASN PRO HIS PRO ASN TRP ILE VAL
SEQRES 19 M 582 GLY GLY MET PRO CYS ALA ILE ASN ILE ASP GLU SER GLY
SEQRES 20 M 582 ALA VAL GLY ALA VAL ASN MET GLU ARG LEU ASN LEU VAL
SEQRES 21 M 582 GLN SER ILE ILE THR ARG THR ALA ASP PHE ILE ASN ASN
SEQRES 22 M 582 VAL MET ILE PRO ASP ALA LEU ALA ILE GLY GLN PHE ASN
SEQRES 23 M 582 LYS PRO TRP SER GLU ILE GLY THR GLY LEU SER ASP LYS
SEQRES 24 M 582 CYS VAL LEU SER TYR GLY ALA PHE PRO ASP ILE ALA ASN
SEQRES 25 M 582 ASP PHE GLY GLU LYS SER LEU LEU MET PRO GLY GLY ALA
SEQRES 26 M 582 VAL ILE ASN GLY ASP PHE ASN ASN VAL LEU PRO VAL ASP
SEQRES 27 M 582 LEU VAL ASP PRO GLN GLN VAL GLN GLU PHE VAL ASP HIS
SEQRES 28 M 582 ALA TRP TYR ARG TYR PRO ASN ASP GLN VAL GLY ARG HIS
SEQRES 29 M 582 PRO PHE ASP GLY ILE THR ASP PRO TRP TYR ASN PRO GLY
SEQRES 30 M 582 ASP VAL LYS GLY SER ASP THR ASN ILE GLN GLN LEU ASN
SEQRES 31 M 582 GLU GLN GLU ARG TYR SER TRP ILE LYS ALA PRO ARG TRP
SEQRES 32 M 582 ARG GLY ASN ALA MET GLU VAL GLY PRO LEU ALA ARG THR
SEQRES 33 M 582 LEU ILE ALA TYR HIS LYS GLY ASP ALA ALA THR VAL GLU
SEQRES 34 M 582 SER VAL ASP ARG MET MET SER ALA LEU ASN LEU PRO LEU
SEQRES 35 M 582 SER GLY ILE GLN SER THR LEU GLY ARG ILE LEU CYS ARG
SEQRES 36 M 582 ALA HIS GLU ALA GLN TRP ALA ALA GLY LYS LEU GLN TYR
SEQRES 37 M 582 PHE PHE ASP LYS LEU MET THR ASN LEU LYS ASN GLY ASN
SEQRES 38 M 582 LEU ALA THR ALA SER THR GLU LYS TRP GLU PRO ALA THR
SEQRES 39 M 582 TRP PRO THR GLU CYS ARG GLY VAL GLY PHE THR GLU ALA
SEQRES 40 M 582 PRO ARG GLY ALA LEU GLY HIS TRP ALA ALA ILE ARG ASP
SEQRES 41 M 582 GLY LYS ILE ASP LEU TYR GLN CYS VAL VAL PRO THR THR
SEQRES 42 M 582 TRP ASN ALA SER PRO ARG ASP PRO LYS GLY GLN ILE GLY
SEQRES 43 M 582 ALA TYR GLU ALA ALA LEU MET ASN THR LYS MET ALA ILE
SEQRES 44 M 582 PRO GLU GLN PRO LEU GLU ILE LEU ARG THR LEU HIS SER
SEQRES 45 M 582 PHE ASP PRO CYS LEU ALA CYS SER THR HIS
SEQRES 1 Q 335 LEU GLU ASN LYS PRO ARG ILE PRO VAL VAL TRP ILE HIS
SEQRES 2 Q 335 GLY LEU GLU CYS THR GLY CYS THR GLU SER PHE ILE ARG
SEQRES 3 Q 335 SER ALA HIS PRO LEU ALA LYS ASP VAL ILE LEU SER LEU
SEQRES 4 Q 335 ILE SER LEU ASP TYR ASP ASP THR LEU MET ALA ALA ALA
SEQRES 5 Q 335 GLY THR GLN ALA GLU GLU VAL PHE GLU ASP ILE ILE THR
SEQRES 6 Q 335 GLN TYR ASN GLY LYS TYR ILE LEU ALA VAL GLU GLY ASN
SEQRES 7 Q 335 PRO PRO LEU GLY GLU GLN GLY MET PHE CYS ILE SER SER
SEQRES 8 Q 335 GLY ARG PRO PHE ILE GLU LYS LEU LYS ARG ALA ALA ALA
SEQRES 9 Q 335 GLY ALA SER ALA ILE ILE ALA TRP GLY THR CYS ALA SER
SEQRES 10 Q 335 TRP GLY CYS VAL GLN ALA ALA ARG PRO ASN PRO THR GLN
SEQRES 11 Q 335 ALA THR PRO ILE ASP LYS VAL ILE THR ASP LYS PRO ILE
SEQRES 12 Q 335 ILE LYS VAL PRO GLY CYS PRO PRO ILE PRO ASP VAL MET
SEQRES 13 Q 335 SER ALA ILE ILE THR TYR MET VAL THR PHE ASP ARG LEU
SEQRES 14 Q 335 PRO ASP VAL ASP ARG MET GLY ARG PRO LEU MET PHE TYR
SEQRES 15 Q 335 GLY GLN ARG ILE HIS ASP LYS CYS TYR ARG ARG ALA HIS
SEQRES 16 Q 335 PHE ASP ALA GLY GLU PHE VAL GLN SER TRP ASP ASP ASP
SEQRES 17 Q 335 ALA ALA ARG LYS GLY TYR CYS LEU TYR LYS MET GLY CYS
SEQRES 18 Q 335 LYS GLY PRO THR THR TYR ASN ALA CYS SER SER THR ARG
SEQRES 19 Q 335 TRP ASN ASP GLY VAL SER PHE PRO ILE GLN SER GLY HIS
SEQRES 20 Q 335 GLY CYS LEU GLY CYS ALA GLU ASN GLY PHE TRP ASP ARG
SEQRES 21 Q 335 GLY SER PHE TYR SER ARG VAL VAL ASP ILE PRO GLN MET
SEQRES 22 Q 335 GLY THR HIS SER THR ALA ASP THR VAL GLY LEU THR ALA
SEQRES 23 Q 335 LEU GLY VAL VAL ALA ALA ALA VAL GLY VAL HIS ALA VAL
SEQRES 24 Q 335 ALA SER ALA VAL ASP GLN ARG ARG ARG HIS ASN GLN GLN
SEQRES 25 Q 335 PRO THR GLU THR GLU HIS GLN PRO GLY ASN GLU ASP LYS
SEQRES 26 Q 335 GLN ALA ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 J 582 MET SER THR GLN TYR GLU THR GLN GLY TYR THR ILE ASN
SEQRES 2 J 582 ASN ALA GLY ARG ARG LEU VAL VAL ASP PRO ILE THR ARG
SEQRES 3 J 582 ILE GLU GLY HIS MET ARG CYS GLU VAL ASN ILE ASN ASP
SEQRES 4 J 582 GLN ASN VAL ILE THR ASN ALA VAL SER CYS GLY THR MET
SEQRES 5 J 582 PHE ARG GLY LEU GLU ILE ILE LEU GLN GLY ARG ASP PRO
SEQRES 6 J 582 ARG ASP ALA TRP ALA PHE VAL GLU ARG ILE CYS GLY VAL
SEQRES 7 J 582 CYS THR GLY VAL HIS ALA LEU ALA SER VAL TYR ALA ILE
SEQRES 8 J 582 GLU ASP ALA ILE GLY ILE LYS VAL PRO ASP ASN ALA ASN
SEQRES 9 J 582 ILE ILE ARG ASN ILE MET LEU ALA THR LEU TRP CYS HIS
SEQRES 10 J 582 ASP HIS LEU VAL HIS PHE TYR GLN LEU ALA GLY MET ASP
SEQRES 11 J 582 TRP ILE ASP VAL LEU ASP ALA LEU LYS ALA ASP PRO ARG
SEQRES 12 J 582 LYS THR SER GLU LEU ALA GLN SER LEU SER SER TRP PRO
SEQRES 13 J 582 LYS SER SER PRO GLY TYR PHE PHE ASP VAL GLN ASN ARG
SEQRES 14 J 582 LEU LYS LYS PHE VAL GLU GLY GLY GLN LEU GLY ILE PHE
SEQRES 15 J 582 ARG ASN GLY TYR TRP GLY HIS PRO GLN TYR LYS LEU PRO
SEQRES 16 J 582 PRO GLU ALA ASN LEU MET GLY PHE ALA HIS TYR LEU GLU
SEQRES 17 J 582 ALA LEU ASP PHE GLN ARG GLU ILE VAL LYS ILE HIS ALA
SEQRES 18 J 582 VAL PHE GLY GLY LYS ASN PRO HIS PRO ASN TRP ILE VAL
SEQRES 19 J 582 GLY GLY MET PRO CYS ALA ILE ASN ILE ASP GLU SER GLY
SEQRES 20 J 582 ALA VAL GLY ALA VAL ASN MET GLU ARG LEU ASN LEU VAL
SEQRES 21 J 582 GLN SER ILE ILE THR ARG THR ALA ASP PHE ILE ASN ASN
SEQRES 22 J 582 VAL MET ILE PRO ASP ALA LEU ALA ILE GLY GLN PHE ASN
SEQRES 23 J 582 LYS PRO TRP SER GLU ILE GLY THR GLY LEU SER ASP LYS
SEQRES 24 J 582 CYS VAL LEU SER TYR GLY ALA PHE PRO ASP ILE ALA ASN
SEQRES 25 J 582 ASP PHE GLY GLU LYS SER LEU LEU MET PRO GLY GLY ALA
SEQRES 26 J 582 VAL ILE ASN GLY ASP PHE ASN ASN VAL LEU PRO VAL ASP
SEQRES 27 J 582 LEU VAL ASP PRO GLN GLN VAL GLN GLU PHE VAL ASP HIS
SEQRES 28 J 582 ALA TRP TYR ARG TYR PRO ASN ASP GLN VAL GLY ARG HIS
SEQRES 29 J 582 PRO PHE ASP GLY ILE THR ASP PRO TRP TYR ASN PRO GLY
SEQRES 30 J 582 ASP VAL LYS GLY SER ASP THR ASN ILE GLN GLN LEU ASN
SEQRES 31 J 582 GLU GLN GLU ARG TYR SER TRP ILE LYS ALA PRO ARG TRP
SEQRES 32 J 582 ARG GLY ASN ALA MET GLU VAL GLY PRO LEU ALA ARG THR
SEQRES 33 J 582 LEU ILE ALA TYR HIS LYS GLY ASP ALA ALA THR VAL GLU
SEQRES 34 J 582 SER VAL ASP ARG MET MET SER ALA LEU ASN LEU PRO LEU
SEQRES 35 J 582 SER GLY ILE GLN SER THR LEU GLY ARG ILE LEU CYS ARG
SEQRES 36 J 582 ALA HIS GLU ALA GLN TRP ALA ALA GLY LYS LEU GLN TYR
SEQRES 37 J 582 PHE PHE ASP LYS LEU MET THR ASN LEU LYS ASN GLY ASN
SEQRES 38 J 582 LEU ALA THR ALA SER THR GLU LYS TRP GLU PRO ALA THR
SEQRES 39 J 582 TRP PRO THR GLU CYS ARG GLY VAL GLY PHE THR GLU ALA
SEQRES 40 J 582 PRO ARG GLY ALA LEU GLY HIS TRP ALA ALA ILE ARG ASP
SEQRES 41 J 582 GLY LYS ILE ASP LEU TYR GLN CYS VAL VAL PRO THR THR
SEQRES 42 J 582 TRP ASN ALA SER PRO ARG ASP PRO LYS GLY GLN ILE GLY
SEQRES 43 J 582 ALA TYR GLU ALA ALA LEU MET ASN THR LYS MET ALA ILE
SEQRES 44 J 582 PRO GLU GLN PRO LEU GLU ILE LEU ARG THR LEU HIS SER
SEQRES 45 J 582 PHE ASP PRO CYS LEU ALA CYS SER THR HIS
SEQRES 1 R 335 LEU GLU ASN LYS PRO ARG ILE PRO VAL VAL TRP ILE HIS
SEQRES 2 R 335 GLY LEU GLU CYS THR GLY CYS THR GLU SER PHE ILE ARG
SEQRES 3 R 335 SER ALA HIS PRO LEU ALA LYS ASP VAL ILE LEU SER LEU
SEQRES 4 R 335 ILE SER LEU ASP TYR ASP ASP THR LEU MET ALA ALA ALA
SEQRES 5 R 335 GLY THR GLN ALA GLU GLU VAL PHE GLU ASP ILE ILE THR
SEQRES 6 R 335 GLN TYR ASN GLY LYS TYR ILE LEU ALA VAL GLU GLY ASN
SEQRES 7 R 335 PRO PRO LEU GLY GLU GLN GLY MET PHE CYS ILE SER SER
SEQRES 8 R 335 GLY ARG PRO PHE ILE GLU LYS LEU LYS ARG ALA ALA ALA
SEQRES 9 R 335 GLY ALA SER ALA ILE ILE ALA TRP GLY THR CYS ALA SER
SEQRES 10 R 335 TRP GLY CYS VAL GLN ALA ALA ARG PRO ASN PRO THR GLN
SEQRES 11 R 335 ALA THR PRO ILE ASP LYS VAL ILE THR ASP LYS PRO ILE
SEQRES 12 R 335 ILE LYS VAL PRO GLY CYS PRO PRO ILE PRO ASP VAL MET
SEQRES 13 R 335 SER ALA ILE ILE THR TYR MET VAL THR PHE ASP ARG LEU
SEQRES 14 R 335 PRO ASP VAL ASP ARG MET GLY ARG PRO LEU MET PHE TYR
SEQRES 15 R 335 GLY GLN ARG ILE HIS ASP LYS CYS TYR ARG ARG ALA HIS
SEQRES 16 R 335 PHE ASP ALA GLY GLU PHE VAL GLN SER TRP ASP ASP ASP
SEQRES 17 R 335 ALA ALA ARG LYS GLY TYR CYS LEU TYR LYS MET GLY CYS
SEQRES 18 R 335 LYS GLY PRO THR THR TYR ASN ALA CYS SER SER THR ARG
SEQRES 19 R 335 TRP ASN ASP GLY VAL SER PHE PRO ILE GLN SER GLY HIS
SEQRES 20 R 335 GLY CYS LEU GLY CYS ALA GLU ASN GLY PHE TRP ASP ARG
SEQRES 21 R 335 GLY SER PHE TYR SER ARG VAL VAL ASP ILE PRO GLN MET
SEQRES 22 R 335 GLY THR HIS SER THR ALA ASP THR VAL GLY LEU THR ALA
SEQRES 23 R 335 LEU GLY VAL VAL ALA ALA ALA VAL GLY VAL HIS ALA VAL
SEQRES 24 R 335 ALA SER ALA VAL ASP GLN ARG ARG ARG HIS ASN GLN GLN
SEQRES 25 R 335 PRO THR GLU THR GLU HIS GLN PRO GLY ASN GLU ASP LYS
SEQRES 26 R 335 GLN ALA ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 K 582 MET SER THR GLN TYR GLU THR GLN GLY TYR THR ILE ASN
SEQRES 2 K 582 ASN ALA GLY ARG ARG LEU VAL VAL ASP PRO ILE THR ARG
SEQRES 3 K 582 ILE GLU GLY HIS MET ARG CYS GLU VAL ASN ILE ASN ASP
SEQRES 4 K 582 GLN ASN VAL ILE THR ASN ALA VAL SER CYS GLY THR MET
SEQRES 5 K 582 PHE ARG GLY LEU GLU ILE ILE LEU GLN GLY ARG ASP PRO
SEQRES 6 K 582 ARG ASP ALA TRP ALA PHE VAL GLU ARG ILE CYS GLY VAL
SEQRES 7 K 582 CYS THR GLY VAL HIS ALA LEU ALA SER VAL TYR ALA ILE
SEQRES 8 K 582 GLU ASP ALA ILE GLY ILE LYS VAL PRO ASP ASN ALA ASN
SEQRES 9 K 582 ILE ILE ARG ASN ILE MET LEU ALA THR LEU TRP CYS HIS
SEQRES 10 K 582 ASP HIS LEU VAL HIS PHE TYR GLN LEU ALA GLY MET ASP
SEQRES 11 K 582 TRP ILE ASP VAL LEU ASP ALA LEU LYS ALA ASP PRO ARG
SEQRES 12 K 582 LYS THR SER GLU LEU ALA GLN SER LEU SER SER TRP PRO
SEQRES 13 K 582 LYS SER SER PRO GLY TYR PHE PHE ASP VAL GLN ASN ARG
SEQRES 14 K 582 LEU LYS LYS PHE VAL GLU GLY GLY GLN LEU GLY ILE PHE
SEQRES 15 K 582 ARG ASN GLY TYR TRP GLY HIS PRO GLN TYR LYS LEU PRO
SEQRES 16 K 582 PRO GLU ALA ASN LEU MET GLY PHE ALA HIS TYR LEU GLU
SEQRES 17 K 582 ALA LEU ASP PHE GLN ARG GLU ILE VAL LYS ILE HIS ALA
SEQRES 18 K 582 VAL PHE GLY GLY LYS ASN PRO HIS PRO ASN TRP ILE VAL
SEQRES 19 K 582 GLY GLY MET PRO CYS ALA ILE ASN ILE ASP GLU SER GLY
SEQRES 20 K 582 ALA VAL GLY ALA VAL ASN MET GLU ARG LEU ASN LEU VAL
SEQRES 21 K 582 GLN SER ILE ILE THR ARG THR ALA ASP PHE ILE ASN ASN
SEQRES 22 K 582 VAL MET ILE PRO ASP ALA LEU ALA ILE GLY GLN PHE ASN
SEQRES 23 K 582 LYS PRO TRP SER GLU ILE GLY THR GLY LEU SER ASP LYS
SEQRES 24 K 582 CYS VAL LEU SER TYR GLY ALA PHE PRO ASP ILE ALA ASN
SEQRES 25 K 582 ASP PHE GLY GLU LYS SER LEU LEU MET PRO GLY GLY ALA
SEQRES 26 K 582 VAL ILE ASN GLY ASP PHE ASN ASN VAL LEU PRO VAL ASP
SEQRES 27 K 582 LEU VAL ASP PRO GLN GLN VAL GLN GLU PHE VAL ASP HIS
SEQRES 28 K 582 ALA TRP TYR ARG TYR PRO ASN ASP GLN VAL GLY ARG HIS
SEQRES 29 K 582 PRO PHE ASP GLY ILE THR ASP PRO TRP TYR ASN PRO GLY
SEQRES 30 K 582 ASP VAL LYS GLY SER ASP THR ASN ILE GLN GLN LEU ASN
SEQRES 31 K 582 GLU GLN GLU ARG TYR SER TRP ILE LYS ALA PRO ARG TRP
SEQRES 32 K 582 ARG GLY ASN ALA MET GLU VAL GLY PRO LEU ALA ARG THR
SEQRES 33 K 582 LEU ILE ALA TYR HIS LYS GLY ASP ALA ALA THR VAL GLU
SEQRES 34 K 582 SER VAL ASP ARG MET MET SER ALA LEU ASN LEU PRO LEU
SEQRES 35 K 582 SER GLY ILE GLN SER THR LEU GLY ARG ILE LEU CYS ARG
SEQRES 36 K 582 ALA HIS GLU ALA GLN TRP ALA ALA GLY LYS LEU GLN TYR
SEQRES 37 K 582 PHE PHE ASP LYS LEU MET THR ASN LEU LYS ASN GLY ASN
SEQRES 38 K 582 LEU ALA THR ALA SER THR GLU LYS TRP GLU PRO ALA THR
SEQRES 39 K 582 TRP PRO THR GLU CYS ARG GLY VAL GLY PHE THR GLU ALA
SEQRES 40 K 582 PRO ARG GLY ALA LEU GLY HIS TRP ALA ALA ILE ARG ASP
SEQRES 41 K 582 GLY LYS ILE ASP LEU TYR GLN CYS VAL VAL PRO THR THR
SEQRES 42 K 582 TRP ASN ALA SER PRO ARG ASP PRO LYS GLY GLN ILE GLY
SEQRES 43 K 582 ALA TYR GLU ALA ALA LEU MET ASN THR LYS MET ALA ILE
SEQRES 44 K 582 PRO GLU GLN PRO LEU GLU ILE LEU ARG THR LEU HIS SER
SEQRES 45 K 582 PHE ASP PRO CYS LEU ALA CYS SER THR HIS
SEQRES 1 A 235 MET GLN GLN LYS SER ASP ASN VAL VAL SER HIS TYR VAL
SEQRES 2 A 235 PHE GLU ALA PRO VAL ARG ILE TRP HIS TRP LEU THR VAL
SEQRES 3 A 235 LEU CYS MET ALA VAL LEU MET VAL THR GLY TYR PHE ILE
SEQRES 4 A 235 GLY LYS PRO LEU PRO SER VAL SER GLY GLU ALA THR TYR
SEQRES 5 A 235 LEU PHE TYR MET GLY TYR ILE ARG LEU ILE HIS PHE SER
SEQRES 6 A 235 ALA GLY MET VAL PHE THR VAL VAL LEU LEU MET ARG ILE
SEQRES 7 A 235 TYR TRP ALA PHE VAL GLY ASN ARG TYR SER ARG GLU LEU
SEQRES 8 A 235 PHE ILE VAL PRO VAL TRP ARG LYS SER TRP TRP GLN GLY
SEQRES 9 A 235 VAL TRP TYR GLU ILE ARG TRP TYR LEU PHE LEU ALA LYS
SEQRES 10 A 235 ARG PRO SER ALA ASP ILE GLY HIS ASN PRO ILE ALA GLN
SEQRES 11 A 235 ALA ALA MET PHE GLY TYR PHE LEU MET SER VAL PHE MET
SEQRES 12 A 235 ILE ILE THR GLY PHE ALA LEU TYR SER GLU HIS SER GLN
SEQRES 13 A 235 TYR ALA ILE PHE ALA PRO PHE ARG TYR VAL VAL GLU PHE
SEQRES 14 A 235 PHE TYR TRP THR GLY GLY ASN SER MET ASP ILE HIS SER
SEQRES 15 A 235 TRP HIS ARG LEU GLY MET TRP LEU ILE GLY ALA PHE VAL
SEQRES 16 A 235 ILE GLY HIS VAL TYR MET ALA LEU ARG GLU ASP ILE MET
SEQRES 17 A 235 SER ASP ASP THR VAL ILE SER THR MET VAL ASN GLY TYR
SEQRES 18 A 235 ARG SER HIS LYS PHE GLY LYS ILE SER ASN LYS GLU ARG
SEQRES 19 A 235 SER
SEQRES 1 B 235 MET GLN GLN LYS SER ASP ASN VAL VAL SER HIS TYR VAL
SEQRES 2 B 235 PHE GLU ALA PRO VAL ARG ILE TRP HIS TRP LEU THR VAL
SEQRES 3 B 235 LEU CYS MET ALA VAL LEU MET VAL THR GLY TYR PHE ILE
SEQRES 4 B 235 GLY LYS PRO LEU PRO SER VAL SER GLY GLU ALA THR TYR
SEQRES 5 B 235 LEU PHE TYR MET GLY TYR ILE ARG LEU ILE HIS PHE SER
SEQRES 6 B 235 ALA GLY MET VAL PHE THR VAL VAL LEU LEU MET ARG ILE
SEQRES 7 B 235 TYR TRP ALA PHE VAL GLY ASN ARG TYR SER ARG GLU LEU
SEQRES 8 B 235 PHE ILE VAL PRO VAL TRP ARG LYS SER TRP TRP GLN GLY
SEQRES 9 B 235 VAL TRP TYR GLU ILE ARG TRP TYR LEU PHE LEU ALA LYS
SEQRES 10 B 235 ARG PRO SER ALA ASP ILE GLY HIS ASN PRO ILE ALA GLN
SEQRES 11 B 235 ALA ALA MET PHE GLY TYR PHE LEU MET SER VAL PHE MET
SEQRES 12 B 235 ILE ILE THR GLY PHE ALA LEU TYR SER GLU HIS SER GLN
SEQRES 13 B 235 TYR ALA ILE PHE ALA PRO PHE ARG TYR VAL VAL GLU PHE
SEQRES 14 B 235 PHE TYR TRP THR GLY GLY ASN SER MET ASP ILE HIS SER
SEQRES 15 B 235 TRP HIS ARG LEU GLY MET TRP LEU ILE GLY ALA PHE VAL
SEQRES 16 B 235 ILE GLY HIS VAL TYR MET ALA LEU ARG GLU ASP ILE MET
SEQRES 17 B 235 SER ASP ASP THR VAL ILE SER THR MET VAL ASN GLY TYR
SEQRES 18 B 235 ARG SER HIS LYS PHE GLY LYS ILE SER ASN LYS GLU ARG
SEQRES 19 B 235 SER
HET SF4 S 401 8
HET F3S S 402 7
HET ER2 S 403 8
HET FCO L 601 7
HET NI L 602 1
HET MG L 603 1
HET CL L 604 1
HET SF4 T 401 8
HET F3S T 402 7
HET ER2 T 403 8
HET FCO M 601 7
HET NI M 602 1
HET MG M 603 1
HET CL M 604 1
HET SF4 Q 401 8
HET F3S Q 402 7
HET ER2 Q 403 8
HET FCO J 601 7
HET NI J 602 1
HET MG J 603 1
HET CL J 604 1
HET SF4 R 401 8
HET F3S R 402 7
HET ER2 R 403 8
HET FCO K 601 7
HET NI K 602 1
HET MG K 603 1
HET CL K 604 1
HET HEM A 301 43
HET HEM B 301 43
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM ER2 FE4S4
HETNAM FCO CARBONMONOXIDE-(DICYANO) IRON
HETNAM NI NICKEL (II) ION
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 11 SF4 4(FE4 S4)
FORMUL 12 F3S 4(FE3 S4)
FORMUL 13 ER2 4(FE4 S4)
FORMUL 14 FCO 4(C3 FE N2 O)
FORMUL 15 NI 4(NI 2+)
FORMUL 16 MG 4(MG 2+)
FORMUL 17 CL 4(CL 1-)
FORMUL 39 HEM 2(C34 H32 FE N4 O4)
FORMUL 41 HOH *702(H2 O)
HELIX 1 AA1 THR S 18 ILE S 25 1 8
HELIX 2 AA2 LEU S 31 LEU S 39 1 9
HELIX 3 AA3 ALA S 52 TYR S 67 1 16
HELIX 4 AA4 LEU S 81 MET S 86 5 6
HELIX 5 AA5 PHE S 95 GLY S 105 1 11
HELIX 6 AA6 GLY S 113 TRP S 118 1 6
HELIX 7 AA7 GLY S 119 ALA S 124 5 6
HELIX 8 AA8 PRO S 133 VAL S 137 5 5
HELIX 9 AA9 ILE S 152 PHE S 166 1 15
HELIX 10 AB1 PRO S 178 GLY S 183 1 6
HELIX 11 AB2 ARG S 185 LYS S 189 5 5
HELIX 12 AB3 ARG S 192 GLY S 199 1 8
HELIX 13 AB4 ALA S 209 GLY S 213 5 5
HELIX 14 AB5 LEU S 216 GLY S 220 5 5
HELIX 15 AB6 LYS S 222 THR S 226 5 5
HELIX 16 AB7 GLY S 256 ARG S 260 5 5
HELIX 17 AB8 GLY S 274 GLY S 295 1 22
HELIX 18 AB9 GLY L 55 LEU L 60 1 6
HELIX 19 AC1 ASP L 64 ARG L 66 5 3
HELIX 20 AC2 ASP L 67 ARG L 74 1 8
HELIX 21 AC3 GLY L 81 GLY L 96 1 16
HELIX 22 AC4 PRO L 100 LEU L 126 1 27
HELIX 23 AC5 ALA L 127 TRP L 131 5 5
HELIX 24 AC6 VAL L 134 ALA L 140 5 7
HELIX 25 AC7 ASP L 141 SER L 153 1 13
HELIX 26 AC8 SER L 159 GLY L 176 1 18
HELIX 27 AC9 LEU L 179 ARG L 183 5 5
HELIX 28 AD1 PRO L 195 VAL L 217 1 23
HELIX 29 AD2 VAL L 217 GLY L 225 1 9
HELIX 30 AD3 GLY L 247 ALA L 251 5 5
HELIX 31 AD4 ASN L 253 VAL L 274 1 22
HELIX 32 AD5 VAL L 274 ASN L 286 1 13
HELIX 33 AD6 LYS L 287 GLU L 291 5 5
HELIX 34 AD7 THR L 294 LYS L 299 5 6
HELIX 35 AD8 HIS L 364 GLY L 368 5 5
HELIX 36 AD9 GLY L 411 LYS L 422 1 12
HELIX 37 AE1 ASP L 424 ALA L 437 1 14
HELIX 38 AE2 PRO L 441 GLN L 446 5 6
HELIX 39 AE3 SER L 447 ASN L 479 1 33
HELIX 40 AE4 GLU L 491 TRP L 495 5 5
HELIX 41 AE5 VAL L 530 ALA L 536 1 7
HELIX 42 AE6 GLY L 546 MET L 553 1 8
HELIX 43 AE7 PRO L 563 ASP L 574 1 12
HELIX 44 AE8 CYS L 576 HIS L 582 1 7
HELIX 45 AE9 THR T 18 ILE T 25 1 8
HELIX 46 AF1 LEU T 31 LEU T 39 1 9
HELIX 47 AF2 ALA T 52 TYR T 67 1 16
HELIX 48 AF3 LEU T 81 MET T 86 5 6
HELIX 49 AF4 PHE T 95 GLY T 105 1 11
HELIX 50 AF5 GLY T 113 TRP T 118 1 6
HELIX 51 AF6 CYS T 120 ALA T 124 5 5
HELIX 52 AF7 PRO T 133 VAL T 137 5 5
HELIX 53 AF8 ILE T 152 ASP T 167 1 16
HELIX 54 AF9 PRO T 178 GLY T 183 1 6
HELIX 55 AG1 ARG T 185 LYS T 189 5 5
HELIX 56 AG2 ARG T 192 GLY T 199 1 8
HELIX 57 AG3 ALA T 209 GLY T 213 5 5
HELIX 58 AG4 LEU T 216 GLY T 220 5 5
HELIX 59 AG5 LYS T 222 THR T 226 5 5
HELIX 60 AG6 PHE T 241 GLY T 246 5 6
HELIX 61 AG7 GLY T 256 ARG T 260 5 5
HELIX 62 AG8 ILE T 270 GLY T 274 5 5
HELIX 63 AG9 THR T 278 HIS T 297 1 20
HELIX 64 AH1 GLY M 55 LEU M 60 1 6
HELIX 65 AH2 ASP M 64 ARG M 66 5 3
HELIX 66 AH3 ASP M 67 ARG M 74 1 8
HELIX 67 AH4 GLY M 81 GLY M 96 1 16
HELIX 68 AH5 PRO M 100 LEU M 126 1 27
HELIX 69 AH6 ALA M 127 TRP M 131 5 5
HELIX 70 AH7 VAL M 134 ALA M 140 5 7
HELIX 71 AH8 ASP M 141 SER M 153 1 13
HELIX 72 AH9 SER M 159 GLU M 175 1 17
HELIX 73 AI1 LEU M 179 ARG M 183 5 5
HELIX 74 AI2 PRO M 195 VAL M 217 1 23
HELIX 75 AI3 VAL M 217 GLY M 225 1 9
HELIX 76 AI4 GLY M 247 ALA M 251 5 5
HELIX 77 AI5 ASN M 253 VAL M 274 1 22
HELIX 78 AI6 VAL M 274 ASN M 286 1 13
HELIX 79 AI7 LYS M 287 GLU M 291 5 5
HELIX 80 AI8 THR M 294 LYS M 299 5 6
HELIX 81 AI9 HIS M 364 GLY M 368 5 5
HELIX 82 AJ1 GLY M 411 LYS M 422 1 12
HELIX 83 AJ2 ASP M 424 ASN M 439 1 16
HELIX 84 AJ3 PRO M 441 GLN M 446 5 6
HELIX 85 AJ4 SER M 447 ASN M 479 1 33
HELIX 86 AJ5 GLU M 491 TRP M 495 5 5
HELIX 87 AJ6 VAL M 530 ALA M 536 1 7
HELIX 88 AJ7 GLY M 546 MET M 553 1 8
HELIX 89 AJ8 PRO M 563 ASP M 574 1 12
HELIX 90 AJ9 CYS M 576 HIS M 582 1 7
HELIX 91 AK1 THR Q 18 ILE Q 25 1 8
HELIX 92 AK2 LEU Q 31 LEU Q 39 1 9
HELIX 93 AK3 ALA Q 52 TYR Q 67 1 16
HELIX 94 AK4 LEU Q 81 MET Q 86 5 6
HELIX 95 AK5 PHE Q 95 GLY Q 105 1 11
HELIX 96 AK6 GLY Q 113 TRP Q 118 1 6
HELIX 97 AK7 CYS Q 120 ALA Q 124 5 5
HELIX 98 AK8 PRO Q 133 ILE Q 138 1 6
HELIX 99 AK9 ILE Q 152 PHE Q 166 1 15
HELIX 100 AL1 PRO Q 178 GLY Q 183 1 6
HELIX 101 AL2 ARG Q 185 LYS Q 189 5 5
HELIX 102 AL3 ARG Q 192 GLY Q 199 1 8
HELIX 103 AL4 ALA Q 209 GLY Q 213 5 5
HELIX 104 AL5 LEU Q 216 GLY Q 220 5 5
HELIX 105 AL6 LYS Q 222 THR Q 226 5 5
HELIX 106 AL7 GLY Q 256 ARG Q 260 5 5
HELIX 107 AL8 THR Q 275 GLY Q 295 1 21
HELIX 108 AL9 GLY J 55 LEU J 60 1 6
HELIX 109 AM1 ASP J 64 ARG J 66 5 3
HELIX 110 AM2 ASP J 67 ARG J 74 1 8
HELIX 111 AM3 GLY J 81 GLY J 96 1 16
HELIX 112 AM4 PRO J 100 LEU J 126 1 27
HELIX 113 AM5 ALA J 127 TRP J 131 5 5
HELIX 114 AM6 VAL J 134 ALA J 140 5 7
HELIX 115 AM7 ASP J 141 SER J 153 1 13
HELIX 116 AM8 SER J 159 GLU J 175 1 17
HELIX 117 AM9 LEU J 179 ARG J 183 5 5
HELIX 118 AN1 PRO J 195 VAL J 217 1 23
HELIX 119 AN2 VAL J 217 GLY J 225 1 9
HELIX 120 AN3 GLY J 247 ALA J 251 5 5
HELIX 121 AN4 ASN J 253 VAL J 274 1 22
HELIX 122 AN5 VAL J 274 ASN J 286 1 13
HELIX 123 AN6 LYS J 287 GLU J 291 5 5
HELIX 124 AN7 THR J 294 LYS J 299 5 6
HELIX 125 AN8 HIS J 364 GLY J 368 5 5
HELIX 126 AN9 GLY J 411 LYS J 422 1 12
HELIX 127 AO1 ASP J 424 LEU J 438 1 15
HELIX 128 AO2 PRO J 441 GLN J 446 5 6
HELIX 129 AO3 SER J 447 ASN J 479 1 33
HELIX 130 AO4 GLU J 491 TRP J 495 5 5
HELIX 131 AO5 VAL J 530 ALA J 536 1 7
HELIX 132 AO6 GLY J 546 MET J 553 1 8
HELIX 133 AO7 PRO J 563 PHE J 573 1 11
HELIX 134 AO8 CYS J 576 HIS J 582 1 7
HELIX 135 AO9 THR R 18 ARG R 26 1 9
HELIX 136 AP1 LEU R 31 LEU R 39 1 9
HELIX 137 AP2 ALA R 52 TYR R 67 1 16
HELIX 138 AP3 LEU R 81 MET R 86 5 6
HELIX 139 AP4 PHE R 95 GLY R 105 1 11
HELIX 140 AP5 GLY R 113 TRP R 118 1 6
HELIX 141 AP6 GLY R 119 ALA R 124 5 6
HELIX 142 AP7 PRO R 133 VAL R 137 5 5
HELIX 143 AP8 ILE R 152 PHE R 166 1 15
HELIX 144 AP9 PRO R 178 GLY R 183 1 6
HELIX 145 AQ1 ARG R 185 LYS R 189 5 5
HELIX 146 AQ2 ARG R 192 GLY R 199 1 8
HELIX 147 AQ3 ASP R 207 LYS R 212 1 6
HELIX 148 AQ4 LEU R 216 GLY R 220 5 5
HELIX 149 AQ5 LYS R 222 THR R 226 5 5
HELIX 150 AQ6 GLY R 256 ARG R 260 5 5
HELIX 151 AQ7 ILE R 270 GLY R 274 5 5
HELIX 152 AQ8 THR R 278 VAL R 294 1 17
HELIX 153 AQ9 GLY K 55 LEU K 60 1 6
HELIX 154 AR1 ASP K 64 ARG K 66 5 3
HELIX 155 AR2 ASP K 67 ARG K 74 1 8
HELIX 156 AR3 GLY K 81 GLY K 96 1 16
HELIX 157 AR4 PRO K 100 LEU K 126 1 27
HELIX 158 AR5 ALA K 127 TRP K 131 5 5
HELIX 159 AR6 ASP K 133 ALA K 140 5 8
HELIX 160 AR7 ASP K 141 SER K 153 1 13
HELIX 161 AR8 SER K 159 GLY K 176 1 18
HELIX 162 AR9 LEU K 179 ARG K 183 5 5
HELIX 163 AS1 PRO K 195 VAL K 217 1 23
HELIX 164 AS2 VAL K 217 GLY K 225 1 9
HELIX 165 AS3 GLY K 247 ALA K 251 5 5
HELIX 166 AS4 ASN K 253 VAL K 274 1 22
HELIX 167 AS5 VAL K 274 ASN K 286 1 13
HELIX 168 AS6 LYS K 287 GLU K 291 5 5
HELIX 169 AS7 THR K 294 LYS K 299 5 6
HELIX 170 AS8 HIS K 364 GLY K 368 5 5
HELIX 171 AS9 GLY K 411 LYS K 422 1 12
HELIX 172 AT1 ASP K 424 LEU K 438 1 15
HELIX 173 AT2 PRO K 441 GLN K 446 5 6
HELIX 174 AT3 SER K 447 ASN K 479 1 33
HELIX 175 AT4 GLU K 491 TRP K 495 5 5
HELIX 176 AT5 VAL K 530 ALA K 536 1 7
HELIX 177 AT6 GLY K 546 MET K 553 1 8
HELIX 178 AT7 PRO K 563 ASP K 574 1 12
HELIX 179 AT8 CYS K 576 HIS K 582 1 7
HELIX 180 AT9 ARG A 19 LYS A 41 1 23
HELIX 181 AU1 PHE A 54 GLY A 84 1 31
HELIX 182 AU2 TRP A 101 TYR A 112 1 12
HELIX 183 AU3 ALA A 129 SER A 152 1 24
HELIX 184 AU4 PHE A 160 ARG A 164 5 5
HELIX 185 AU5 TYR A 165 THR A 173 1 9
HELIX 186 AU6 ASN A 176 ARG A 204 1 29
HELIX 187 AU7 ARG B 19 LYS B 41 1 23
HELIX 188 AU8 PHE B 54 VAL B 83 1 30
HELIX 189 AU9 VAL B 105 ARG B 110 1 6
HELIX 190 AV1 ALA B 129 GLU B 153 1 25
HELIX 191 AV2 PHE B 160 PRO B 162 5 3
HELIX 192 AV3 PHE B 163 THR B 173 1 11
HELIX 193 AV4 ASN B 176 VAL B 199 1 24
SHEET 1 AA1 5 ILE S 40 ASP S 45 0
SHEET 2 AA1 5 ILE S 7 HIS S 13 1 N VAL S 9 O SER S 41
SHEET 3 AA1 5 TYR S 71 GLU S 76 1 O ALA S 74 N VAL S 10
SHEET 4 AA1 5 ALA S 106 TRP S 112 1 O ILE S 110 N VAL S 75
SHEET 5 AA1 5 ILE S 143 VAL S 146 1 O ILE S 144 N ALA S 111
SHEET 1 AA2 2 ILE S 89 SER S 90 0
SHEET 2 AA2 2 ARG S 93 PRO S 94 -1 O ARG S 93 N SER S 90
SHEET 1 AA3 2 GLN L 4 THR L 7 0
SHEET 2 AA3 2 TYR L 10 ASN L 13 -1 O TYR L 10 N THR L 7
SHEET 1 AA4 3 ARG L 17 VAL L 21 0
SHEET 2 AA4 3 MET L 31 ILE L 37 -1 O VAL L 35 N LEU L 19
SHEET 3 AA4 3 ILE L 43 GLY L 50 -1 O THR L 44 N ASN L 36
SHEET 1 AA5 2 VAL L 301 SER L 303 0
SHEET 2 AA5 2 GLY L 324 VAL L 326 -1 O GLY L 324 N SER L 303
SHEET 1 AA6 2 ALA L 306 PRO L 308 0
SHEET 2 AA6 2 LEU L 319 MET L 321 -1 O LEU L 320 N PHE L 307
SHEET 1 AA7 2 VAL L 345 PHE L 348 0
SHEET 2 AA7 2 ALA L 400 TRP L 403 -1 O ARG L 402 N GLN L 346
SHEET 1 AA8 3 GLU L 498 ALA L 507 0
SHEET 2 AA8 3 GLY L 510 ARG L 519 -1 O ILE L 518 N CYS L 499
SHEET 3 AA8 3 LYS L 522 VAL L 529 -1 O ASP L 524 N ALA L 517
SHEET 1 AA9 5 ILE T 40 ASP T 45 0
SHEET 2 AA9 5 ILE T 7 HIS T 13 1 N TRP T 11 O TYR T 44
SHEET 3 AA9 5 TYR T 71 GLU T 76 1 O ALA T 74 N VAL T 10
SHEET 4 AA9 5 ALA T 106 TRP T 112 1 O ILE T 110 N VAL T 75
SHEET 5 AA9 5 ILE T 143 VAL T 146 1 O ILE T 144 N ILE T 109
SHEET 1 AB1 2 ILE T 89 SER T 90 0
SHEET 2 AB1 2 ARG T 93 PRO T 94 -1 O ARG T 93 N SER T 90
SHEET 1 AB2 2 GLN M 4 THR M 7 0
SHEET 2 AB2 2 TYR M 10 ASN M 13 -1 O ILE M 12 N TYR M 5
SHEET 1 AB3 3 ARG M 17 VAL M 21 0
SHEET 2 AB3 3 MET M 31 ILE M 37 -1 O VAL M 35 N LEU M 19
SHEET 3 AB3 3 ILE M 43 GLY M 50 -1 O CYS M 49 N ARG M 32
SHEET 1 AB4 2 VAL M 301 SER M 303 0
SHEET 2 AB4 2 GLY M 324 VAL M 326 -1 O GLY M 324 N SER M 303
SHEET 1 AB5 2 ALA M 306 PRO M 308 0
SHEET 2 AB5 2 LEU M 319 MET M 321 -1 O LEU M 320 N PHE M 307
SHEET 1 AB6 2 VAL M 345 PHE M 348 0
SHEET 2 AB6 2 ALA M 400 TRP M 403 -1 O ALA M 400 N PHE M 348
SHEET 1 AB7 3 GLU M 498 ALA M 507 0
SHEET 2 AB7 3 GLY M 510 ARG M 519 -1 O ILE M 518 N CYS M 499
SHEET 3 AB7 3 LYS M 522 VAL M 529 -1 O LEU M 525 N ALA M 517
SHEET 1 AB8 5 ILE Q 40 ASP Q 45 0
SHEET 2 AB8 5 ILE Q 7 HIS Q 13 1 N VAL Q 9 O SER Q 41
SHEET 3 AB8 5 TYR Q 71 GLU Q 76 1 O ALA Q 74 N VAL Q 10
SHEET 4 AB8 5 ALA Q 106 TRP Q 112 1 O ILE Q 110 N VAL Q 75
SHEET 5 AB8 5 ILE Q 143 VAL Q 146 1 O ILE Q 144 N ALA Q 111
SHEET 1 AB9 2 ILE Q 89 SER Q 90 0
SHEET 2 AB9 2 ARG Q 93 PRO Q 94 -1 O ARG Q 93 N SER Q 90
SHEET 1 AC1 2 GLN J 4 THR J 7 0
SHEET 2 AC1 2 TYR J 10 ASN J 13 -1 O TYR J 10 N THR J 7
SHEET 1 AC2 3 ARG J 17 VAL J 21 0
SHEET 2 AC2 3 MET J 31 ILE J 37 -1 O CYS J 33 N VAL J 21
SHEET 3 AC2 3 ILE J 43 GLY J 50 -1 O CYS J 49 N ARG J 32
SHEET 1 AC3 3 GLY J 324 VAL J 326 0
SHEET 2 AC3 3 VAL J 301 SER J 303 -1 N SER J 303 O GLY J 324
SHEET 3 AC3 3 GLU J 409 VAL J 410 1 O GLU J 409 N LEU J 302
SHEET 1 AC4 2 ALA J 306 PRO J 308 0
SHEET 2 AC4 2 LEU J 319 MET J 321 -1 O LEU J 320 N PHE J 307
SHEET 1 AC5 2 VAL J 345 PHE J 348 0
SHEET 2 AC5 2 ALA J 400 TRP J 403 -1 O ALA J 400 N PHE J 348
SHEET 1 AC6 3 GLU J 498 ALA J 507 0
SHEET 2 AC6 3 GLY J 510 ARG J 519 -1 O ILE J 518 N CYS J 499
SHEET 3 AC6 3 LYS J 522 VAL J 529 -1 O ASP J 524 N ALA J 517
SHEET 1 AC7 5 ILE R 40 ASP R 45 0
SHEET 2 AC7 5 ILE R 7 HIS R 13 1 N TRP R 11 O TYR R 44
SHEET 3 AC7 5 TYR R 71 GLU R 76 1 O ALA R 74 N VAL R 10
SHEET 4 AC7 5 ALA R 106 TRP R 112 1 O ILE R 110 N VAL R 75
SHEET 5 AC7 5 ILE R 143 VAL R 146 1 O ILE R 144 N ALA R 111
SHEET 1 AC8 2 ILE R 89 SER R 90 0
SHEET 2 AC8 2 ARG R 93 PRO R 94 -1 O ARG R 93 N SER R 90
SHEET 1 AC9 2 GLN K 4 THR K 7 0
SHEET 2 AC9 2 TYR K 10 ASN K 13 -1 O TYR K 10 N THR K 7
SHEET 1 AD1 3 ARG K 17 VAL K 21 0
SHEET 2 AD1 3 MET K 31 ILE K 37 -1 O CYS K 33 N VAL K 21
SHEET 3 AD1 3 ILE K 43 GLY K 50 -1 O CYS K 49 N ARG K 32
SHEET 1 AD2 3 GLY K 324 VAL K 326 0
SHEET 2 AD2 3 VAL K 301 SER K 303 -1 N SER K 303 O GLY K 324
SHEET 3 AD2 3 GLU K 409 VAL K 410 1 O GLU K 409 N LEU K 302
SHEET 1 AD3 2 ALA K 306 PRO K 308 0
SHEET 2 AD3 2 LEU K 319 MET K 321 -1 O LEU K 320 N PHE K 307
SHEET 1 AD4 2 VAL K 345 PHE K 348 0
SHEET 2 AD4 2 ALA K 400 TRP K 403 -1 O ALA K 400 N PHE K 348
SHEET 1 AD5 2 LYS K 380 GLY K 381 0
SHEET 2 AD5 2 ILE K 386 GLN K 388 -1 O GLN K 388 N LYS K 380
SHEET 1 AD6 3 GLU K 498 ALA K 507 0
SHEET 2 AD6 3 GLY K 510 ARG K 519 -1 O ILE K 518 N CYS K 499
SHEET 3 AD6 3 LYS K 522 VAL K 529 -1 O ASP K 524 N ALA K 517
LINK SG CYS S 17 FE1 ER2 S 403 1555 1555 2.21
LINK SG CYS S 20 FE4 ER2 S 403 1555 1555 2.35
LINK SG CYS S 115 FE2 ER2 S 403 1555 1555 2.20
LINK SG CYS S 120 FE3 ER2 S 403 1555 1555 2.34
LINK SG CYS S 149 FE3 ER2 S 403 1555 1555 2.34
LINK ND1 HIS S 187 FE3 SF4 S 401 1555 1555 1.98
LINK SG CYS S 190 FE2 SF4 S 401 1555 1555 2.34
LINK SG CYS S 215 FE1 SF4 S 401 1555 1555 2.25
LINK SG CYS S 221 FE4 SF4 S 401 1555 1555 2.36
LINK SG CYS S 230 FE3 F3S S 402 1555 1555 2.29
LINK SG CYS S 249 FE4 F3S S 402 1555 1555 2.29
LINK SG CYS S 252 FE1 F3S S 402 1555 1555 2.28
LINK OE1 GLU L 57 MG MG L 603 1555 1555 2.05
LINK SG CYS L 76 NI NI L 602 1555 1555 2.15
LINK SG CYS L 79 FE FCO L 601 1555 1555 2.29
LINK SG CYS L 79 NI NI L 602 1555 1555 2.25
LINK O CYS L 528 MG MG L 603 1555 1555 2.07
LINK SG CYS L 576 NI NI L 602 1555 1555 2.12
LINK SG CYS L 579 FE FCO L 601 1555 1555 2.29
LINK SG CYS L 579 NI NI L 602 1555 1555 2.65
LINK NE2 HIS L 582 MG MG L 603 1555 1555 2.16
LINK FE FCO L 601 O HOH L 808 1555 1555 2.09
LINK NI NI L 602 O HOH L 808 1555 1555 1.84
LINK MG MG L 603 O HOH L 745 1555 1555 2.02
LINK MG MG L 603 O HOH L 770 1555 1555 1.98
LINK MG MG L 603 O HOH L 799 1555 1555 2.00
LINK SG CYS T 17 FE1 ER2 T 403 1555 1555 2.25
LINK SG CYS T 20 FE4 ER2 T 403 1555 1555 2.34
LINK SG CYS T 115 FE2 ER2 T 403 1555 1555 2.20
LINK SG CYS T 120 FE3 ER2 T 403 1555 1555 2.30
LINK SG CYS T 149 FE3 ER2 T 403 1555 1555 2.33
LINK ND1 HIS T 187 FE3 SF4 T 401 1555 1555 2.11
LINK SG CYS T 190 FE2 SF4 T 401 1555 1555 2.39
LINK SG CYS T 215 FE1 SF4 T 401 1555 1555 2.20
LINK SG CYS T 221 FE4 SF4 T 401 1555 1555 2.37
LINK SG CYS T 230 FE3 F3S T 402 1555 1555 2.30
LINK SG CYS T 249 FE4 F3S T 402 1555 1555 2.36
LINK SG CYS T 252 FE1 F3S T 402 1555 1555 2.22
LINK OE1 GLU M 57 MG MG M 603 1555 1555 2.27
LINK SG CYS M 76 NI NI M 602 1555 1555 2.20
LINK SG CYS M 79 FE FCO M 601 1555 1555 2.31
LINK SG CYS M 79 NI NI M 602 1555 1555 2.26
LINK O CYS M 528 MG MG M 603 1555 1555 2.09
LINK SG CYS M 576 NI NI M 602 1555 1555 2.17
LINK SG CYS M 579 FE FCO M 601 1555 1555 2.31
LINK SG CYS M 579 NI NI M 602 1555 1555 2.64
LINK NE2 HIS M 582 MG MG M 603 1555 1555 2.05
LINK FE FCO M 601 O HOH M 812 1555 1555 2.14
LINK NI NI M 602 O HOH M 812 1555 1555 1.84
LINK MG MG M 603 O HOH M 755 1555 1555 1.98
LINK MG MG M 603 O HOH M 770 1555 1555 1.97
LINK MG MG M 603 O HOH M 784 1555 1555 2.02
LINK SG CYS Q 17 FE1 ER2 Q 403 1555 1555 2.13
LINK SG CYS Q 20 FE4 ER2 Q 403 1555 1555 2.31
LINK SG CYS Q 115 FE2 ER2 Q 403 1555 1555 2.20
LINK SG CYS Q 120 FE3 ER2 Q 403 1555 1555 2.25
LINK SG CYS Q 149 FE3 ER2 Q 403 1555 1555 2.40
LINK ND1 HIS Q 187 FE3 SF4 Q 401 1555 1555 1.99
LINK SG CYS Q 190 FE2 SF4 Q 401 1555 1555 2.31
LINK SG CYS Q 215 FE1 SF4 Q 401 1555 1555 2.30
LINK SG CYS Q 221 FE4 SF4 Q 401 1555 1555 2.29
LINK SG CYS Q 230 FE3 F3S Q 402 1555 1555 2.34
LINK SG CYS Q 249 FE4 F3S Q 402 1555 1555 2.35
LINK SG CYS Q 252 FE1 F3S Q 402 1555 1555 2.33
LINK OE1 GLU J 57 MG MG J 603 1555 1555 2.04
LINK SG CYS J 76 NI NI J 602 1555 1555 2.17
LINK SG CYS J 79 FE FCO J 601 1555 1555 2.38
LINK SG CYS J 79 NI NI J 602 1555 1555 2.27
LINK O CYS J 528 MG MG J 603 1555 1555 2.15
LINK SG CYS J 576 NI NI J 602 1555 1555 2.12
LINK SG CYS J 579 FE FCO J 601 1555 1555 2.32
LINK SG CYS J 579 NI NI J 602 1555 1555 2.63
LINK NE2 HIS J 582 MG MG J 603 1555 1555 2.24
LINK FE FCO J 601 O HOH J 806 1555 1555 2.23
LINK NI NI J 602 O HOH J 806 1555 1555 1.90
LINK MG MG J 603 O HOH J 707 1555 1555 1.94
LINK MG MG J 603 O HOH J 738 1555 1555 1.91
LINK MG MG J 603 O HOH J 788 1555 1555 1.97
LINK SG CYS R 17 FE1 ER2 R 403 1555 1555 2.17
LINK SG CYS R 20 FE4 ER2 R 403 1555 1555 2.41
LINK SG CYS R 115 FE2 ER2 R 403 1555 1555 2.27
LINK SG CYS R 120 FE3 ER2 R 403 1555 1555 2.28
LINK SG CYS R 149 FE3 ER2 R 403 1555 1555 2.26
LINK ND1 HIS R 187 FE3 SF4 R 401 1555 1555 2.05
LINK SG CYS R 190 FE2 SF4 R 401 1555 1555 2.26
LINK SG CYS R 215 FE1 SF4 R 401 1555 1555 2.22
LINK SG CYS R 221 FE4 SF4 R 401 1555 1555 2.41
LINK SG CYS R 230 FE3 F3S R 402 1555 1555 2.27
LINK SG CYS R 249 FE4 F3S R 402 1555 1555 2.24
LINK SG CYS R 252 FE1 F3S R 402 1555 1555 2.32
LINK OE1 GLU K 57 MG MG K 603 1555 1555 2.07
LINK SG CYS K 76 NI NI K 602 1555 1555 2.18
LINK SG CYS K 79 FE FCO K 601 1555 1555 2.37
LINK SG CYS K 79 NI NI K 602 1555 1555 2.28
LINK O CYS K 528 MG MG K 603 1555 1555 2.20
LINK SG CYS K 576 NI NI K 602 1555 1555 2.11
LINK SG CYS K 579 FE FCO K 601 1555 1555 2.31
LINK NE2 HIS K 582 MG MG K 603 1555 1555 2.15
LINK FE FCO K 601 O HOH K 805 1555 1555 2.14
LINK NI NI K 602 O HOH K 805 1555 1555 1.95
LINK MG MG K 603 O HOH K 731 1555 1555 1.99
LINK MG MG K 603 O HOH K 769 1555 1555 1.93
LINK MG MG K 603 O HOH K 802 1555 1555 2.00
LINK NE2 HIS A 63 FE HEM A 301 1555 1555 2.15
LINK NE2 HIS A 184 FE HEM A 301 1555 1555 2.19
LINK NE2 HIS B 63 FE HEM B 301 1555 1555 2.06
LINK NE2 HIS B 184 FE HEM B 301 1555 1555 2.20
CISPEP 1 HIS S 29 PRO S 30 0 -4.46
CISPEP 2 ARG S 125 PRO S 126 0 5.84
CISPEP 3 CYS S 149 PRO S 150 0 -6.18
CISPEP 4 ASP L 22 PRO L 23 0 9.67
CISPEP 5 ASN L 227 PRO L 228 0 2.50
CISPEP 6 HIS T 29 PRO T 30 0 -3.80
CISPEP 7 ARG T 125 PRO T 126 0 3.31
CISPEP 8 CYS T 149 PRO T 150 0 -8.05
CISPEP 9 ASP M 22 PRO M 23 0 9.77
CISPEP 10 ASN M 227 PRO M 228 0 -0.22
CISPEP 11 HIS Q 29 PRO Q 30 0 -4.77
CISPEP 12 ARG Q 125 PRO Q 126 0 -0.45
CISPEP 13 CYS Q 149 PRO Q 150 0 -3.48
CISPEP 14 ASP J 22 PRO J 23 0 10.49
CISPEP 15 ASN J 227 PRO J 228 0 0.39
CISPEP 16 HIS R 29 PRO R 30 0 -5.27
CISPEP 17 ARG R 125 PRO R 126 0 4.59
CISPEP 18 CYS R 149 PRO R 150 0 -6.42
CISPEP 19 ASP K 22 PRO K 23 0 8.37
CISPEP 20 ASN K 227 PRO K 228 0 2.27
SITE 1 AC1 6 HIS S 187 CYS S 190 ARG S 193 CYS S 215
SITE 2 AC1 6 LEU S 216 CYS S 221
SITE 1 AC2 8 LYS L 226 THR S 226 ASN S 228 CYS S 230
SITE 2 AC2 8 PRO S 242 CYS S 249 LEU S 250 CYS S 252
SITE 1 AC3 11 HIS L 229 GLU S 16 CYS S 17 GLY S 19
SITE 2 AC3 11 CYS S 20 THR S 114 CYS S 115 CYS S 120
SITE 3 AC3 11 GLY S 148 CYS S 149 PRO S 150
SITE 1 AC4 13 CYS L 79 VAL L 82 HIS L 83 ALA L 507
SITE 2 AC4 13 PRO L 508 ARG L 509 LEU L 512 VAL L 530
SITE 3 AC4 13 PRO L 531 THR L 532 CYS L 579 NI L 602
SITE 4 AC4 13 HOH L 808
SITE 1 AC5 6 CYS L 76 CYS L 79 CYS L 576 CYS L 579
SITE 2 AC5 6 FCO L 601 HOH L 808
SITE 1 AC6 6 GLU L 57 CYS L 528 HIS L 582 HOH L 745
SITE 2 AC6 6 HOH L 770 HOH L 799
SITE 1 AC7 2 PHE L 212 ARG L 266
SITE 1 AC8 8 HIS T 187 CYS T 190 ARG T 192 ARG T 193
SITE 2 AC8 8 CYS T 215 LEU T 216 CYS T 221 ILE T 243
SITE 1 AC9 9 LYS M 226 ASN T 228 CYS T 230 TRP T 235
SITE 2 AC9 9 PRO T 242 CYS T 249 LEU T 250 CYS T 252
SITE 3 AC9 9 HOH T 550
SITE 1 AD1 10 ARG M 74 HIS M 229 CYS T 17 GLY T 19
SITE 2 AD1 10 CYS T 20 THR T 114 CYS T 115 CYS T 120
SITE 3 AD1 10 CYS T 149 PRO T 150
SITE 1 AD2 13 CYS M 79 VAL M 82 HIS M 83 ALA M 507
SITE 2 AD2 13 PRO M 508 ARG M 509 LEU M 512 VAL M 530
SITE 3 AD2 13 PRO M 531 THR M 532 CYS M 579 NI M 602
SITE 4 AD2 13 HOH M 812
SITE 1 AD3 6 CYS M 76 CYS M 79 CYS M 576 CYS M 579
SITE 2 AD3 6 FCO M 601 HOH M 812
SITE 1 AD4 6 GLU M 57 CYS M 528 HIS M 582 HOH M 755
SITE 2 AD4 6 HOH M 770 HOH M 784
SITE 1 AD5 2 PHE M 212 ARG M 266
SITE 1 AD6 7 HIS Q 187 CYS Q 190 ARG Q 193 CYS Q 215
SITE 2 AD6 7 LEU Q 216 CYS Q 221 ILE Q 243
SITE 1 AD7 9 THR Q 226 ASN Q 228 CYS Q 230 TRP Q 235
SITE 2 AD7 9 PRO Q 242 CYS Q 249 LEU Q 250 CYS Q 252
SITE 3 AD7 9 HOH Q 547
SITE 1 AD8 11 HIS J 229 GLU Q 16 CYS Q 17 GLY Q 19
SITE 2 AD8 11 CYS Q 20 THR Q 114 CYS Q 115 CYS Q 120
SITE 3 AD8 11 GLY Q 148 CYS Q 149 PRO Q 150
SITE 1 AD9 13 CYS J 79 VAL J 82 HIS J 83 ALA J 507
SITE 2 AD9 13 PRO J 508 ARG J 509 LEU J 512 VAL J 530
SITE 3 AD9 13 PRO J 531 THR J 532 CYS J 579 NI J 602
SITE 4 AD9 13 HOH J 806
SITE 1 AE1 6 CYS J 76 CYS J 79 CYS J 576 CYS J 579
SITE 2 AE1 6 FCO J 601 HOH J 806
SITE 1 AE2 6 GLU J 57 CYS J 528 HIS J 582 HOH J 707
SITE 2 AE2 6 HOH J 738 HOH J 788
SITE 1 AE3 2 PHE J 212 ARG J 266
SITE 1 AE4 9 HIS R 187 CYS R 190 ARG R 192 ARG R 193
SITE 2 AE4 9 CYS R 215 LEU R 216 TYR R 217 CYS R 221
SITE 3 AE4 9 ILE R 243
SITE 1 AE5 10 LYS K 226 ASN R 228 CYS R 230 TRP R 235
SITE 2 AE5 10 PRO R 242 CYS R 249 LEU R 250 GLY R 251
SITE 3 AE5 10 CYS R 252 HOH R 549
SITE 1 AE6 10 HIS K 229 CYS R 17 GLY R 19 CYS R 20
SITE 2 AE6 10 THR R 114 CYS R 115 CYS R 120 GLY R 148
SITE 3 AE6 10 CYS R 149 PRO R 150
SITE 1 AE7 13 CYS K 79 VAL K 82 HIS K 83 ALA K 507
SITE 2 AE7 13 PRO K 508 ARG K 509 LEU K 512 VAL K 530
SITE 3 AE7 13 PRO K 531 THR K 532 CYS K 579 NI K 602
SITE 4 AE7 13 HOH K 805
SITE 1 AE8 6 CYS K 76 CYS K 79 CYS K 576 CYS K 579
SITE 2 AE8 6 FCO K 601 HOH K 805
SITE 1 AE9 6 GLU K 57 CYS K 528 HIS K 582 HOH K 731
SITE 2 AE9 6 HOH K 769 HOH K 802
SITE 1 AF1 2 PHE K 212 ARG K 266
SITE 1 AF2 20 MET A 29 LEU A 32 GLY A 36 TYR A 37
SITE 2 AF2 20 ILE A 39 GLY A 40 ARG A 60 HIS A 63
SITE 3 AF2 20 PHE A 64 GLY A 67 THR A 71 MET A 143
SITE 4 AF2 20 GLY A 147 PHE A 148 LEU A 150 TYR A 151
SITE 5 AF2 20 HIS A 181 HIS A 184 ARG A 185 MET A 188
SITE 1 AF3 18 MET B 29 LEU B 32 GLY B 36 ILE B 39
SITE 2 AF3 18 GLY B 40 ARG B 60 HIS B 63 PHE B 64
SITE 3 AF3 18 GLY B 67 MET B 143 GLY B 147 PHE B 148
SITE 4 AF3 18 LEU B 150 HIS B 181 HIS B 184 ARG B 185
SITE 5 AF3 18 MET B 188 HOH R 548
CRYST1 124.410 165.030 206.220 90.00 90.00 90.00 P 21 21 21 16
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 0.008038 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004849 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.970771 0.034110 -0.237571 -37.92921 1
MTRIX2 2 0.042785 -0.949401 -0.311140 13.40058 1
MTRIX3 2 -0.236163 -0.312210 0.920191 -2.48158 1
MTRIX1 3 -0.661269 0.002711 0.750144 37.21914 1
MTRIX2 3 0.006076 -0.999941 0.008970 10.25319 1
MTRIX3 3 0.750125 0.010490 0.661213 -16.81736 1
MTRIX1 4 0.467220 -0.038955 -0.883283 -69.72984 1
MTRIX2 4 -0.268795 0.945483 -0.183880 10.53673 1
MTRIX3 4 0.842291 0.323334 0.431278 -29.80826 1
MTRIX1 5 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 5 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 5 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 6 -0.970417 0.032000 -0.239304 -37.97910 1
MTRIX2 6 0.044519 -0.950464 -0.307630 13.58366 1
MTRIX3 6 -0.237294 -0.309183 0.920922 -2.51463 1
MTRIX1 7 -0.662567 0.004344 0.748990 37.24781 1
MTRIX2 7 0.005723 -0.999925 0.010862 10.28590 1
MTRIX3 7 0.748981 0.011483 0.662492 -16.75021 1
MTRIX1 8 0.463731 -0.038301 -0.885148 -69.72364 1
MTRIX2 8 -0.266431 0.946792 -0.180553 10.63286 1
MTRIX3 8 0.844966 0.319559 0.428852 -29.99988 1
MTRIX1 9 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 9 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 9 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 10 -0.969517 0.038297 -0.242014 -38.01234 1
MTRIX2 10 0.039248 -0.950684 -0.307669 13.42070 1
MTRIX3 10 -0.241862 -0.307788 0.920201 -2.65974 1
MTRIX1 11 -0.664418 0.003850 0.747351 37.21303 1
MTRIX2 11 0.006083 -0.999926 0.010559 10.30006 1
MTRIX3 11 0.747336 0.011562 0.664346 -16.63049 1
MTRIX1 12 0.464551 -0.043644 -0.884470 -69.66700 1
MTRIX2 12 -0.262389 0.947150 -0.184552 10.26564 1
MTRIX3 12 0.845780 0.317809 0.428548 -30.05929 1
MTRIX1 13 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 13 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 13 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 14 -0.687530 0.005137 0.726138 36.54364 1
MTRIX2 14 0.006834 -0.999885 0.013544 10.41147 1
MTRIX3 14 0.726124 0.014274 0.687416 -14.98331 1
MTRIX1 15 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 15 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 15 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 16 -0.691494 -0.003064 0.722376 36.00779 1
MTRIX2 16 0.010238 -0.999932 0.005559 9.93381 1
MTRIX3 16 0.722310 0.011239 0.691478 -14.70131 1
MTRIX1 17 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 17 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 17 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 18 -0.971193 0.033234 -0.235967 -37.89340 1
MTRIX2 18 0.043357 -0.949055 -0.312115 13.33099 1
MTRIX3 18 -0.234318 -0.313354 0.920274 -2.46327 1
MTRIX1 19 -0.660269 0.000507 0.751029 37.20414 1
MTRIX2 19 0.009078 -0.999921 0.008656 10.13498 1
MTRIX3 19 0.750974 0.012533 0.660213 -16.91804 1
MTRIX1 20 0.469595 -0.034389 -0.882212 -69.87370 1
MTRIX2 20 -0.270266 0.945672 -0.180724 10.67083 1
MTRIX3 20 0.840498 0.323299 0.434788 -29.61018 1
MTRIX1 21 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 21 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 21 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 22 -0.971122 0.034825 -0.236030 -37.88398 1
MTRIX2 22 0.042138 -0.948703 -0.313348 13.29166 1
MTRIX3 22 -0.234835 -0.314245 0.919838 -2.49758 1
MTRIX1 23 -0.661890 0.002236 0.749598 37.24445 1
MTRIX2 23 0.008190 -0.999914 0.010215 10.21703 1
MTRIX3 23 0.749556 0.012901 0.661815 -16.80514 1
MTRIX1 24 0.468879 -0.036942 -0.882490 -69.81789 1
MTRIX2 24 -0.270096 0.945268 -0.183075 10.56085 1
MTRIX3 24 0.840952 0.324197 0.433239 -29.72534 1
MTRIX1 25 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 25 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 25 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 26 -0.971088 0.032368 -0.236519 -37.94660 1
MTRIX2 26 0.044931 -0.948276 -0.314250 13.33624 1
MTRIX3 26 -0.234457 -0.315791 0.919405 -2.55277 1
MTRIX1 27 -0.662517 -0.000349 0.749046 37.16881 1
MTRIX2 27 0.009600 -0.999922 0.008026 10.09418 1
MTRIX3 27 0.748985 0.012508 0.662469 -16.76333 1
MTRIX1 28 0.467532 -0.033096 -0.883357 -69.93391 1
MTRIX2 28 -0.272235 0.945339 -0.179503 10.80165 1
MTRIX3 28 0.841013 0.324404 0.432966 -29.73614 1
MTRIX1 29 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 29 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 29 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 30 -0.971268 0.031071 -0.235951 -37.97193 1
MTRIX2 30 0.045669 -0.948681 -0.312919 13.39108 1
MTRIX3 30 -0.233565 -0.314704 0.920005 -2.47105 1
MTRIX1 31 -0.660069 -0.003946 0.751195 37.02187 1
MTRIX2 31 0.012104 -0.999912 0.005383 9.95238 1
MTRIX3 31 0.751108 0.012645 0.660058 -16.92249 1
MTRIX1 32 0.469431 -0.030042 -0.882458 -70.05372 1
MTRIX2 32 -0.272197 0.945823 -0.176997 10.94780 1
MTRIX3 32 0.839966 0.323290 0.435821 -29.52831 1
MTRIX1 33 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 33 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 33 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 34 -0.656074 0.012424 0.754594 37.32196 1
MTRIX2 34 -0.019205 -0.999816 -0.000235 10.00363 1
MTRIX3 34 0.754452 -0.014646 0.656192 -16.70690 1
MTRIX1 35 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 35 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 35 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 36 -0.685688 0.033296 0.727133 35.40579 1
MTRIX2 36 -0.021969 -0.999445 0.025048 11.50258 1
MTRIX3 36 0.727564 0.001201 0.686039 -14.73069 1
MTRIX1 37 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 37 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 37 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 38 -0.668455 -0.000138 0.743753 37.03980 1
MTRIX2 38 0.014214 -0.999820 0.012590 10.34618 1
MTRIX3 38 0.743617 0.018988 0.668336 -16.35074 1
MTRIX1 39 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 39 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 39 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 40 -0.970946 0.034352 -0.236819 -37.88424 1
MTRIX2 40 0.042740 -0.948835 -0.312866 13.31695 1
MTRIX3 40 -0.235449 -0.313898 0.919800 -2.50124 1
MTRIX1 41 -0.662227 0.001049 0.749303 37.23011 1
MTRIX2 41 0.008591 -0.999923 0.008992 10.17634 1
MTRIX3 41 0.749254 0.012392 0.662167 -16.78222 1
MTRIX1 42 0.467727 -0.036806 -0.883106 -69.77690 1
MTRIX2 42 -0.269977 0.945434 -0.182393 10.60632 1
MTRIX3 42 0.841632 0.323728 0.432268 -29.77041 1
(ATOM LINES ARE NOT SHOWN.)
END
