HEADER CONTRACTILE PROTEIN 30-APR-10 3MTU
TITLE STRUCTURE OF THE TROPOMYOSIN OVERLAP COMPLEX FROM CHICKEN SMOOTH
TITLE 2 MUSCLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPOMYOSIN ALPHA-1 CHAIN,MICROTUBULE-ASSOCIATED PROTEIN
COMPND 3 RP/EB FAMILY MEMBER 1;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: FUSION PROTEIN OF RESIDUES 1-29 OF CHICKEN SMOOTH MUSCLE
COMPND 6 TROPOMYOSIN AND RESIDUES 215-257 OF HUMAN EB1 PROTEIN,FUSION PROTEIN
COMPND 7 OF RESIDUES 1-29 OF CHICKEN SMOOTH MUSCLE TROPOMYOSIN AND RESIDUES
COMPND 8 215-257 OF HUMAN EB1 PROTEIN;
COMPND 9 SYNONYM: ALPHA-TROPOMYOSIN,TROPOMYOSIN-1,APC-BINDING PROTEIN EB1,END-
COMPND 10 BINDING PROTEIN 1,EB1;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: CAPSID ASSEMBLY SCAFFOLDING PROTEIN,TROPOMYOSIN ALPHA-1
COMPND 14 CHAIN;
COMPND 15 CHAIN: E, F;
COMPND 16 FRAGMENT: FUSION PROTEIN OF RESIDUES 2-45 OF PHAGE PHI29 GP7 PROTEIN
COMPND 17 AND RESIDUES 256-284 OF CHICKEN SMOOTH MUSCLE TROPOMYOSIN,FUSION
COMPND 18 PROTEIN OF RESIDUES 2-45 OF PHAGE PHI29 GP7 PROTEIN AND RESIDUES 256-
COMPND 19 284 OF CHICKEN SMOOTH MUSCLE TROPOMYOSIN;
COMPND 20 SYNONYM: GENE PRODUCT 7,GP7,HEAD MORPHOGENESIS PROTEIN,PROTEIN P7,
COMPND 21 SCAFFOLD PROTEIN,ALPHA-TROPOMYOSIN,TROPOMYOSIN-1;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: CHICKEN, HUMAN;
SOURCE 4 ORGANISM_TAXID: 9031, 9606;
SOURCE 5 GENE: TPM1, MAPRE1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PRIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET31B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: BACILLUS PHAGE PHI29, GALLUS GALLUS;
SOURCE 13 ORGANISM_COMMON: CHICKEN;
SOURCE 14 ORGANISM_TAXID: 10756, 9031;
SOURCE 15 GENE: TPM1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PRIL;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET31B
KEYWDS TROPOMYSOIN, OVERLAP COMPLEX, COILED-COILS, CONTRACTILE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.A.KLENCHIN,J.FRYE,I.RAYMENT
REVDAT 3 24-JAN-18 3MTU 1 AUTHOR
REVDAT 2 31-MAY-17 3MTU 1 COMPND REMARK DBREF
REVDAT 1 23-JUN-10 3MTU 0
JRNL AUTH J.FRYE,V.A.KLENCHIN,I.RAYMENT
JRNL TITL STRUCTURE OF THE TROPOMYOSIN OVERLAP COMPLEX FROM CHICKEN
JRNL TITL 2 SMOOTH MUSCLE: INSIGHT INTO THE DIVERSITY OF N-TERMINAL
JRNL TITL 3 RECOGNITION .
JRNL REF BIOCHEMISTRY V. 49 4908 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20465283
JRNL DOI 10.1021/BI100349A
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 31424
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1666
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2237
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3320
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 347
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.44000
REMARK 3 B22 (A**2) : -0.91000
REMARK 3 B33 (A**2) : -0.52000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.178
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.393
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3438 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4586 ; 1.069 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 414 ; 3.956 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 196 ;40.068 ;26.888
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 689 ;15.676 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;21.251 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 501 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2569 ; 0.004 ; 0.020
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): 2071 ; 2.562 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3314 ; 4.922 ;50.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1367 ; 6.256 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1267 ; 9.817 ;70.000
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 : 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 -2 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5470 84.5040 42.1100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0643 T22: 0.1053
REMARK 3 T33: 0.0319 T12: 0.0144
REMARK 3 T13: 0.0281 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.1312 L22: 4.9050
REMARK 3 L33: 0.1722 L12: -0.2580
REMARK 3 L13: 0.0037 L23: -0.5298
REMARK 3 S TENSOR
REMARK 3 S11: 0.0749 S12: 0.0478 S13: 0.0203
REMARK 3 S21: 0.1504 S22: -0.0624 S23: 0.1864
REMARK 3 S31: -0.0109 S32: -0.0249 S33: -0.0125
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 -2 B 257
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0490 81.7970 44.0380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1064 T22: 0.1315
REMARK 3 T33: 0.0413 T12: 0.0284
REMARK 3 T13: -0.0201 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0677 L22: 7.7216
REMARK 3 L33: 0.3238 L12: 0.3015
REMARK 3 L13: 0.0791 L23: 1.1808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0866 S12: 0.0010 S13: -0.0121
REMARK 3 S21: -0.0047 S22: -0.1406 S23: -0.0915
REMARK 3 S31: 0.0207 S32: -0.0776 S33: 0.0540
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 -2 C 257
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1530 64.5560 21.2780
REMARK 3 T TENSOR
REMARK 3 T11: 0.0628 T22: 0.1243
REMARK 3 T33: 0.0216 T12: -0.0093
REMARK 3 T13: -0.0318 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.1217 L22: 8.1029
REMARK 3 L33: 1.0128 L12: -0.5689
REMARK 3 L13: -0.3274 L23: 2.3490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0419 S12: -0.0170 S13: -0.0040
REMARK 3 S21: -0.0435 S22: -0.0311 S23: -0.0903
REMARK 3 S31: -0.0769 S32: 0.0049 S33: -0.0108
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 -2 D 257
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8930 64.4890 22.4290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0579 T22: 0.1279
REMARK 3 T33: 0.0337 T12: 0.0277
REMARK 3 T13: -0.0078 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.0125 L22: 4.7034
REMARK 3 L33: 0.8709 L12: 0.1261
REMARK 3 L13: -0.0099 L23: -0.8349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: 0.0130 S13: -0.0011
REMARK 3 S21: -0.1257 S22: -0.0269 S23: 0.0928
REMARK 3 S31: -0.0456 S32: -0.0298 S33: 0.0012
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 1 E 284
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8270 13.2880 32.9060
REMARK 3 T TENSOR
REMARK 3 T11: 0.3321 T22: 0.0816
REMARK 3 T33: 0.0757 T12: 0.0101
REMARK 3 T13: 0.0251 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.2618 L22: 11.6682
REMARK 3 L33: 0.5496 L12: -0.7791
REMARK 3 L13: -0.1042 L23: 0.0689
REMARK 3 S TENSOR
REMARK 3 S11: -0.0613 S12: -0.0265 S13: -0.0489
REMARK 3 S21: -1.3548 S22: 0.1090 S23: -0.1243
REMARK 3 S31: 0.2441 S32: 0.0426 S33: -0.0477
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 1 F 284
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5060 12.9300 38.2490
REMARK 3 T TENSOR
REMARK 3 T11: 0.4397 T22: 0.0828
REMARK 3 T33: 0.1997 T12: -0.1499
REMARK 3 T13: -0.0239 T23: -0.0485
REMARK 3 L TENSOR
REMARK 3 L11: 6.8174 L22: 21.9186
REMARK 3 L33: 1.9678 L12: -12.1873
REMARK 3 L13: -2.9096 L23: 5.2808
REMARK 3 S TENSOR
REMARK 3 S11: -0.2567 S12: -0.0892 S13: 0.1988
REMARK 3 S21: 0.6526 S22: 0.1386 S23: -0.4463
REMARK 3 S31: 0.5622 S32: -0.1954 S33: 0.1181
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.25
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 3MTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000058987.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33097
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% MEPEG 5000, 100 MM MES, PH 6.0,
REMARK 280 140 MM CACL2, 2% METHANOL , VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 44.56550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 142.66400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.56550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 142.66400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.56550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 142.66400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.56550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 142.66400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 10460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 306 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 304 LIES ON A SPECIAL POSITION.
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 GLU B 251
REMARK 465 GLY B 252
REMARK 465 PHE B 253
REMARK 465 VAL B 254
REMARK 465 ILE B 255
REMARK 465 PRO B 256
REMARK 465 ASP B 257
REMARK 465 GLY C -2
REMARK 465 ALA C -1
REMARK 465 GLU C 251
REMARK 465 GLY C 252
REMARK 465 PHE C 253
REMARK 465 VAL C 254
REMARK 465 ILE C 255
REMARK 465 PRO C 256
REMARK 465 ASP C 257
REMARK 465 GLY D -2
REMARK 465 ALA D -1
REMARK 465 GLY D 252
REMARK 465 PHE D 253
REMARK 465 VAL D 254
REMARK 465 ILE D 255
REMARK 465 PRO D 256
REMARK 465 ASP D 257
REMARK 465 GLY E -2
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 GLY E 1
REMARK 465 PRO E 2
REMARK 465 LEU E 3
REMARK 465 LYS E 4
REMARK 465 GLU E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 GLY F -2
REMARK 465 GLY F -1
REMARK 465 SER F 0
REMARK 465 GLY F 1
REMARK 465 PRO F 2
REMARK 465 LEU F 3
REMARK 465 LYS F 4
REMARK 465 GLU F 19
REMARK 465 LEU F 20
REMARK 465 ALA F 21
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 GLU B 232 CG CD OE1 OE2
REMARK 470 GLU B 234 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A -2 N GLY A -2 CA -0.278
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A -2 CA - C - O ANGL. DEV. = -12.0 DEGREES
REMARK 500 ARG A 241 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A -2 -18.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 32 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 53 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A 113 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 129 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A 130 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH B 97 DISTANCE = 6.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH C 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH B 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH B 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH D 260
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G9J RELATED DB: PDB
REMARK 900 RELATED ID: 3MUD RELATED DB: PDB
DBREF 3MTU A 2 29 UNP P04268 TPM1_CHICK 2 29
DBREF 3MTU A 216 257 UNP Q15691 MARE1_HUMAN 216 257
DBREF 3MTU B 2 29 UNP P04268 TPM1_CHICK 2 29
DBREF 3MTU B 216 257 UNP Q15691 MARE1_HUMAN 216 257
DBREF 3MTU C 2 29 UNP P04268 TPM1_CHICK 2 29
DBREF 3MTU C 216 257 UNP Q15691 MARE1_HUMAN 216 257
DBREF 3MTU D 2 29 UNP P04268 TPM1_CHICK 2 29
DBREF 3MTU D 216 257 UNP Q15691 MARE1_HUMAN 216 257
DBREF 3MTU E 2 256 UNP P13848 SCAF_BPPH2 2 46
DBREF 3MTU E 257 283 UNP P04268 TPM1_CHICK 257 283
DBREF 3MTU F 2 256 UNP P13848 SCAF_BPPH2 2 46
DBREF 3MTU F 257 283 UNP P04268 TPM1_CHICK 257 283
SEQADV 3MTU GLY A -2 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ALA A -1 UNP P04268 EXPRESSION TAG
SEQADV 3MTU SER A 0 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ASP A 215 UNP P04268 LINKER
SEQADV 3MTU GLY B -2 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ALA B -1 UNP P04268 EXPRESSION TAG
SEQADV 3MTU SER B 0 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ASP B 215 UNP P04268 LINKER
SEQADV 3MTU GLY C -2 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ALA C -1 UNP P04268 EXPRESSION TAG
SEQADV 3MTU SER C 0 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ASP C 215 UNP P04268 LINKER
SEQADV 3MTU GLY D -2 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ALA D -1 UNP P04268 EXPRESSION TAG
SEQADV 3MTU SER D 0 UNP P04268 EXPRESSION TAG
SEQADV 3MTU ASP D 215 UNP P04268 LINKER
SEQADV 3MTU GLY E -2 UNP P13848 EXPRESSION TAG
SEQADV 3MTU GLY E -1 UNP P13848 EXPRESSION TAG
SEQADV 3MTU SER E 0 UNP P13848 EXPRESSION TAG
SEQADV 3MTU GLY E 1 UNP P13848 EXPRESSION TAG
SEQADV 3MTU MSE E 284 UNP P04268 EXPRESSION TAG
SEQADV 3MTU GLY F -2 UNP P13848 EXPRESSION TAG
SEQADV 3MTU GLY F -1 UNP P13848 EXPRESSION TAG
SEQADV 3MTU SER F 0 UNP P13848 EXPRESSION TAG
SEQADV 3MTU GLY F 1 UNP P13848 EXPRESSION TAG
SEQADV 3MTU MSE F 284 UNP P04268 EXPRESSION TAG
SEQRES 1 A 75 GLY ALA SER MSE ASP ALA ILE LYS LYS LYS MSE GLN MSE
SEQRES 2 A 75 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 A 75 GLN ALA GLU ALA ASP LYS ASP PHE TYR PHE GLY LYS LEU
SEQRES 4 A 75 ARG ASN ILE GLU LEU ILE CYS GLN GLU ASN GLU GLY GLU
SEQRES 5 A 75 ASN ASP PRO VAL LEU GLN ARG ILE VAL ASP ILE LEU TYR
SEQRES 6 A 75 ALA THR ASP GLU GLY PHE VAL ILE PRO ASP
SEQRES 1 B 75 GLY ALA SER MSE ASP ALA ILE LYS LYS LYS MSE GLN MSE
SEQRES 2 B 75 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 B 75 GLN ALA GLU ALA ASP LYS ASP PHE TYR PHE GLY LYS LEU
SEQRES 4 B 75 ARG ASN ILE GLU LEU ILE CYS GLN GLU ASN GLU GLY GLU
SEQRES 5 B 75 ASN ASP PRO VAL LEU GLN ARG ILE VAL ASP ILE LEU TYR
SEQRES 6 B 75 ALA THR ASP GLU GLY PHE VAL ILE PRO ASP
SEQRES 1 C 75 GLY ALA SER MSE ASP ALA ILE LYS LYS LYS MSE GLN MSE
SEQRES 2 C 75 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 C 75 GLN ALA GLU ALA ASP LYS ASP PHE TYR PHE GLY LYS LEU
SEQRES 4 C 75 ARG ASN ILE GLU LEU ILE CYS GLN GLU ASN GLU GLY GLU
SEQRES 5 C 75 ASN ASP PRO VAL LEU GLN ARG ILE VAL ASP ILE LEU TYR
SEQRES 6 C 75 ALA THR ASP GLU GLY PHE VAL ILE PRO ASP
SEQRES 1 D 75 GLY ALA SER MSE ASP ALA ILE LYS LYS LYS MSE GLN MSE
SEQRES 2 D 75 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 D 75 GLN ALA GLU ALA ASP LYS ASP PHE TYR PHE GLY LYS LEU
SEQRES 4 D 75 ARG ASN ILE GLU LEU ILE CYS GLN GLU ASN GLU GLY GLU
SEQRES 5 D 75 ASN ASP PRO VAL LEU GLN ARG ILE VAL ASP ILE LEU TYR
SEQRES 6 D 75 ALA THR ASP GLU GLY PHE VAL ILE PRO ASP
SEQRES 1 E 77 GLY GLY SER GLY PRO LEU LYS PRO GLU GLU HIS GLU ASP
SEQRES 2 E 77 ILE LEU ASN LYS LEU LEU ASP PRO GLU LEU ALA GLN SER
SEQRES 3 E 77 GLU ARG THR GLU ALA LEU GLN GLN LEU ARG VAL ASN TYR
SEQRES 4 E 77 GLY SER PHE VAL SER GLU TYR ASN ASP LEU GLU GLU LYS
SEQRES 5 E 77 VAL ALA HIS ALA LYS GLU GLU ASN LEU ASN MSE HIS GLN
SEQRES 6 E 77 MSE LEU ASP GLN THR LEU LEU GLU LEU ASN ASN MSE
SEQRES 1 F 77 GLY GLY SER GLY PRO LEU LYS PRO GLU GLU HIS GLU ASP
SEQRES 2 F 77 ILE LEU ASN LYS LEU LEU ASP PRO GLU LEU ALA GLN SER
SEQRES 3 F 77 GLU ARG THR GLU ALA LEU GLN GLN LEU ARG VAL ASN TYR
SEQRES 4 F 77 GLY SER PHE VAL SER GLU TYR ASN ASP LEU GLU GLU LYS
SEQRES 5 F 77 VAL ALA HIS ALA LYS GLU GLU ASN LEU ASN MSE HIS GLN
SEQRES 6 F 77 MSE LEU ASP GLN THR LEU LEU GLU LEU ASN ASN MSE
MODRES 3MTU MSE A 1 MODIFIED RESIDUE
MODRES 3MTU MSE A 8 MET MODIFIED RESIDUE
MODRES 3MTU MSE A 10 MET MODIFIED RESIDUE
MODRES 3MTU MSE B 1 MODIFIED RESIDUE
MODRES 3MTU MSE B 8 MET MODIFIED RESIDUE
MODRES 3MTU MSE B 10 MET MODIFIED RESIDUE
MODRES 3MTU MSE C 1 MODIFIED RESIDUE
MODRES 3MTU MSE C 8 MET MODIFIED RESIDUE
MODRES 3MTU MSE C 10 MET MODIFIED RESIDUE
MODRES 3MTU MSE D 1 MODIFIED RESIDUE
MODRES 3MTU MSE D 8 MET MODIFIED RESIDUE
MODRES 3MTU MSE D 10 MET MODIFIED RESIDUE
MODRES 3MTU MSE E 270 MET MODIFIED RESIDUE
MODRES 3MTU MSE E 273 MET MODIFIED RESIDUE
MODRES 3MTU MSE F 270 MET MODIFIED RESIDUE
MODRES 3MTU MSE F 273 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 8 12
HET MSE A 10 13
HET MSE B 1 8
HET MSE B 8 13
HET MSE B 10 8
HET MSE C 1 8
HET MSE C 8 8
HET MSE C 10 8
HET MSE D 1 8
HET MSE D 8 8
HET MSE D 10 8
HET MSE E 270 8
HET MSE E 273 12
HET MSE E 284 9
HET MSE F 270 8
HET MSE F 273 8
HET MSE F 284 9
HET CL A 258 1
HET EDO A 259 4
HET EDO A 260 4
HET EDO A 261 4
HET EDO A 262 4
HET EOH A 263 3
HET EOH A 264 3
HET EOH A 265 3
HET CL B 258 1
HET EDO B 259 4
HET EOH B 260 3
HET EOH B 261 3
HET EDO C 258 4
HET EOH C 259 3
HET EDO D 258 4
HET EDO D 259 4
HET EOH D 260 3
HET EDO F 285 4
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM EOH ETHANOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 7 CL 2(CL 1-)
FORMUL 8 EDO 9(C2 H6 O2)
FORMUL 12 EOH 7(C2 H6 O)
FORMUL 25 HOH *347(H2 O)
HELIX 1 1 GLY A -2 ASN A 231 1 49
HELIX 2 2 GLU A 232 ASN A 235 5 4
HELIX 3 3 ASP A 236 ALA A 248 1 13
HELIX 4 4 GLY B -2 ASN B 231 1 49
HELIX 5 5 GLU B 232 ASN B 235 5 4
HELIX 6 6 ASP B 236 TYR B 247 1 12
HELIX 7 7 SER C 0 ASN C 231 1 47
HELIX 8 8 GLU C 232 ASN C 235 5 4
HELIX 9 9 ASP C 236 TYR C 247 1 12
HELIX 10 10 SER D 0 ASN D 231 1 47
HELIX 11 11 GLU D 232 ASN D 235 5 4
HELIX 12 12 ASP D 236 TYR D 247 1 12
HELIX 13 13 PRO E 5 LEU E 15 1 11
HELIX 14 14 GLN E 22 MSE E 284 1 53
HELIX 15 15 PRO F 5 LEU F 15 1 11
HELIX 16 16 GLN F 22 ASN F 283 1 52
LINK C SER A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N ASP A 2 1555 1555 1.34
LINK C LYS A 7 N MSE A 8 1555 1555 1.33
LINK C MSE A 8 N GLN A 9 1555 1555 1.34
LINK C GLN A 9 N MSE A 10 1555 1555 1.34
LINK C MSE A 10 N LEU A 11 1555 1555 1.33
LINK C SER B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N ASP B 2 1555 1555 1.33
LINK C LYS B 7 N MSE B 8 1555 1555 1.34
LINK C MSE B 8 N GLN B 9 1555 1555 1.34
LINK C GLN B 9 N MSE B 10 1555 1555 1.34
LINK C MSE B 10 N LEU B 11 1555 1555 1.33
LINK C SER C 0 N MSE C 1 1555 1555 1.34
LINK C MSE C 1 N ASP C 2 1555 1555 1.34
LINK C LYS C 7 N MSE C 8 1555 1555 1.33
LINK C MSE C 8 N GLN C 9 1555 1555 1.34
LINK C GLN C 9 N MSE C 10 1555 1555 1.33
LINK C MSE C 10 N LEU C 11 1555 1555 1.33
LINK C SER D 0 N MSE D 1 1555 1555 1.33
LINK C MSE D 1 N ASP D 2 1555 1555 1.33
LINK C LYS D 7 N MSE D 8 1555 1555 1.32
LINK C MSE D 8 N GLN D 9 1555 1555 1.33
LINK C GLN D 9 N MSE D 10 1555 1555 1.33
LINK C MSE D 10 N LEU D 11 1555 1555 1.33
LINK C ASN E 269 N MSE E 270 1555 1555 1.33
LINK C MSE E 270 N HIS E 271 1555 1555 1.33
LINK C GLN E 272 N MSE E 273 1555 1555 1.34
LINK C MSE E 273 N LEU E 274 1555 1555 1.34
LINK C ASN E 283 N MSE E 284 1555 1555 1.33
LINK C ASN F 269 N MSE F 270 1555 1555 1.33
LINK C MSE F 270 N HIS F 271 1555 1555 1.33
LINK C GLN F 272 N MSE F 273 1555 1555 1.33
LINK C MSE F 273 N LEU F 274 1555 1555 1.33
LINK C ASN F 283 N MSE F 284 1555 1555 1.33
SITE 1 AC1 4 GLY B -2 MSE B 1 HOH B 140 HOH F 179
SITE 1 AC2 3 ILE A 255 LYS C 12 LYS D 7
SITE 1 AC3 8 ALA A -1 HOH A 156 HOH A 270 GLN B 229
SITE 2 AC3 8 HOH B 283 GLU C 232 GLY C 233 HOH C 313
SITE 1 AC4 8 SER A 0 HOH B 36 ASN B 223 LEU B 226
SITE 2 AC4 8 ILE B 227 GLU B 230 ASP E 275 LEU E 278
SITE 1 AC5 4 GLY B -2 ASP B 2 CYS D 228 GLU D 232
SITE 1 AC6 3 GLY A 219 ARG A 222 EOH B 260
SITE 1 AC7 4 HOH B 134 HOH B 272 HOH E 180 ASN E 283
SITE 1 AC8 3 GLU A 225 LEU A 246 LYS B 220
SITE 1 AC9 1 LEU B 246
SITE 1 BC1 4 GLN B 24 HOH B 280 ASN C 17 ASP C 20
SITE 1 BC2 2 ALA A 27 ASP A 28
SITE 1 BC3 6 ASP A 2 HOH C 67 CYS C 228 GLU C 232
SITE 2 BC3 6 LEU C 239 VAL C 243
SITE 1 BC4 2 EDO A 261 ASP B 250
SITE 1 BC5 3 GLN B 240 HOH B 287 ASP D 2
SITE 1 BC6 5 HOH A 112 ASN A 235 PRO A 237 GLN A 240
SITE 2 BC6 5 LEU E 268
SITE 1 BC7 3 ASN A 17 ARG A 21 HOH A 278
SITE 1 BC8 1 HOH D 76
CRYST1 89.131 285.328 43.457 90.00 90.00 90.00 C 2 2 2 32
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 0.011219 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023011 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
