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HEADER UNKNOWN FUNCTION 09-APR-15 4Z8Z
TITLE CRYSTAL STRUCTURE OF THE HYPOTHETICAL PROTEIN FROM RUMINICLOSTRIDIUM
TITLE 2 THERMOCELLUM ATCC 27405
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM (STRAIN ATCC 27405 /
SOURCE 3 DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372);
SOURCE 4 ORGANISM_TAXID: 203119;
SOURCE 5 STRAIN: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-
SOURCE 6 4536 / VPI 7372;
SOURCE 7 GENE: CTHE_0134;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS STRUCTURAL GENOMICS, HUMAN MICROBIOME, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, PSI-BIOLOGY
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,Z.WAWRZAK,O.KIRYUKHINA,M.ENDRES,J.JOACHIMIAK,
AUTHOR 2 W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 06-MAY-15 4Z8Z 0
JRNL AUTH E.V.FILIPPOVA,Z.WAWRZAK,O.KIRYUKHINA,M.ENDRES,J.JOACHIMIAK,
JRNL AUTH 2 W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL CRYSTAL STRUCTURE OF THE HYPOTHETICAL PROTEIN FROM
JRNL TITL 2 RUMINICLOSTRIDIUM THERMOCELLUM ATCC 27405
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 13496
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 694
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 970
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2619
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.02000
REMARK 3 B22 (A**2) : -2.02000
REMARK 3 B33 (A**2) : 6.56000
REMARK 3 B12 (A**2) : -1.01000
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): 0.433
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.210
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.269
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2675 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2590 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3607 ; 1.733 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5959 ; 1.016 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 318 ; 7.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;36.910 ;24.545
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 463 ;17.505 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;16.900 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 399 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2984 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 627 ; 0.002 ; 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): 1278 ; 2.065 ; 4.389
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1277 ; 2.064 ; 4.387
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1594 ; 3.250 ; 6.576
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1595 ; 3.249 ; 6.578
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1397 ; 2.493 ; 4.654
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1398 ; 2.493 ; 4.656
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2014 ; 3.922 ; 6.866
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2903 ; 5.327 ;34.323
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2903 ; 5.323 ;34.331
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 : NULL
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 1 A 17
REMARK 3 ORIGIN FOR THE GROUP (A): 106.6335 133.5031 123.8781
REMARK 3 T TENSOR
REMARK 3 T11: 0.2857 T22: 0.2760
REMARK 3 T33: 0.0654 T12: -0.0854
REMARK 3 T13: -0.0496 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 2.1125 L22: 8.9912
REMARK 3 L33: 0.3007 L12: -1.6498
REMARK 3 L13: -0.6855 L23: 1.0819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0900 S12: -0.0797 S13: -0.1656
REMARK 3 S21: -0.1945 S22: 0.0047 S23: 0.1604
REMARK 3 S31: -0.0596 S32: 0.1119 S33: 0.0854
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 : A 18 A 48
REMARK 3 ORIGIN FOR THE GROUP (A): 96.9550 108.2275 130.7690
REMARK 3 T TENSOR
REMARK 3 T11: 0.2016 T22: 0.0384
REMARK 3 T33: 0.1429 T12: 0.0405
REMARK 3 T13: -0.0182 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 3.0093 L22: 1.4283
REMARK 3 L33: 3.4290 L12: 0.6996
REMARK 3 L13: -0.0328 L23: 0.5067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0673 S12: -0.0780 S13: -0.6175
REMARK 3 S21: -0.3279 S22: 0.0010 S23: -0.0432
REMARK 3 S31: 0.3965 S32: 0.1326 S33: 0.0662
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 : A 49 A 71
REMARK 3 ORIGIN FOR THE GROUP (A): 103.2341 113.9036 152.6684
REMARK 3 T TENSOR
REMARK 3 T11: 0.0450 T22: 0.5775
REMARK 3 T33: 0.1369 T12: 0.0686
REMARK 3 T13: -0.0292 T23: 0.1703
REMARK 3 L TENSOR
REMARK 3 L11: 2.9796 L22: 5.8184
REMARK 3 L33: 2.1965 L12: 0.4520
REMARK 3 L13: 1.6910 L23: -2.3464
REMARK 3 S TENSOR
REMARK 3 S11: 0.1681 S12: -0.4977 S13: -0.4224
REMARK 3 S21: 0.2366 S22: -0.2370 S23: -0.6663
REMARK 3 S31: 0.0293 S32: -0.0369 S33: 0.0689
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 : A 72 A 105
REMARK 3 ORIGIN FOR THE GROUP (A): 101.5222 118.5096 144.7921
REMARK 3 T TENSOR
REMARK 3 T11: 0.0996 T22: 0.4643
REMARK 3 T33: 0.0665 T12: 0.0544
REMARK 3 T13: -0.0545 T23: 0.0933
REMARK 3 L TENSOR
REMARK 3 L11: 1.6428 L22: 3.2722
REMARK 3 L33: 2.6056 L12: -0.1822
REMARK 3 L13: -1.4184 L23: 1.8020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: -0.7237 S13: -0.1653
REMARK 3 S21: 0.0848 S22: 0.0173 S23: -0.0989
REMARK 3 S31: 0.0919 S32: 0.5286 S33: 0.0354
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 : A 106 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): 104.5293 132.5613 143.5191
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.3304
REMARK 3 T33: 0.0994 T12: -0.0396
REMARK 3 T13: -0.0177 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 7.7172 L22: 1.7904
REMARK 3 L33: 4.6375 L12: -3.4555
REMARK 3 L13: -5.0555 L23: 2.8168
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: -0.6229 S13: 0.2507
REMARK 3 S21: -0.0831 S22: 0.1712 S23: -0.1087
REMARK 3 S31: -0.1838 S32: 0.2672 S33: -0.1509
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 : A 120 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): 93.0358 122.0074 133.6760
REMARK 3 T TENSOR
REMARK 3 T11: 0.1311 T22: 0.1906
REMARK 3 T33: 0.0421 T12: 0.0302
REMARK 3 T13: -0.0571 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 2.1020 L22: 1.3020
REMARK 3 L33: 1.7510 L12: 0.3985
REMARK 3 L13: -0.4209 L23: 0.0514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0599 S12: -0.3299 S13: -0.0839
REMARK 3 S21: -0.2294 S22: -0.0196 S23: 0.1683
REMARK 3 S31: -0.0248 S32: 0.1308 S33: 0.0795
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4Z8Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208818.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-MAX
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14192
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 51.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M TRIMETHYLAMINE N-OXIDE, 0.1 M
REMARK 280 TRIS, 20% PEG2000, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 70.67650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.80510
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.55867
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 70.67650
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 40.80510
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.55867
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 70.67650
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 40.80510
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.55867
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 70.67650
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 40.80510
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.55867
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 70.67650
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 40.80510
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.55867
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 70.67650
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 40.80510
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.55867
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 81.61019
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 75.11733
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 81.61019
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 75.11733
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 81.61019
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 75.11733
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 81.61019
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 75.11733
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 81.61019
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 75.11733
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 81.61019
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 75.11733
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 58
REMARK 465 ASP A 59
REMARK 465 LYS A 60
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 CYS A 322 SG
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 195 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 200 NE - CZ - NH1 ANGL. DEV. = 3.9 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 LYS A 21 -70.88 -138.53
REMARK 500 LYS A 30 -66.67 -129.03
REMARK 500 LEU A 62 141.52 -173.39
REMARK 500 TYR A 103 18.08 52.30
REMARK 500 LYS A 121 32.15 82.86
REMARK 500 PHE A 133 -132.43 53.25
REMARK 500 SER A 187 -123.58 57.44
REMARK 500 ASP A 201 59.42 -108.12
REMARK 500 ASP A 214 109.01 -162.08
REMARK 500 ASN A 263 36.78 -99.79
REMARK 500 HIS A 299 71.79 -101.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 42 LEU A 43 -148.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC113005 RELATED DB: TARGETTRACK
DBREF 4Z8Z A 1 323 UNP A3DBP6 A3DBP6_CLOTH 1 323
SEQRES 1 A 323 MSE ASN GLU ALA SER SER LYS PHE VAL ASP ASN ILE ALA
SEQRES 2 A 323 ILE GLU LYS LEU LEU ASN GLU LYS LEU LEU ARG VAL SER
SEQRES 3 A 323 HIS ARG PRO LYS ASN LEU PHE TYR ASP ASP GLU LYS VAL
SEQRES 4 A 323 PHE ASP ASP LEU CYS LYS CYS GLU THR ASP MSE SER LYS
SEQRES 5 A 323 VAL LYS LEU ALA GLU GLY ASP LYS ASN LEU LYS ARG PHE
SEQRES 6 A 323 GLU PHE PRO SER PHE LEU LYS THR GLU GLU TYR ILE GLU
SEQRES 7 A 323 ASN ASN ILE VAL TYR LEU TYR TYR HIS PRO ALA LYS ASP
SEQRES 8 A 323 PRO VAL CYS ASN ILE LEU LEU LEU HIS GLY LEU TYR ASP
SEQRES 9 A 323 ASP ASN MSE LEU ASN TYR GLY PHE LEU THR ARG MSE LEU
SEQRES 10 A 323 ASN GLU LEU LYS PHE ASN VAL PHE LEU MSE GLU LEU PRO
SEQRES 11 A 323 PHE HIS PHE ASN ARG LYS PRO ALA GLU SER PHE PHE SER
SEQRES 12 A 323 GLY GLU TYR PHE ILE SER ALA ASP LEU LEU ARG ALA ARG
SEQRES 13 A 323 ASN ALA PHE ILE GLN SER ILE TYR ASP ILE GLU ALA SER
SEQRES 14 A 323 ARG ASN LEU ILE GLY ASN ILE ASN THR LEU PRO CYS LEU
SEQRES 15 A 323 LEU VAL GLY PHE SER MSE GLY GLY CYS ILE SER PHE ARG
SEQRES 16 A 323 TYR HIS MSE LEU ARG ASP SER PHE LYS GLY THR PHE LEU
SEQRES 17 A 323 ILE ASN PRO VAL THR ASP MSE LEU LEU LEU VAL TRP ASP
SEQRES 18 A 323 ASN PRO LEU LEU VAL LYS VAL LYS LYS ASP LEU GLU ASP
SEQRES 19 A 323 SER GLY VAL GLY LYS GLU GLN VAL MSE ASP VAL PHE ARG
SEQRES 20 A 323 ILE ILE ASP PRO CYS GLU ASN ILE ASN THR ARG PHE ASN
SEQRES 21 A 323 THR ASP ASN ILE ALA VAL VAL TYR SER ILE TYR ASP GLN
SEQRES 22 A 323 ILE VAL GLY GLU GLU LYS ASN ALA ILE PHE VAL GLU LYS
SEQRES 23 A 323 ILE LYS LYS ALA GLY LEU LYS LYS ILE LEU GLU TYR HIS
SEQRES 24 A 323 ALA GLY HIS LEU ASN ILE LEU ARG VAL PRO LYS LEU SER
SEQRES 25 A 323 ASN ASP ILE TYR GLU PHE PHE MSE SER CYS LEU
MODRES 4Z8Z MSE A 1 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 50 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 107 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 116 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 127 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 188 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 198 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 215 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 243 MET MODIFIED RESIDUE
MODRES 4Z8Z MSE A 320 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 50 8
HET MSE A 107 8
HET MSE A 116 8
HET MSE A 127 8
HET MSE A 188 8
HET MSE A 198 8
HET MSE A 215 8
HET MSE A 243 8
HET MSE A 320 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 2 HOH *27(H2 O)
HELIX 1 AA1 ASN A 2 LYS A 21 1 20
HELIX 2 AA2 LEU A 22 VAL A 25 5 4
HELIX 3 AA3 ASP A 49 VAL A 53 5 5
HELIX 4 AA4 TYR A 76 ASN A 79 5 4
HELIX 5 AA5 ASN A 106 ASN A 109 5 4
HELIX 6 AA6 TYR A 110 LEU A 120 1 11
HELIX 7 AA7 HIS A 132 LYS A 136 5 5
HELIX 8 AA8 ASP A 151 ASN A 177 1 27
HELIX 9 AA9 SER A 187 ARG A 200 1 14
HELIX 10 AB1 LEU A 217 ASN A 222 1 6
HELIX 11 AB2 LEU A 225 SER A 235 1 11
HELIX 12 AB3 GLY A 238 ARG A 247 1 10
HELIX 13 AB4 ILE A 248 ASP A 250 5 3
HELIX 14 AB5 PRO A 251 ILE A 255 5 5
HELIX 15 AB6 GLY A 276 ALA A 290 1 15
HELIX 16 AB7 LEU A 303 VAL A 308 5 6
HELIX 17 AB8 PRO A 309 SER A 321 1 13
SHEET 1 AA1 9 LYS A 54 ALA A 56 0
SHEET 2 AA1 9 LYS A 63 PRO A 68 -1 O ARG A 64 N ALA A 56
SHEET 3 AA1 9 ILE A 81 HIS A 87 -1 O VAL A 82 N PHE A 67
SHEET 4 AA1 9 PHE A 122 MSE A 127 -1 O VAL A 124 N HIS A 87
SHEET 5 AA1 9 CYS A 94 LEU A 99 1 N ILE A 96 O ASN A 123
SHEET 6 AA1 9 CYS A 181 PHE A 186 1 O VAL A 184 N LEU A 97
SHEET 7 AA1 9 GLY A 205 ILE A 209 1 O ILE A 209 N GLY A 185
SHEET 8 AA1 9 ILE A 264 SER A 269 1 O VAL A 267 N LEU A 208
SHEET 9 AA1 9 LYS A 294 TYR A 298 1 O LEU A 296 N VAL A 266
LINK C MSE A 1 N ASN A 2 1555 1555 1.32
LINK C ASP A 49 N MSE A 50 1555 1555 1.34
LINK C MSE A 50 N SER A 51 1555 1555 1.33
LINK C ASN A 106 N MSE A 107 1555 1555 1.33
LINK C MSE A 107 N LEU A 108 1555 1555 1.32
LINK C ARG A 115 N MSE A 116 1555 1555 1.32
LINK C MSE A 116 N LEU A 117 1555 1555 1.33
LINK C LEU A 126 N MSE A 127 1555 1555 1.34
LINK C MSE A 127 N GLU A 128 1555 1555 1.34
LINK C SER A 187 N MSE A 188 1555 1555 1.31
LINK C MSE A 188 N GLY A 189 1555 1555 1.33
LINK C HIS A 197 N MSE A 198 1555 1555 1.33
LINK C MSE A 198 N LEU A 199 1555 1555 1.32
LINK C ASP A 214 N MSE A 215 1555 1555 1.33
LINK C MSE A 215 N LEU A 216 1555 1555 1.33
LINK C VAL A 242 N MSE A 243 1555 1555 1.32
LINK C MSE A 243 N ASP A 244 1555 1555 1.32
LINK C PHE A 319 N MSE A 320 1555 1555 1.33
LINK C MSE A 320 N SER A 321 1555 1555 1.34
CRYST1 141.353 141.353 112.676 90.00 90.00 120.00 H 3 2 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 0.007074 0.004084 0.000000 0.00000
SCALE2 0.000000 0.008169 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008875 0.00000
TER 2620 LEU A 323
MASTER 480 0 10 17 9 0 0 6 2646 1 99 25
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