HEADER OXIDOREDUCTASE 20-DEC-14 4UEW
TITLE STRUCTURE OF H2-TREATED ANAEROBICALLY PURIFIED D. FRUCTOSOVORANS NIFE-
TITLE 2 HYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC [NIFE] HYDROGENASE SMALL SUBUNIT;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: NIFE HYDROGENLYASE SMALL CHAIN, NIFE-HYDROGENASE SMALL
COMPND 5 SUBUNIT;
COMPND 6 EC: 1.12.2.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PERIPLASMIC [NIFE] HYDROGENASE LARGE SUBUNIT;
COMPND 9 CHAIN: Q, R, S;
COMPND 10 SYNONYM: NIFE HYDROGENLYASE LARGE CHAIN, NIFE-HYDROGENASE LARGE
COMPND 11 SUBUNIT;
COMPND 12 EC: 1.12.2.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO FRUCTOSIVORANS JJ;
SOURCE 3 ORGANISM_TAXID: 596151;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: DESULFOVIBRIO FRUCTOSOVORANS JJ;
SOURCE 6 ORGANISM_TAXID: 596151
KEYWDS OXIDOREDUCTASE, NIFE-HYDROGENASE, NI-SIB STATE, NI-C STATE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VOLBEDA,L.MARTIN,P.-P.LIEBGOTT,J.C.FONTECILLA-CAMPS
REVDAT 4 20-DEC-23 4UEW 1 REMARK LINK
REVDAT 3 30-JAN-19 4UEW 1 JRNL REMARK LINK ATOM
REVDAT 2 22-APR-15 4UEW 1 JRNL
REVDAT 1 25-MAR-15 4UEW 0
JRNL AUTH A.VOLBEDA,L.MARTIN,P.P.LIEBGOTT,A.L.DE LACEY,
JRNL AUTH 2 J.C.FONTECILLA-CAMPS
JRNL TITL [NIFE]-HYDROGENASES REVISITED: NICKEL-CARBOXAMIDO BOND
JRNL TITL 2 FORMATION IN A VARIANT WITH ACCRUED O2-TOLERANCE AND A
JRNL TITL 3 TENTATIVE RE-INTERPRETATION OF NI-SI STATES.
JRNL REF METALLOMICS V. 7 710 2015
JRNL REFN ESSN 1756-591X
JRNL PMID 25780984
JRNL DOI 10.1039/C4MT00309H
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 117248
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6255
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5893
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 336
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18409
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 1701
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.44000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : -2.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.67000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.325
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.159
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.917
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19209 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26016 ; 1.320 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2415 ; 5.810 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 773 ;34.737 ;24.450
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3055 ;14.958 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;16.261 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2852 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14386 ; 0.006 ; 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): 9672 ; 0.418 ; 1.020
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12083 ; 0.718 ; 2.293
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9537 ; 0.571 ; 1.061
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 : 14
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 7 3
REMARK 3 1 B 7 B 7 3
REMARK 3 1 C 7 C 7 3
REMARK 3 2 A 8 A 28 1
REMARK 3 2 B 8 B 28 1
REMARK 3 2 C 8 C 28 1
REMARK 3 3 A 29 A 30 3
REMARK 3 3 B 29 B 30 3
REMARK 3 3 C 29 C 30 3
REMARK 3 4 A 31 A 36 1
REMARK 3 4 B 31 B 36 1
REMARK 3 4 C 31 C 36 1
REMARK 3 5 A 37 A 39 3
REMARK 3 5 B 37 B 39 3
REMARK 3 5 C 37 C 39 3
REMARK 3 6 A 40 A 53 1
REMARK 3 6 B 40 B 53 1
REMARK 3 6 C 40 C 53 1
REMARK 3 7 A 54 A 54 3
REMARK 3 7 B 54 B 54 3
REMARK 3 7 C 54 C 54 3
REMARK 3 8 A 55 A 55 4
REMARK 3 8 B 55 B 55 4
REMARK 3 8 C 55 C 55 4
REMARK 3 9 A 56 A 57 1
REMARK 3 9 B 56 B 57 1
REMARK 3 9 C 56 C 57 1
REMARK 3 10 A 58 A 58 4
REMARK 3 10 B 58 B 58 4
REMARK 3 10 C 58 C 58 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 743 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 743 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 743 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 A (A): 359 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 359 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 359 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 A (A): 354 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 354 ; 0.10 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 354 ; 0.11 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 A (A): 148 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 148 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 148 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 A (A): 147 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 147 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 147 ; 0.03 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 10 ; 0.09 ; 0.20
REMARK 3 MEDIUM POSITIONAL 1 B (A): 10 ; 0.07 ; 0.20
REMARK 3 MEDIUM POSITIONAL 1 C (A): 10 ; 0.10 ; 0.20
REMARK 3 LOOSE POSITIONAL 1 A (A): 27 ; 0.20 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 27 ; 0.15 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 27 ; 0.25 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 350 ; 3.73 ; 1.00
REMARK 3 TIGHT THERMAL 1 B (A**2): 350 ; 1.08 ; 1.00
REMARK 3 TIGHT THERMAL 1 C (A**2): 350 ; 3.44 ; 1.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 10 ; 2.99 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 10 ; 1.83 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 10 ; 4.78 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 27 ; 2.80 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 27 ; 1.07 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 27 ; 2.94 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 59 A 60 1
REMARK 3 1 B 59 B 60 1
REMARK 3 1 C 59 C 60 1
REMARK 3 2 A 62 A 62 2
REMARK 3 2 B 62 B 62 2
REMARK 3 2 C 62 C 62 2
REMARK 3 3 A 63 A 64 1
REMARK 3 3 B 63 B 64 1
REMARK 3 3 C 63 C 64 1
REMARK 3 4 A 65 A 68 3
REMARK 3 4 B 65 B 68 3
REMARK 3 4 C 65 C 68 3
REMARK 3 5 A 69 A 70 1
REMARK 3 5 B 69 B 70 1
REMARK 3 5 C 69 C 70 1
REMARK 3 6 A 71 A 71 2
REMARK 3 6 B 71 B 71 2
REMARK 3 6 C 71 C 71 2
REMARK 3 7 A 72 A 81 1
REMARK 3 7 B 72 B 81 1
REMARK 3 7 C 72 C 81 1
REMARK 3 8 A 82 A 85 3
REMARK 3 8 B 82 B 85 3
REMARK 3 8 C 82 C 85 3
REMARK 3 9 A 86 A 91 1
REMARK 3 9 B 86 B 91 1
REMARK 3 9 C 86 C 91 1
REMARK 3 10 A 92 A 92 3
REMARK 3 10 B 92 B 92 3
REMARK 3 10 C 92 C 92 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 13 ; 0.24 ; 0.20
REMARK 3 MEDIUM POSITIONAL 2 B (A): 13 ; 0.24 ; 0.20
REMARK 3 MEDIUM POSITIONAL 2 C (A): 13 ; 0.47 ; 0.20
REMARK 3 LOOSE POSITIONAL 2 A (A): 29 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 B (A): 29 ; 0.05 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 C (A): 29 ; 0.04 ; 5.00
REMARK 3 TIGHT THERMAL 2 A (A**2): 197 ; 4.17 ; 1.00
REMARK 3 TIGHT THERMAL 2 B (A**2): 197 ; 1.42 ; 1.00
REMARK 3 TIGHT THERMAL 2 C (A**2): 197 ; 4.41 ; 1.00
REMARK 3 MEDIUM THERMAL 2 A (A**2): 13 ; 4.29 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 13 ; 2.29 ; 2.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 13 ; 6.01 ; 2.00
REMARK 3 LOOSE THERMAL 2 A (A**2): 29 ; 4.35 ; 10.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 29 ; 1.15 ; 10.00
REMARK 3 LOOSE THERMAL 2 C (A**2): 29 ; 4.83 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 93 A 94 1
REMARK 3 1 B 93 B 94 1
REMARK 3 1 C 93 C 94 1
REMARK 3 2 A 95 A 99 3
REMARK 3 2 B 95 B 99 3
REMARK 3 2 C 95 C 99 3
REMARK 3 3 A 101 A 101 1
REMARK 3 3 B 101 B 101 1
REMARK 3 3 C 101 C 101 1
REMARK 3 4 A 104 A 104 3
REMARK 3 4 B 104 B 104 3
REMARK 3 4 C 104 C 104 3
REMARK 3 5 A 105 A 105 4
REMARK 3 5 B 105 B 105 4
REMARK 3 5 C 105 C 105 4
REMARK 3 6 A 106 A 106 3
REMARK 3 6 B 106 B 106 3
REMARK 3 6 C 106 C 106 3
REMARK 3 7 A 107 A 130 1
REMARK 3 7 B 107 B 130 1
REMARK 3 7 C 107 C 130 1
REMARK 3 8 A 131 A 131 2
REMARK 3 8 B 131 B 131 2
REMARK 3 8 C 131 C 131 2
REMARK 3 9 A 132 A 133 1
REMARK 3 9 B 132 B 133 1
REMARK 3 9 C 132 C 133 1
REMARK 3 10 A 141 A 159 1
REMARK 3 10 B 141 B 159 1
REMARK 3 10 C 141 C 159 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 10 ; 0.07 ; 0.20
REMARK 3 MEDIUM POSITIONAL 3 B (A): 10 ; 0.05 ; 0.20
REMARK 3 MEDIUM POSITIONAL 3 C (A): 10 ; 0.04 ; 0.20
REMARK 3 LOOSE POSITIONAL 3 A (A): 26 ; 0.14 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 B (A): 26 ; 0.17 ; 5.00
REMARK 3 LOOSE POSITIONAL 3 C (A): 26 ; 0.10 ; 5.00
REMARK 3 TIGHT THERMAL 3 A (A**2): 360 ; 4.44 ; 1.00
REMARK 3 TIGHT THERMAL 3 B (A**2): 360 ; 2.93 ; 1.00
REMARK 3 TIGHT THERMAL 3 C (A**2): 360 ; 2.20 ; 1.00
REMARK 3 MEDIUM THERMAL 3 A (A**2): 10 ; 4.48 ; 2.00
REMARK 3 MEDIUM THERMAL 3 B (A**2): 10 ; 1.53 ; 2.00
REMARK 3 MEDIUM THERMAL 3 C (A**2): 10 ; 2.98 ; 2.00
REMARK 3 LOOSE THERMAL 3 A (A**2): 26 ; 4.59 ; 10.00
REMARK 3 LOOSE THERMAL 3 B (A**2): 26 ; 2.44 ; 10.00
REMARK 3 LOOSE THERMAL 3 C (A**2): 26 ; 3.25 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 160 A 160 2
REMARK 3 1 B 160 B 160 2
REMARK 3 1 C 160 C 160 2
REMARK 3 2 A 161 A 162 3
REMARK 3 2 B 161 B 162 3
REMARK 3 2 C 161 C 162 3
REMARK 3 3 A 163 A 163 6
REMARK 3 3 B 163 B 163 6
REMARK 3 3 C 163 C 163 6
REMARK 3 4 A 164 A 164 3
REMARK 3 4 B 164 B 164 3
REMARK 3 4 C 164 C 164 3
REMARK 3 5 A 165 A 167 2
REMARK 3 5 B 165 B 167 2
REMARK 3 5 C 165 C 167 2
REMARK 3 6 A 168 A 169 3
REMARK 3 6 B 168 B 169 3
REMARK 3 6 C 168 C 169 3
REMARK 3 7 A 170 A 171 6
REMARK 3 7 B 170 B 171 6
REMARK 3 7 C 170 C 171 6
REMARK 3 8 A 267 A 267 1
REMARK 3 8 B 267 B 267 1
REMARK 3 8 C 267 C 267 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 A (A): 13 ; 0.03 ; 0.20
REMARK 3 MEDIUM POSITIONAL 4 B (A): 13 ; 0.05 ; 0.20
REMARK 3 MEDIUM POSITIONAL 4 C (A): 13 ; 0.03 ; 0.20
REMARK 3 LOOSE POSITIONAL 4 A (A): 44 ; 0.09 ; 5.00
REMARK 3 LOOSE POSITIONAL 4 B (A): 44 ; 0.09 ; 5.00
REMARK 3 LOOSE POSITIONAL 4 C (A): 44 ; 0.14 ; 5.00
REMARK 3 TIGHT THERMAL 4 A (A**2): 44 ; 4.11 ; 1.00
REMARK 3 TIGHT THERMAL 4 B (A**2): 44 ; 1.90 ; 1.00
REMARK 3 TIGHT THERMAL 4 C (A**2): 44 ; 2.54 ; 1.00
REMARK 3 MEDIUM THERMAL 4 A (A**2): 13 ; 4.01 ; 2.00
REMARK 3 MEDIUM THERMAL 4 B (A**2): 13 ; 2.28 ; 2.00
REMARK 3 MEDIUM THERMAL 4 C (A**2): 13 ; 1.84 ; 2.00
REMARK 3 LOOSE THERMAL 4 A (A**2): 44 ; 4.75 ; 10.00
REMARK 3 LOOSE THERMAL 4 B (A**2): 44 ; 2.19 ; 10.00
REMARK 3 LOOSE THERMAL 4 C (A**2): 44 ; 3.22 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 173 A 175 1
REMARK 3 1 B 173 B 175 1
REMARK 3 1 C 173 C 175 1
REMARK 3 2 A 176 A 177 3
REMARK 3 2 B 176 B 177 3
REMARK 3 2 C 176 C 177 3
REMARK 3 3 A 178 A 179 1
REMARK 3 3 B 178 B 179 1
REMARK 3 3 C 178 C 179 1
REMARK 3 4 A 180 A 182 3
REMARK 3 4 B 180 B 182 3
REMARK 3 4 C 180 C 182 3
REMARK 3 5 A 183 A 187 1
REMARK 3 5 B 183 B 187 1
REMARK 3 5 C 183 C 187 1
REMARK 3 6 A 188 A 190 2
REMARK 3 6 B 188 B 190 2
REMARK 3 6 C 188 C 190 2
REMARK 3 7 A 191 A 194 3
REMARK 3 7 B 191 B 194 3
REMARK 3 7 C 191 C 194 3
REMARK 3 8 A 195 A 196 2
REMARK 3 8 B 195 B 196 2
REMARK 3 8 C 195 C 196 2
REMARK 3 9 A 197 A 198 3
REMARK 3 9 B 197 B 198 3
REMARK 3 9 C 197 C 198 3
REMARK 3 10 A 199 A 202 1
REMARK 3 10 B 199 B 202 1
REMARK 3 10 C 199 C 202 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 5 A (A): 17 ; 0.05 ; 0.20
REMARK 3 MEDIUM POSITIONAL 5 B (A): 17 ; 0.03 ; 0.20
REMARK 3 MEDIUM POSITIONAL 5 C (A): 17 ; 0.05 ; 0.20
REMARK 3 LOOSE POSITIONAL 5 A (A): 51 ; 0.05 ; 5.00
REMARK 3 LOOSE POSITIONAL 5 B (A): 51 ; 0.03 ; 5.00
REMARK 3 LOOSE POSITIONAL 5 C (A): 51 ; 0.04 ; 5.00
REMARK 3 TIGHT THERMAL 5 A (A**2): 177 ; 4.52 ; 1.00
REMARK 3 TIGHT THERMAL 5 B (A**2): 177 ; 5.52 ; 1.00
REMARK 3 TIGHT THERMAL 5 C (A**2): 177 ; 1.94 ; 1.00
REMARK 3 MEDIUM THERMAL 5 A (A**2): 17 ; 4.78 ; 2.00
REMARK 3 MEDIUM THERMAL 5 B (A**2): 17 ; 6.55 ; 2.00
REMARK 3 MEDIUM THERMAL 5 C (A**2): 17 ; 1.85 ; 2.00
REMARK 3 LOOSE THERMAL 5 A (A**2): 51 ; 4.90 ; 10.00
REMARK 3 LOOSE THERMAL 5 B (A**2): 51 ; 6.97 ; 10.00
REMARK 3 LOOSE THERMAL 5 C (A**2): 51 ; 2.67 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 203 A 203 3
REMARK 3 1 B 203 B 203 3
REMARK 3 1 C 203 C 203 3
REMARK 3 2 A 204 A 204 1
REMARK 3 2 B 204 B 204 1
REMARK 3 2 C 204 C 204 1
REMARK 3 3 A 205 A 206 3
REMARK 3 3 B 205 B 206 3
REMARK 3 3 C 205 C 206 3
REMARK 3 4 A 207 A 208 1
REMARK 3 4 B 207 B 208 1
REMARK 3 4 C 207 C 208 1
REMARK 3 5 A 209 A 209 3
REMARK 3 5 B 209 B 209 3
REMARK 3 5 C 209 C 209 3
REMARK 3 6 A 210 A 213 1
REMARK 3 6 B 210 B 213 1
REMARK 3 6 C 210 C 213 1
REMARK 3 7 A 214 A 215 3
REMARK 3 7 B 214 B 215 3
REMARK 3 7 C 214 C 215 3
REMARK 3 8 A 216 A 220 1
REMARK 3 8 B 216 B 220 1
REMARK 3 8 C 216 C 220 1
REMARK 3 9 A 221 A 221 2
REMARK 3 9 B 221 B 221 2
REMARK 3 9 C 221 C 221 2
REMARK 3 10 A 222 A 228 1
REMARK 3 10 B 222 B 228 1
REMARK 3 10 C 222 C 228 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 6 A (A): 3 ; 0.03 ; 0.20
REMARK 3 MEDIUM POSITIONAL 6 B (A): 3 ; 0.02 ; 0.20
REMARK 3 MEDIUM POSITIONAL 6 C (A): 3 ; 0.02 ; 0.20
REMARK 3 LOOSE POSITIONAL 6 A (A): 32 ; 0.36 ; 5.00
REMARK 3 LOOSE POSITIONAL 6 B (A): 32 ; 0.15 ; 5.00
REMARK 3 LOOSE POSITIONAL 6 C (A): 32 ; 0.27 ; 5.00
REMARK 3 TIGHT THERMAL 6 A (A**2): 163 ; 3.41 ; 1.00
REMARK 3 TIGHT THERMAL 6 B (A**2): 163 ; 4.47 ; 1.00
REMARK 3 TIGHT THERMAL 6 C (A**2): 163 ; 1.26 ; 1.00
REMARK 3 MEDIUM THERMAL 6 A (A**2): 3 ; 3.91 ; 2.00
REMARK 3 MEDIUM THERMAL 6 B (A**2): 3 ; 5.05 ; 2.00
REMARK 3 MEDIUM THERMAL 6 C (A**2): 3 ; 1.14 ; 2.00
REMARK 3 LOOSE THERMAL 6 A (A**2): 32 ; 3.84 ; 10.00
REMARK 3 LOOSE THERMAL 6 B (A**2): 32 ; 4.93 ; 10.00
REMARK 3 LOOSE THERMAL 6 C (A**2): 32 ; 1.25 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 9
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 229 A 229 3
REMARK 3 1 B 229 B 229 3
REMARK 3 1 C 229 C 229 3
REMARK 3 2 A 230 A 233 1
REMARK 3 2 B 230 B 233 1
REMARK 3 2 C 230 C 233 1
REMARK 3 3 A 234 A 234 2
REMARK 3 3 B 234 B 234 2
REMARK 3 3 C 234 C 234 2
REMARK 3 4 A 235 A 254 1
REMARK 3 4 B 235 B 254 1
REMARK 3 4 C 235 C 254 1
REMARK 3 5 A 255 A 255 4
REMARK 3 5 B 255 B 255 4
REMARK 3 5 C 255 C 255 4
REMARK 3 6 A 256 A 258 1
REMARK 3 6 B 256 B 258 1
REMARK 3 6 C 256 C 258 1
REMARK 3 7 A 259 A 259 2
REMARK 3 7 B 259 B 259 2
REMARK 3 7 C 259 C 259 2
REMARK 3 8 A 260 A 261 1
REMARK 3 8 B 260 B 261 1
REMARK 3 8 C 260 C 261 1
REMARK 3 9 A 265 A 266 1
REMARK 3 9 B 265 B 266 1
REMARK 3 9 C 265 C 266 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 7 A (A): 16 ; 0.05 ; 0.20
REMARK 3 MEDIUM POSITIONAL 7 B (A): 16 ; 0.06 ; 0.20
REMARK 3 MEDIUM POSITIONAL 7 C (A): 16 ; 0.07 ; 0.20
REMARK 3 LOOSE POSITIONAL 7 A (A): 1 ; 0.07 ; 5.00
REMARK 3 LOOSE POSITIONAL 7 B (A): 1 ; 0.03 ; 5.00
REMARK 3 LOOSE POSITIONAL 7 C (A): 1 ; 0.05 ; 5.00
REMARK 3 TIGHT THERMAL 7 A (A**2): 263 ; 3.67 ; 1.00
REMARK 3 TIGHT THERMAL 7 B (A**2): 263 ; 3.38 ; 1.00
REMARK 3 TIGHT THERMAL 7 C (A**2): 263 ; 1.10 ; 1.00
REMARK 3 MEDIUM THERMAL 7 A (A**2): 16 ; 3.22 ; 2.00
REMARK 3 MEDIUM THERMAL 7 B (A**2): 16 ; 1.71 ; 2.00
REMARK 3 MEDIUM THERMAL 7 C (A**2): 16 ; 2.16 ; 2.00
REMARK 3 LOOSE THERMAL 7 A (A**2): 1 ; 1.11 ; 10.00
REMARK 3 LOOSE THERMAL 7 B (A**2): 1 ; 2.02 ; 10.00
REMARK 3 LOOSE THERMAL 7 C (A**2): 1 ; 0.91 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : Q R S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 7 Q 14 3
REMARK 3 1 R 7 R 14 3
REMARK 3 1 S 7 S 14 3
REMARK 3 2 Q 15 Q 32 1
REMARK 3 2 R 15 R 32 1
REMARK 3 2 S 15 S 32 1
REMARK 3 3 Q 33 Q 40 3
REMARK 3 3 R 33 R 40 3
REMARK 3 3 S 33 S 40 3
REMARK 3 4 Q 41 Q 56 1
REMARK 3 4 R 41 R 56 1
REMARK 3 4 S 41 S 56 1
REMARK 3 5 Q 57 Q 57 3
REMARK 3 5 R 57 R 57 3
REMARK 3 5 S 57 S 57 3
REMARK 3 6 Q 58 Q 61 1
REMARK 3 6 R 58 R 61 1
REMARK 3 6 S 58 S 61 1
REMARK 3 7 Q 62 Q 62 3
REMARK 3 7 R 62 R 62 3
REMARK 3 7 S 62 S 62 3
REMARK 3 8 Q 58 Q 91 1
REMARK 3 8 R 58 R 91 1
REMARK 3 8 S 58 S 91 1
REMARK 3 9 Q 92 Q 94 3
REMARK 3 9 R 92 R 94 3
REMARK 3 9 S 92 S 94 3
REMARK 3 10 Q 95 Q 115 1
REMARK 3 10 R 95 R 115 1
REMARK 3 10 S 95 S 115 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 8 Q (A): 70 ; 0.09 ; 5.00
REMARK 3 LOOSE POSITIONAL 8 R (A): 70 ; 0.08 ; 5.00
REMARK 3 LOOSE POSITIONAL 8 S (A): 70 ; 0.12 ; 5.00
REMARK 3 TIGHT THERMAL 8 Q (A**2): 809 ; 3.40 ; 1.00
REMARK 3 TIGHT THERMAL 8 R (A**2): 809 ; 1.87 ; 1.00
REMARK 3 TIGHT THERMAL 8 S (A**2): 809 ; 3.25 ; 1.00
REMARK 3 LOOSE THERMAL 8 Q (A**2): 70 ; 3.38 ; 10.00
REMARK 3 LOOSE THERMAL 8 R (A**2): 70 ; 2.29 ; 10.00
REMARK 3 LOOSE THERMAL 8 S (A**2): 70 ; 4.58 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : Q R S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 116 Q 116 3
REMARK 3 1 R 116 R 116 3
REMARK 3 1 S 116 S 116 3
REMARK 3 2 Q 117 Q 130 1
REMARK 3 2 R 117 R 130 1
REMARK 3 2 S 117 S 130 1
REMARK 3 3 Q 131 Q 133 5
REMARK 3 3 R 131 R 133 5
REMARK 3 3 S 131 S 133 5
REMARK 3 4 Q 141 Q 142 4
REMARK 3 4 R 141 R 142 4
REMARK 3 4 S 141 S 142 4
REMARK 3 5 Q 151 Q 159 3
REMARK 3 5 R 151 R 159 3
REMARK 3 5 S 151 S 159 3
REMARK 3 6 Q 161 Q 176 3
REMARK 3 6 R 161 R 176 3
REMARK 3 6 S 161 S 176 3
REMARK 3 7 Q 177 Q 180 1
REMARK 3 7 R 177 R 180 1
REMARK 3 7 S 177 S 180 1
REMARK 3 8 Q 181 Q 185 3
REMARK 3 8 R 181 R 185 3
REMARK 3 8 S 181 S 185 3
REMARK 3 9 Q 190 Q 196 3
REMARK 3 9 R 190 R 196 3
REMARK 3 9 S 190 S 196 3
REMARK 3 10 Q 197 Q 205 1
REMARK 3 10 R 197 R 205 1
REMARK 3 10 S 197 S 205 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 9 Q (A): 22 ; 0.05 ; 0.20
REMARK 3 MEDIUM POSITIONAL 9 R (A): 22 ; 0.04 ; 0.20
REMARK 3 MEDIUM POSITIONAL 9 S (A): 22 ; 0.03 ; 0.20
REMARK 3 LOOSE POSITIONAL 9 Q (A): 140 ; 0.08 ; 5.00
REMARK 3 LOOSE POSITIONAL 9 R (A): 140 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 9 S (A): 140 ; 0.08 ; 5.00
REMARK 3 TIGHT THERMAL 9 Q (A**2): 377 ; 3.72 ; 1.00
REMARK 3 TIGHT THERMAL 9 R (A**2): 377 ; 2.14 ; 1.00
REMARK 3 TIGHT THERMAL 9 S (A**2): 377 ; 5.69 ; 1.00
REMARK 3 MEDIUM THERMAL 9 Q (A**2): 22 ; 2.06 ; 2.00
REMARK 3 MEDIUM THERMAL 9 R (A**2): 22 ; 1.93 ; 2.00
REMARK 3 MEDIUM THERMAL 9 S (A**2): 22 ; 3.90 ; 2.00
REMARK 3 LOOSE THERMAL 9 Q (A**2): 140 ; 3.81 ; 10.00
REMARK 3 LOOSE THERMAL 9 R (A**2): 140 ; 2.54 ; 10.00
REMARK 3 LOOSE THERMAL 9 S (A**2): 140 ; 5.98 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : Q R S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 206 Q 214 2
REMARK 3 1 R 206 R 214 2
REMARK 3 1 S 206 S 214 2
REMARK 3 2 Q 215 Q 240 1
REMARK 3 2 R 215 R 240 1
REMARK 3 2 S 215 S 240 1
REMARK 3 3 Q 241 Q 278 3
REMARK 3 3 R 241 R 278 3
REMARK 3 3 S 241 S 278 3
REMARK 3 4 Q 415 Q 421 2
REMARK 3 4 R 415 R 421 2
REMARK 3 4 S 415 S 421 2
REMARK 3 5 Q 422 Q 422 3
REMARK 3 5 R 422 R 422 3
REMARK 3 5 S 422 S 422 3
REMARK 3 6 Q 423 Q 439 1
REMARK 3 6 R 423 R 439 1
REMARK 3 6 S 423 S 439 1
REMARK 3 7 Q 440 Q 446 3
REMARK 3 7 R 440 R 446 3
REMARK 3 7 S 440 S 446 3
REMARK 3 8 Q 456 Q 467 3
REMARK 3 8 R 456 R 467 3
REMARK 3 8 S 456 S 467 3
REMARK 3 9 Q 468 Q 483 1
REMARK 3 9 R 468 R 483 1
REMARK 3 9 S 468 S 483 1
REMARK 3 10 Q 484 Q 492 3
REMARK 3 10 R 484 R 492 3
REMARK 3 10 S 484 S 492 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 10 Q (A): 57 ; 0.04 ; 0.20
REMARK 3 MEDIUM POSITIONAL 10 R (A): 57 ; 0.05 ; 0.20
REMARK 3 MEDIUM POSITIONAL 10 S (A): 57 ; 0.05 ; 0.20
REMARK 3 LOOSE POSITIONAL 10 Q (A): 273 ; 0.12 ; 5.00
REMARK 3 LOOSE POSITIONAL 10 R (A): 273 ; 0.07 ; 5.00
REMARK 3 LOOSE POSITIONAL 10 S (A): 273 ; 0.07 ; 5.00
REMARK 3 TIGHT THERMAL 10 Q (A**2): 743 ; 3.96 ; 1.00
REMARK 3 TIGHT THERMAL 10 R (A**2): 743 ; 2.09 ; 1.00
REMARK 3 TIGHT THERMAL 10 S (A**2): 743 ; 3.40 ; 1.00
REMARK 3 MEDIUM THERMAL 10 Q (A**2): 57 ; 4.28 ; 2.00
REMARK 3 MEDIUM THERMAL 10 R (A**2): 57 ; 2.07 ; 2.00
REMARK 3 MEDIUM THERMAL 10 S (A**2): 57 ; 5.73 ; 2.00
REMARK 3 LOOSE THERMAL 10 Q (A**2): 273 ; 4.01 ; 10.00
REMARK 3 LOOSE THERMAL 10 R (A**2): 273 ; 2.69 ; 10.00
REMARK 3 LOOSE THERMAL 10 S (A**2): 273 ; 2.92 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : Q R S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 493 Q 505 1
REMARK 3 1 R 493 R 505 1
REMARK 3 1 S 493 S 505 1
REMARK 3 2 Q 506 Q 520 3
REMARK 3 2 R 506 R 520 3
REMARK 3 2 S 506 S 520 3
REMARK 3 3 Q 521 Q 525 1
REMARK 3 3 R 521 R 525 1
REMARK 3 3 S 521 S 525 1
REMARK 3 4 Q 530 Q 533 1
REMARK 3 4 R 530 R 533 1
REMARK 3 4 S 530 S 533 1
REMARK 3 5 Q 534 Q 549 1
REMARK 3 5 R 534 R 549 1
REMARK 3 5 S 534 S 549 1
REMARK 3 6 Q 550 Q 553 1
REMARK 3 6 R 550 R 553 1
REMARK 3 6 S 550 S 553 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : Q R S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 279 Q 279 3
REMARK 3 1 R 279 R 279 3
REMARK 3 1 S 279 S 279 3
REMARK 3 2 Q 280 Q 286 1
REMARK 3 2 R 280 R 286 1
REMARK 3 2 S 280 S 286 1
REMARK 3 3 Q 287 Q 288 2
REMARK 3 3 R 287 R 288 2
REMARK 3 3 S 287 S 288 2
REMARK 3 4 Q 289 Q 299 1
REMARK 3 4 R 289 R 299 1
REMARK 3 4 S 289 S 299 1
REMARK 3 5 Q 301 Q 302 1
REMARK 3 5 R 301 R 302 1
REMARK 3 5 S 301 S 302 1
REMARK 3 6 Q 304 Q 318 1
REMARK 3 6 R 304 R 318 1
REMARK 3 6 S 304 S 318 1
REMARK 3 7 Q 319 Q 329 3
REMARK 3 7 R 319 R 329 3
REMARK 3 7 S 319 S 329 3
REMARK 3 8 Q 331 Q 337 3
REMARK 3 8 R 331 R 337 3
REMARK 3 8 S 331 S 337 3
REMARK 3 9 Q 338 Q 341 2
REMARK 3 9 R 338 R 341 2
REMARK 3 9 S 338 S 341 2
REMARK 3 10 Q 345 Q 345 4
REMARK 3 10 R 345 R 345 4
REMARK 3 10 S 345 S 345 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 12 Q (A): 38 ; 0.53 ; 0.20
REMARK 3 MEDIUM POSITIONAL 12 R (A): 38 ; 0.29 ; 0.20
REMARK 3 MEDIUM POSITIONAL 12 S (A): 38 ; 0.28 ; 0.20
REMARK 3 LOOSE POSITIONAL 12 Q (A): 76 ; 0.26 ; 5.00
REMARK 3 LOOSE POSITIONAL 12 R (A): 76 ; 0.25 ; 5.00
REMARK 3 LOOSE POSITIONAL 12 S (A): 76 ; 0.43 ; 5.00
REMARK 3 TIGHT THERMAL 12 Q (A**2): 354 ; 4.30 ; 1.00
REMARK 3 TIGHT THERMAL 12 R (A**2): 354 ; 1.52 ; 1.00
REMARK 3 TIGHT THERMAL 12 S (A**2): 354 ; 4.37 ; 1.00
REMARK 3 MEDIUM THERMAL 12 Q (A**2): 38 ; 4.01 ; 2.00
REMARK 3 MEDIUM THERMAL 12 R (A**2): 38 ; 1.72 ; 2.00
REMARK 3 MEDIUM THERMAL 12 S (A**2): 38 ; 5.13 ; 2.00
REMARK 3 LOOSE THERMAL 12 Q (A**2): 76 ; 4.61 ; 10.00
REMARK 3 LOOSE THERMAL 12 R (A**2): 76 ; 1.43 ; 10.00
REMARK 3 LOOSE THERMAL 12 S (A**2): 76 ; 5.13 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : Q R S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 346 Q 348 3
REMARK 3 1 R 346 R 348 3
REMARK 3 1 S 346 S 348 3
REMARK 3 2 Q 349 Q 351 2
REMARK 3 2 R 349 R 351 2
REMARK 3 2 S 349 S 351 2
REMARK 3 3 Q 352 Q 359 3
REMARK 3 3 R 352 R 359 3
REMARK 3 3 S 352 S 359 3
REMARK 3 4 Q 365 Q 367 3
REMARK 3 4 R 365 R 367 3
REMARK 3 4 S 365 S 367 3
REMARK 3 5 Q 368 Q 376 1
REMARK 3 5 R 368 R 376 1
REMARK 3 5 S 368 S 376 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 13 Q (A): 17 ; 0.05 ; 0.20
REMARK 3 MEDIUM POSITIONAL 13 R (A): 17 ; 0.04 ; 0.20
REMARK 3 MEDIUM POSITIONAL 13 S (A): 17 ; 0.03 ; 0.20
REMARK 3 LOOSE POSITIONAL 13 Q (A): 48 ; 0.07 ; 5.00
REMARK 3 LOOSE POSITIONAL 13 R (A): 48 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 13 S (A): 48 ; 0.04 ; 5.00
REMARK 3 TIGHT THERMAL 13 Q (A**2): 148 ; 4.44 ; 1.00
REMARK 3 TIGHT THERMAL 13 R (A**2): 148 ; 1.07 ; 1.00
REMARK 3 TIGHT THERMAL 13 S (A**2): 148 ; 5.06 ; 1.00
REMARK 3 MEDIUM THERMAL 13 Q (A**2): 17 ; 4.60 ; 2.00
REMARK 3 MEDIUM THERMAL 13 R (A**2): 17 ; 1.01 ; 2.00
REMARK 3 MEDIUM THERMAL 13 S (A**2): 17 ; 5.58 ; 2.00
REMARK 3 LOOSE THERMAL 13 Q (A**2): 48 ; 4.45 ; 10.00
REMARK 3 LOOSE THERMAL 13 R (A**2): 48 ; 1.16 ; 10.00
REMARK 3 LOOSE THERMAL 13 S (A**2): 48 ; 4.38 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : Q R S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 380 Q 392 1
REMARK 3 1 R 380 R 392 1
REMARK 3 1 S 380 S 392 1
REMARK 3 2 Q 393 Q 393 2
REMARK 3 2 R 393 R 393 2
REMARK 3 2 S 393 S 393 2
REMARK 3 3 Q 394 Q 395 3
REMARK 3 3 R 394 R 395 3
REMARK 3 3 S 394 S 395 3
REMARK 3 4 Q 396 Q 400 2
REMARK 3 4 R 396 R 400 2
REMARK 3 4 S 396 S 400 2
REMARK 3 5 Q 401 Q 401 3
REMARK 3 5 R 401 R 401 3
REMARK 3 5 S 401 S 401 3
REMARK 3 6 Q 407 Q 408 5
REMARK 3 6 R 407 R 408 5
REMARK 3 6 S 407 S 408 5
REMARK 3 7 Q 411 Q 414 3
REMARK 3 7 R 411 R 414 3
REMARK 3 7 S 411 S 414 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 14 Q (A): 35 ; 0.03 ; 0.20
REMARK 3 MEDIUM POSITIONAL 14 R (A): 35 ; 0.03 ; 0.20
REMARK 3 MEDIUM POSITIONAL 14 S (A): 35 ; 0.03 ; 0.20
REMARK 3 LOOSE POSITIONAL 14 Q (A): 26 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 14 R (A): 26 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 14 S (A): 26 ; 0.09 ; 5.00
REMARK 3 TIGHT THERMAL 14 Q (A**2): 147 ; 4.61 ; 1.00
REMARK 3 TIGHT THERMAL 14 R (A**2): 147 ; 1.25 ; 1.00
REMARK 3 TIGHT THERMAL 14 S (A**2): 147 ; 5.05 ; 1.00
REMARK 3 MEDIUM THERMAL 14 Q (A**2): 35 ; 5.46 ; 2.00
REMARK 3 MEDIUM THERMAL 14 R (A**2): 35 ; 0.91 ; 2.00
REMARK 3 MEDIUM THERMAL 14 S (A**2): 35 ; 5.37 ; 2.00
REMARK 3 LOOSE THERMAL 14 Q (A**2): 26 ; 4.32 ; 10.00
REMARK 3 LOOSE THERMAL 14 R (A**2): 26 ; 2.53 ; 10.00
REMARK 3 LOOSE THERMAL 14 S (A**2): 26 ; 5.33 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 : A 3 A 264
REMARK 3 RESIDUE RANGE : A 265 A 267
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3463 14.7855 5.1264
REMARK 3 T TENSOR
REMARK 3 T11: 0.0384 T22: 0.0378
REMARK 3 T33: 0.1600 T12: -0.0061
REMARK 3 T13: -0.0502 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.8111 L22: 0.7361
REMARK 3 L33: 1.1401 L12: -0.0490
REMARK 3 L13: -0.3375 L23: -0.0584
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: 0.0028 S13: 0.0835
REMARK 3 S21: 0.0875 S22: 0.0325 S23: -0.0507
REMARK 3 S31: -0.1275 S32: 0.0372 S33: -0.0349
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 : Q 6 Q 549
REMARK 3 RESIDUE RANGE : Q 550 Q 553
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0942 -6.8015 14.9962
REMARK 3 T TENSOR
REMARK 3 T11: 0.0713 T22: 0.0473
REMARK 3 T33: 0.1533 T12: 0.0072
REMARK 3 T13: -0.0472 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4873 L22: 0.7434
REMARK 3 L33: 0.8723 L12: 0.0465
REMARK 3 L13: -0.0408 L23: 0.1075
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: -0.0365 S13: -0.0547
REMARK 3 S21: 0.1719 S22: 0.0037 S23: -0.0436
REMARK 3 S31: 0.1633 S32: 0.0394 S33: -0.0093
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 : B 3 B 264
REMARK 3 RESIDUE RANGE : B 265 B 267
REMARK 3 ORIGIN FOR THE GROUP (A): -39.0545 -46.4796 52.7081
REMARK 3 T TENSOR
REMARK 3 T11: 0.2329 T22: 0.2216
REMARK 3 T33: 0.2842 T12: -0.0357
REMARK 3 T13: 0.0799 T23: 0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 0.8506 L22: 0.9587
REMARK 3 L33: 1.3928 L12: -0.0959
REMARK 3 L13: -0.0761 L23: -0.1045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0833 S12: -0.0991 S13: -0.2136
REMARK 3 S21: 0.2462 S22: -0.0610 S23: 0.2590
REMARK 3 S31: 0.2939 S32: -0.2131 S33: 0.1443
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 : R 5 R 549
REMARK 3 RESIDUE RANGE : R 550 R 553
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2318 -33.1029 49.2412
REMARK 3 T TENSOR
REMARK 3 T11: 0.1374 T22: 0.1932
REMARK 3 T33: 0.1636 T12: 0.0225
REMARK 3 T13: -0.0185 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.6704 L22: 0.8708
REMARK 3 L33: 1.1145 L12: -0.1152
REMARK 3 L13: -0.1801 L23: 0.3283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0611 S12: -0.1414 S13: -0.0022
REMARK 3 S21: 0.1985 S22: 0.0781 S23: -0.0385
REMARK 3 S31: 0.0597 S32: 0.1511 S33: -0.0169
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 : C 5 C 264
REMARK 3 RESIDUE RANGE : C 265 C 267
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8986 5.7527 61.7759
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.2081
REMARK 3 T33: 0.1822 T12: -0.0451
REMARK 3 T13: 0.0239 T23: -0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 1.0530 L22: 1.4163
REMARK 3 L33: 2.2632 L12: 0.5451
REMARK 3 L13: -0.7504 L23: -0.3927
REMARK 3 S TENSOR
REMARK 3 S11: 0.1118 S12: -0.1127 S13: 0.0267
REMARK 3 S21: 0.1870 S22: -0.1243 S23: 0.2250
REMARK 3 S31: 0.1417 S32: -0.2452 S33: 0.0125
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 : S 6 S 549
REMARK 3 RESIDUE RANGE : S 550 S 553
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0769 18.9012 78.1830
REMARK 3 T TENSOR
REMARK 3 T11: 0.4168 T22: 0.3155
REMARK 3 T33: 0.1522 T12: -0.1823
REMARK 3 T13: 0.0636 T23: -0.0922
REMARK 3 L TENSOR
REMARK 3 L11: 1.1008 L22: 1.2576
REMARK 3 L33: 1.9066 L12: 0.3959
REMARK 3 L13: -0.5696 L23: -0.1106
REMARK 3 S TENSOR
REMARK 3 S11: 0.3212 S12: -0.4364 S13: 0.1407
REMARK 3 S21: 0.3988 S22: -0.2699 S23: 0.0856
REMARK 3 S31: -0.3190 S32: 0.1961 S33: -0.0513
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
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 4UEW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1290062634.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123504
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 22.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2FRV
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: INSIDE GLOVE ANAEROBIC BOX, PEG6000,
REMARK 280 MES, PH 6.3, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 50.20000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, S
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Q
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 A 1
REMARK 465 THR A 2
REMARK 465 LEU B 1
REMARK 465 THR B 2
REMARK 465 LEU C 1
REMARK 465 THR C 2
REMARK 465 ALA C 3
REMARK 465 LYS C 4
REMARK 465 MET Q 1
REMARK 465 ALA Q 2
REMARK 465 GLU Q 3
REMARK 465 SER Q 4
REMARK 465 LYS Q 5
REMARK 465 MET R 1
REMARK 465 ALA R 2
REMARK 465 GLU R 3
REMARK 465 SER R 4
REMARK 465 MET S 1
REMARK 465 ALA S 2
REMARK 465 GLU S 3
REMARK 465 SER S 4
REMARK 465 LYS S 5
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 ALA A 3 CB
REMARK 470 LYS R 5 CB CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 215 CD GLU A 215 OE2 -0.068
REMARK 500 PHE A 232 CG PHE A 232 CD2 -0.119
REMARK 500 PHE A 232 CG PHE A 232 CD1 -0.115
REMARK 500 TYR C 224 CE1 TYR C 224 CZ -0.083
REMARK 500 TYR C 261 CG TYR C 261 CD2 -0.118
REMARK 500 TYR C 261 CG TYR C 261 CD1 -0.113
REMARK 500 TYR C 261 CE1 TYR C 261 CZ -0.137
REMARK 500 TYR C 261 CZ TYR C 261 CE2 -0.096
REMARK 500 GLU Q 464 CD GLU Q 464 OE1 -0.103
REMARK 500 GLU Q 517 CD GLU Q 517 OE1 -0.069
REMARK 500 GLU R 517 CD GLU R 517 OE2 -0.116
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 203 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 GLU C 215 OE1 - CD - OE2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 LYS Q 166 CD - CE - NZ ANGL. DEV. = 13.9 DEGREES
REMARK 500 GLU Q 464 OE1 - CD - OE2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 GLU Q 517 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 GLU R 517 OE1 - CD - OE2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 LYS S 161 CD - CE - NZ ANGL. DEV. = 18.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 14 -117.23 -108.63
REMARK 500 GLN A 45 94.98 -168.08
REMARK 500 LEU A 231 169.67 64.65
REMARK 500 ASN B 14 -127.07 -107.17
REMARK 500 GLN B 45 98.95 -160.88
REMARK 500 ILE B 144 76.63 -118.07
REMARK 500 LEU B 231 172.50 66.03
REMARK 500 ASN C 14 -119.33 -114.04
REMARK 500 GLN C 45 96.42 -162.57
REMARK 500 ILE C 144 75.76 -118.40
REMARK 500 LEU C 231 168.79 63.66
REMARK 500 TYR Q 77 -48.98 71.17
REMARK 500 PRO Q 150 151.16 -49.82
REMARK 500 HIS Q 228 83.16 68.89
REMARK 500 GLN Q 230 65.01 -157.39
REMARK 500 PHE Q 231 -9.72 -143.64
REMARK 500 CYS Q 265 -53.23 -121.87
REMARK 500 THR Q 360 -88.92 -113.70
REMARK 500 ASP Q 453 116.33 -167.65
REMARK 500 ASP R 19 112.52 -164.81
REMARK 500 TYR R 77 -49.32 70.95
REMARK 500 HIS R 228 82.09 67.49
REMARK 500 GLN R 230 67.69 -153.96
REMARK 500 PHE R 231 -7.72 -145.51
REMARK 500 ARG R 319 15.12 57.39
REMARK 500 THR R 360 -89.94 -117.43
REMARK 500 TYR R 368 13.24 -140.34
REMARK 500 ASP S 19 112.39 -161.81
REMARK 500 TYR S 77 -47.77 73.72
REMARK 500 HIS S 228 78.81 73.07
REMARK 500 GLN S 230 68.91 -155.03
REMARK 500 PHE S 231 -8.74 -147.66
REMARK 500 PHE S 295 48.22 70.30
REMARK 500 THR S 360 -91.66 -106.04
REMARK 500 ALA S 478 108.81 -56.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C2076 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH Q2018 DISTANCE = 6.05 ANGSTROMS
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 SF4 A1267 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 17 SG
REMARK 620 2 SF4 A1267 S2 116.5
REMARK 620 3 SF4 A1267 S3 100.5 109.1
REMARK 620 4 SF4 A1267 S4 120.3 104.5 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1267 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 SF4 A1267 S1 47.4
REMARK 620 3 SF4 A1267 S2 121.0 107.5
REMARK 620 4 SF4 A1267 S3 55.7 103.1 108.4
REMARK 620 5 CYS A 147 SG 140.4 114.5 97.2 125.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1267 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 114 SG
REMARK 620 2 SF4 A1267 S1 113.6
REMARK 620 3 SF4 A1267 S2 100.9 110.0
REMARK 620 4 SF4 A1267 S4 127.6 101.1 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1265 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 184 ND1
REMARK 620 2 SF4 A1265 S1 102.4
REMARK 620 3 SF4 A1265 S2 118.0 105.6
REMARK 620 4 SF4 A1265 S3 120.2 106.1 103.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1265 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 187 SG
REMARK 620 2 SF4 A1265 S1 111.1
REMARK 620 3 SF4 A1265 S2 103.4 106.4
REMARK 620 4 SF4 A1265 S4 123.4 105.5 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1265 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 212 SG
REMARK 620 2 SF4 A1265 S1 119.7
REMARK 620 3 SF4 A1265 S3 101.6 106.4
REMARK 620 4 SF4 A1265 S4 121.0 103.8 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1265 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 218 SG
REMARK 620 2 SF4 A1265 S2 113.5
REMARK 620 3 SF4 A1265 S3 110.3 103.8
REMARK 620 4 SF4 A1265 S4 118.2 105.9 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A1266 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 227 SG
REMARK 620 2 F3S A1266 S2 110.7
REMARK 620 3 F3S A1266 S3 113.4 102.4
REMARK 620 4 F3S A1266 S4 116.1 112.4 100.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A1266 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 245 SG
REMARK 620 2 F3S A1266 S1 111.2
REMARK 620 3 F3S A1266 S3 112.7 102.0
REMARK 620 4 F3S A1266 S4 115.4 113.4 100.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A1266 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 248 SG
REMARK 620 2 F3S A1266 S1 108.0
REMARK 620 3 F3S A1266 S2 110.7 117.2
REMARK 620 4 F3S A1266 S3 118.4 100.8 101.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1267 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 17 SG
REMARK 620 2 SF4 B1267 S2 121.6
REMARK 620 3 SF4 B1267 S3 116.6 106.1
REMARK 620 4 SF4 B1267 S4 99.0 104.8 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1267 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 20 SG
REMARK 620 2 SF4 B1267 S1 105.2
REMARK 620 3 SF4 B1267 S2 115.2 105.2
REMARK 620 4 SF4 B1267 S4 119.7 106.3 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1267 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 114 SG
REMARK 620 2 SF4 B1267 S1 109.1
REMARK 620 3 SF4 B1267 S2 131.2 104.5
REMARK 620 4 SF4 B1267 S3 97.2 108.9 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1267 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 147 SG
REMARK 620 2 SF4 B1267 S1 114.6
REMARK 620 3 SF4 B1267 S3 97.1 107.8
REMARK 620 4 SF4 B1267 S4 123.3 106.0 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1265 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 184 ND1
REMARK 620 2 SF4 B1265 S1 101.2
REMARK 620 3 SF4 B1265 S2 120.3 106.2
REMARK 620 4 SF4 B1265 S3 119.5 104.8 103.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1265 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 187 SG
REMARK 620 2 SF4 B1265 S1 109.4
REMARK 620 3 SF4 B1265 S2 108.1 106.2
REMARK 620 4 SF4 B1265 S4 121.5 105.2 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1265 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 212 SG
REMARK 620 2 SF4 B1265 S1 118.3
REMARK 620 3 SF4 B1265 S3 99.7 104.5
REMARK 620 4 SF4 B1265 S4 121.3 104.9 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1265 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 218 SG
REMARK 620 2 SF4 B1265 S2 109.6
REMARK 620 3 SF4 B1265 S3 111.6 102.6
REMARK 620 4 SF4 B1265 S4 119.9 105.7 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B1266 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 227 SG
REMARK 620 2 F3S B1266 S2 114.7
REMARK 620 3 F3S B1266 S3 109.8 102.4
REMARK 620 4 F3S B1266 S4 114.2 111.0 103.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B1266 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 245 SG
REMARK 620 2 F3S B1266 S1 110.4
REMARK 620 3 F3S B1266 S3 109.3 101.9
REMARK 620 4 F3S B1266 S4 115.9 115.3 102.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B1266 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 248 SG
REMARK 620 2 F3S B1266 S1 109.5
REMARK 620 3 F3S B1266 S2 107.6 112.8
REMARK 620 4 F3S B1266 S3 123.7 102.2 101.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1267 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 17 SG
REMARK 620 2 SF4 C1267 S2 121.8
REMARK 620 3 SF4 C1267 S3 112.7 103.2
REMARK 620 4 SF4 C1267 S4 104.3 107.0 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1267 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 20 SG
REMARK 620 2 SF4 C1267 S1 101.8
REMARK 620 3 SF4 C1267 S2 121.3 103.8
REMARK 620 4 SF4 C1267 S4 118.1 102.0 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1267 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 114 SG
REMARK 620 2 SF4 C1267 S1 114.2
REMARK 620 3 SF4 C1267 S2 128.2 102.8
REMARK 620 4 SF4 C1267 S3 97.1 110.2 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1267 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 147 SG
REMARK 620 2 SF4 C1267 S1 116.1
REMARK 620 3 SF4 C1267 S3 98.8 108.6
REMARK 620 4 SF4 C1267 S4 124.9 101.0 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1265 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 184 ND1
REMARK 620 2 SF4 C1265 S1 101.1
REMARK 620 3 SF4 C1265 S2 118.1 106.4
REMARK 620 4 SF4 C1265 S3 119.5 105.9 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1265 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 187 SG
REMARK 620 2 SF4 C1265 S1 111.1
REMARK 620 3 SF4 C1265 S2 105.9 105.6
REMARK 620 4 SF4 C1265 S4 121.0 104.4 107.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1265 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 212 SG
REMARK 620 2 SF4 C1265 S1 117.0
REMARK 620 3 SF4 C1265 S3 103.3 105.6
REMARK 620 4 SF4 C1265 S4 119.9 104.6 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1265 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 218 SG
REMARK 620 2 SF4 C1265 S2 114.0
REMARK 620 3 SF4 C1265 S3 109.3 105.1
REMARK 620 4 SF4 C1265 S4 115.8 107.2 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S C1266 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 227 SG
REMARK 620 2 F3S C1266 S2 112.4
REMARK 620 3 F3S C1266 S3 115.5 102.1
REMARK 620 4 F3S C1266 S4 113.2 111.5 101.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S C1266 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 245 SG
REMARK 620 2 F3S C1266 S1 114.6
REMARK 620 3 F3S C1266 S3 104.8 102.3
REMARK 620 4 F3S C1266 S4 114.6 115.5 102.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S C1266 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 248 SG
REMARK 620 2 F3S C1266 S1 107.8
REMARK 620 3 F3S C1266 S2 107.1 115.2
REMARK 620 4 F3S C1266 S3 120.5 101.9 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Q1553 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU Q 53 OE2
REMARK 620 2 LEU Q 495 O 94.2
REMARK 620 3 HIS Q 549 NE2 88.3 88.5
REMARK 620 4 HOH Q2046 O 88.3 177.6 91.7
REMARK 620 5 HOH Q2047 O 86.3 88.4 173.6 91.7
REMARK 620 6 HOH Q2283 O 178.1 87.3 92.9 90.3 92.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI Q1551 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 72 SG
REMARK 620 2 CYS Q 75 SG 98.6
REMARK 620 3 CSO Q 543 SG 89.7 171.4
REMARK 620 4 CYS Q 546 SG 106.9 72.8 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO Q1550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 75 SG
REMARK 620 2 FCO Q1550 C1 162.4
REMARK 620 3 FCO Q1550 C2 95.5 90.0
REMARK 620 4 FCO Q1550 C3 107.2 89.7 85.7
REMARK 620 5 CYS Q 546 SG 79.0 94.5 174.1 98.1
REMARK 620 6 NI Q1551 NI 52.2 110.3 112.3 152.2 62.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG R1553 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU R 53 OE2
REMARK 620 2 LEU R 495 O 96.1
REMARK 620 3 HIS R 549 NE2 83.1 89.1
REMARK 620 4 HOH R2049 O 91.0 172.7 90.0
REMARK 620 5 HOH R2050 O 88.2 96.0 170.3 85.9
REMARK 620 6 HOH R2240 O 176.6 86.7 95.0 86.2 93.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI R1551 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 72 SG
REMARK 620 2 CYS R 75 SG 101.6
REMARK 620 3 CSO R 543 SG 85.6 169.8
REMARK 620 4 CYS R 546 SG 111.6 75.7 108.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO R1550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 75 SG
REMARK 620 2 FCO R1550 C1 162.7
REMARK 620 3 FCO R1550 C2 95.8 95.8
REMARK 620 4 FCO R1550 C3 99.1 94.3 86.9
REMARK 620 5 CYS R 546 SG 78.7 89.1 174.2 95.8
REMARK 620 6 NI R1551 NI 54.4 108.7 116.6 144.1 58.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG S1553 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU S 53 OE2
REMARK 620 2 LEU S 495 O 96.7
REMARK 620 3 HIS S 549 NE2 86.9 91.9
REMARK 620 4 HOH S2021 O 86.3 176.9 89.3
REMARK 620 5 HOH S2022 O 86.5 89.6 173.4 89.5
REMARK 620 6 HOH S2166 O 175.7 87.4 94.4 89.7 92.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI S1551 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 72 SG
REMARK 620 2 CYS S 75 SG 99.2
REMARK 620 3 CSO S 543 SG 88.7 172.0
REMARK 620 4 CYS S 546 SG 106.4 76.1 103.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO S1550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 75 SG
REMARK 620 2 FCO S1550 C1 166.0
REMARK 620 3 FCO S1550 C2 94.1 91.0
REMARK 620 4 FCO S1550 C3 101.7 91.5 87.2
REMARK 620 5 CYS S 546 SG 79.7 94.3 173.2 96.9
REMARK 620 6 NI S1551 NI 55.0 111.0 112.7 148.8 61.3
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 A 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S C 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCO Q 1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI Q 1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Q 1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Q 1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Q 1563
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Q 1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCO R 1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI R 1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL R 1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL R 1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL R 1563
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL R 1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL R 1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL R 1566
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCO S 1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI S 1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG S 1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 1561
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UE2 RELATED DB: PDB
REMARK 900 STRUCTURE OF AIR-TREATED ANAEROBICALLY PURIFIED D. FRUCTOSOVORANS
REMARK 900 NIFE-HYDROGENASE
REMARK 900 RELATED ID: 4UE6 RELATED DB: PDB
REMARK 900 STRUCTURE OF METHYLENE BLUE-TREATED ANAEROBICALLY PURIFIED D.
REMARK 900 FRUCTOSOVORANS NIFE-HYDROGENASE
REMARK 900 RELATED ID: 4UEQ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE V74C LARGE SUBUNIT MUTANT OF D. FRUCTOSOVORANS
REMARK 900 NIFE-HYDROGENASE
DBREF 4UEW A 1 264 UNP P18187 PHNS_DESFR 51 314
DBREF 4UEW B 1 264 UNP P18187 PHNS_DESFR 51 314
DBREF 4UEW C 1 264 UNP P18187 PHNS_DESFR 51 314
DBREF 4UEW Q 1 549 UNP P18188 PHNL_DESFR 1 549
DBREF 4UEW R 1 549 UNP P18188 PHNL_DESFR 1 549
DBREF 4UEW S 1 549 UNP P18188 PHNL_DESFR 1 549
SEQRES 1 A 264 LEU THR ALA LYS HIS ARG PRO SER VAL VAL TRP LEU HIS
SEQRES 2 A 264 ASN ALA GLU CYS THR GLY CYS THR GLU ALA ALA ILE ARG
SEQRES 3 A 264 THR ILE LYS PRO TYR ILE ASP ALA LEU ILE LEU ASP THR
SEQRES 4 A 264 ILE SER LEU ASP TYR GLN GLU THR ILE MET ALA ALA ALA
SEQRES 5 A 264 GLY GLU ALA ALA GLU ALA ALA LEU HIS GLN ALA LEU GLU
SEQRES 6 A 264 GLY LYS ASP GLY TYR TYR LEU VAL VAL GLU GLY GLY LEU
SEQRES 7 A 264 PRO THR ILE ASP GLY GLY GLN TRP GLY MET VAL ALA GLY
SEQRES 8 A 264 HIS PRO MET ILE GLU THR THR LYS LYS ALA ALA ALA LYS
SEQRES 9 A 264 ALA LYS GLY ILE ILE CYS ILE GLY THR CYS SER ALA TYR
SEQRES 10 A 264 GLY GLY VAL GLN LYS ALA LYS PRO ASN PRO SER GLN ALA
SEQRES 11 A 264 LYS GLY VAL SER GLU ALA LEU GLY VAL LYS THR ILE ASN
SEQRES 12 A 264 ILE PRO GLY CYS PRO PRO ASN PRO ILE ASN PHE VAL GLY
SEQRES 13 A 264 ALA VAL VAL HIS VAL LEU THR LYS GLY ILE PRO ASP LEU
SEQRES 14 A 264 ASP GLU ASN GLY ARG PRO LYS LEU PHE TYR GLY GLU LEU
SEQRES 15 A 264 VAL HIS ASP ASN CYS PRO ARG LEU PRO HIS PHE GLU ALA
SEQRES 16 A 264 SER GLU PHE ALA PRO SER PHE ASP SER GLU GLU ALA LYS
SEQRES 17 A 264 LYS GLY PHE CYS LEU TYR GLU LEU GLY CYS LYS GLY PRO
SEQRES 18 A 264 VAL THR TYR ASN ASN CYS PRO LYS VAL LEU PHE ASN GLN
SEQRES 19 A 264 VAL ASN TRP PRO VAL GLN ALA GLY HIS PRO CYS LEU GLY
SEQRES 20 A 264 CYS SER GLU PRO ASP PHE TRP ASP THR MET THR PRO PHE
SEQRES 21 A 264 TYR GLU GLN GLY
SEQRES 1 B 264 LEU THR ALA LYS HIS ARG PRO SER VAL VAL TRP LEU HIS
SEQRES 2 B 264 ASN ALA GLU CYS THR GLY CYS THR GLU ALA ALA ILE ARG
SEQRES 3 B 264 THR ILE LYS PRO TYR ILE ASP ALA LEU ILE LEU ASP THR
SEQRES 4 B 264 ILE SER LEU ASP TYR GLN GLU THR ILE MET ALA ALA ALA
SEQRES 5 B 264 GLY GLU ALA ALA GLU ALA ALA LEU HIS GLN ALA LEU GLU
SEQRES 6 B 264 GLY LYS ASP GLY TYR TYR LEU VAL VAL GLU GLY GLY LEU
SEQRES 7 B 264 PRO THR ILE ASP GLY GLY GLN TRP GLY MET VAL ALA GLY
SEQRES 8 B 264 HIS PRO MET ILE GLU THR THR LYS LYS ALA ALA ALA LYS
SEQRES 9 B 264 ALA LYS GLY ILE ILE CYS ILE GLY THR CYS SER ALA TYR
SEQRES 10 B 264 GLY GLY VAL GLN LYS ALA LYS PRO ASN PRO SER GLN ALA
SEQRES 11 B 264 LYS GLY VAL SER GLU ALA LEU GLY VAL LYS THR ILE ASN
SEQRES 12 B 264 ILE PRO GLY CYS PRO PRO ASN PRO ILE ASN PHE VAL GLY
SEQRES 13 B 264 ALA VAL VAL HIS VAL LEU THR LYS GLY ILE PRO ASP LEU
SEQRES 14 B 264 ASP GLU ASN GLY ARG PRO LYS LEU PHE TYR GLY GLU LEU
SEQRES 15 B 264 VAL HIS ASP ASN CYS PRO ARG LEU PRO HIS PHE GLU ALA
SEQRES 16 B 264 SER GLU PHE ALA PRO SER PHE ASP SER GLU GLU ALA LYS
SEQRES 17 B 264 LYS GLY PHE CYS LEU TYR GLU LEU GLY CYS LYS GLY PRO
SEQRES 18 B 264 VAL THR TYR ASN ASN CYS PRO LYS VAL LEU PHE ASN GLN
SEQRES 19 B 264 VAL ASN TRP PRO VAL GLN ALA GLY HIS PRO CYS LEU GLY
SEQRES 20 B 264 CYS SER GLU PRO ASP PHE TRP ASP THR MET THR PRO PHE
SEQRES 21 B 264 TYR GLU GLN GLY
SEQRES 1 C 264 LEU THR ALA LYS HIS ARG PRO SER VAL VAL TRP LEU HIS
SEQRES 2 C 264 ASN ALA GLU CYS THR GLY CYS THR GLU ALA ALA ILE ARG
SEQRES 3 C 264 THR ILE LYS PRO TYR ILE ASP ALA LEU ILE LEU ASP THR
SEQRES 4 C 264 ILE SER LEU ASP TYR GLN GLU THR ILE MET ALA ALA ALA
SEQRES 5 C 264 GLY GLU ALA ALA GLU ALA ALA LEU HIS GLN ALA LEU GLU
SEQRES 6 C 264 GLY LYS ASP GLY TYR TYR LEU VAL VAL GLU GLY GLY LEU
SEQRES 7 C 264 PRO THR ILE ASP GLY GLY GLN TRP GLY MET VAL ALA GLY
SEQRES 8 C 264 HIS PRO MET ILE GLU THR THR LYS LYS ALA ALA ALA LYS
SEQRES 9 C 264 ALA LYS GLY ILE ILE CYS ILE GLY THR CYS SER ALA TYR
SEQRES 10 C 264 GLY GLY VAL GLN LYS ALA LYS PRO ASN PRO SER GLN ALA
SEQRES 11 C 264 LYS GLY VAL SER GLU ALA LEU GLY VAL LYS THR ILE ASN
SEQRES 12 C 264 ILE PRO GLY CYS PRO PRO ASN PRO ILE ASN PHE VAL GLY
SEQRES 13 C 264 ALA VAL VAL HIS VAL LEU THR LYS GLY ILE PRO ASP LEU
SEQRES 14 C 264 ASP GLU ASN GLY ARG PRO LYS LEU PHE TYR GLY GLU LEU
SEQRES 15 C 264 VAL HIS ASP ASN CYS PRO ARG LEU PRO HIS PHE GLU ALA
SEQRES 16 C 264 SER GLU PHE ALA PRO SER PHE ASP SER GLU GLU ALA LYS
SEQRES 17 C 264 LYS GLY PHE CYS LEU TYR GLU LEU GLY CYS LYS GLY PRO
SEQRES 18 C 264 VAL THR TYR ASN ASN CYS PRO LYS VAL LEU PHE ASN GLN
SEQRES 19 C 264 VAL ASN TRP PRO VAL GLN ALA GLY HIS PRO CYS LEU GLY
SEQRES 20 C 264 CYS SER GLU PRO ASP PHE TRP ASP THR MET THR PRO PHE
SEQRES 21 C 264 TYR GLU GLN GLY
SEQRES 1 Q 549 MET ALA GLU SER LYS PRO THR PRO GLN SER THR PHE THR
SEQRES 2 Q 549 GLY PRO ILE VAL VAL ASP PRO ILE THR ARG ILE GLU GLY
SEQRES 3 Q 549 HIS LEU ARG ILE MET VAL GLU VAL GLU ASN GLY LYS VAL
SEQRES 4 Q 549 LYS ASP ALA TRP SER SER SER GLN LEU PHE ARG GLY LEU
SEQRES 5 Q 549 GLU ILE ILE LEU LYS GLY ARG ASP PRO ARG ASP ALA GLN
SEQRES 6 Q 549 HIS PHE THR GLN ARG ALA CYS GLY VAL CYS THR TYR VAL
SEQRES 7 Q 549 HIS ALA LEU ALA SER SER ARG CYS VAL ASP ASP ALA VAL
SEQRES 8 Q 549 LYS VAL SER ILE PRO ALA ASN ALA ARG MET MET ARG ASN
SEQRES 9 Q 549 LEU VAL MET ALA SER GLN TYR LEU HIS ASP HIS LEU VAL
SEQRES 10 Q 549 HIS PHE TYR HIS LEU HIS ALA LEU ASP TRP VAL ASP VAL
SEQRES 11 Q 549 THR ALA ALA LEU LYS ALA ASP PRO ASN LYS ALA ALA LYS
SEQRES 12 Q 549 LEU ALA ALA SER ILE ALA PRO ALA ARG PRO GLY ASN SER
SEQRES 13 Q 549 ALA LYS ALA LEU LYS ALA VAL GLN ASP LYS LEU LYS ALA
SEQRES 14 Q 549 PHE VAL GLU SER GLY GLN LEU GLY ILE PHE THR ASN ALA
SEQRES 15 Q 549 TYR PHE LEU GLY GLY HIS LYS ALA TYR TYR LEU PRO PRO
SEQRES 16 Q 549 GLU VAL ASP LEU ILE ALA THR ALA HIS TYR LEU GLU ALA
SEQRES 17 Q 549 LEU HIS MET GLN VAL LYS ALA ALA SER ALA MET ALA ILE
SEQRES 18 Q 549 LEU GLY GLY LYS ASN PRO HIS THR GLN PHE THR VAL VAL
SEQRES 19 Q 549 GLY GLY CYS SER ASN TYR GLN GLY LEU THR LYS ASP PRO
SEQRES 20 Q 549 LEU ALA ASN TYR LEU ALA LEU SER LYS GLU VAL CYS GLN
SEQRES 21 Q 549 PHE VAL ASN GLU CYS TYR ILE PRO ASP LEU LEU ALA VAL
SEQRES 22 Q 549 ALA GLY PHE TYR LYS ASP TRP GLY GLY ILE GLY GLY THR
SEQRES 23 Q 549 SER ASN TYR LEU ALA PHE GLY GLU PHE ALA THR ASP ASP
SEQRES 24 Q 549 SER SER PRO GLU LYS HIS LEU ALA THR SER GLN PHE PRO
SEQRES 25 Q 549 SER GLY VAL ILE THR GLY ARG ASP LEU GLY LYS VAL ASP
SEQRES 26 Q 549 ASN VAL ASP LEU GLY ALA ILE TYR GLU ASP VAL LYS TYR
SEQRES 27 Q 549 SER TRP TYR ALA PRO GLY GLY ASP GLY LYS HIS PRO TYR
SEQRES 28 Q 549 ASP GLY VAL THR ASP PRO LYS TYR THR LYS LEU ASP ASP
SEQRES 29 Q 549 LYS ASP HIS TYR SER TRP MET LYS ALA PRO ARG TYR LYS
SEQRES 30 Q 549 GLY LYS ALA MET GLU VAL GLY PRO LEU ALA ARG THR PHE
SEQRES 31 Q 549 ILE ALA TYR ALA LYS GLY GLN PRO ASP PHE LYS LYS VAL
SEQRES 32 Q 549 VAL ASP MET VAL LEU GLY LYS LEU SER VAL PRO ALA THR
SEQRES 33 Q 549 ALA LEU HIS SER THR LEU GLY ARG THR ALA ALA ARG GLY
SEQRES 34 Q 549 ILE GLU THR ALA ILE VAL CYS ALA ASN MET GLU LYS TRP
SEQRES 35 Q 549 ILE LYS GLU MET ALA ASP SER GLY ALA LYS ASP ASN THR
SEQRES 36 Q 549 LEU CYS ALA LYS TRP GLU MET PRO GLU GLU SER LYS GLY
SEQRES 37 Q 549 VAL GLY LEU ALA ASP ALA PRO ARG GLY ALA LEU SER HIS
SEQRES 38 Q 549 TRP ILE ARG ILE LYS GLY LYS LYS ILE ASP ASN PHE GLN
SEQRES 39 Q 549 LEU VAL VAL PRO SER THR TRP ASN LEU GLY PRO ARG GLY
SEQRES 40 Q 549 ALA GLN GLY ASP LYS SER PRO VAL GLU GLU ALA LEU ILE
SEQRES 41 Q 549 GLY THR PRO ILE ALA ASP PRO LYS ARG PRO VAL GLU ILE
SEQRES 42 Q 549 LEU ARG THR VAL HIS ALA PHE ASP PRO CSO ILE ALA CYS
SEQRES 43 Q 549 GLY VAL HIS
SEQRES 1 R 549 MET ALA GLU SER LYS PRO THR PRO GLN SER THR PHE THR
SEQRES 2 R 549 GLY PRO ILE VAL VAL ASP PRO ILE THR ARG ILE GLU GLY
SEQRES 3 R 549 HIS LEU ARG ILE MET VAL GLU VAL GLU ASN GLY LYS VAL
SEQRES 4 R 549 LYS ASP ALA TRP SER SER SER GLN LEU PHE ARG GLY LEU
SEQRES 5 R 549 GLU ILE ILE LEU LYS GLY ARG ASP PRO ARG ASP ALA GLN
SEQRES 6 R 549 HIS PHE THR GLN ARG ALA CYS GLY VAL CYS THR TYR VAL
SEQRES 7 R 549 HIS ALA LEU ALA SER SER ARG CYS VAL ASP ASP ALA VAL
SEQRES 8 R 549 LYS VAL SER ILE PRO ALA ASN ALA ARG MET MET ARG ASN
SEQRES 9 R 549 LEU VAL MET ALA SER GLN TYR LEU HIS ASP HIS LEU VAL
SEQRES 10 R 549 HIS PHE TYR HIS LEU HIS ALA LEU ASP TRP VAL ASP VAL
SEQRES 11 R 549 THR ALA ALA LEU LYS ALA ASP PRO ASN LYS ALA ALA LYS
SEQRES 12 R 549 LEU ALA ALA SER ILE ALA PRO ALA ARG PRO GLY ASN SER
SEQRES 13 R 549 ALA LYS ALA LEU LYS ALA VAL GLN ASP LYS LEU LYS ALA
SEQRES 14 R 549 PHE VAL GLU SER GLY GLN LEU GLY ILE PHE THR ASN ALA
SEQRES 15 R 549 TYR PHE LEU GLY GLY HIS LYS ALA TYR TYR LEU PRO PRO
SEQRES 16 R 549 GLU VAL ASP LEU ILE ALA THR ALA HIS TYR LEU GLU ALA
SEQRES 17 R 549 LEU HIS MET GLN VAL LYS ALA ALA SER ALA MET ALA ILE
SEQRES 18 R 549 LEU GLY GLY LYS ASN PRO HIS THR GLN PHE THR VAL VAL
SEQRES 19 R 549 GLY GLY CYS SER ASN TYR GLN GLY LEU THR LYS ASP PRO
SEQRES 20 R 549 LEU ALA ASN TYR LEU ALA LEU SER LYS GLU VAL CYS GLN
SEQRES 21 R 549 PHE VAL ASN GLU CYS TYR ILE PRO ASP LEU LEU ALA VAL
SEQRES 22 R 549 ALA GLY PHE TYR LYS ASP TRP GLY GLY ILE GLY GLY THR
SEQRES 23 R 549 SER ASN TYR LEU ALA PHE GLY GLU PHE ALA THR ASP ASP
SEQRES 24 R 549 SER SER PRO GLU LYS HIS LEU ALA THR SER GLN PHE PRO
SEQRES 25 R 549 SER GLY VAL ILE THR GLY ARG ASP LEU GLY LYS VAL ASP
SEQRES 26 R 549 ASN VAL ASP LEU GLY ALA ILE TYR GLU ASP VAL LYS TYR
SEQRES 27 R 549 SER TRP TYR ALA PRO GLY GLY ASP GLY LYS HIS PRO TYR
SEQRES 28 R 549 ASP GLY VAL THR ASP PRO LYS TYR THR LYS LEU ASP ASP
SEQRES 29 R 549 LYS ASP HIS TYR SER TRP MET LYS ALA PRO ARG TYR LYS
SEQRES 30 R 549 GLY LYS ALA MET GLU VAL GLY PRO LEU ALA ARG THR PHE
SEQRES 31 R 549 ILE ALA TYR ALA LYS GLY GLN PRO ASP PHE LYS LYS VAL
SEQRES 32 R 549 VAL ASP MET VAL LEU GLY LYS LEU SER VAL PRO ALA THR
SEQRES 33 R 549 ALA LEU HIS SER THR LEU GLY ARG THR ALA ALA ARG GLY
SEQRES 34 R 549 ILE GLU THR ALA ILE VAL CYS ALA ASN MET GLU LYS TRP
SEQRES 35 R 549 ILE LYS GLU MET ALA ASP SER GLY ALA LYS ASP ASN THR
SEQRES 36 R 549 LEU CYS ALA LYS TRP GLU MET PRO GLU GLU SER LYS GLY
SEQRES 37 R 549 VAL GLY LEU ALA ASP ALA PRO ARG GLY ALA LEU SER HIS
SEQRES 38 R 549 TRP ILE ARG ILE LYS GLY LYS LYS ILE ASP ASN PHE GLN
SEQRES 39 R 549 LEU VAL VAL PRO SER THR TRP ASN LEU GLY PRO ARG GLY
SEQRES 40 R 549 ALA GLN GLY ASP LYS SER PRO VAL GLU GLU ALA LEU ILE
SEQRES 41 R 549 GLY THR PRO ILE ALA ASP PRO LYS ARG PRO VAL GLU ILE
SEQRES 42 R 549 LEU ARG THR VAL HIS ALA PHE ASP PRO CSO ILE ALA CYS
SEQRES 43 R 549 GLY VAL HIS
SEQRES 1 S 549 MET ALA GLU SER LYS PRO THR PRO GLN SER THR PHE THR
SEQRES 2 S 549 GLY PRO ILE VAL VAL ASP PRO ILE THR ARG ILE GLU GLY
SEQRES 3 S 549 HIS LEU ARG ILE MET VAL GLU VAL GLU ASN GLY LYS VAL
SEQRES 4 S 549 LYS ASP ALA TRP SER SER SER GLN LEU PHE ARG GLY LEU
SEQRES 5 S 549 GLU ILE ILE LEU LYS GLY ARG ASP PRO ARG ASP ALA GLN
SEQRES 6 S 549 HIS PHE THR GLN ARG ALA CYS GLY VAL CYS THR TYR VAL
SEQRES 7 S 549 HIS ALA LEU ALA SER SER ARG CYS VAL ASP ASP ALA VAL
SEQRES 8 S 549 LYS VAL SER ILE PRO ALA ASN ALA ARG MET MET ARG ASN
SEQRES 9 S 549 LEU VAL MET ALA SER GLN TYR LEU HIS ASP HIS LEU VAL
SEQRES 10 S 549 HIS PHE TYR HIS LEU HIS ALA LEU ASP TRP VAL ASP VAL
SEQRES 11 S 549 THR ALA ALA LEU LYS ALA ASP PRO ASN LYS ALA ALA LYS
SEQRES 12 S 549 LEU ALA ALA SER ILE ALA PRO ALA ARG PRO GLY ASN SER
SEQRES 13 S 549 ALA LYS ALA LEU LYS ALA VAL GLN ASP LYS LEU LYS ALA
SEQRES 14 S 549 PHE VAL GLU SER GLY GLN LEU GLY ILE PHE THR ASN ALA
SEQRES 15 S 549 TYR PHE LEU GLY GLY HIS LYS ALA TYR TYR LEU PRO PRO
SEQRES 16 S 549 GLU VAL ASP LEU ILE ALA THR ALA HIS TYR LEU GLU ALA
SEQRES 17 S 549 LEU HIS MET GLN VAL LYS ALA ALA SER ALA MET ALA ILE
SEQRES 18 S 549 LEU GLY GLY LYS ASN PRO HIS THR GLN PHE THR VAL VAL
SEQRES 19 S 549 GLY GLY CYS SER ASN TYR GLN GLY LEU THR LYS ASP PRO
SEQRES 20 S 549 LEU ALA ASN TYR LEU ALA LEU SER LYS GLU VAL CYS GLN
SEQRES 21 S 549 PHE VAL ASN GLU CYS TYR ILE PRO ASP LEU LEU ALA VAL
SEQRES 22 S 549 ALA GLY PHE TYR LYS ASP TRP GLY GLY ILE GLY GLY THR
SEQRES 23 S 549 SER ASN TYR LEU ALA PHE GLY GLU PHE ALA THR ASP ASP
SEQRES 24 S 549 SER SER PRO GLU LYS HIS LEU ALA THR SER GLN PHE PRO
SEQRES 25 S 549 SER GLY VAL ILE THR GLY ARG ASP LEU GLY LYS VAL ASP
SEQRES 26 S 549 ASN VAL ASP LEU GLY ALA ILE TYR GLU ASP VAL LYS TYR
SEQRES 27 S 549 SER TRP TYR ALA PRO GLY GLY ASP GLY LYS HIS PRO TYR
SEQRES 28 S 549 ASP GLY VAL THR ASP PRO LYS TYR THR LYS LEU ASP ASP
SEQRES 29 S 549 LYS ASP HIS TYR SER TRP MET LYS ALA PRO ARG TYR LYS
SEQRES 30 S 549 GLY LYS ALA MET GLU VAL GLY PRO LEU ALA ARG THR PHE
SEQRES 31 S 549 ILE ALA TYR ALA LYS GLY GLN PRO ASP PHE LYS LYS VAL
SEQRES 32 S 549 VAL ASP MET VAL LEU GLY LYS LEU SER VAL PRO ALA THR
SEQRES 33 S 549 ALA LEU HIS SER THR LEU GLY ARG THR ALA ALA ARG GLY
SEQRES 34 S 549 ILE GLU THR ALA ILE VAL CYS ALA ASN MET GLU LYS TRP
SEQRES 35 S 549 ILE LYS GLU MET ALA ASP SER GLY ALA LYS ASP ASN THR
SEQRES 36 S 549 LEU CYS ALA LYS TRP GLU MET PRO GLU GLU SER LYS GLY
SEQRES 37 S 549 VAL GLY LEU ALA ASP ALA PRO ARG GLY ALA LEU SER HIS
SEQRES 38 S 549 TRP ILE ARG ILE LYS GLY LYS LYS ILE ASP ASN PHE GLN
SEQRES 39 S 549 LEU VAL VAL PRO SER THR TRP ASN LEU GLY PRO ARG GLY
SEQRES 40 S 549 ALA GLN GLY ASP LYS SER PRO VAL GLU GLU ALA LEU ILE
SEQRES 41 S 549 GLY THR PRO ILE ALA ASP PRO LYS ARG PRO VAL GLU ILE
SEQRES 42 S 549 LEU ARG THR VAL HIS ALA PHE ASP PRO CSO ILE ALA CYS
SEQRES 43 S 549 GLY VAL HIS
MODRES 4UEW CSO Q 543 CYS S-HYDROXYCYSTEINE
MODRES 4UEW CSO R 543 CYS S-HYDROXYCYSTEINE
MODRES 4UEW CSO S 543 CYS S-HYDROXYCYSTEINE
HET CSO Q 543 7
HET CSO R 543 7
HET CSO S 543 7
HET SF4 A1265 8
HET F3S A1266 7
HET SF4 A1267 8
HET GOL A1271 6
HET GOL A1272 6
HET GOL A1273 6
HET SF4 B1265 8
HET F3S B1266 7
HET SF4 B1267 8
HET SF4 C1265 8
HET F3S C1266 7
HET SF4 C1267 8
HET FCO Q1550 7
HET NI Q1551 1
HET MG Q1553 1
HET GOL Q1561 6
HET GOL Q1562 6
HET GOL Q1563 6
HET GOL Q1564 6
HET FCO R1550 7
HET NI R1551 1
HET MG R1553 1
HET GOL R1561 6
HET GOL R1562 6
HET GOL R1563 6
HET GOL R1564 6
HET GOL R1565 6
HET GOL R1566 6
HET FCO S1550 7
HET NI S1551 1
HET MG S1553 1
HET GOL S1561 6
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM GOL GLYCEROL
HETNAM FCO CARBONMONOXIDE-(DICYANO) IRON
HETNAM NI NICKEL (II) ION
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 CSO 3(C3 H7 N O3 S)
FORMUL 7 SF4 6(FE4 S4)
FORMUL 8 F3S 3(FE3 S4)
FORMUL 10 GOL 14(C3 H8 O3)
FORMUL 19 FCO 3(C3 FE N2 O)
FORMUL 20 NI 3(NI 2+)
FORMUL 21 MG 3(MG 2+)
FORMUL 39 HOH *1701(H2 O)
HELIX 1 1 THR A 18 ILE A 25 1 8
HELIX 2 2 TYR A 31 THR A 39 1 9
HELIX 3 3 ALA A 52 GLU A 65 1 14
HELIX 4 4 ILE A 81 GLN A 85 5 5
HELIX 5 5 MET A 94 LYS A 104 1 11
HELIX 6 6 GLY A 112 GLY A 118 1 7
HELIX 7 7 GLY A 119 ALA A 123 5 5
HELIX 8 8 GLY A 132 GLY A 138 1 7
HELIX 9 9 ASN A 150 LYS A 164 1 15
HELIX 10 10 PRO A 175 GLY A 180 1 6
HELIX 11 11 VAL A 183 CYS A 187 5 5
HELIX 12 12 ARG A 189 ALA A 195 1 7
HELIX 13 13 SER A 204 LYS A 209 1 6
HELIX 14 14 LEU A 213 GLY A 217 5 5
HELIX 15 15 LYS A 219 THR A 223 5 5
HELIX 16 16 ASN A 226 LEU A 231 1 6
HELIX 17 17 ASP A 252 MET A 257 1 6
HELIX 18 18 THR B 18 ILE B 25 1 8
HELIX 19 19 TYR B 31 THR B 39 1 9
HELIX 20 20 ALA B 52 GLU B 65 1 14
HELIX 21 21 ILE B 81 GLN B 85 5 5
HELIX 22 22 MET B 94 ALA B 105 1 12
HELIX 23 23 GLY B 112 GLY B 118 1 7
HELIX 24 24 GLY B 119 ALA B 123 5 5
HELIX 25 25 GLY B 132 GLY B 138 1 7
HELIX 26 26 ASN B 150 LYS B 164 1 15
HELIX 27 27 PRO B 175 GLY B 180 1 6
HELIX 28 28 VAL B 183 CYS B 187 5 5
HELIX 29 29 ARG B 189 ALA B 195 1 7
HELIX 30 30 SER B 204 LYS B 209 1 6
HELIX 31 31 LEU B 213 GLY B 217 5 5
HELIX 32 32 LYS B 219 THR B 223 5 5
HELIX 33 33 ASN B 226 LEU B 231 1 6
HELIX 34 34 ASP B 252 MET B 257 1 6
HELIX 35 35 THR C 18 ILE C 25 1 8
HELIX 36 36 TYR C 31 THR C 39 1 9
HELIX 37 37 GLY C 53 GLU C 65 1 13
HELIX 38 38 ILE C 81 GLN C 85 5 5
HELIX 39 39 MET C 94 ALA C 105 1 12
HELIX 40 40 GLY C 112 GLY C 118 1 7
HELIX 41 41 GLY C 119 ALA C 123 5 5
HELIX 42 42 GLY C 132 GLY C 138 1 7
HELIX 43 43 ASN C 150 LYS C 164 1 15
HELIX 44 44 PRO C 175 GLY C 180 1 6
HELIX 45 45 VAL C 183 CYS C 187 5 5
HELIX 46 46 ARG C 189 ALA C 195 1 7
HELIX 47 47 SER C 204 LYS C 209 1 6
HELIX 48 48 LEU C 213 GLY C 217 5 5
HELIX 49 49 LYS C 219 THR C 223 5 5
HELIX 50 50 ASN C 226 LEU C 231 1 6
HELIX 51 51 ASP C 252 MET C 257 1 6
HELIX 52 52 GLY Q 51 LYS Q 57 1 7
HELIX 53 53 ASP Q 60 ARG Q 62 5 3
HELIX 54 54 ASP Q 63 ARG Q 70 1 8
HELIX 55 55 TYR Q 77 LYS Q 92 1 16
HELIX 56 56 PRO Q 96 LEU Q 122 1 27
HELIX 57 57 HIS Q 123 TRP Q 127 5 5
HELIX 58 58 VAL Q 130 ALA Q 136 5 7
HELIX 59 59 ASP Q 137 SER Q 147 1 11
HELIX 60 60 ARG Q 152 ASN Q 155 5 4
HELIX 61 61 SER Q 156 SER Q 173 1 18
HELIX 62 62 LEU Q 176 THR Q 180 5 5
HELIX 63 63 PRO Q 194 GLY Q 224 1 31
HELIX 64 64 ASN Q 239 LEU Q 243 5 5
HELIX 65 65 THR Q 244 CYS Q 265 1 22
HELIX 66 66 CYS Q 265 TYR Q 277 1 13
HELIX 67 67 LYS Q 278 ILE Q 283 5 6
HELIX 68 68 SER Q 301 THR Q 308 1 8
HELIX 69 69 ASP Q 328 GLY Q 330 5 3
HELIX 70 70 HIS Q 349 GLY Q 353 5 5
HELIX 71 71 GLY Q 384 LYS Q 395 1 12
HELIX 72 72 GLN Q 397 SER Q 412 1 16
HELIX 73 73 PRO Q 414 HIS Q 419 5 6
HELIX 74 74 SER Q 420 ASP Q 453 1 34
HELIX 75 75 VAL Q 497 GLY Q 504 1 8
HELIX 76 76 SER Q 513 ILE Q 520 1 8
HELIX 77 77 PRO Q 530 PHE Q 540 1 11
HELIX 78 78 CSO Q 543 HIS Q 549 1 7
HELIX 79 79 GLY R 51 LYS R 57 1 7
HELIX 80 80 ASP R 60 ARG R 62 5 3
HELIX 81 81 ASP R 63 GLN R 69 1 7
HELIX 82 82 ARG R 70 CYS R 72 5 3
HELIX 83 83 TYR R 77 VAL R 91 1 15
HELIX 84 84 PRO R 96 LEU R 122 1 27
HELIX 85 85 HIS R 123 TRP R 127 5 5
HELIX 86 86 VAL R 130 ALA R 136 5 7
HELIX 87 87 ASP R 137 ALA R 149 1 13
HELIX 88 88 ARG R 152 ASN R 155 5 4
HELIX 89 89 SER R 156 SER R 173 1 18
HELIX 90 90 LEU R 176 THR R 180 5 5
HELIX 91 91 PRO R 194 GLY R 224 1 31
HELIX 92 92 ASN R 239 LEU R 243 5 5
HELIX 93 93 THR R 244 CYS R 265 1 22
HELIX 94 94 CYS R 265 TYR R 277 1 13
HELIX 95 95 LYS R 278 ILE R 283 5 6
HELIX 96 96 SER R 301 THR R 308 1 8
HELIX 97 97 ASP R 328 GLY R 330 5 3
HELIX 98 98 HIS R 349 GLY R 353 5 5
HELIX 99 99 GLY R 384 LYS R 395 1 12
HELIX 100 100 GLN R 397 SER R 412 1 16
HELIX 101 101 PRO R 414 HIS R 419 5 6
HELIX 102 102 SER R 420 ASP R 453 1 34
HELIX 103 103 VAL R 497 GLY R 504 1 8
HELIX 104 104 SER R 513 ILE R 520 1 8
HELIX 105 105 PRO R 530 PHE R 540 1 11
HELIX 106 106 CSO R 543 HIS R 549 1 7
HELIX 107 107 GLY S 51 LYS S 57 1 7
HELIX 108 108 ASP S 60 ARG S 62 5 3
HELIX 109 109 ASP S 63 ARG S 70 1 8
HELIX 110 110 TYR S 77 VAL S 91 1 15
HELIX 111 111 PRO S 96 LEU S 122 1 27
HELIX 112 112 HIS S 123 TRP S 127 5 5
HELIX 113 113 VAL S 130 LYS S 135 5 6
HELIX 114 114 ASP S 137 ALA S 149 1 13
HELIX 115 115 ARG S 152 ASN S 155 5 4
HELIX 116 116 SER S 156 SER S 173 1 18
HELIX 117 117 LEU S 176 THR S 180 5 5
HELIX 118 118 PRO S 194 GLY S 224 1 31
HELIX 119 119 ASN S 239 LEU S 243 5 5
HELIX 120 120 THR S 244 CYS S 265 1 22
HELIX 121 121 CYS S 265 TYR S 277 1 13
HELIX 122 122 LYS S 278 GLY S 282 5 5
HELIX 123 123 SER S 301 THR S 308 1 8
HELIX 124 124 ASP S 328 GLY S 330 5 3
HELIX 125 125 HIS S 349 GLY S 353 5 5
HELIX 126 126 GLY S 384 LYS S 395 1 12
HELIX 127 127 GLN S 397 SER S 412 1 16
HELIX 128 128 PRO S 414 HIS S 419 5 6
HELIX 129 129 SER S 420 ASP S 453 1 34
HELIX 130 130 VAL S 497 GLY S 504 1 8
HELIX 131 131 SER S 513 ILE S 520 1 8
HELIX 132 132 PRO S 530 PHE S 540 1 11
HELIX 133 133 CSO S 543 HIS S 549 1 7
SHEET 1 AA 5 SER A 41 TYR A 44 0
SHEET 2 AA 5 SER A 8 HIS A 13 1 O VAL A 9 N ASP A 43
SHEET 3 AA 5 TYR A 70 GLU A 75 1 O TYR A 71 N VAL A 10
SHEET 4 AA 5 ILE A 108 ILE A 111 1 O ILE A 109 N VAL A 74
SHEET 5 AA 5 ILE A 142 ILE A 144 1 O ILE A 142 N CYS A 110
SHEET 1 AB 2 LEU A 78 PRO A 79 0
SHEET 2 AB 2 ALA A 130 LYS A 131 -1 O LYS A 131 N LEU A 78
SHEET 1 AC 2 MET A 88 VAL A 89 0
SHEET 2 AC 2 HIS A 92 PRO A 93 -1 O HIS A 92 N VAL A 89
SHEET 1 BA 5 SER B 41 TYR B 44 0
SHEET 2 BA 5 SER B 8 HIS B 13 1 O VAL B 9 N ASP B 43
SHEET 3 BA 5 TYR B 70 GLU B 75 1 O TYR B 71 N VAL B 10
SHEET 4 BA 5 ILE B 108 ILE B 111 1 O ILE B 109 N VAL B 74
SHEET 5 BA 5 ILE B 142 ILE B 144 1 O ILE B 142 N CYS B 110
SHEET 1 BB 2 LEU B 78 PRO B 79 0
SHEET 2 BB 2 ALA B 130 LYS B 131 -1 O LYS B 131 N LEU B 78
SHEET 1 BC 2 MET B 88 VAL B 89 0
SHEET 2 BC 2 HIS B 92 PRO B 93 -1 O HIS B 92 N VAL B 89
SHEET 1 CA 5 SER C 41 GLN C 45 0
SHEET 2 CA 5 SER C 8 HIS C 13 1 O VAL C 9 N ASP C 43
SHEET 3 CA 5 TYR C 70 GLU C 75 1 O TYR C 71 N VAL C 10
SHEET 4 CA 5 ILE C 108 ILE C 111 1 O ILE C 109 N VAL C 74
SHEET 5 CA 5 ILE C 142 ILE C 144 1 O ILE C 142 N CYS C 110
SHEET 1 CB 2 LEU C 78 PRO C 79 0
SHEET 2 CB 2 ALA C 130 LYS C 131 -1 O LYS C 131 N LEU C 78
SHEET 1 CC 2 MET C 88 VAL C 89 0
SHEET 2 CC 2 HIS C 92 PRO C 93 -1 O HIS C 92 N VAL C 89
SHEET 1 QA 3 GLY Q 14 VAL Q 18 0
SHEET 2 QA 3 LEU Q 28 GLU Q 35 -1 O ILE Q 30 N VAL Q 18
SHEET 3 QA 3 LYS Q 38 SER Q 46 -1 O LYS Q 38 N GLU Q 35
SHEET 1 QB 2 THR Q 232 VAL Q 233 0
SHEET 2 QB 2 GLY Q 236 CYS Q 237 -1 O GLY Q 236 N VAL Q 233
SHEET 1 QC 2 TYR Q 289 ALA Q 291 0
SHEET 2 QC 2 GLY Q 314 ILE Q 316 -1 O GLY Q 314 N ALA Q 291
SHEET 1 QD 2 GLU Q 294 ALA Q 296 0
SHEET 2 QD 2 SER Q 309 PHE Q 311 -1 N GLN Q 310 O PHE Q 295
SHEET 1 QE 2 ILE Q 332 ASP Q 335 0
SHEET 2 QE 2 ALA Q 373 TYR Q 376 -1 O ALA Q 373 N ASP Q 335
SHEET 1 QF 3 GLU Q 465 ALA Q 474 0
SHEET 2 QF 3 GLY Q 477 LYS Q 486 -1 O GLY Q 477 N ALA Q 474
SHEET 3 QF 3 LYS Q 489 VAL Q 496 -1 O LYS Q 489 N LYS Q 486
SHEET 1 RA 3 GLY R 14 VAL R 18 0
SHEET 2 RA 3 LEU R 28 GLU R 35 -1 O ILE R 30 N VAL R 18
SHEET 3 RA 3 LYS R 38 SER R 46 -1 O LYS R 38 N GLU R 35
SHEET 1 RB 2 THR R 232 VAL R 233 0
SHEET 2 RB 2 GLY R 236 CYS R 237 -1 O GLY R 236 N VAL R 233
SHEET 1 RC 2 TYR R 289 ALA R 291 0
SHEET 2 RC 2 GLY R 314 ILE R 316 -1 O GLY R 314 N ALA R 291
SHEET 1 RD 2 GLU R 294 ALA R 296 0
SHEET 2 RD 2 SER R 309 PHE R 311 -1 N GLN R 310 O PHE R 295
SHEET 1 RE 2 ILE R 332 ASP R 335 0
SHEET 2 RE 2 ALA R 373 TYR R 376 -1 O ALA R 373 N ASP R 335
SHEET 1 RF 3 GLU R 465 ALA R 474 0
SHEET 2 RF 3 GLY R 477 LYS R 486 -1 O GLY R 477 N ALA R 474
SHEET 3 RF 3 LYS R 489 VAL R 496 -1 O LYS R 489 N LYS R 486
SHEET 1 SA 3 GLY S 14 VAL S 18 0
SHEET 2 SA 3 LEU S 28 GLU S 35 -1 O ILE S 30 N VAL S 18
SHEET 3 SA 3 LYS S 38 SER S 46 -1 O LYS S 38 N GLU S 35
SHEET 1 SB 2 THR S 232 VAL S 233 0
SHEET 2 SB 2 GLY S 236 CYS S 237 -1 O GLY S 236 N VAL S 233
SHEET 1 SC 2 TYR S 289 ALA S 291 0
SHEET 2 SC 2 GLY S 314 ILE S 316 -1 O GLY S 314 N ALA S 291
SHEET 1 SD 2 GLU S 294 ALA S 296 0
SHEET 2 SD 2 SER S 309 PHE S 311 -1 N GLN S 310 O PHE S 295
SHEET 1 SE 2 ILE S 332 ASP S 335 0
SHEET 2 SE 2 ALA S 373 TYR S 376 -1 O ALA S 373 N ASP S 335
SHEET 1 SF 3 GLU S 465 ALA S 474 0
SHEET 2 SF 3 GLY S 477 LYS S 486 -1 O GLY S 477 N ALA S 474
SHEET 3 SF 3 LYS S 489 VAL S 496 -1 O LYS S 489 N LYS S 486
SSBOND 1 CYS Q 75 CYS Q 546 1555 1555 2.80
SSBOND 2 CYS Q 259 CYS Q 436 1555 1555 2.10
SSBOND 3 CYS R 75 CYS R 546 1555 1555 2.82
SSBOND 4 CYS R 259 CYS R 436 1555 1555 2.05
SSBOND 5 CYS S 75 CYS S 546 1555 1555 2.88
SSBOND 6 CYS S 259 CYS S 436 1555 1555 2.02
LINK C PRO Q 542 N CSO Q 543 1555 1555 1.32
LINK C CSO Q 543 N ILE Q 544 1555 1555 1.33
LINK C PRO R 542 N CSO R 543 1555 1555 1.34
LINK C CSO R 543 N ILE R 544 1555 1555 1.34
LINK C PRO S 542 N CSO S 543 1555 1555 1.32
LINK C CSO S 543 N ILE S 544 1555 1555 1.33
LINK SG CYS A 17 FE1 SF4 A1267 1555 1555 2.31
LINK SG CYS A 20 FE4 SF4 A1267 1555 1555 4.77
LINK SG CYS A 114 FE3 SF4 A1267 1555 1555 2.32
LINK SG CYS A 147 FE4 SF4 A1267 1555 1555 2.29
LINK ND1 HIS A 184 FE4 SF4 A1265 1555 1555 2.07
LINK SG CYS A 187 FE3 SF4 A1265 1555 1555 2.32
LINK SG CYS A 212 FE2 SF4 A1265 1555 1555 2.28
LINK SG CYS A 218 FE1 SF4 A1265 1555 1555 2.33
LINK SG CYS A 227 FE4 F3S A1266 1555 1555 2.30
LINK SG CYS A 245 FE3 F3S A1266 1555 1555 2.24
LINK SG CYS A 248 FE1 F3S A1266 1555 1555 2.35
LINK SG CYS B 17 FE1 SF4 B1267 1555 1555 2.29
LINK SG CYS B 20 FE3 SF4 B1267 1555 1555 2.30
LINK SG CYS B 114 FE4 SF4 B1267 1555 1555 2.29
LINK SG CYS B 147 FE2 SF4 B1267 1555 1555 2.31
LINK ND1 HIS B 184 FE4 SF4 B1265 1555 1555 2.04
LINK SG CYS B 187 FE3 SF4 B1265 1555 1555 2.31
LINK SG CYS B 212 FE2 SF4 B1265 1555 1555 2.31
LINK SG CYS B 218 FE1 SF4 B1265 1555 1555 2.31
LINK SG CYS B 227 FE4 F3S B1266 1555 1555 2.32
LINK SG CYS B 245 FE3 F3S B1266 1555 1555 2.31
LINK SG CYS B 248 FE1 F3S B1266 1555 1555 2.31
LINK SG CYS C 17 FE1 SF4 C1267 1555 1555 2.26
LINK SG CYS C 20 FE3 SF4 C1267 1555 1555 2.31
LINK SG CYS C 114 FE4 SF4 C1267 1555 1555 2.31
LINK SG CYS C 147 FE2 SF4 C1267 1555 1555 2.31
LINK ND1 HIS C 184 FE4 SF4 C1265 1555 1555 2.07
LINK SG CYS C 187 FE3 SF4 C1265 1555 1555 2.29
LINK SG CYS C 212 FE2 SF4 C1265 1555 1555 2.27
LINK SG CYS C 218 FE1 SF4 C1265 1555 1555 2.32
LINK SG CYS C 227 FE4 F3S C1266 1555 1555 2.31
LINK SG CYS C 245 FE3 F3S C1266 1555 1555 2.29
LINK SG CYS C 248 FE1 F3S C1266 1555 1555 2.33
LINK OE2 GLU Q 53 MG MG Q1553 1555 1555 2.08
LINK SG CYS Q 72 NI NI Q1551 1555 1555 2.19
LINK SG CYS Q 75 FE FCO Q1550 1555 1555 2.16
LINK SG CYS Q 75 NI NI Q1551 1555 1555 2.14
LINK O LEU Q 495 MG MG Q1553 1555 1555 2.15
LINK SG CSO Q 543 NI NI Q1551 1555 1555 2.12
LINK SG CYS Q 546 FE FCO Q1550 1555 1555 2.23
LINK SG CYS Q 546 NI NI Q1551 1555 1555 2.54
LINK NE2 HIS Q 549 MG MG Q1553 1555 1555 2.23
LINK FE FCO Q1550 NI NI Q1551 1555 1555 2.62
LINK MG MG Q1553 O HOH Q2046 1555 1555 2.05
LINK MG MG Q1553 O HOH Q2047 1555 1555 2.03
LINK MG MG Q1553 O HOH Q2283 1555 1555 2.04
LINK OE2 GLU R 53 MG MG R1553 1555 1555 2.14
LINK SG CYS R 72 NI NI R1551 1555 1555 2.14
LINK SG CYS R 75 FE FCO R1550 1555 1555 2.20
LINK SG CYS R 75 NI NI R1551 1555 1555 2.21
LINK O LEU R 495 MG MG R1553 1555 1555 2.14
LINK SG CSO R 543 NI NI R1551 1555 1555 2.10
LINK SG CYS R 546 FE FCO R1550 1555 1555 2.25
LINK SG CYS R 546 NI NI R1551 1555 1555 2.38
LINK NE2 HIS R 549 MG MG R1553 1555 1555 2.25
LINK FE FCO R1550 NI NI R1551 1555 1555 2.58
LINK MG MG R1553 O HOH R2049 1555 1555 1.98
LINK MG MG R1553 O HOH R2050 1555 1555 2.02
LINK MG MG R1553 O HOH R2240 1555 1555 2.04
LINK OE2 GLU S 53 MG MG S1553 1555 1555 2.11
LINK SG CYS S 72 NI NI S1551 1555 1555 2.20
LINK SG CYS S 75 FE FCO S1550 1555 1555 2.21
LINK SG CYS S 75 NI NI S1551 1555 1555 2.21
LINK O LEU S 495 MG MG S1553 1555 1555 2.13
LINK SG CSO S 543 NI NI S1551 1555 1555 2.14
LINK SG CYS S 546 FE FCO S1550 1555 1555 2.29
LINK SG CYS S 546 NI NI S1551 1555 1555 2.46
LINK NE2 HIS S 549 MG MG S1553 1555 1555 2.21
LINK FE FCO S1550 NI NI S1551 1555 1555 2.53
LINK MG MG S1553 O HOH S2021 1555 1555 2.01
LINK MG MG S1553 O HOH S2022 1555 1555 2.03
LINK MG MG S1553 O HOH S2166 1555 1555 2.02
CISPEP 1 LYS A 29 PRO A 30 0 0.67
CISPEP 2 LYS A 124 PRO A 125 0 3.13
CISPEP 3 CYS A 147 PRO A 148 0 6.69
CISPEP 4 THR A 258 PRO A 259 0 -1.87
CISPEP 5 LYS B 29 PRO B 30 0 -4.04
CISPEP 6 LYS B 124 PRO B 125 0 4.27
CISPEP 7 CYS B 147 PRO B 148 0 10.42
CISPEP 8 THR B 258 PRO B 259 0 -1.18
CISPEP 9 LYS C 29 PRO C 30 0 4.00
CISPEP 10 LYS C 124 PRO C 125 0 5.78
CISPEP 11 CYS C 147 PRO C 148 0 6.99
CISPEP 12 THR C 258 PRO C 259 0 -0.73
CISPEP 13 ASP Q 19 PRO Q 20 0 12.29
CISPEP 14 ASN Q 226 PRO Q 227 0 3.48
CISPEP 15 ASP R 19 PRO R 20 0 3.76
CISPEP 16 ASN R 226 PRO R 227 0 6.78
CISPEP 17 ASP S 19 PRO S 20 0 6.86
CISPEP 18 ASN S 226 PRO S 227 0 5.71
SITE 1 AC1 8 HIS A 184 CYS A 187 ARG A 189 LEU A 190
SITE 2 AC1 8 CYS A 212 LEU A 213 CYS A 218 PRO A 221
SITE 1 AC2 9 ASN A 225 CYS A 227 PHE A 232 TRP A 237
SITE 2 AC2 9 CYS A 245 LEU A 246 CYS A 248 LYS Q 225
SITE 3 AC2 9 GLN Q 230
SITE 1 AC3 9 GLU A 16 CYS A 17 CYS A 20 THR A 113
SITE 2 AC3 9 CYS A 114 GLY A 146 CYS A 147 PRO A 148
SITE 3 AC3 9 ARG Q 70
SITE 1 AC4 5 ASP A 168 LEU A 169 LYS A 176 GOL A1272
SITE 2 AC4 5 HOH A2309
SITE 1 AC5 7 LYS A 140 LEU A 169 ASP A 170 GLU A 171
SITE 2 AC5 7 GOL A1271 HOH A2204 HOH A2308
SITE 1 AC6 5 ARG A 6 LEU A 37 HOH A2310 ALA Q 169
SITE 2 AC6 5 PHE Q 170
SITE 1 AC7 8 HIS B 184 CYS B 187 ARG B 189 LEU B 190
SITE 2 AC7 8 CYS B 212 LEU B 213 CYS B 218 PRO B 221
SITE 1 AC8 9 ASN B 225 CYS B 227 PHE B 232 TRP B 237
SITE 2 AC8 9 CYS B 245 LEU B 246 CYS B 248 LYS R 225
SITE 3 AC8 9 GLN R 230
SITE 1 AC9 10 GLU B 16 CYS B 17 CYS B 20 THR B 113
SITE 2 AC9 10 CYS B 114 GLY B 146 CYS B 147 PRO B 148
SITE 3 AC9 10 ARG R 70 HIS R 228
SITE 1 BC1 8 HIS C 184 CYS C 187 ARG C 189 LEU C 190
SITE 2 BC1 8 CYS C 212 LEU C 213 CYS C 218 PRO C 221
SITE 1 BC2 10 THR C 223 ASN C 225 CYS C 227 PHE C 232
SITE 2 BC2 10 TRP C 237 CYS C 245 LEU C 246 CYS C 248
SITE 3 BC2 10 LYS S 225 GLN S 230
SITE 1 BC3 12 GLU C 16 CYS C 17 GLY C 19 CYS C 20
SITE 2 BC3 12 GLY C 112 THR C 113 CYS C 114 GLY C 146
SITE 3 BC3 12 CYS C 147 PRO C 148 ARG S 70 HIS S 228
SITE 1 BC4 13 CYS Q 75 VAL Q 78 HIS Q 79 ALA Q 474
SITE 2 BC4 13 PRO Q 475 ARG Q 476 LEU Q 479 VAL Q 497
SITE 3 BC4 13 PRO Q 498 SER Q 499 CSO Q 543 CYS Q 546
SITE 4 BC4 13 NI Q1551
SITE 1 BC5 5 CYS Q 72 CYS Q 75 CSO Q 543 CYS Q 546
SITE 2 BC5 5 FCO Q1550
SITE 1 BC6 6 GLU Q 53 LEU Q 495 HIS Q 549 HOH Q2046
SITE 2 BC6 6 HOH Q2047 HOH Q2283
SITE 1 BC7 8 ARG Q 100 ASN Q 104 PHE Q 295 ALA Q 296
SITE 2 BC7 8 THR Q 297 GLU Q 445 HOH Q2104 HOH Q2404
SITE 1 BC8 9 ALA A 55 PHE C 198 HOH C2157 HOH C2177
SITE 2 BC8 9 ASN Q 181 ALA Q 182 TYR Q 183 LEU Q 185
SITE 3 BC8 9 ARG Q 529
SITE 1 BC9 10 GLY Q 281 GLY Q 282 ILE Q 283 GLY Q 284
SITE 2 BC9 10 GLY Q 285 ARG Q 319 THR Q 416 HIS Q 419
SITE 3 BC9 10 HOH Q2266 HOH Q2341
SITE 1 CC1 5 LYS Q 245 LYS Q 337 TYR Q 338 ASP Q 366
SITE 2 CC1 5 HOH Q2405
SITE 1 CC2 13 CYS R 75 VAL R 78 HIS R 79 ALA R 474
SITE 2 CC2 13 PRO R 475 ARG R 476 LEU R 479 VAL R 497
SITE 3 CC2 13 PRO R 498 SER R 499 CSO R 543 CYS R 546
SITE 4 CC2 13 NI R1551
SITE 1 CC3 5 CYS R 72 CYS R 75 CSO R 543 CYS R 546
SITE 2 CC3 5 FCO R1550
SITE 1 CC4 6 GLU R 53 LEU R 495 HIS R 549 HOH R2049
SITE 2 CC4 6 HOH R2050 HOH R2240
SITE 1 CC5 7 ALA B 55 ASN R 181 ALA R 182 TYR R 183
SITE 2 CC5 7 LEU R 185 ARG R 529 HOH R2340
SITE 1 CC6 3 LEU B 137 LYS R 410 HOH R2299
SITE 1 CC7 9 ARG R 100 ASN R 104 PHE R 295 ALA R 296
SITE 2 CC7 9 THR R 297 GLN R 310 GLU R 445 HOH R2089
SITE 3 CC7 9 HOH R2216
SITE 1 CC8 10 GLY R 281 GLY R 282 ILE R 283 GLY R 284
SITE 2 CC8 10 GLY R 285 ARG R 319 HIS R 419 HOH R2194
SITE 3 CC8 10 HOH R2195 HOH R2228
SITE 1 CC9 7 THR R 286 SER R 287 ASN R 288 ALA R 380
SITE 2 CC9 7 PRO R 514 HOH R2197 HOH R2333
SITE 1 DC1 8 ARG R 152 PRO R 153 SER R 156 HOH R2115
SITE 2 DC1 8 HOH R2121 HOH R2341 HOH R2342 ALA S 451
SITE 1 DC2 13 CYS S 75 VAL S 78 HIS S 79 ALA S 474
SITE 2 DC2 13 PRO S 475 ARG S 476 LEU S 479 VAL S 497
SITE 3 DC2 13 PRO S 498 SER S 499 CSO S 543 CYS S 546
SITE 4 DC2 13 NI S1551
SITE 1 DC3 5 CYS S 72 CYS S 75 CSO S 543 CYS S 546
SITE 2 DC3 5 FCO S1550
SITE 1 DC4 6 GLU S 53 LEU S 495 HIS S 549 HOH S2021
SITE 2 DC4 6 HOH S2022 HOH S2166
SITE 1 DC5 8 ARG S 100 ASN S 104 PHE S 295 ALA S 296
SITE 2 DC5 8 THR S 297 GLU S 445 HOH S2153 HOH S2236
CRYST1 64.770 100.400 183.430 90.00 91.55 90.00 P 1 21 1 6
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 0.015439 0.000000 0.000418 0.00000
SCALE2 0.000000 0.009960 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005454 0.00000
MTRIX1 1 0.385830 -0.741475 0.548953 -35.67500 1
MTRIX2 1 -0.752107 -0.597400 -0.278297 -26.93000 1
MTRIX3 1 0.534295 -0.305496 -0.788163 54.65700 1
MTRIX1 2 -0.380984 -0.735909 -0.559722 1.35400 1
MTRIX2 2 0.730438 -0.610712 0.305765 4.23700 1
MTRIX3 2 -0.566844 -0.292351 0.770207 69.27300 1
MTRIX1 3 0.382829 -0.740399 0.552495 -35.65900 1
MTRIX2 3 -0.748136 -0.599331 -0.284773 -26.87700 1
MTRIX3 3 0.541973 -0.304322 -0.783360 54.55000 1
MTRIX1 4 -0.374865 -0.739484 -0.559142 1.28100 1
MTRIX2 4 0.730622 -0.606905 0.312822 4.17400 1
MTRIX3 4 -0.570673 -0.291256 0.767791 69.33400 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 0.382054 -0.751371 0.538030 -35.96402 1
MTRIX2 6 -0.742566 -0.596164 -0.305261 -25.83834 1
MTRIX3 6 0.550119 -0.282896 -0.785709 54.89409 1
MTRIX1 7 -0.373545 0.729294 -0.573232 37.25006 1
MTRIX2 7 -0.737488 -0.608321 -0.293354 23.86848 1
MTRIX3 7 -0.562650 0.313170 0.765081 -53.62646 1
MTRIX1 8 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 8 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 8 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 9 0.383053 -0.752455 0.535801 -35.90758 1
MTRIX2 9 -0.743311 -0.595457 -0.304827 -25.84453 1
MTRIX3 9 0.548415 -0.281502 -0.787399 55.03253 1
MTRIX1 10 -0.372580 0.731467 -0.571087 37.17153 1
MTRIX2 10 -0.737537 -0.606899 -0.296163 24.09790 1
MTRIX3 10 -0.563226 0.310853 0.765602 -53.55692 1
MTRIX1 11 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 11 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 11 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 12 0.387456 -0.750340 0.535600 -35.59795 1
MTRIX2 12 -0.742452 -0.598373 -0.301188 -26.10445 1
MTRIX3 12 0.546483 -0.280960 -0.788935 55.02672 1
MTRIX1 13 -0.377146 0.731161 -0.568475 36.93143 1
MTRIX2 13 -0.735769 -0.609329 -0.295572 24.06841 1
MTRIX3 13 -0.562499 0.306792 0.767772 -53.75022 1
MTRIX1 14 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 14 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 14 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 15 0.391049 -0.746156 0.538824 -35.42058 1
MTRIX2 15 -0.734649 -0.605714 -0.305616 -26.00340 1
MTRIX3 15 0.554410 -0.276336 -0.785027 55.32904 1
MTRIX1 16 -0.379979 0.732158 -0.565297 36.68073 1
MTRIX2 16 -0.737264 -0.608798 -0.292928 23.85812 1
MTRIX3 16 -0.558621 0.305467 0.771124 -53.90741 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 0.401481 -0.752267 0.522405 -34.30780 1
MTRIX2 18 -0.737710 -0.603649 -0.302311 -26.25784 1
MTRIX3 18 0.542768 -0.264011 -0.797309 56.17042 1
MTRIX1 19 -0.385647 0.740277 -0.550696 35.75050 1
MTRIX2 19 -0.739698 -0.604818 -0.295027 23.81386 1
MTRIX3 19 -0.551473 0.293572 0.780828 -54.18481 1
MTRIX1 20 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 20 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 20 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 21 0.389684 -0.755362 0.526854 -35.12664 1
MTRIX2 21 -0.743580 -0.595585 -0.303919 -25.99972 1
MTRIX3 21 0.543355 -0.273326 -0.793762 55.55422 1
MTRIX1 22 -0.382347 0.734922 -0.560090 36.28050 1
MTRIX2 22 -0.737743 -0.607768 -0.293860 23.81971 1
MTRIX3 22 -0.556369 0.300846 0.774562 -54.03187 1
MTRIX1 23 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 23 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 23 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 24 0.386086 -0.753351 0.532353 -35.54553 1
MTRIX2 24 -0.738491 -0.598248 -0.311016 -25.41391 1
MTRIX3 24 0.552783 -0.273059 -0.787318 55.49051 1
MTRIX1 25 -0.380565 0.730819 -0.566634 36.71600 1
MTRIX2 25 -0.738460 -0.608994 -0.289486 23.61721 1
MTRIX3 25 -0.556639 0.308268 0.771443 -53.96901 1
MTRIX1 26 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 26 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 26 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 27 0.383958 -0.748340 0.540892 -35.95586 1
MTRIX2 27 -0.739905 -0.599796 -0.304607 -25.89696 1
MTRIX3 27 0.552374 -0.283252 -0.783997 54.87771 1
MTRIX1 28 -0.377766 0.729880 -0.569709 36.95549 1
MTRIX2 28 -0.737155 -0.609405 -0.291939 23.75672 1
MTRIX3 28 -0.560264 0.309679 0.768247 -53.80813 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 0.384405 -0.747180 0.542176 -35.94498 1
MTRIX2 30 -0.741281 -0.599863 -0.301108 -26.04287 1
MTRIX3 30 0.550213 -0.286158 -0.784461 54.71978 1
MTRIX1 31 -0.373850 0.727169 -0.575727 37.51352 1
MTRIX2 31 -0.737969 -0.609218 -0.290267 23.77587 1
MTRIX3 31 -0.561816 0.316352 0.764384 -53.61886 1
MTRIX1 32 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 32 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 32 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 33 0.383806 -0.749077 0.539979 -35.90520 1
MTRIX2 33 -0.739714 -0.599434 -0.305781 -25.81222 1
MTRIX3 33 0.552735 -0.282070 -0.784169 54.89740 1
MTRIX1 34 -0.374463 0.730785 -0.570728 36.97086 1
MTRIX2 34 -0.740305 -0.606247 -0.290540 23.60106 1
MTRIX3 34 -0.558324 0.313717 0.768021 -53.87592 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 0.381602 -0.748052 0.542954 -36.07614 1
MTRIX2 36 -0.742394 -0.597987 -0.302099 -26.01747 1
MTRIX3 36 0.550664 -0.287804 -0.783542 54.71325 1
MTRIX1 37 -0.373029 0.732554 -0.569398 36.94576 1
MTRIX2 37 -0.737892 -0.606267 -0.296574 24.08813 1
MTRIX3 37 -0.562463 0.309523 0.766701 -53.72120 1
MTRIX1 38 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 38 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 38 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 39 0.382971 -0.747340 0.542970 -35.99257 1
MTRIX2 39 -0.740191 -0.599925 -0.303656 -25.93536 1
MTRIX3 39 0.552676 -0.285610 -0.782928 54.76598 1
MTRIX1 40 -0.375395 0.730636 -0.570306 36.96508 1
MTRIX2 40 -0.739789 -0.606879 -0.290536 23.57652 1
MTRIX3 40 -0.558383 0.312840 0.768336 -53.89859 1
MTRIX1 41 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 41 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 41 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 42 0.384643 -0.742734 0.548084 -36.15726 1
MTRIX2 42 -0.738695 -0.603731 -0.299731 -26.10934 1
MTRIX3 42 0.553516 -0.289577 -0.780875 54.62579 1
MTRIX1 43 -0.377306 0.731526 -0.567899 36.83431 1
MTRIX2 43 -0.738433 -0.607723 -0.292217 23.75626 1
MTRIX3 43 -0.558889 0.309100 0.769480 -54.00787 1
MTRIX1 44 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 44 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 44 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 45 0.375829 -0.747124 0.548232 -36.33874 1
MTRIX2 45 -0.743608 -0.596174 -0.302694 -25.95498 1
MTRIX3 45 0.552992 -0.293909 -0.779627 54.38087 1
MTRIX1 46 -0.377049 0.725509 -0.575736 37.54118 1
MTRIX2 46 -0.737350 -0.611304 -0.287440 23.39750 1
MTRIX3 46 -0.560490 0.316140 0.765445 -53.74420 1
(ATOM LINES ARE NOT SHOWN.)
END
