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HEADER HYDROLASE 07-JUL-10 3NUZ
TITLE CRYSTAL STRUCTURE OF A PUTATIVE ACETYL XYLAN ESTERASE (BF1801) FROM
TITLE 2 BACTEROIDES FRAGILIS NCTC 9343 AT 2.30 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 20-416;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES FRAGILIS;
SOURCE 3 ORGANISM_TAXID: 272559;
SOURCE 4 STRAIN: ATCC 25285 / NCTC 9343;
SOURCE 5 GENE: BF1801;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 04-AUG-10 3NUZ 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE ACETYL XYLAN ESTERASE
JRNL TITL 2 (BF1801) FROM BACTEROIDES FRAGILIS NCTC 9343 AT 2.30 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 126305
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 6616
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9066
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.1630
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18820
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 253
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.11000
REMARK 3 B22 (A**2) : 10.11000
REMARK 3 B33 (A**2) : -20.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.036
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.385
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19407 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 13638 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26346 ; 1.440 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 33023 ; 0.970 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2329 ; 3.084 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 932 ;27.571 ;23.240
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3256 ;10.966 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 153 ; 9.547 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2766 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21478 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4109 ; 0.001 ; 0.020
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): 11667 ; 0.791 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4622 ; 0.334 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18908 ; 1.307 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7740 ; 2.628 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7430 ; 3.395 ;11.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 15
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 25 A 53 1
REMARK 3 1 B 25 B 53 1
REMARK 3 1 C 25 C 53 1
REMARK 3 1 D 25 D 53 1
REMARK 3 1 E 25 E 53 1
REMARK 3 1 F 25 F 53 1
REMARK 3 2 A 54 A 89 3
REMARK 3 2 B 54 B 89 3
REMARK 3 2 C 54 C 89 3
REMARK 3 2 D 54 D 89 3
REMARK 3 2 E 54 E 89 3
REMARK 3 2 F 54 F 89 3
REMARK 3 3 A 90 A 114 3
REMARK 3 3 B 90 B 114 3
REMARK 3 3 C 90 C 114 3
REMARK 3 3 D 90 D 114 3
REMARK 3 3 E 90 E 114 3
REMARK 3 3 F 90 F 114 3
REMARK 3 4 A 115 A 130 1
REMARK 3 4 B 115 B 130 1
REMARK 3 4 C 115 C 130 1
REMARK 3 4 D 115 D 130 1
REMARK 3 4 E 115 E 130 1
REMARK 3 4 F 115 F 130 1
REMARK 3 5 A 131 A 132 3
REMARK 3 5 B 131 B 132 3
REMARK 3 5 C 131 C 132 3
REMARK 3 5 D 131 D 132 3
REMARK 3 5 E 131 E 132 3
REMARK 3 5 F 131 F 132 3
REMARK 3 6 A 133 A 157 2
REMARK 3 6 B 133 B 157 2
REMARK 3 6 C 133 C 157 2
REMARK 3 6 D 133 D 157 2
REMARK 3 6 E 133 E 157 2
REMARK 3 6 F 133 F 157 2
REMARK 3 7 A 158 A 169 4
REMARK 3 7 B 158 B 169 4
REMARK 3 7 C 158 C 169 4
REMARK 3 7 D 158 D 169 4
REMARK 3 7 E 158 E 169 4
REMARK 3 7 F 158 F 169 4
REMARK 3 8 A 170 A 241 1
REMARK 3 8 B 170 B 241 1
REMARK 3 8 C 170 C 241 1
REMARK 3 8 D 170 D 241 1
REMARK 3 8 E 170 E 241 1
REMARK 3 8 F 170 F 241 1
REMARK 3 9 A 242 A 247 3
REMARK 3 9 B 242 B 247 3
REMARK 3 9 C 242 C 247 3
REMARK 3 9 D 242 D 247 3
REMARK 3 9 E 242 E 247 3
REMARK 3 9 F 242 F 247 3
REMARK 3 10 A 248 A 303 1
REMARK 3 10 B 248 B 303 1
REMARK 3 10 C 248 C 303 1
REMARK 3 10 D 248 D 303 1
REMARK 3 10 E 248 E 303 1
REMARK 3 10 F 248 F 303 1
REMARK 3 11 A 304 A 308 3
REMARK 3 11 B 304 B 308 3
REMARK 3 11 C 304 C 308 3
REMARK 3 11 D 304 D 308 3
REMARK 3 11 E 304 E 308 3
REMARK 3 11 F 304 F 308 3
REMARK 3 12 A 309 A 349 1
REMARK 3 12 B 309 B 349 1
REMARK 3 12 C 309 C 349 1
REMARK 3 12 D 309 D 349 1
REMARK 3 12 E 309 E 349 1
REMARK 3 12 F 309 F 349 1
REMARK 3 13 A 350 A 357 4
REMARK 3 13 B 350 B 357 4
REMARK 3 13 C 350 C 357 4
REMARK 3 13 D 350 D 357 4
REMARK 3 13 E 350 E 357 4
REMARK 3 13 F 350 F 357 4
REMARK 3 14 A 358 A 409 1
REMARK 3 14 B 358 B 409 1
REMARK 3 14 C 358 C 409 1
REMARK 3 14 D 358 D 409 1
REMARK 3 14 E 358 E 409 1
REMARK 3 14 F 358 F 409 1
REMARK 3 15 A 410 A 413 5
REMARK 3 15 B 410 B 413 5
REMARK 3 15 C 410 C 413 5
REMARK 3 15 D 410 D 413 5
REMARK 3 15 E 410 E 413 5
REMARK 3 15 F 410 F 413 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4196 ; 0.230 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 4196 ; 0.230 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 4196 ; 0.250 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 4196 ; 0.240 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 E (A): 4196 ; 0.230 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 F (A): 4196 ; 0.230 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 387 ; 0.390 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 387 ; 0.390 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 387 ; 0.320 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 387 ; 0.370 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 E (A): 387 ; 0.400 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 F (A): 387 ; 0.280 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 674 ; 0.420 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 674 ; 0.480 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 674 ; 0.450 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 674 ; 0.400 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 E (A): 674 ; 0.390 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 F (A): 674 ; 0.400 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 4196 ; 0.480 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 4196 ; 0.500 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 4196 ; 0.500 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 4196 ; 0.500 ; 0.500
REMARK 3 TIGHT THERMAL 1 E (A**2): 4196 ; 0.450 ; 0.500
REMARK 3 TIGHT THERMAL 1 F (A**2): 4196 ; 0.460 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 387 ; 0.440 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 387 ; 0.390 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 387 ; 0.400 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 387 ; 0.410 ; 2.000
REMARK 3 MEDIUM THERMAL 1 E (A**2): 387 ; 0.460 ; 2.000
REMARK 3 MEDIUM THERMAL 1 F (A**2): 387 ; 0.360 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 674 ; 0.480 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 674 ; 0.450 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 674 ; 0.490 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 674 ; 0.440 ;10.000
REMARK 3 LOOSE THERMAL 1 E (A**2): 674 ; 0.410 ;10.000
REMARK 3 LOOSE THERMAL 1 F (A**2): 674 ; 0.440 ;10.000
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 4
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.382
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, H+K, -L
REMARK 3 TWIN FRACTION : 0.136
REMARK 3 TWIN DOMAIN : 3
REMARK 3 TWIN OPERATOR : -H, -K, L
REMARK 3 TWIN FRACTION : 0.162
REMARK 3 TWIN DOMAIN : 4
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.320
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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 25 A 415
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5174 -52.3946 34.4374
REMARK 3 T TENSOR
REMARK 3 T11: 0.0846 T22: 0.0081
REMARK 3 T33: 0.0623 T12: -0.0143
REMARK 3 T13: -0.0006 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.5642 L22: 0.8554
REMARK 3 L33: 0.9026 L12: 0.2245
REMARK 3 L13: -0.0158 L23: 0.1650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0372 S12: 0.0137 S13: -0.1134
REMARK 3 S21: 0.0258 S22: 0.0036 S23: 0.0051
REMARK 3 S31: 0.2129 S32: -0.0151 S33: 0.0336
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 25 B 415
REMARK 3 ORIGIN FOR THE GROUP (A): 71.3249 -19.6992 26.2958
REMARK 3 T TENSOR
REMARK 3 T11: 0.0727 T22: 0.0551
REMARK 3 T33: 0.0756 T12: -0.0442
REMARK 3 T13: 0.0097 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.4979 L22: 0.8842
REMARK 3 L33: 0.8011 L12: 0.2326
REMARK 3 L13: 0.0348 L23: 0.2279
REMARK 3 S TENSOR
REMARK 3 S11: -0.0055 S12: 0.0325 S13: 0.0837
REMARK 3 S21: -0.0213 S22: 0.0478 S23: -0.0770
REMARK 3 S31: -0.1441 S32: 0.1781 S33: -0.0423
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 25 C 415
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4167 20.2093 21.1636
REMARK 3 T TENSOR
REMARK 3 T11: 0.0633 T22: 0.0458
REMARK 3 T33: 0.0713 T12: -0.0374
REMARK 3 T13: -0.0019 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.5705 L22: 0.5558
REMARK 3 L33: 0.8117 L12: 0.3187
REMARK 3 L13: -0.1098 L23: -0.0273
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: 0.0247 S13: -0.0596
REMARK 3 S21: 0.0010 S22: 0.0048 S23: 0.0916
REMARK 3 S31: 0.1266 S32: -0.1527 S33: 0.0049
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 25 D 415
REMARK 3 ORIGIN FOR THE GROUP (A): 72.8938 51.9931 29.2590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0959 T22: 0.0199
REMARK 3 T33: 0.0534 T12: -0.0289
REMARK 3 T13: 0.0231 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.4981 L22: 0.8825
REMARK 3 L33: 0.7882 L12: 0.2185
REMARK 3 L13: -0.0244 L23: -0.1649
REMARK 3 S TENSOR
REMARK 3 S11: 0.0276 S12: -0.0093 S13: 0.1201
REMARK 3 S21: 0.0702 S22: 0.0072 S23: -0.0029
REMARK 3 S31: -0.2068 S32: 0.0515 S33: -0.0348
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 25 E 413
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5589 -10.3202 36.8891
REMARK 3 T TENSOR
REMARK 3 T11: 0.1295 T22: 0.0900
REMARK 3 T33: 0.2319 T12: -0.0153
REMARK 3 T13: 0.0023 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.5833 L22: 0.1911
REMARK 3 L33: 0.4232 L12: -0.0666
REMARK 3 L13: -0.0284 L23: -0.0314
REMARK 3 S TENSOR
REMARK 3 S11: -0.0254 S12: 0.0084 S13: -0.0335
REMARK 3 S21: 0.0176 S22: 0.0207 S23: -0.0502
REMARK 3 S31: 0.0335 S32: 0.0402 S33: 0.0047
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 25 F 413
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0584 9.6118 28.5767
REMARK 3 T TENSOR
REMARK 3 T11: 0.1131 T22: 0.1208
REMARK 3 T33: 0.2321 T12: -0.0310
REMARK 3 T13: 0.0060 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.3392 L22: 0.5472
REMARK 3 L33: 0.4670 L12: -0.2119
REMARK 3 L13: -0.0807 L23: 0.0554
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: 0.0086 S13: -0.0133
REMARK 3 S21: 0.0198 S22: 0.0008 S23: 0.1159
REMARK 3 S31: -0.0174 S32: -0.1118 S33: -0.0356
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: 1.HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2.A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3.ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 4.SOLVENT MOLECULES WERE EXCLUDED FROM AUTOMATIC TLS
REMARK 3 ASSIGNMENT. 5.RESIDUES THAT ARE RAMACHANDRAN OUTLIERS ARE
REMARK 3 SUPPORTED BY ELECTRON DENSITY. 6.THE STRUCTURE IS TETARTOHEDRALLY
REMARK 3 TWINNED AND WAS REFINED WITH THE FOLLOWING TWIN OPERATORS AND
REMARK 3 TWIN FRACTIONS: (H, K, L) 0.382; (-H, H+K, -L) 0.137; (-H, -K, L)
REMARK 3 0.162; (K, H, -L) 0.319. SEE REMARK 200 FOR ADDITIONAL REMARKS ON
REMARK 3 TWINNING. 7.DUE TO THE USE OF THIN SHELLS FOR R-FREE SET
REMARK 3 SELECTION, THE HIGHEST RESOLUTION SHELL (2.36-2.30) DID NOT
REMARK 3 CONTAIN ANY FREE REFLECTIONS. THE 842 HIGHEST RESOLUTION
REMARK 3 REFLECTIONS IN THE FREE SET (2.41-2.40) HAD AN R-FREE OF 0.24.
REMARK 4
REMARK 4 3NUZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060311.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837,0.97934,0.97920
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : FLAT COLLIMATING MIRROR, TOROID
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126358
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.665
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE WAS INITIALLY SOLVED BY MAD IN THE APPARENT
REMARK 200 SPACE GROUP P3221 WITH TWO MOLECULES PER ASYMMETRIC UNIT AND
REMARK 200 TWINNED WITH THE TWIN LAW (-H, -K, L). THE RESULTING STRUCTURE
REMARK 200 SUGGESTED A THIRD MOLECULE IN THE ASYMMETRIC UNIT. HOWEVER,
REMARK 200 DENSITY FOR THIS MOLECULE WAS UNINTERPRETABLE. FURTHER
REMARK 200 EXAMINATION SUGGESTED THE CORRECT SPACE GROUP WAS P32 WITH 6
REMARK 200 MOLECULES PER ASYMMETRIC UNIT AND 4 TWIN DOMAINS. EXPERIMENTAL
REMARK 200 PHASES WERE RECALCULATED IN THE CORRECT SPACE GROUP P32.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40.0000% MPD, 0.1M CITRATE PH 4.0,
REMARK 280 NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 108.42600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.21300
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 300 REMARK: CRYSTAL PACKING ANALYSIS AND SIZE-EXCLUSION CHROMATOGRAPHY
REMARK 300 COUPLED WITH STATIC LIGHT SCATTERING SUPPORT THE ASSIGNMENT OF A
REMARK 300 DIMER AS THE SIGNIFICANT OLIGOMERIC FORM IN SOLUTION.
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: 6600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 6560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 6590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 ALA A 20
REMARK 465 GLN A 21
REMARK 465 SER A 22
REMARK 465 ASP A 23
REMARK 465 GLY A 24
REMARK 465 ILE A 91
REMARK 465 LYS A 92
REMARK 465 ASN A 93
REMARK 465 ARG A 416
REMARK 465 GLY B 0
REMARK 465 ALA B 20
REMARK 465 GLN B 21
REMARK 465 SER B 22
REMARK 465 ASP B 23
REMARK 465 GLY B 24
REMARK 465 LYS B 92
REMARK 465 ASN B 93
REMARK 465 ARG B 416
REMARK 465 GLY C 0
REMARK 465 ALA C 20
REMARK 465 GLN C 21
REMARK 465 SER C 22
REMARK 465 ASP C 23
REMARK 465 GLY C 24
REMARK 465 ILE C 91
REMARK 465 LYS C 92
REMARK 465 ASN C 93
REMARK 465 ARG C 416
REMARK 465 GLY D 0
REMARK 465 ALA D 20
REMARK 465 GLN D 21
REMARK 465 SER D 22
REMARK 465 ASP D 23
REMARK 465 GLY D 24
REMARK 465 LYS D 92
REMARK 465 ASN D 93
REMARK 465 ARG D 416
REMARK 465 GLY E 0
REMARK 465 ALA E 20
REMARK 465 GLN E 21
REMARK 465 SER E 22
REMARK 465 ASP E 23
REMARK 465 GLY E 24
REMARK 465 GLN E 90
REMARK 465 ILE E 91
REMARK 465 LYS E 92
REMARK 465 ASN E 93
REMARK 465 GLU E 414
REMARK 465 GLU E 415
REMARK 465 ARG E 416
REMARK 465 GLY F 0
REMARK 465 ALA F 20
REMARK 465 GLN F 21
REMARK 465 SER F 22
REMARK 465 ASP F 23
REMARK 465 GLY F 24
REMARK 465 ILE F 91
REMARK 465 LYS F 92
REMARK 465 ASN F 93
REMARK 465 GLU F 414
REMARK 465 GLU F 415
REMARK 465 ARG F 416
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 GLN A 90 CG CD OE1 NE2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 ARG A 166 CD NE CZ NH1 NH2
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 LYS A 411 CG CD CE NZ
REMARK 470 GLU A 414 CG CD OE1 OE2
REMARK 470 LYS B 69 CE NZ
REMARK 470 GLN B 90 CG CD OE1 NE2
REMARK 470 ILE B 91 CG1 CG2 CD1
REMARK 470 LYS B 135 CD CE NZ
REMARK 470 ARG B 166 CD NE CZ NH1 NH2
REMARK 470 LYS B 168 CG CD CE NZ
REMARK 470 GLU B 414 CG CD OE1 OE2
REMARK 470 GLU B 415 CG CD OE1 OE2
REMARK 470 GLN C 90 CG CD OE1 NE2
REMARK 470 LYS C 135 CG CD CE NZ
REMARK 470 ARG C 166 CD NE CZ NH1 NH2
REMARK 470 LYS C 168 CG CD CE NZ
REMARK 470 GLU C 414 CG CD OE1 OE2
REMARK 470 GLU C 415 CG CD OE1 OE2
REMARK 470 LYS D 69 CE NZ
REMARK 470 GLN D 90 CG CD OE1 NE2
REMARK 470 ILE D 91 CG1 CG2 CD1
REMARK 470 LYS D 135 CD CE NZ
REMARK 470 ARG D 166 CD NE CZ NH1 NH2
REMARK 470 LYS D 168 CG CD CE NZ
REMARK 470 GLU D 414 CG CD OE1 OE2
REMARK 470 GLU D 415 CG CD OE1 OE2
REMARK 470 ARG E 166 CD NE CZ NH1 NH2
REMARK 470 LYS E 168 CG CD CE NZ
REMARK 470 LYS F 76 CD CE NZ
REMARK 470 GLN F 90 CG CD OE1 NE2
REMARK 470 LYS F 135 CE NZ
REMARK 470 ARG F 166 CD NE CZ NH1 NH2
REMARK 470 LYS F 168 CG CD CE NZ
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 ILE A 33 63.28 -111.89
REMARK 500 GLU A 106 99.78 -68.15
REMARK 500 ASN A 134 -81.84 -113.78
REMARK 500 ARG A 166 52.00 -93.86
REMARK 500 ALA A 192 -2.96 78.54
REMARK 500 ASP A 198 -93.39 -111.23
REMARK 500 THR A 203 -65.86 -124.14
REMARK 500 TRP A 222 -151.98 -112.69
REMARK 500 ARG A 249 60.89 -114.50
REMARK 500 SER A 256 -113.90 59.04
REMARK 500 ALA B 192 -8.17 83.07
REMARK 500 ASP B 198 -97.72 -108.83
REMARK 500 THR B 203 -79.74 -126.36
REMARK 500 TRP B 222 -155.84 -104.14
REMARK 500 SER B 256 -114.66 55.10
REMARK 500 ASP B 394 72.16 -112.97
REMARK 500 GLU B 414 74.12 172.21
REMARK 500 ASN C 134 -68.26 -92.80
REMARK 500 LYS C 168 54.82 -102.89
REMARK 500 PRO C 170 -14.10 -49.77
REMARK 500 THR C 173 70.43 -69.75
REMARK 500 ALA C 192 -4.68 81.11
REMARK 500 ASP C 198 -83.05 -101.09
REMARK 500 THR C 203 -74.07 -130.89
REMARK 500 TRP C 222 -168.03 -126.48
REMARK 500 SER C 256 -110.73 50.82
REMARK 500 THR C 292 13.15 -141.27
REMARK 500 ILE D 33 71.62 -101.68
REMARK 500 ASN D 134 -82.74 -105.22
REMARK 500 PRO D 161 -35.39 -39.54
REMARK 500 LEU D 163 20.35 -77.86
REMARK 500 ALA D 192 -8.41 82.07
REMARK 500 ASP D 198 -104.02 -105.52
REMARK 500 THR D 203 -100.53 -130.63
REMARK 500 TRP D 222 -156.90 -112.55
REMARK 500 SER D 256 -124.28 47.32
REMARK 500 ASP D 356 32.03 -98.07
REMARK 500 LEU D 413 72.74 -108.11
REMARK 500 GLU D 414 -54.45 -174.02
REMARK 500 ILE E 33 78.42 -109.75
REMARK 500 LEU E 163 44.43 -92.15
REMARK 500 LYS E 168 -14.67 85.25
REMARK 500 ALA E 192 1.66 85.02
REMARK 500 ASP E 198 -101.91 -115.61
REMARK 500 THR E 203 -90.01 -107.09
REMARK 500 TRP E 222 -162.90 -114.60
REMARK 500 SER E 256 -123.07 60.74
REMARK 500 TYR F 60 40.64 -101.89
REMARK 500 ALA F 192 -2.72 78.06
REMARK 500 ASP F 198 -94.57 -99.81
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 393240 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT (RESIDUES 20-416) WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3NUZ A 20 416 UNP Q5LEF1 Q5LEF1_BACFN 20 416
DBREF 3NUZ B 20 416 UNP Q5LEF1 Q5LEF1_BACFN 20 416
DBREF 3NUZ C 20 416 UNP Q5LEF1 Q5LEF1_BACFN 20 416
DBREF 3NUZ D 20 416 UNP Q5LEF1 Q5LEF1_BACFN 20 416
DBREF 3NUZ E 20 416 UNP Q5LEF1 Q5LEF1_BACFN 20 416
DBREF 3NUZ F 20 416 UNP Q5LEF1 Q5LEF1_BACFN 20 416
SEQADV 3NUZ GLY A 0 UNP Q5LEF1 EXPRESSION TAG
SEQADV 3NUZ GLY B 0 UNP Q5LEF1 EXPRESSION TAG
SEQADV 3NUZ GLY C 0 UNP Q5LEF1 EXPRESSION TAG
SEQADV 3NUZ GLY D 0 UNP Q5LEF1 EXPRESSION TAG
SEQADV 3NUZ GLY E 0 UNP Q5LEF1 EXPRESSION TAG
SEQADV 3NUZ GLY F 0 UNP Q5LEF1 EXPRESSION TAG
SEQRES 1 A 398 GLY ALA GLN SER ASP GLY TRP SER PRO LYS ASP HIS ASN
SEQRES 2 A 398 LEU ILE LYS SER VAL ARG GLU ASP GLY ARG PHE LEU SER
SEQRES 3 A 398 SER TYR GLY VAL VAL HIS ALA MSE LEU ARG ASN THR GLU
SEQRES 4 A 398 PRO ARG TYR ALA PHE HIS ARG ASP PHE SER PRO LYS GLU
SEQRES 5 A 398 PHE ARG LYS TRP GLN LYS GLY LEU ARG HIS ALA MSE GLU
SEQRES 6 A 398 GLU ILE MSE LYS PHE PRO GLN ILE LYS ASN SER PRO ALA
SEQRES 7 A 398 PRO VAL CYS ILE LYS ARG GLU GLN ARG GLU GLY TYR ARG
SEQRES 8 A 398 LEU GLU LYS TRP GLU PHE TYR PRO LEU PRO LYS CYS VAL
SEQRES 9 A 398 SER THR PHE LEU VAL LEU ILE PRO ASP ASN ILE ASN LYS
SEQRES 10 A 398 PRO VAL PRO ALA ILE LEU CYS ILE PRO GLY SER GLY GLY
SEQRES 11 A 398 ASN LYS GLU GLY LEU ALA GLY GLU PRO GLY ILE ALA PRO
SEQRES 12 A 398 LYS LEU ASN ASP ARG TYR LYS ASP PRO LYS LEU THR GLN
SEQRES 13 A 398 ALA LEU ASN PHE VAL LYS GLU GLY TYR ILE ALA VAL ALA
SEQRES 14 A 398 VAL ASP ASN PRO ALA ALA GLY GLU ALA SER ASP LEU GLU
SEQRES 15 A 398 ARG TYR THR LEU GLY SER ASN TYR ASP TYR ASP VAL VAL
SEQRES 16 A 398 SER ARG TYR LEU LEU GLU LEU GLY TRP SER TYR LEU GLY
SEQRES 17 A 398 TYR ALA SER TYR LEU ASP MSE GLN VAL LEU ASN TRP MSE
SEQRES 18 A 398 LYS THR GLN LYS HIS ILE ARG LYS ASP ARG ILE VAL VAL
SEQRES 19 A 398 SER GLY PHE SER LEU GLY THR GLU PRO MSE MSE VAL LEU
SEQRES 20 A 398 GLY THR LEU ASP THR SER ILE TYR ALA PHE VAL TYR ASN
SEQRES 21 A 398 ASP PHE LEU CYS GLN THR GLN GLU ARG ALA GLU VAL MSE
SEQRES 22 A 398 THR MSE PRO ASP LYS ASN GLY ARG ARG PRO PHE PRO ASN
SEQRES 23 A 398 SER ILE ARG HIS LEU ILE PRO ASP PHE TRP LYS ASN PHE
SEQRES 24 A 398 ASN PHE PRO ASP ILE VAL ALA ALA LEU ALA PRO ARG PRO
SEQRES 25 A 398 ILE ILE LEU THR GLU GLY GLY LEU ASP ARG ASP LEU ASP
SEQRES 26 A 398 LEU VAL ARG LYS ALA TYR ALA ILE VAL GLY THR PRO ASP
SEQRES 27 A 398 ASN VAL LYS ILE TYR HIS TYR LYS LYS PHE SER ASP PRO
SEQRES 28 A 398 ASP THR ARG LYS ASN VAL GLU TYR LEU PRO GLU GLY LEU
SEQRES 29 A 398 ASP ARG ASN GLU TYR PHE ARG MSE VAL ASN VAL ASP GLY
SEQRES 30 A 398 PRO ASN HIS TYR PHE LYS SER GLU LEU VAL VAL PRO TRP
SEQRES 31 A 398 LEU ARG LYS LEU LEU GLU GLU ARG
SEQRES 1 B 398 GLY ALA GLN SER ASP GLY TRP SER PRO LYS ASP HIS ASN
SEQRES 2 B 398 LEU ILE LYS SER VAL ARG GLU ASP GLY ARG PHE LEU SER
SEQRES 3 B 398 SER TYR GLY VAL VAL HIS ALA MSE LEU ARG ASN THR GLU
SEQRES 4 B 398 PRO ARG TYR ALA PHE HIS ARG ASP PHE SER PRO LYS GLU
SEQRES 5 B 398 PHE ARG LYS TRP GLN LYS GLY LEU ARG HIS ALA MSE GLU
SEQRES 6 B 398 GLU ILE MSE LYS PHE PRO GLN ILE LYS ASN SER PRO ALA
SEQRES 7 B 398 PRO VAL CYS ILE LYS ARG GLU GLN ARG GLU GLY TYR ARG
SEQRES 8 B 398 LEU GLU LYS TRP GLU PHE TYR PRO LEU PRO LYS CYS VAL
SEQRES 9 B 398 SER THR PHE LEU VAL LEU ILE PRO ASP ASN ILE ASN LYS
SEQRES 10 B 398 PRO VAL PRO ALA ILE LEU CYS ILE PRO GLY SER GLY GLY
SEQRES 11 B 398 ASN LYS GLU GLY LEU ALA GLY GLU PRO GLY ILE ALA PRO
SEQRES 12 B 398 LYS LEU ASN ASP ARG TYR LYS ASP PRO LYS LEU THR GLN
SEQRES 13 B 398 ALA LEU ASN PHE VAL LYS GLU GLY TYR ILE ALA VAL ALA
SEQRES 14 B 398 VAL ASP ASN PRO ALA ALA GLY GLU ALA SER ASP LEU GLU
SEQRES 15 B 398 ARG TYR THR LEU GLY SER ASN TYR ASP TYR ASP VAL VAL
SEQRES 16 B 398 SER ARG TYR LEU LEU GLU LEU GLY TRP SER TYR LEU GLY
SEQRES 17 B 398 TYR ALA SER TYR LEU ASP MSE GLN VAL LEU ASN TRP MSE
SEQRES 18 B 398 LYS THR GLN LYS HIS ILE ARG LYS ASP ARG ILE VAL VAL
SEQRES 19 B 398 SER GLY PHE SER LEU GLY THR GLU PRO MSE MSE VAL LEU
SEQRES 20 B 398 GLY THR LEU ASP THR SER ILE TYR ALA PHE VAL TYR ASN
SEQRES 21 B 398 ASP PHE LEU CYS GLN THR GLN GLU ARG ALA GLU VAL MSE
SEQRES 22 B 398 THR MSE PRO ASP LYS ASN GLY ARG ARG PRO PHE PRO ASN
SEQRES 23 B 398 SER ILE ARG HIS LEU ILE PRO ASP PHE TRP LYS ASN PHE
SEQRES 24 B 398 ASN PHE PRO ASP ILE VAL ALA ALA LEU ALA PRO ARG PRO
SEQRES 25 B 398 ILE ILE LEU THR GLU GLY GLY LEU ASP ARG ASP LEU ASP
SEQRES 26 B 398 LEU VAL ARG LYS ALA TYR ALA ILE VAL GLY THR PRO ASP
SEQRES 27 B 398 ASN VAL LYS ILE TYR HIS TYR LYS LYS PHE SER ASP PRO
SEQRES 28 B 398 ASP THR ARG LYS ASN VAL GLU TYR LEU PRO GLU GLY LEU
SEQRES 29 B 398 ASP ARG ASN GLU TYR PHE ARG MSE VAL ASN VAL ASP GLY
SEQRES 30 B 398 PRO ASN HIS TYR PHE LYS SER GLU LEU VAL VAL PRO TRP
SEQRES 31 B 398 LEU ARG LYS LEU LEU GLU GLU ARG
SEQRES 1 C 398 GLY ALA GLN SER ASP GLY TRP SER PRO LYS ASP HIS ASN
SEQRES 2 C 398 LEU ILE LYS SER VAL ARG GLU ASP GLY ARG PHE LEU SER
SEQRES 3 C 398 SER TYR GLY VAL VAL HIS ALA MSE LEU ARG ASN THR GLU
SEQRES 4 C 398 PRO ARG TYR ALA PHE HIS ARG ASP PHE SER PRO LYS GLU
SEQRES 5 C 398 PHE ARG LYS TRP GLN LYS GLY LEU ARG HIS ALA MSE GLU
SEQRES 6 C 398 GLU ILE MSE LYS PHE PRO GLN ILE LYS ASN SER PRO ALA
SEQRES 7 C 398 PRO VAL CYS ILE LYS ARG GLU GLN ARG GLU GLY TYR ARG
SEQRES 8 C 398 LEU GLU LYS TRP GLU PHE TYR PRO LEU PRO LYS CYS VAL
SEQRES 9 C 398 SER THR PHE LEU VAL LEU ILE PRO ASP ASN ILE ASN LYS
SEQRES 10 C 398 PRO VAL PRO ALA ILE LEU CYS ILE PRO GLY SER GLY GLY
SEQRES 11 C 398 ASN LYS GLU GLY LEU ALA GLY GLU PRO GLY ILE ALA PRO
SEQRES 12 C 398 LYS LEU ASN ASP ARG TYR LYS ASP PRO LYS LEU THR GLN
SEQRES 13 C 398 ALA LEU ASN PHE VAL LYS GLU GLY TYR ILE ALA VAL ALA
SEQRES 14 C 398 VAL ASP ASN PRO ALA ALA GLY GLU ALA SER ASP LEU GLU
SEQRES 15 C 398 ARG TYR THR LEU GLY SER ASN TYR ASP TYR ASP VAL VAL
SEQRES 16 C 398 SER ARG TYR LEU LEU GLU LEU GLY TRP SER TYR LEU GLY
SEQRES 17 C 398 TYR ALA SER TYR LEU ASP MSE GLN VAL LEU ASN TRP MSE
SEQRES 18 C 398 LYS THR GLN LYS HIS ILE ARG LYS ASP ARG ILE VAL VAL
SEQRES 19 C 398 SER GLY PHE SER LEU GLY THR GLU PRO MSE MSE VAL LEU
SEQRES 20 C 398 GLY THR LEU ASP THR SER ILE TYR ALA PHE VAL TYR ASN
SEQRES 21 C 398 ASP PHE LEU CYS GLN THR GLN GLU ARG ALA GLU VAL MSE
SEQRES 22 C 398 THR MSE PRO ASP LYS ASN GLY ARG ARG PRO PHE PRO ASN
SEQRES 23 C 398 SER ILE ARG HIS LEU ILE PRO ASP PHE TRP LYS ASN PHE
SEQRES 24 C 398 ASN PHE PRO ASP ILE VAL ALA ALA LEU ALA PRO ARG PRO
SEQRES 25 C 398 ILE ILE LEU THR GLU GLY GLY LEU ASP ARG ASP LEU ASP
SEQRES 26 C 398 LEU VAL ARG LYS ALA TYR ALA ILE VAL GLY THR PRO ASP
SEQRES 27 C 398 ASN VAL LYS ILE TYR HIS TYR LYS LYS PHE SER ASP PRO
SEQRES 28 C 398 ASP THR ARG LYS ASN VAL GLU TYR LEU PRO GLU GLY LEU
SEQRES 29 C 398 ASP ARG ASN GLU TYR PHE ARG MSE VAL ASN VAL ASP GLY
SEQRES 30 C 398 PRO ASN HIS TYR PHE LYS SER GLU LEU VAL VAL PRO TRP
SEQRES 31 C 398 LEU ARG LYS LEU LEU GLU GLU ARG
SEQRES 1 D 398 GLY ALA GLN SER ASP GLY TRP SER PRO LYS ASP HIS ASN
SEQRES 2 D 398 LEU ILE LYS SER VAL ARG GLU ASP GLY ARG PHE LEU SER
SEQRES 3 D 398 SER TYR GLY VAL VAL HIS ALA MSE LEU ARG ASN THR GLU
SEQRES 4 D 398 PRO ARG TYR ALA PHE HIS ARG ASP PHE SER PRO LYS GLU
SEQRES 5 D 398 PHE ARG LYS TRP GLN LYS GLY LEU ARG HIS ALA MSE GLU
SEQRES 6 D 398 GLU ILE MSE LYS PHE PRO GLN ILE LYS ASN SER PRO ALA
SEQRES 7 D 398 PRO VAL CYS ILE LYS ARG GLU GLN ARG GLU GLY TYR ARG
SEQRES 8 D 398 LEU GLU LYS TRP GLU PHE TYR PRO LEU PRO LYS CYS VAL
SEQRES 9 D 398 SER THR PHE LEU VAL LEU ILE PRO ASP ASN ILE ASN LYS
SEQRES 10 D 398 PRO VAL PRO ALA ILE LEU CYS ILE PRO GLY SER GLY GLY
SEQRES 11 D 398 ASN LYS GLU GLY LEU ALA GLY GLU PRO GLY ILE ALA PRO
SEQRES 12 D 398 LYS LEU ASN ASP ARG TYR LYS ASP PRO LYS LEU THR GLN
SEQRES 13 D 398 ALA LEU ASN PHE VAL LYS GLU GLY TYR ILE ALA VAL ALA
SEQRES 14 D 398 VAL ASP ASN PRO ALA ALA GLY GLU ALA SER ASP LEU GLU
SEQRES 15 D 398 ARG TYR THR LEU GLY SER ASN TYR ASP TYR ASP VAL VAL
SEQRES 16 D 398 SER ARG TYR LEU LEU GLU LEU GLY TRP SER TYR LEU GLY
SEQRES 17 D 398 TYR ALA SER TYR LEU ASP MSE GLN VAL LEU ASN TRP MSE
SEQRES 18 D 398 LYS THR GLN LYS HIS ILE ARG LYS ASP ARG ILE VAL VAL
SEQRES 19 D 398 SER GLY PHE SER LEU GLY THR GLU PRO MSE MSE VAL LEU
SEQRES 20 D 398 GLY THR LEU ASP THR SER ILE TYR ALA PHE VAL TYR ASN
SEQRES 21 D 398 ASP PHE LEU CYS GLN THR GLN GLU ARG ALA GLU VAL MSE
SEQRES 22 D 398 THR MSE PRO ASP LYS ASN GLY ARG ARG PRO PHE PRO ASN
SEQRES 23 D 398 SER ILE ARG HIS LEU ILE PRO ASP PHE TRP LYS ASN PHE
SEQRES 24 D 398 ASN PHE PRO ASP ILE VAL ALA ALA LEU ALA PRO ARG PRO
SEQRES 25 D 398 ILE ILE LEU THR GLU GLY GLY LEU ASP ARG ASP LEU ASP
SEQRES 26 D 398 LEU VAL ARG LYS ALA TYR ALA ILE VAL GLY THR PRO ASP
SEQRES 27 D 398 ASN VAL LYS ILE TYR HIS TYR LYS LYS PHE SER ASP PRO
SEQRES 28 D 398 ASP THR ARG LYS ASN VAL GLU TYR LEU PRO GLU GLY LEU
SEQRES 29 D 398 ASP ARG ASN GLU TYR PHE ARG MSE VAL ASN VAL ASP GLY
SEQRES 30 D 398 PRO ASN HIS TYR PHE LYS SER GLU LEU VAL VAL PRO TRP
SEQRES 31 D 398 LEU ARG LYS LEU LEU GLU GLU ARG
SEQRES 1 E 398 GLY ALA GLN SER ASP GLY TRP SER PRO LYS ASP HIS ASN
SEQRES 2 E 398 LEU ILE LYS SER VAL ARG GLU ASP GLY ARG PHE LEU SER
SEQRES 3 E 398 SER TYR GLY VAL VAL HIS ALA MSE LEU ARG ASN THR GLU
SEQRES 4 E 398 PRO ARG TYR ALA PHE HIS ARG ASP PHE SER PRO LYS GLU
SEQRES 5 E 398 PHE ARG LYS TRP GLN LYS GLY LEU ARG HIS ALA MSE GLU
SEQRES 6 E 398 GLU ILE MSE LYS PHE PRO GLN ILE LYS ASN SER PRO ALA
SEQRES 7 E 398 PRO VAL CYS ILE LYS ARG GLU GLN ARG GLU GLY TYR ARG
SEQRES 8 E 398 LEU GLU LYS TRP GLU PHE TYR PRO LEU PRO LYS CYS VAL
SEQRES 9 E 398 SER THR PHE LEU VAL LEU ILE PRO ASP ASN ILE ASN LYS
SEQRES 10 E 398 PRO VAL PRO ALA ILE LEU CYS ILE PRO GLY SER GLY GLY
SEQRES 11 E 398 ASN LYS GLU GLY LEU ALA GLY GLU PRO GLY ILE ALA PRO
SEQRES 12 E 398 LYS LEU ASN ASP ARG TYR LYS ASP PRO LYS LEU THR GLN
SEQRES 13 E 398 ALA LEU ASN PHE VAL LYS GLU GLY TYR ILE ALA VAL ALA
SEQRES 14 E 398 VAL ASP ASN PRO ALA ALA GLY GLU ALA SER ASP LEU GLU
SEQRES 15 E 398 ARG TYR THR LEU GLY SER ASN TYR ASP TYR ASP VAL VAL
SEQRES 16 E 398 SER ARG TYR LEU LEU GLU LEU GLY TRP SER TYR LEU GLY
SEQRES 17 E 398 TYR ALA SER TYR LEU ASP MSE GLN VAL LEU ASN TRP MSE
SEQRES 18 E 398 LYS THR GLN LYS HIS ILE ARG LYS ASP ARG ILE VAL VAL
SEQRES 19 E 398 SER GLY PHE SER LEU GLY THR GLU PRO MSE MSE VAL LEU
SEQRES 20 E 398 GLY THR LEU ASP THR SER ILE TYR ALA PHE VAL TYR ASN
SEQRES 21 E 398 ASP PHE LEU CYS GLN THR GLN GLU ARG ALA GLU VAL MSE
SEQRES 22 E 398 THR MSE PRO ASP LYS ASN GLY ARG ARG PRO PHE PRO ASN
SEQRES 23 E 398 SER ILE ARG HIS LEU ILE PRO ASP PHE TRP LYS ASN PHE
SEQRES 24 E 398 ASN PHE PRO ASP ILE VAL ALA ALA LEU ALA PRO ARG PRO
SEQRES 25 E 398 ILE ILE LEU THR GLU GLY GLY LEU ASP ARG ASP LEU ASP
SEQRES 26 E 398 LEU VAL ARG LYS ALA TYR ALA ILE VAL GLY THR PRO ASP
SEQRES 27 E 398 ASN VAL LYS ILE TYR HIS TYR LYS LYS PHE SER ASP PRO
SEQRES 28 E 398 ASP THR ARG LYS ASN VAL GLU TYR LEU PRO GLU GLY LEU
SEQRES 29 E 398 ASP ARG ASN GLU TYR PHE ARG MSE VAL ASN VAL ASP GLY
SEQRES 30 E 398 PRO ASN HIS TYR PHE LYS SER GLU LEU VAL VAL PRO TRP
SEQRES 31 E 398 LEU ARG LYS LEU LEU GLU GLU ARG
SEQRES 1 F 398 GLY ALA GLN SER ASP GLY TRP SER PRO LYS ASP HIS ASN
SEQRES 2 F 398 LEU ILE LYS SER VAL ARG GLU ASP GLY ARG PHE LEU SER
SEQRES 3 F 398 SER TYR GLY VAL VAL HIS ALA MSE LEU ARG ASN THR GLU
SEQRES 4 F 398 PRO ARG TYR ALA PHE HIS ARG ASP PHE SER PRO LYS GLU
SEQRES 5 F 398 PHE ARG LYS TRP GLN LYS GLY LEU ARG HIS ALA MSE GLU
SEQRES 6 F 398 GLU ILE MSE LYS PHE PRO GLN ILE LYS ASN SER PRO ALA
SEQRES 7 F 398 PRO VAL CYS ILE LYS ARG GLU GLN ARG GLU GLY TYR ARG
SEQRES 8 F 398 LEU GLU LYS TRP GLU PHE TYR PRO LEU PRO LYS CYS VAL
SEQRES 9 F 398 SER THR PHE LEU VAL LEU ILE PRO ASP ASN ILE ASN LYS
SEQRES 10 F 398 PRO VAL PRO ALA ILE LEU CYS ILE PRO GLY SER GLY GLY
SEQRES 11 F 398 ASN LYS GLU GLY LEU ALA GLY GLU PRO GLY ILE ALA PRO
SEQRES 12 F 398 LYS LEU ASN ASP ARG TYR LYS ASP PRO LYS LEU THR GLN
SEQRES 13 F 398 ALA LEU ASN PHE VAL LYS GLU GLY TYR ILE ALA VAL ALA
SEQRES 14 F 398 VAL ASP ASN PRO ALA ALA GLY GLU ALA SER ASP LEU GLU
SEQRES 15 F 398 ARG TYR THR LEU GLY SER ASN TYR ASP TYR ASP VAL VAL
SEQRES 16 F 398 SER ARG TYR LEU LEU GLU LEU GLY TRP SER TYR LEU GLY
SEQRES 17 F 398 TYR ALA SER TYR LEU ASP MSE GLN VAL LEU ASN TRP MSE
SEQRES 18 F 398 LYS THR GLN LYS HIS ILE ARG LYS ASP ARG ILE VAL VAL
SEQRES 19 F 398 SER GLY PHE SER LEU GLY THR GLU PRO MSE MSE VAL LEU
SEQRES 20 F 398 GLY THR LEU ASP THR SER ILE TYR ALA PHE VAL TYR ASN
SEQRES 21 F 398 ASP PHE LEU CYS GLN THR GLN GLU ARG ALA GLU VAL MSE
SEQRES 22 F 398 THR MSE PRO ASP LYS ASN GLY ARG ARG PRO PHE PRO ASN
SEQRES 23 F 398 SER ILE ARG HIS LEU ILE PRO ASP PHE TRP LYS ASN PHE
SEQRES 24 F 398 ASN PHE PRO ASP ILE VAL ALA ALA LEU ALA PRO ARG PRO
SEQRES 25 F 398 ILE ILE LEU THR GLU GLY GLY LEU ASP ARG ASP LEU ASP
SEQRES 26 F 398 LEU VAL ARG LYS ALA TYR ALA ILE VAL GLY THR PRO ASP
SEQRES 27 F 398 ASN VAL LYS ILE TYR HIS TYR LYS LYS PHE SER ASP PRO
SEQRES 28 F 398 ASP THR ARG LYS ASN VAL GLU TYR LEU PRO GLU GLY LEU
SEQRES 29 F 398 ASP ARG ASN GLU TYR PHE ARG MSE VAL ASN VAL ASP GLY
SEQRES 30 F 398 PRO ASN HIS TYR PHE LYS SER GLU LEU VAL VAL PRO TRP
SEQRES 31 F 398 LEU ARG LYS LEU LEU GLU GLU ARG
MODRES 3NUZ MSE A 52 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 82 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 86 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 233 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 239 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 262 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 263 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 291 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 293 MET SELENOMETHIONINE
MODRES 3NUZ MSE A 390 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 52 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 82 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 86 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 233 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 239 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 262 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 263 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 291 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 293 MET SELENOMETHIONINE
MODRES 3NUZ MSE B 390 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 52 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 82 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 86 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 233 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 239 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 262 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 263 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 291 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 293 MET SELENOMETHIONINE
MODRES 3NUZ MSE C 390 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 52 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 82 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 86 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 233 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 239 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 262 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 263 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 291 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 293 MET SELENOMETHIONINE
MODRES 3NUZ MSE D 390 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 52 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 82 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 86 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 233 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 239 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 262 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 263 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 291 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 293 MET SELENOMETHIONINE
MODRES 3NUZ MSE E 390 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 52 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 82 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 86 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 233 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 239 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 262 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 263 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 291 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 293 MET SELENOMETHIONINE
MODRES 3NUZ MSE F 390 MET SELENOMETHIONINE
HET MSE A 52 8
HET MSE A 82 8
HET MSE A 86 8
HET MSE A 233 8
HET MSE A 239 8
HET MSE A 262 8
HET MSE A 263 8
HET MSE A 291 8
HET MSE A 293 8
HET MSE A 390 8
HET MSE B 52 8
HET MSE B 82 8
HET MSE B 86 8
HET MSE B 233 8
HET MSE B 239 8
HET MSE B 262 8
HET MSE B 263 8
HET MSE B 291 8
HET MSE B 293 8
HET MSE B 390 8
HET MSE C 52 8
HET MSE C 82 8
HET MSE C 86 8
HET MSE C 233 8
HET MSE C 239 8
HET MSE C 262 8
HET MSE C 263 8
HET MSE C 291 8
HET MSE C 293 8
HET MSE C 390 8
HET MSE D 52 8
HET MSE D 82 8
HET MSE D 86 8
HET MSE D 233 8
HET MSE D 239 8
HET MSE D 262 8
HET MSE D 263 8
HET MSE D 291 8
HET MSE D 293 8
HET MSE D 390 8
HET MSE E 52 8
HET MSE E 82 8
HET MSE E 86 8
HET MSE E 233 8
HET MSE E 239 8
HET MSE E 262 8
HET MSE E 263 8
HET MSE E 291 8
HET MSE E 293 8
HET MSE E 390 8
HET MSE F 52 8
HET MSE F 82 8
HET MSE F 86 8
HET MSE F 233 8
HET MSE F 239 8
HET MSE F 262 8
HET MSE F 263 8
HET MSE F 291 8
HET MSE F 293 8
HET MSE F 390 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 60(C5 H11 N O2 SE)
FORMUL 7 HOH *253(H2 O)
HELIX 1 1 SER A 26 HIS A 30 5 5
HELIX 2 2 SER A 44 ASN A 55 1 12
HELIX 3 3 SER A 67 LYS A 87 1 21
HELIX 4 4 ASN A 149 GLY A 155 1 7
HELIX 5 5 THR A 173 LYS A 180 1 8
HELIX 6 6 ALA A 193 SER A 197 5 5
HELIX 7 7 LEU A 199 THR A 203 5 5
HELIX 8 8 ASP A 209 LEU A 220 1 12
HELIX 9 9 SER A 223 LYS A 240 1 18
HELIX 10 10 GLY A 258 ASP A 269 1 12
HELIX 11 11 GLN A 283 MSE A 291 1 9
HELIX 12 12 SER A 305 LEU A 309 5 5
HELIX 13 13 ASP A 312 PHE A 317 1 6
HELIX 14 14 ASN A 318 LEU A 326 1 9
HELIX 15 15 LEU A 338 GLY A 353 1 16
HELIX 16 16 TYR A 363 SER A 367 5 5
HELIX 17 17 ASP A 368 ARG A 372 5 5
HELIX 18 18 ASP A 383 VAL A 391 1 9
HELIX 19 19 ASP A 394 HIS A 398 5 5
HELIX 20 20 LYS A 401 GLU A 415 1 15
HELIX 21 21 SER B 26 HIS B 30 5 5
HELIX 22 22 SER B 44 ASN B 55 1 12
HELIX 23 23 SER B 67 LYS B 87 1 21
HELIX 24 24 ASN B 149 GLY B 155 1 7
HELIX 25 25 ALA B 160 ASN B 164 5 5
HELIX 26 26 THR B 173 LYS B 180 1 8
HELIX 27 27 ALA B 193 SER B 197 5 5
HELIX 28 28 ASP B 209 LEU B 220 1 12
HELIX 29 29 SER B 223 LYS B 240 1 18
HELIX 30 30 GLY B 258 ASP B 269 1 12
HELIX 31 31 GLN B 283 MSE B 291 1 9
HELIX 32 32 SER B 305 LEU B 309 5 5
HELIX 33 33 ASP B 312 PHE B 317 1 6
HELIX 34 34 ASN B 318 ALA B 325 1 8
HELIX 35 35 LEU B 338 GLY B 353 1 16
HELIX 36 36 THR B 354 ASP B 356 5 3
HELIX 37 37 TYR B 363 SER B 367 5 5
HELIX 38 38 ASP B 368 ARG B 372 5 5
HELIX 39 39 ASP B 383 VAL B 391 1 9
HELIX 40 40 ASP B 394 HIS B 398 5 5
HELIX 41 41 LYS B 401 LEU B 413 1 13
HELIX 42 42 SER C 26 HIS C 30 5 5
HELIX 43 43 SER C 44 ASN C 55 1 12
HELIX 44 44 SER C 67 LYS C 87 1 21
HELIX 45 45 ASN C 149 ALA C 154 1 6
HELIX 46 46 ALA C 160 ASN C 164 5 5
HELIX 47 47 THR C 173 LYS C 180 1 8
HELIX 48 48 ALA C 193 SER C 197 5 5
HELIX 49 49 ASP C 209 LEU C 220 1 12
HELIX 50 50 SER C 223 LYS C 240 1 18
HELIX 51 51 GLY C 258 ASP C 269 1 12
HELIX 52 52 GLN C 283 MSE C 291 1 9
HELIX 53 53 SER C 305 LEU C 309 5 5
HELIX 54 54 ASN C 318 ALA C 325 1 8
HELIX 55 55 LEU C 338 VAL C 352 1 15
HELIX 56 56 THR C 354 ASP C 356 5 3
HELIX 57 57 TYR C 363 SER C 367 5 5
HELIX 58 58 ASP C 368 ARG C 372 5 5
HELIX 59 59 ASP C 383 VAL C 391 1 9
HELIX 60 60 ASP C 394 HIS C 398 5 5
HELIX 61 61 LYS C 401 GLU C 415 1 15
HELIX 62 62 SER D 26 HIS D 30 5 5
HELIX 63 63 SER D 44 ASN D 55 1 12
HELIX 64 64 SER D 67 LYS D 87 1 21
HELIX 65 65 ASN D 149 ALA D 154 1 6
HELIX 66 66 THR D 173 GLU D 181 1 9
HELIX 67 67 ALA D 193 SER D 197 5 5
HELIX 68 68 LEU D 199 THR D 203 5 5
HELIX 69 69 ASP D 209 LEU D 220 1 12
HELIX 70 70 SER D 223 LYS D 240 1 18
HELIX 71 71 GLY D 258 ASP D 269 1 12
HELIX 72 72 GLN D 283 MSE D 291 1 9
HELIX 73 73 SER D 305 LEU D 309 5 5
HELIX 74 74 ASN D 318 ALA D 325 1 8
HELIX 75 75 LEU D 338 VAL D 352 1 15
HELIX 76 76 THR D 354 ASP D 356 5 3
HELIX 77 77 ASP D 368 ARG D 372 5 5
HELIX 78 78 ASP D 383 VAL D 391 1 9
HELIX 79 79 ASP D 394 HIS D 398 5 5
HELIX 80 80 LYS D 401 LEU D 413 1 13
HELIX 81 81 SER E 26 HIS E 30 5 5
HELIX 82 82 SER E 44 THR E 56 1 13
HELIX 83 83 SER E 67 LYS E 87 1 21
HELIX 84 84 ASN E 149 GLY E 155 1 7
HELIX 85 85 THR E 173 LYS E 180 1 8
HELIX 86 86 ALA E 193 SER E 197 5 5
HELIX 87 87 ASP E 209 LEU E 220 1 12
HELIX 88 88 SER E 223 LYS E 240 1 18
HELIX 89 89 GLY E 258 ASP E 269 1 12
HELIX 90 90 GLN E 283 MSE E 291 1 9
HELIX 91 91 SER E 305 LEU E 309 5 5
HELIX 92 92 ASN E 318 ALA E 325 1 8
HELIX 93 93 LEU E 338 VAL E 352 1 15
HELIX 94 94 THR E 354 ASP E 356 5 3
HELIX 95 95 TYR E 363 SER E 367 5 5
HELIX 96 96 ASP E 368 ARG E 372 5 5
HELIX 97 97 ASP E 383 VAL E 391 1 9
HELIX 98 98 ASP E 394 HIS E 398 5 5
HELIX 99 99 LYS E 401 LEU E 413 1 13
HELIX 100 100 SER F 26 HIS F 30 5 5
HELIX 101 101 SER F 44 ASN F 55 1 12
HELIX 102 102 SER F 67 LYS F 87 1 21
HELIX 103 103 ASN F 149 ALA F 154 1 6
HELIX 104 104 ALA F 160 ASN F 164 5 5
HELIX 105 105 THR F 173 LYS F 180 1 8
HELIX 106 106 ALA F 193 SER F 197 5 5
HELIX 107 107 ASP F 209 LEU F 220 1 12
HELIX 108 108 SER F 223 LYS F 240 1 18
HELIX 109 109 GLY F 258 ASP F 269 1 12
HELIX 110 110 GLN F 283 MSE F 291 1 9
HELIX 111 111 SER F 305 LEU F 309 5 5
HELIX 112 112 ASP F 312 PHE F 317 1 6
HELIX 113 113 ASN F 318 ALA F 325 1 8
HELIX 114 114 LEU F 338 VAL F 352 1 15
HELIX 115 115 THR F 354 ASP F 356 5 3
HELIX 116 116 TYR F 363 SER F 367 5 5
HELIX 117 117 ASP F 368 ARG F 372 5 5
HELIX 118 118 ASP F 383 VAL F 391 1 9
HELIX 119 119 ASP F 394 HIS F 398 5 5
HELIX 120 120 LYS F 401 LEU F 413 1 13
SHEET 1 A 9 VAL A 98 GLN A 104 0
SHEET 2 A 9 TYR A 108 PHE A 115 -1 O GLU A 114 N VAL A 98
SHEET 3 A 9 SER A 123 PRO A 130 -1 O VAL A 127 N GLU A 111
SHEET 4 A 9 ILE A 184 VAL A 188 -1 O ALA A 187 N LEU A 126
SHEET 5 A 9 VAL A 137 ILE A 143 1 N CYS A 142 O VAL A 186
SHEET 6 A 9 ILE A 245 PHE A 255 1 O PHE A 255 N ILE A 143
SHEET 7 A 9 ALA A 274 ASN A 278 1 O ASN A 278 N GLY A 254
SHEET 8 A 9 ILE A 331 LEU A 333 1 O ILE A 332 N TYR A 277
SHEET 9 A 9 VAL A 358 ILE A 360 1 O LYS A 359 N ILE A 331
SHEET 1 B 9 VAL B 98 ARG B 105 0
SHEET 2 B 9 TYR B 108 PHE B 115 -1 O GLU B 114 N VAL B 98
SHEET 3 B 9 SER B 123 PRO B 130 -1 O VAL B 127 N GLU B 111
SHEET 4 B 9 ILE B 184 ALA B 187 -1 O ALA B 187 N LEU B 126
SHEET 5 B 9 VAL B 137 ILE B 143 1 N CYS B 142 O VAL B 186
SHEET 6 B 9 ILE B 245 PHE B 255 1 O SER B 253 N LEU B 141
SHEET 7 B 9 ALA B 274 ASN B 278 1 O VAL B 276 N GLY B 254
SHEET 8 B 9 ILE B 331 LEU B 333 1 O ILE B 332 N TYR B 277
SHEET 9 B 9 VAL B 358 ILE B 360 1 O LYS B 359 N LEU B 333
SHEET 1 C 9 VAL C 98 GLN C 104 0
SHEET 2 C 9 TYR C 108 PHE C 115 -1 O LYS C 112 N ILE C 100
SHEET 3 C 9 SER C 123 PRO C 130 -1 O VAL C 127 N GLU C 111
SHEET 4 C 9 ILE C 184 VAL C 188 -1 O ALA C 185 N LEU C 128
SHEET 5 C 9 VAL C 137 ILE C 143 1 N CYS C 142 O VAL C 186
SHEET 6 C 9 ILE C 245 PHE C 255 1 O SER C 253 N LEU C 141
SHEET 7 C 9 ALA C 274 ASN C 278 1 O VAL C 276 N GLY C 254
SHEET 8 C 9 ILE C 331 LEU C 333 1 O ILE C 332 N TYR C 277
SHEET 9 C 9 VAL C 358 ILE C 360 1 O LYS C 359 N LEU C 333
SHEET 1 D 9 VAL D 98 GLN D 104 0
SHEET 2 D 9 TYR D 108 PHE D 115 -1 O LEU D 110 N GLU D 103
SHEET 3 D 9 SER D 123 PRO D 130 -1 O VAL D 127 N GLU D 111
SHEET 4 D 9 ILE D 184 ALA D 187 -1 O ALA D 185 N LEU D 128
SHEET 5 D 9 VAL D 137 ILE D 143 1 N CYS D 142 O VAL D 186
SHEET 6 D 9 ILE D 245 PHE D 255 1 O VAL D 251 N ALA D 139
SHEET 7 D 9 ALA D 274 ASN D 278 1 O VAL D 276 N GLY D 254
SHEET 8 D 9 ILE D 331 LEU D 333 1 O ILE D 332 N TYR D 277
SHEET 9 D 9 VAL D 358 ILE D 360 1 O LYS D 359 N LEU D 333
SHEET 1 E 9 VAL E 98 ARG E 105 0
SHEET 2 E 9 TYR E 108 PHE E 115 -1 O LEU E 110 N GLU E 103
SHEET 3 E 9 SER E 123 PRO E 130 -1 O VAL E 127 N GLU E 111
SHEET 4 E 9 ILE E 184 ALA E 187 -1 O ALA E 185 N LEU E 128
SHEET 5 E 9 VAL E 137 ILE E 143 1 N CYS E 142 O VAL E 186
SHEET 6 E 9 ILE E 245 PHE E 255 1 O SER E 253 N LEU E 141
SHEET 7 E 9 ALA E 274 ASN E 278 1 O VAL E 276 N GLY E 254
SHEET 8 E 9 ILE E 331 LEU E 333 1 O ILE E 332 N TYR E 277
SHEET 9 E 9 VAL E 358 ILE E 360 1 O LYS E 359 N LEU E 333
SHEET 1 F 9 VAL F 98 ARG F 105 0
SHEET 2 F 9 TYR F 108 PHE F 115 -1 O GLU F 114 N VAL F 98
SHEET 3 F 9 SER F 123 PRO F 130 -1 O VAL F 127 N GLU F 111
SHEET 4 F 9 ILE F 184 ALA F 187 -1 O ALA F 185 N LEU F 128
SHEET 5 F 9 VAL F 137 ILE F 143 1 N CYS F 142 O VAL F 186
SHEET 6 F 9 ILE F 245 PHE F 255 1 O SER F 253 N LEU F 141
SHEET 7 F 9 ALA F 274 ASN F 278 1 O ASN F 278 N GLY F 254
SHEET 8 F 9 ILE F 331 LEU F 333 1 O ILE F 332 N TYR F 277
SHEET 9 F 9 VAL F 358 ILE F 360 1 O LYS F 359 N LEU F 333
LINK C ALA A 51 N MSE A 52 1555 1555 1.33
LINK C MSE A 52 N LEU A 53 1555 1555 1.34
LINK C ALA A 81 N MSE A 82 1555 1555 1.34
LINK C MSE A 82 N GLU A 83 1555 1555 1.34
LINK C ILE A 85 N MSE A 86 1555 1555 1.33
LINK C MSE A 86 N LYS A 87 1555 1555 1.33
LINK C ASP A 232 N MSE A 233 1555 1555 1.33
LINK C MSE A 233 N GLN A 234 1555 1555 1.34
LINK C TRP A 238 N MSE A 239 1555 1555 1.33
LINK C MSE A 239 N LYS A 240 1555 1555 1.33
LINK C PRO A 261 N MSE A 262 1555 1555 1.33
LINK C MSE A 262 N MSE A 263 1555 1555 1.34
LINK C MSE A 263 N VAL A 264 1555 1555 1.33
LINK C VAL A 290 N MSE A 291 1555 1555 1.33
LINK C MSE A 291 N THR A 292 1555 1555 1.33
LINK C THR A 292 N MSE A 293 1555 1555 1.34
LINK C MSE A 293 N PRO A 294 1555 1555 1.34
LINK C ARG A 389 N MSE A 390 1555 1555 1.33
LINK C MSE A 390 N VAL A 391 1555 1555 1.33
LINK C ALA B 51 N MSE B 52 1555 1555 1.32
LINK C MSE B 52 N LEU B 53 1555 1555 1.33
LINK C ALA B 81 N MSE B 82 1555 1555 1.33
LINK C MSE B 82 N GLU B 83 1555 1555 1.33
LINK C ILE B 85 N MSE B 86 1555 1555 1.33
LINK C MSE B 86 N LYS B 87 1555 1555 1.33
LINK C ASP B 232 N MSE B 233 1555 1555 1.33
LINK C MSE B 233 N GLN B 234 1555 1555 1.33
LINK C TRP B 238 N MSE B 239 1555 1555 1.33
LINK C MSE B 239 N LYS B 240 1555 1555 1.33
LINK C PRO B 261 N MSE B 262 1555 1555 1.33
LINK C MSE B 262 N MSE B 263 1555 1555 1.34
LINK C MSE B 263 N VAL B 264 1555 1555 1.33
LINK C VAL B 290 N MSE B 291 1555 1555 1.33
LINK C MSE B 291 N THR B 292 1555 1555 1.33
LINK C THR B 292 N MSE B 293 1555 1555 1.33
LINK C MSE B 293 N PRO B 294 1555 1555 1.34
LINK C ARG B 389 N MSE B 390 1555 1555 1.34
LINK C MSE B 390 N VAL B 391 1555 1555 1.34
LINK C ALA C 51 N MSE C 52 1555 1555 1.33
LINK C MSE C 52 N LEU C 53 1555 1555 1.33
LINK C ALA C 81 N MSE C 82 1555 1555 1.33
LINK C MSE C 82 N GLU C 83 1555 1555 1.33
LINK C ILE C 85 N MSE C 86 1555 1555 1.33
LINK C MSE C 86 N LYS C 87 1555 1555 1.33
LINK C ASP C 232 N MSE C 233 1555 1555 1.33
LINK C MSE C 233 N GLN C 234 1555 1555 1.34
LINK C TRP C 238 N MSE C 239 1555 1555 1.33
LINK C MSE C 239 N LYS C 240 1555 1555 1.34
LINK C PRO C 261 N MSE C 262 1555 1555 1.33
LINK C MSE C 262 N MSE C 263 1555 1555 1.34
LINK C MSE C 263 N VAL C 264 1555 1555 1.33
LINK C VAL C 290 N MSE C 291 1555 1555 1.33
LINK C MSE C 291 N THR C 292 1555 1555 1.34
LINK C THR C 292 N MSE C 293 1555 1555 1.33
LINK C MSE C 293 N PRO C 294 1555 1555 1.35
LINK C ARG C 389 N MSE C 390 1555 1555 1.34
LINK C MSE C 390 N VAL C 391 1555 1555 1.34
LINK C ALA D 51 N MSE D 52 1555 1555 1.33
LINK C MSE D 52 N LEU D 53 1555 1555 1.33
LINK C ALA D 81 N MSE D 82 1555 1555 1.33
LINK C MSE D 82 N GLU D 83 1555 1555 1.33
LINK C ILE D 85 N MSE D 86 1555 1555 1.33
LINK C MSE D 86 N LYS D 87 1555 1555 1.34
LINK C ASP D 232 N MSE D 233 1555 1555 1.34
LINK C MSE D 233 N GLN D 234 1555 1555 1.33
LINK C TRP D 238 N MSE D 239 1555 1555 1.33
LINK C MSE D 239 N LYS D 240 1555 1555 1.33
LINK C PRO D 261 N MSE D 262 1555 1555 1.34
LINK C MSE D 262 N MSE D 263 1555 1555 1.33
LINK C MSE D 263 N VAL D 264 1555 1555 1.33
LINK C VAL D 290 N MSE D 291 1555 1555 1.33
LINK C MSE D 291 N THR D 292 1555 1555 1.33
LINK C THR D 292 N MSE D 293 1555 1555 1.34
LINK C MSE D 293 N PRO D 294 1555 1555 1.34
LINK C ARG D 389 N MSE D 390 1555 1555 1.33
LINK C MSE D 390 N VAL D 391 1555 1555 1.34
LINK C ALA E 51 N MSE E 52 1555 1555 1.34
LINK C MSE E 52 N LEU E 53 1555 1555 1.33
LINK C ALA E 81 N MSE E 82 1555 1555 1.33
LINK C MSE E 82 N GLU E 83 1555 1555 1.33
LINK C ILE E 85 N MSE E 86 1555 1555 1.33
LINK C MSE E 86 N LYS E 87 1555 1555 1.34
LINK C ASP E 232 N MSE E 233 1555 1555 1.34
LINK C MSE E 233 N GLN E 234 1555 1555 1.34
LINK C TRP E 238 N MSE E 239 1555 1555 1.34
LINK C MSE E 239 N LYS E 240 1555 1555 1.33
LINK C PRO E 261 N MSE E 262 1555 1555 1.34
LINK C MSE E 262 N MSE E 263 1555 1555 1.34
LINK C MSE E 263 N VAL E 264 1555 1555 1.33
LINK C VAL E 290 N MSE E 291 1555 1555 1.33
LINK C MSE E 291 N THR E 292 1555 1555 1.33
LINK C THR E 292 N MSE E 293 1555 1555 1.33
LINK C MSE E 293 N PRO E 294 1555 1555 1.35
LINK C ARG E 389 N MSE E 390 1555 1555 1.34
LINK C MSE E 390 N VAL E 391 1555 1555 1.33
LINK C ALA F 51 N MSE F 52 1555 1555 1.33
LINK C MSE F 52 N LEU F 53 1555 1555 1.33
LINK C ALA F 81 N MSE F 82 1555 1555 1.34
LINK C MSE F 82 N GLU F 83 1555 1555 1.33
LINK C ILE F 85 N MSE F 86 1555 1555 1.33
LINK C MSE F 86 N LYS F 87 1555 1555 1.34
LINK C ASP F 232 N MSE F 233 1555 1555 1.33
LINK C MSE F 233 N GLN F 234 1555 1555 1.33
LINK C TRP F 238 N MSE F 239 1555 1555 1.33
LINK C MSE F 239 N LYS F 240 1555 1555 1.33
LINK C PRO F 261 N MSE F 262 1555 1555 1.33
LINK C MSE F 262 N MSE F 263 1555 1555 1.34
LINK C MSE F 263 N VAL F 264 1555 1555 1.33
LINK C VAL F 290 N MSE F 291 1555 1555 1.33
LINK C MSE F 291 N THR F 292 1555 1555 1.34
LINK C THR F 292 N MSE F 293 1555 1555 1.34
LINK C MSE F 293 N PRO F 294 1555 1555 1.34
LINK C ARG F 389 N MSE F 390 1555 1555 1.34
LINK C MSE F 390 N VAL F 391 1555 1555 1.34
CISPEP 1 ALA A 327 PRO A 328 0 1.82
CISPEP 2 ALA B 327 PRO B 328 0 0.91
CISPEP 3 ALA C 327 PRO C 328 0 2.39
CISPEP 4 ALA D 327 PRO D 328 0 1.92
CISPEP 5 ALA E 327 PRO E 328 0 0.94
CISPEP 6 ALA F 327 PRO F 328 0 -0.05
CRYST1 125.612 125.612 162.639 90.00 90.00 120.00 P 32 18
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007961 0.004596 0.000000 0.00000
SCALE2 0.000000 0.009193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006149 0.00000
TER 3148 GLU A 415
TER 6311 GLU B 415
TER 9459 GLU C 415
TER 12608 GLU D 415
TER 15737 LEU E 413
TER 18877 LEU F 413
MASTER 722 0 60 120 54 0 0 619073 6 588 186
END |