HEADER HYDROLASE 19-JUL-09 2WNR
TITLE THE STRUCTURE OF METHANOTHERMOBACTER THERMAUTOTROPHICUS EXOSOME CORE
TITLE 2 ASSEMBLY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE EXOSOME COMPLEX EXONUCLEASE 2;
COMPND 3 CHAIN: A, C, E;
COMPND 4 EC: 3.1.13.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROBABLE EXOSOME COMPLEX EXONUCLEASE 1;
COMPND 8 CHAIN: B, D, F;
COMPND 9 EC: 3.1.13.-;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 STRAIN: DELTA H;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ER2566;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCDFDUET, PET28A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 11 ORGANISM_TAXID: 145262;
SOURCE 12 STRAIN: DELTA H;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: ER2566;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PCDFDUET, PET28A
KEYWDS PHOSPHATE BINDING, 3'-5' EXORIBONUCLEASE, EXOSOME, NUCLEASE,
KEYWDS 2 HYDROLASE, EXONUCLEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.L.NG,D.G.WATERMAN,A.A.ANTSON,M.ORTIZ-LOMBARDIA
REVDAT 5 13-DEC-23 2WNR 1 REMARK
REVDAT 4 30-MAY-12 2WNR 1 JRNL REMARK
REVDAT 3 13-JUL-11 2WNR 1 VERSN
REVDAT 2 19-MAY-10 2WNR 1 JRNL
REVDAT 1 28-APR-10 2WNR 0
JRNL AUTH C.L.NG,D.G.WATERMAN,A.A.ANTSON,M.ORTIZ-LOMBARDIA
JRNL TITL STRUCTURE OF THE METHANOTHERMOBACTER THERMAUTOTROPHICUS
JRNL TITL 2 EXOSOME RNASE PH RING
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 66 522 2010
JRNL REFN ISSN 0907-4449
JRNL PMID 20445227
JRNL DOI 10.1107/S0907444910002908
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 46606
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 973
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3011
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10910
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 125
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 64.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : 0.71000
REMARK 3 B33 (A**2) : -0.35000
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): 1.231
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.327
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.298
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.794
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11080 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14976 ; 1.257 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1414 ; 5.602 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 484 ;36.778 ;24.112
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2053 ;17.141 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 111 ;18.705 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1752 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8215 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7071 ; 1.033 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11455 ; 1.817 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4009 ; 3.110 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3519 ; 4.637 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 37 A 68 1
REMARK 3 1 C 37 C 68 1
REMARK 3 1 E 37 E 68 1
REMARK 3 2 A 80 A 125 1
REMARK 3 2 C 80 C 125 1
REMARK 3 2 E 80 E 125 1
REMARK 3 3 A 133 A 172 1
REMARK 3 3 C 133 C 172 1
REMARK 3 3 E 133 E 172 1
REMARK 3 4 A 194 A 250 1
REMARK 3 4 C 194 C 250 1
REMARK 3 4 E 194 E 250 1
REMARK 3 5 A 266 A 272 1
REMARK 3 5 C 266 C 272 1
REMARK 3 5 E 266 E 272 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1350 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1350 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 1350 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 1350 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1350 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 1350 ; 0.08 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 33 B 63 1
REMARK 3 1 D 33 D 63 1
REMARK 3 1 F 33 F 63 1
REMARK 3 2 B 78 B 94 1
REMARK 3 2 D 78 D 94 1
REMARK 3 2 F 78 F 94 1
REMARK 3 3 B 97 B 115 1
REMARK 3 3 D 97 D 115 1
REMARK 3 3 F 97 F 115 1
REMARK 3 4 B 125 B 169 1
REMARK 3 4 D 125 D 169 1
REMARK 3 4 F 125 F 169 1
REMARK 3 5 B 189 B 194 1
REMARK 3 5 D 189 D 194 1
REMARK 3 5 F 189 F 194 1
REMARK 3 6 B 199 B 213 1
REMARK 3 6 D 199 D 213 1
REMARK 3 6 F 199 F 213 1
REMARK 3 7 B 217 B 233 1
REMARK 3 7 D 217 D 233 1
REMARK 3 7 F 217 F 233 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1104 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 1104 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 F (A): 1104 ; 0.05 ; 0.05
REMARK 3 TIGHT THERMAL 2 B (A**2): 1104 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 1104 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 2 F (A**2): 1104 ; 0.08 ; 0.50
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 9 A 269
REMARK 3 ORIGIN FOR THE GROUP (A): -60.6030 2.5160 13.2580
REMARK 3 T TENSOR
REMARK 3 T11: 0.2692 T22: 0.2807
REMARK 3 T33: 0.3541 T12: 0.0219
REMARK 3 T13: -0.0377 T23: 0.0774
REMARK 3 L TENSOR
REMARK 3 L11: 2.6620 L22: 1.7316
REMARK 3 L33: 4.6621 L12: -0.2859
REMARK 3 L13: 0.0774 L23: 0.7616
REMARK 3 S TENSOR
REMARK 3 S11: -0.0541 S12: -0.2835 S13: -0.2302
REMARK 3 S21: 0.0201 S22: 0.0794 S23: 0.1863
REMARK 3 S31: 0.1025 S32: -1.0044 S33: -0.0253
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 15 B 236
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4030 2.0850 25.7880
REMARK 3 T TENSOR
REMARK 3 T11: 0.3041 T22: 0.0738
REMARK 3 T33: 0.2181 T12: 0.0581
REMARK 3 T13: -0.0713 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 4.6485 L22: 1.2158
REMARK 3 L33: 4.0461 L12: 0.4394
REMARK 3 L13: -0.3422 L23: -0.0845
REMARK 3 S TENSOR
REMARK 3 S11: 0.0243 S12: -0.3625 S13: -0.0571
REMARK 3 S21: 0.0005 S22: 0.1438 S23: 0.0621
REMARK 3 S31: 0.0440 S32: -0.1110 S33: -0.1682
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 13 C 270
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0340 8.1270 -31.0790
REMARK 3 T TENSOR
REMARK 3 T11: 0.3371 T22: 0.2832
REMARK 3 T33: 0.1984 T12: 0.1097
REMARK 3 T13: -0.0239 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 4.2664 L22: 2.0841
REMARK 3 L33: 3.7248 L12: -0.6567
REMARK 3 L13: -0.0314 L23: -0.6138
REMARK 3 S TENSOR
REMARK 3 S11: 0.2315 S12: 0.9056 S13: -0.0941
REMARK 3 S21: -0.2495 S22: -0.0822 S23: 0.0213
REMARK 3 S31: -0.1502 S32: -0.5710 S33: -0.1493
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 16 D 236
REMARK 3 ORIGIN FOR THE GROUP (A): -62.1980 16.2390 -16.1940
REMARK 3 T TENSOR
REMARK 3 T11: 0.3496 T22: 0.4841
REMARK 3 T33: 0.3103 T12: 0.2963
REMARK 3 T13: -0.0186 T23: 0.1252
REMARK 3 L TENSOR
REMARK 3 L11: 3.6895 L22: 1.4419
REMARK 3 L33: 5.8983 L12: -0.7896
REMARK 3 L13: -1.0904 L23: -0.1801
REMARK 3 S TENSOR
REMARK 3 S11: 0.2030 S12: 0.5677 S13: 0.1587
REMARK 3 S21: -0.0475 S22: 0.0314 S23: 0.1068
REMARK 3 S31: -0.4984 S32: -1.1426 S33: -0.2344
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 21 E 270
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8870 -7.3560 5.7860
REMARK 3 T TENSOR
REMARK 3 T11: 0.4021 T22: 0.1908
REMARK 3 T33: 0.3131 T12: 0.2004
REMARK 3 T13: -0.0922 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 3.6378 L22: 1.4833
REMARK 3 L33: 3.8108 L12: 0.2675
REMARK 3 L13: -1.1844 L23: 0.0410
REMARK 3 S TENSOR
REMARK 3 S11: -0.1362 S12: -0.2671 S13: -0.4101
REMARK 3 S21: 0.0726 S22: 0.1129 S23: -0.1412
REMARK 3 S31: 0.5574 S32: 0.7869 S33: 0.0233
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 14 F 237
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3750 6.2030 -17.7440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2791 T22: 0.1415
REMARK 3 T33: 0.2774 T12: -0.0325
REMARK 3 T13: -0.0033 T23: -0.0887
REMARK 3 L TENSOR
REMARK 3 L11: 3.7713 L22: 1.2458
REMARK 3 L33: 4.3715 L12: -1.1463
REMARK 3 L13: 0.2732 L23: -0.9083
REMARK 3 S TENSOR
REMARK 3 S11: 0.0523 S12: 0.0319 S13: 0.0892
REMARK 3 S21: -0.0528 S22: 0.0618 S23: -0.1148
REMARK 3 S31: -0.1000 S32: 0.6210 S33: -0.1141
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2WNR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1290040397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9191
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47654
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2BR2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1M SUCCINIC ACID PH
REMARK 280 7.0, 5% ISOPROPANOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 44.63050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.35400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.11650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.35400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.63050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.11650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 ASN A 3
REMARK 465 LYS A 4
REMARK 465 MET A 5
REMARK 465 ASP A 6
REMARK 465 ILE A 7
REMARK 465 ILE A 8
REMARK 465 THR A 270
REMARK 465 PRO A 271
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 THR B 3
REMARK 465 ILE B 4
REMARK 465 ILE B 5
REMARK 465 THR B 6
REMARK 465 GLN B 7
REMARK 465 ASP B 8
REMARK 465 GLN B 9
REMARK 465 LEU B 10
REMARK 465 LYS B 11
REMARK 465 THR B 12
REMARK 465 SER B 13
REMARK 465 PRO B 14
REMARK 465 ARG B 237
REMARK 465 TYR B 238
REMARK 465 GLY B 239
REMARK 465 GLU B 240
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 ASN C 3
REMARK 465 LYS C 4
REMARK 465 MET C 5
REMARK 465 ASP C 6
REMARK 465 ILE C 7
REMARK 465 ILE C 8
REMARK 465 PRO C 9
REMARK 465 GLU C 10
REMARK 465 ILE C 11
REMARK 465 THR C 12
REMARK 465 PRO C 271
REMARK 465 MET D 1
REMARK 465 ILE D 2
REMARK 465 THR D 3
REMARK 465 ILE D 4
REMARK 465 ILE D 5
REMARK 465 THR D 6
REMARK 465 GLN D 7
REMARK 465 ASP D 8
REMARK 465 GLN D 9
REMARK 465 LEU D 10
REMARK 465 LYS D 11
REMARK 465 THR D 12
REMARK 465 SER D 13
REMARK 465 PRO D 14
REMARK 465 SER D 15
REMARK 465 ALA D 62
REMARK 465 GLN D 63
REMARK 465 ILE D 64
REMARK 465 ARG D 65
REMARK 465 LYS D 66
REMARK 465 LEU D 67
REMARK 465 GLN D 68
REMARK 465 ARG D 69
REMARK 465 PRO D 70
REMARK 465 ASP D 71
REMARK 465 ARG D 72
REMARK 465 ARG D 237
REMARK 465 TYR D 238
REMARK 465 GLY D 239
REMARK 465 GLU D 240
REMARK 465 MET E 1
REMARK 465 VAL E 2
REMARK 465 ASN E 3
REMARK 465 LYS E 4
REMARK 465 MET E 5
REMARK 465 ASP E 6
REMARK 465 ILE E 7
REMARK 465 ILE E 8
REMARK 465 PRO E 9
REMARK 465 GLU E 10
REMARK 465 ILE E 11
REMARK 465 THR E 12
REMARK 465 ARG E 13
REMARK 465 LYS E 14
REMARK 465 SER E 15
REMARK 465 ILE E 16
REMARK 465 THR E 17
REMARK 465 ASP E 18
REMARK 465 LEU E 19
REMARK 465 ILE E 20
REMARK 465 PRO E 271
REMARK 465 MET F 1
REMARK 465 ILE F 2
REMARK 465 THR F 3
REMARK 465 ILE F 4
REMARK 465 ILE F 5
REMARK 465 THR F 6
REMARK 465 GLN F 7
REMARK 465 ASP F 8
REMARK 465 GLN F 9
REMARK 465 LEU F 10
REMARK 465 LYS F 11
REMARK 465 THR F 12
REMARK 465 SER F 13
REMARK 465 GLN F 63
REMARK 465 ILE F 64
REMARK 465 ARG F 65
REMARK 465 LYS F 66
REMARK 465 LEU F 67
REMARK 465 GLN F 68
REMARK 465 ARG F 69
REMARK 465 TYR F 238
REMARK 465 GLY F 239
REMARK 465 GLU F 240
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 ARG A 119 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 119 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 220 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG B 38 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 38 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 91 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 91 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 110 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG B 110 NE - CZ - NH1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG B 110 NE - CZ - NH2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG C 119 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG C 220 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 220 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG D 38 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG D 38 NE - CZ - NH1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG D 38 NE - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG D 110 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG E 119 NE - CZ - NH1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG E 119 NE - CZ - NH2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG E 220 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG E 220 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG F 38 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG F 91 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG F 91 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG F 91 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG F 110 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG F 110 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 92 143.37 -173.79
REMARK 500 SER A 132 -60.47 -164.01
REMARK 500 ASN A 149 76.42 64.54
REMARK 500 ASP A 174 -30.07 62.89
REMARK 500 PRO A 188 98.30 -65.38
REMARK 500 ASP A 208 78.84 59.58
REMARK 500 GLU B 116 -7.32 -52.77
REMARK 500 GLU B 133 46.34 -151.27
REMARK 500 VAL B 167 -61.98 -133.94
REMARK 500 ASP B 174 87.01 57.79
REMARK 500 LYS B 181 -72.18 -67.42
REMARK 500 ALA B 185 147.93 -170.23
REMARK 500 SER C 92 143.15 -176.03
REMARK 500 SER C 132 -47.56 -133.00
REMARK 500 ASN C 149 75.81 66.14
REMARK 500 ASP C 174 1.62 53.31
REMARK 500 ASP C 208 78.81 57.66
REMARK 500 GLU D 133 47.50 -151.37
REMARK 500 VAL D 167 -61.98 -132.99
REMARK 500 ASP D 174 68.40 62.30
REMARK 500 GLU D 182 21.70 -148.70
REMARK 500 ASN E 22 -43.23 -132.94
REMARK 500 THR E 75 75.39 -119.36
REMARK 500 SER E 92 143.60 -174.57
REMARK 500 ILE E 128 -56.21 -122.56
REMARK 500 SER E 132 -37.20 -138.27
REMARK 500 ASN E 149 77.97 64.17
REMARK 500 ASP E 174 92.33 -5.40
REMARK 500 LYS E 183 68.56 -114.25
REMARK 500 ASP E 208 79.27 58.16
REMARK 500 PHE F 118 82.93 -152.15
REMARK 500 GLU F 133 52.63 -152.75
REMARK 500 VAL F 167 -61.58 -132.80
REMARK 500 ASP F 174 80.54 53.35
REMARK 500 ALA F 185 136.27 -178.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 1238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1237
DBREF 2WNR A 1 271 UNP O26778 ECX2_METTH 1 271
DBREF 2WNR B 1 240 UNP O26779 ECX1_METTH 1 240
DBREF 2WNR C 1 271 UNP O26778 ECX2_METTH 1 271
DBREF 2WNR D 1 240 UNP O26779 ECX1_METTH 1 240
DBREF 2WNR E 1 271 UNP O26778 ECX2_METTH 1 271
DBREF 2WNR F 1 240 UNP O26779 ECX1_METTH 1 240
SEQRES 1 A 271 MET VAL ASN LYS MET ASP ILE ILE PRO GLU ILE THR ARG
SEQRES 2 A 271 LYS SER ILE THR ASP LEU ILE ASN ASN LYS GLU ARG ILE
SEQRES 3 A 271 ASP GLY ARG SER LEU HIS GLU PHE ARG ASP ILE SER ILE
SEQRES 4 A 271 GLU THR GLY VAL ILE SER LYS ALA GLU GLY SER SER ARG
SEQRES 5 A 271 VAL LYS LEU GLY ASN THR GLN ILE ILE VAL GLY VAL LYS
SEQRES 6 A 271 PRO GLN ILE GLY GLU PRO PHE PRO ASP THR PRO GLU MET
SEQRES 7 A 271 GLY VAL ILE LEU THR ASN SER GLU LEU LEU PRO MET ALA
SEQRES 8 A 271 SER PRO THR PHE GLU PRO GLY PRO PRO ASP GLU ARG SER
SEQRES 9 A 271 VAL GLU LEU SER ARG VAL VAL ASP ARG CYS ILE ARG GLU
SEQRES 10 A 271 SER ARG MET ILE ASP LEU GLU LYS LEU CYS ILE ILE GLU
SEQRES 11 A 271 GLY SER LYS VAL TRP MET LEU PHE LEU ASP LEU HIS ILE
SEQRES 12 A 271 ILE ASP TYR ASP GLY ASN LEU PHE ASP ALA ALA VAL LEU
SEQRES 13 A 271 ALA THR VAL ALA ALA LEU LEU ASP THR ARG ILE PRO ALA
SEQRES 14 A 271 ALA GLU VAL GLU ASP GLY GLU VAL VAL ILE ASN ARG GLU
SEQRES 15 A 271 LYS MET GLN PRO LEU PRO VAL ASN ARG LYS ALA LEU MET
SEQRES 16 A 271 CYS THR PHE ALA LYS ILE GLY ASN GLU ILE VAL LEU ASP
SEQRES 17 A 271 PRO SER LEU GLU GLU GLU ASP ILE LEU THR ALA ARG ILE
SEQRES 18 A 271 SER ILE GLY VAL THR GLU GLU GLY SER ILE CYS ALA MET
SEQRES 19 A 271 GLN LYS GLY GLY GLU GLY PRO LEU THR ARG ASP ASP VAL
SEQRES 20 A 271 LEU LYS ALA VAL SER ILE ALA VAL GLU LYS VAL PRO GLN
SEQRES 21 A 271 LEU ILE GLU TYR LEU ASP LYS SER MET THR PRO
SEQRES 1 B 240 MET ILE THR ILE ILE THR GLN ASP GLN LEU LYS THR SER
SEQRES 2 B 240 PRO SER VAL ARG GLU ASP GLY ARG ALA PHE ASP GLU LEU
SEQRES 3 B 240 ARG PRO LEU LYS ILE GLU ALA GLY ILE LEU GLU ARG ALA
SEQRES 4 B 240 ASP GLY SER SER TYR LEU GLU PHE GLY GLY ASN LYS ILE
SEQRES 5 B 240 LEU VAL ALA VAL TYR GLY PRO ARG GLU ALA GLN ILE ARG
SEQRES 6 B 240 LYS LEU GLN ARG PRO ASP ARG ALA VAL ILE ARG CYS ARG
SEQRES 7 B 240 TYR ASN MET ALA PRO PHE SER VAL GLU GLU ARG LYS ARG
SEQRES 8 B 240 PRO GLY PRO ASP ARG ARG SER VAL GLU ILE SER LYS ILE
SEQRES 9 B 240 THR ALA GLU ALA LEU ARG PRO ALA LEU ILE LEU GLU LYS
SEQRES 10 B 240 PHE PRO ARG SER VAL ILE ASP VAL PHE ILE GLU VAL LEU
SEQRES 11 B 240 GLU ALA GLU GLY GLY THR ARG CYS ALA GLY ILE THR ALA
SEQRES 12 B 240 ALA SER VAL ALA LEU ALA ASP ALA GLY ILE PRO MET ARG
SEQRES 13 B 240 ASP MET VAL VAL ALA CYS ALA ALA GLY LYS VAL GLY ASP
SEQRES 14 B 240 GLN VAL VAL LEU ASP LEU SER GLU GLU GLU ASP LYS GLU
SEQRES 15 B 240 GLY GLN ALA ASP VAL PRO VAL ALA ILE LEU PRO ARG THR
SEQRES 16 B 240 ARG GLU ILE THR LEU LEU GLN SER ASP GLY ASN LEU THR
SEQRES 17 B 240 PRO GLU GLU PHE GLU ARG ALA LEU ASP LEU ALA VAL GLU
SEQRES 18 B 240 GLY CYS LEU ARG ILE HIS GLU VAL GLN LYS GLU ALA LEU
SEQRES 19 B 240 ARG LYS ARG TYR GLY GLU
SEQRES 1 C 271 MET VAL ASN LYS MET ASP ILE ILE PRO GLU ILE THR ARG
SEQRES 2 C 271 LYS SER ILE THR ASP LEU ILE ASN ASN LYS GLU ARG ILE
SEQRES 3 C 271 ASP GLY ARG SER LEU HIS GLU PHE ARG ASP ILE SER ILE
SEQRES 4 C 271 GLU THR GLY VAL ILE SER LYS ALA GLU GLY SER SER ARG
SEQRES 5 C 271 VAL LYS LEU GLY ASN THR GLN ILE ILE VAL GLY VAL LYS
SEQRES 6 C 271 PRO GLN ILE GLY GLU PRO PHE PRO ASP THR PRO GLU MET
SEQRES 7 C 271 GLY VAL ILE LEU THR ASN SER GLU LEU LEU PRO MET ALA
SEQRES 8 C 271 SER PRO THR PHE GLU PRO GLY PRO PRO ASP GLU ARG SER
SEQRES 9 C 271 VAL GLU LEU SER ARG VAL VAL ASP ARG CYS ILE ARG GLU
SEQRES 10 C 271 SER ARG MET ILE ASP LEU GLU LYS LEU CYS ILE ILE GLU
SEQRES 11 C 271 GLY SER LYS VAL TRP MET LEU PHE LEU ASP LEU HIS ILE
SEQRES 12 C 271 ILE ASP TYR ASP GLY ASN LEU PHE ASP ALA ALA VAL LEU
SEQRES 13 C 271 ALA THR VAL ALA ALA LEU LEU ASP THR ARG ILE PRO ALA
SEQRES 14 C 271 ALA GLU VAL GLU ASP GLY GLU VAL VAL ILE ASN ARG GLU
SEQRES 15 C 271 LYS MET GLN PRO LEU PRO VAL ASN ARG LYS ALA LEU MET
SEQRES 16 C 271 CYS THR PHE ALA LYS ILE GLY ASN GLU ILE VAL LEU ASP
SEQRES 17 C 271 PRO SER LEU GLU GLU GLU ASP ILE LEU THR ALA ARG ILE
SEQRES 18 C 271 SER ILE GLY VAL THR GLU GLU GLY SER ILE CYS ALA MET
SEQRES 19 C 271 GLN LYS GLY GLY GLU GLY PRO LEU THR ARG ASP ASP VAL
SEQRES 20 C 271 LEU LYS ALA VAL SER ILE ALA VAL GLU LYS VAL PRO GLN
SEQRES 21 C 271 LEU ILE GLU TYR LEU ASP LYS SER MET THR PRO
SEQRES 1 D 240 MET ILE THR ILE ILE THR GLN ASP GLN LEU LYS THR SER
SEQRES 2 D 240 PRO SER VAL ARG GLU ASP GLY ARG ALA PHE ASP GLU LEU
SEQRES 3 D 240 ARG PRO LEU LYS ILE GLU ALA GLY ILE LEU GLU ARG ALA
SEQRES 4 D 240 ASP GLY SER SER TYR LEU GLU PHE GLY GLY ASN LYS ILE
SEQRES 5 D 240 LEU VAL ALA VAL TYR GLY PRO ARG GLU ALA GLN ILE ARG
SEQRES 6 D 240 LYS LEU GLN ARG PRO ASP ARG ALA VAL ILE ARG CYS ARG
SEQRES 7 D 240 TYR ASN MET ALA PRO PHE SER VAL GLU GLU ARG LYS ARG
SEQRES 8 D 240 PRO GLY PRO ASP ARG ARG SER VAL GLU ILE SER LYS ILE
SEQRES 9 D 240 THR ALA GLU ALA LEU ARG PRO ALA LEU ILE LEU GLU LYS
SEQRES 10 D 240 PHE PRO ARG SER VAL ILE ASP VAL PHE ILE GLU VAL LEU
SEQRES 11 D 240 GLU ALA GLU GLY GLY THR ARG CYS ALA GLY ILE THR ALA
SEQRES 12 D 240 ALA SER VAL ALA LEU ALA ASP ALA GLY ILE PRO MET ARG
SEQRES 13 D 240 ASP MET VAL VAL ALA CYS ALA ALA GLY LYS VAL GLY ASP
SEQRES 14 D 240 GLN VAL VAL LEU ASP LEU SER GLU GLU GLU ASP LYS GLU
SEQRES 15 D 240 GLY GLN ALA ASP VAL PRO VAL ALA ILE LEU PRO ARG THR
SEQRES 16 D 240 ARG GLU ILE THR LEU LEU GLN SER ASP GLY ASN LEU THR
SEQRES 17 D 240 PRO GLU GLU PHE GLU ARG ALA LEU ASP LEU ALA VAL GLU
SEQRES 18 D 240 GLY CYS LEU ARG ILE HIS GLU VAL GLN LYS GLU ALA LEU
SEQRES 19 D 240 ARG LYS ARG TYR GLY GLU
SEQRES 1 E 271 MET VAL ASN LYS MET ASP ILE ILE PRO GLU ILE THR ARG
SEQRES 2 E 271 LYS SER ILE THR ASP LEU ILE ASN ASN LYS GLU ARG ILE
SEQRES 3 E 271 ASP GLY ARG SER LEU HIS GLU PHE ARG ASP ILE SER ILE
SEQRES 4 E 271 GLU THR GLY VAL ILE SER LYS ALA GLU GLY SER SER ARG
SEQRES 5 E 271 VAL LYS LEU GLY ASN THR GLN ILE ILE VAL GLY VAL LYS
SEQRES 6 E 271 PRO GLN ILE GLY GLU PRO PHE PRO ASP THR PRO GLU MET
SEQRES 7 E 271 GLY VAL ILE LEU THR ASN SER GLU LEU LEU PRO MET ALA
SEQRES 8 E 271 SER PRO THR PHE GLU PRO GLY PRO PRO ASP GLU ARG SER
SEQRES 9 E 271 VAL GLU LEU SER ARG VAL VAL ASP ARG CYS ILE ARG GLU
SEQRES 10 E 271 SER ARG MET ILE ASP LEU GLU LYS LEU CYS ILE ILE GLU
SEQRES 11 E 271 GLY SER LYS VAL TRP MET LEU PHE LEU ASP LEU HIS ILE
SEQRES 12 E 271 ILE ASP TYR ASP GLY ASN LEU PHE ASP ALA ALA VAL LEU
SEQRES 13 E 271 ALA THR VAL ALA ALA LEU LEU ASP THR ARG ILE PRO ALA
SEQRES 14 E 271 ALA GLU VAL GLU ASP GLY GLU VAL VAL ILE ASN ARG GLU
SEQRES 15 E 271 LYS MET GLN PRO LEU PRO VAL ASN ARG LYS ALA LEU MET
SEQRES 16 E 271 CYS THR PHE ALA LYS ILE GLY ASN GLU ILE VAL LEU ASP
SEQRES 17 E 271 PRO SER LEU GLU GLU GLU ASP ILE LEU THR ALA ARG ILE
SEQRES 18 E 271 SER ILE GLY VAL THR GLU GLU GLY SER ILE CYS ALA MET
SEQRES 19 E 271 GLN LYS GLY GLY GLU GLY PRO LEU THR ARG ASP ASP VAL
SEQRES 20 E 271 LEU LYS ALA VAL SER ILE ALA VAL GLU LYS VAL PRO GLN
SEQRES 21 E 271 LEU ILE GLU TYR LEU ASP LYS SER MET THR PRO
SEQRES 1 F 240 MET ILE THR ILE ILE THR GLN ASP GLN LEU LYS THR SER
SEQRES 2 F 240 PRO SER VAL ARG GLU ASP GLY ARG ALA PHE ASP GLU LEU
SEQRES 3 F 240 ARG PRO LEU LYS ILE GLU ALA GLY ILE LEU GLU ARG ALA
SEQRES 4 F 240 ASP GLY SER SER TYR LEU GLU PHE GLY GLY ASN LYS ILE
SEQRES 5 F 240 LEU VAL ALA VAL TYR GLY PRO ARG GLU ALA GLN ILE ARG
SEQRES 6 F 240 LYS LEU GLN ARG PRO ASP ARG ALA VAL ILE ARG CYS ARG
SEQRES 7 F 240 TYR ASN MET ALA PRO PHE SER VAL GLU GLU ARG LYS ARG
SEQRES 8 F 240 PRO GLY PRO ASP ARG ARG SER VAL GLU ILE SER LYS ILE
SEQRES 9 F 240 THR ALA GLU ALA LEU ARG PRO ALA LEU ILE LEU GLU LYS
SEQRES 10 F 240 PHE PRO ARG SER VAL ILE ASP VAL PHE ILE GLU VAL LEU
SEQRES 11 F 240 GLU ALA GLU GLY GLY THR ARG CYS ALA GLY ILE THR ALA
SEQRES 12 F 240 ALA SER VAL ALA LEU ALA ASP ALA GLY ILE PRO MET ARG
SEQRES 13 F 240 ASP MET VAL VAL ALA CYS ALA ALA GLY LYS VAL GLY ASP
SEQRES 14 F 240 GLN VAL VAL LEU ASP LEU SER GLU GLU GLU ASP LYS GLU
SEQRES 15 F 240 GLY GLN ALA ASP VAL PRO VAL ALA ILE LEU PRO ARG THR
SEQRES 16 F 240 ARG GLU ILE THR LEU LEU GLN SER ASP GLY ASN LEU THR
SEQRES 17 F 240 PRO GLU GLU PHE GLU ARG ALA LEU ASP LEU ALA VAL GLU
SEQRES 18 F 240 GLY CYS LEU ARG ILE HIS GLU VAL GLN LYS GLU ALA LEU
SEQRES 19 F 240 ARG LYS ARG TYR GLY GLU
HET PO4 B1237 5
HET PO4 D1237 5
HET PO4 F1238 5
HETNAM PO4 PHOSPHATE ION
FORMUL 7 PO4 3(O4 P 3-)
FORMUL 10 HOH *125(H2 O)
HELIX 1 1 GLU A 10 ASN A 22 1 13
HELIX 2 2 PRO A 89 SER A 92 5 4
HELIX 3 3 ASP A 101 SER A 118 1 18
HELIX 4 4 ASP A 122 LYS A 125 5 4
HELIX 5 5 ASN A 149 THR A 165 1 17
HELIX 6 6 SER A 210 ASP A 215 1 6
HELIX 7 7 THR A 243 MET A 269 1 27
HELIX 8 8 ASP B 95 ARG B 110 1 16
HELIX 9 9 ILE B 114 PHE B 118 5 5
HELIX 10 10 ILE B 141 ALA B 151 1 11
HELIX 11 11 GLU B 177 GLU B 182 1 6
HELIX 12 12 THR B 208 GLU B 221 1 14
HELIX 13 13 CYS B 223 LYS B 236 1 14
HELIX 14 14 ARG C 13 ASP C 18 1 6
HELIX 15 15 PRO C 89 SER C 92 5 4
HELIX 16 16 ASP C 101 SER C 118 1 18
HELIX 17 17 ASP C 122 LYS C 125 5 4
HELIX 18 18 ASN C 149 THR C 165 1 17
HELIX 19 19 SER C 210 ASP C 215 1 6
HELIX 20 20 THR C 243 MET C 269 1 27
HELIX 21 21 ASP D 95 ARG D 110 1 16
HELIX 22 22 ILE D 114 PHE D 118 5 5
HELIX 23 23 ILE D 141 ALA D 151 1 11
HELIX 24 24 THR D 208 GLU D 221 1 14
HELIX 25 25 CYS D 223 LYS D 236 1 14
HELIX 26 26 PRO E 89 SER E 92 5 4
HELIX 27 27 ASP E 101 SER E 118 1 18
HELIX 28 28 ASP E 122 LYS E 125 5 4
HELIX 29 29 ASN E 149 THR E 165 1 17
HELIX 30 30 SER E 210 ASP E 215 1 6
HELIX 31 31 THR E 243 MET E 269 1 27
HELIX 32 32 ASP F 95 ARG F 110 1 16
HELIX 33 33 ILE F 114 PHE F 118 5 5
HELIX 34 34 ILE F 141 ALA F 151 1 11
HELIX 35 35 SER F 176 LYS F 181 1 6
HELIX 36 36 THR F 208 GLU F 221 1 14
HELIX 37 37 CYS F 223 LYS F 236 1 14
SHEET 1 AA 5 SER A 38 GLU A 40 0
SHEET 2 AA 5 SER A 51 LYS A 54 -1 O ARG A 52 N GLU A 40
SHEET 3 AA 5 GLN A 59 VAL A 62 -1 O ILE A 60 N VAL A 53
SHEET 4 AA 5 MET A 136 ASP A 145 -1 O HIS A 142 N ILE A 61
SHEET 5 AA 5 LYS A 65 GLN A 67 -1 O LYS A 65 N PHE A 138
SHEET 1 AB 4 SER A 38 GLU A 40 0
SHEET 2 AB 4 SER A 51 LYS A 54 -1 O ARG A 52 N GLU A 40
SHEET 3 AB 4 GLN A 59 VAL A 62 -1 O ILE A 60 N VAL A 53
SHEET 4 AB 4 MET A 136 ASP A 145 -1 O HIS A 142 N ILE A 61
SHEET 1 AC 2 CYS A 127 ILE A 129 0
SHEET 2 AC 2 LYS A 133 VAL A 134 -1 O LYS A 133 N ILE A 129
SHEET 1 AD 2 ARG A 166 VAL A 172 0
SHEET 2 AD 2 VAL A 177 PRO A 186 -1 O VAL A 178 N GLU A 171
SHEET 1 AE 3 ILE A 205 LEU A 207 0
SHEET 2 AE 3 ALA A 193 LYS A 200 -1 O ALA A 199 N VAL A 206
SHEET 3 AE 3 ALA A 219 THR A 226 -1 O ALA A 219 N LYS A 200
SHEET 1 AF 4 MET A 234 GLN A 235 0
SHEET 2 AF 4 GLU B 197 SER B 203 -1 O SER B 203 N MET A 234
SHEET 3 AF 4 VAL B 187 LEU B 192 -1 O PRO B 188 N GLN B 202
SHEET 4 AF 4 VAL B 160 ALA B 164 -1 O VAL B 160 N ILE B 191
SHEET 1 BA 5 LYS B 30 GLU B 32 0
SHEET 2 BA 5 SER B 43 GLU B 46 -1 O TYR B 44 N GLU B 32
SHEET 3 BA 5 LYS B 51 GLU B 61 -1 O ILE B 52 N LEU B 45
SHEET 4 BA 5 SER B 121 GLU B 131 -1 O VAL B 122 N ARG B 60
SHEET 5 BA 5 VAL B 74 MET B 81 1 O VAL B 74 N ILE B 123
SHEET 1 CA 5 SER C 38 GLU C 40 0
SHEET 2 CA 5 SER C 51 LYS C 54 -1 O ARG C 52 N GLU C 40
SHEET 3 CA 5 GLN C 59 VAL C 62 -1 O ILE C 60 N VAL C 53
SHEET 4 CA 5 MET C 136 ASP C 145 -1 O HIS C 142 N ILE C 61
SHEET 5 CA 5 LYS C 65 GLN C 67 -1 O LYS C 65 N PHE C 138
SHEET 1 CB 4 SER C 38 GLU C 40 0
SHEET 2 CB 4 SER C 51 LYS C 54 -1 O ARG C 52 N GLU C 40
SHEET 3 CB 4 GLN C 59 VAL C 62 -1 O ILE C 60 N VAL C 53
SHEET 4 CB 4 MET C 136 ASP C 145 -1 O HIS C 142 N ILE C 61
SHEET 1 CC 2 CYS C 127 ILE C 129 0
SHEET 2 CC 2 LYS C 133 VAL C 134 -1 O LYS C 133 N ILE C 129
SHEET 1 CD 2 ARG C 166 VAL C 172 0
SHEET 2 CD 2 VAL C 177 PRO C 186 -1 O VAL C 178 N GLU C 171
SHEET 1 CE 3 ILE C 205 LEU C 207 0
SHEET 2 CE 3 ALA C 193 LYS C 200 -1 O ALA C 199 N VAL C 206
SHEET 3 CE 3 ALA C 219 THR C 226 -1 O ALA C 219 N LYS C 200
SHEET 1 CF 4 MET C 234 GLN C 235 0
SHEET 2 CF 4 GLU D 197 SER D 203 -1 O SER D 203 N MET C 234
SHEET 3 CF 4 VAL D 187 LEU D 192 -1 O PRO D 188 N GLN D 202
SHEET 4 CF 4 VAL D 160 ALA D 164 -1 O VAL D 160 N ILE D 191
SHEET 1 DA 5 LYS D 30 GLU D 32 0
SHEET 2 DA 5 SER D 43 GLU D 46 -1 O TYR D 44 N GLU D 32
SHEET 3 DA 5 LYS D 51 ARG D 60 -1 O ILE D 52 N LEU D 45
SHEET 4 DA 5 VAL D 122 GLU D 131 -1 O VAL D 122 N ARG D 60
SHEET 5 DA 5 VAL D 74 MET D 81 1 O VAL D 74 N ILE D 123
SHEET 1 EA 5 SER E 38 GLU E 40 0
SHEET 2 EA 5 SER E 51 LYS E 54 -1 O ARG E 52 N GLU E 40
SHEET 3 EA 5 GLN E 59 VAL E 62 -1 O ILE E 60 N VAL E 53
SHEET 4 EA 5 MET E 136 ASP E 145 -1 O HIS E 142 N ILE E 61
SHEET 5 EA 5 LYS E 65 GLN E 67 -1 O LYS E 65 N PHE E 138
SHEET 1 EB 4 SER E 38 GLU E 40 0
SHEET 2 EB 4 SER E 51 LYS E 54 -1 O ARG E 52 N GLU E 40
SHEET 3 EB 4 GLN E 59 VAL E 62 -1 O ILE E 60 N VAL E 53
SHEET 4 EB 4 MET E 136 ASP E 145 -1 O HIS E 142 N ILE E 61
SHEET 1 EC 2 CYS E 127 ILE E 129 0
SHEET 2 EC 2 LYS E 133 VAL E 134 -1 O LYS E 133 N ILE E 129
SHEET 1 ED 2 ARG E 166 VAL E 172 0
SHEET 2 ED 2 VAL E 177 PRO E 186 -1 O VAL E 178 N GLU E 171
SHEET 1 EE 3 ILE E 205 LEU E 207 0
SHEET 2 EE 3 ALA E 193 LYS E 200 -1 O ALA E 199 N VAL E 206
SHEET 3 EE 3 ALA E 219 THR E 226 -1 O ALA E 219 N LYS E 200
SHEET 1 EF 4 MET E 234 GLN E 235 0
SHEET 2 EF 4 GLU F 197 SER F 203 -1 O SER F 203 N MET E 234
SHEET 3 EF 4 VAL F 187 LEU F 192 -1 O PRO F 188 N GLN F 202
SHEET 4 EF 4 VAL F 160 ALA F 164 -1 O VAL F 160 N ILE F 191
SHEET 1 FA 5 LYS F 30 GLU F 32 0
SHEET 2 FA 5 SER F 43 GLU F 46 -1 O TYR F 44 N GLU F 32
SHEET 3 FA 5 LYS F 51 ARG F 60 -1 O ILE F 52 N LEU F 45
SHEET 4 FA 5 VAL F 122 GLU F 131 -1 O VAL F 122 N ARG F 60
SHEET 5 FA 5 ILE F 75 MET F 81 1 O ARG F 76 N VAL F 125
CISPEP 1 GLY B 58 PRO B 59 0 5.15
CISPEP 2 GLY D 58 PRO D 59 0 4.43
CISPEP 3 GLY F 58 PRO F 59 0 4.31
SITE 1 AC1 4 ARG B 97 GLY B 135 THR B 136 ARG B 137
SITE 1 AC2 8 ARG F 97 GLY F 134 GLY F 135 THR F 136
SITE 2 AC2 8 ARG F 137 HOH F2025 HOH F2026 HOH F2027
SITE 1 AC3 4 ARG D 97 GLY D 135 THR D 136 ARG D 137
CRYST1 89.261 118.233 154.708 90.00 90.00 90.00 P 21 21 21 12
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 0.011203 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008458 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006464 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
