HEADER LIGASE,BIOSYNTHETIC PROTEIN 07-SEP-10 3ORR
TITLE CRYSTAL STRUCTURE OF N5-CARBOXYAMINOIMIDAZOLE SYNTHETASE FROM
TITLE 2 STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE, ATPASE SUBUNIT;
COMPND 5 EC: 6.3.4.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE 3 ORGANISM_TAXID: 426430;
SOURCE 4 STRAIN: NEWMAN;
SOURCE 5 GENE: NWMN_0934, PURK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS ATP-GRASP SUPERFAMILY, LIGASE,BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BRUGAROLAS,E.M.DUGUID,W.ZHANG,C.B.POOR,C.HE
REVDAT 3 24-APR-13 3ORR 1 REMARK
REVDAT 2 28-MAR-12 3ORR 1 JRNL
REVDAT 1 20-JUL-11 3ORR 0
JRNL AUTH P.BRUGAROLAS,E.M.DUGUID,W.ZHANG,C.B.POOR,C.HE
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF
JRNL TITL 2 N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE AND
JRNL TITL 3 N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE MUTASE FROM
JRNL TITL 4 STAPHYLOCOCCUS AUREUS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 67 707 2011
JRNL REFN ISSN 0907-4449
JRNL PMID 21795812
JRNL DOI 10.1107/S0907444911023821
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 34554
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1869
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) : 2.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2468
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5881
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.51000
REMARK 3 B22 (A**2) : 2.29000
REMARK 3 B33 (A**2) : -0.89000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.240
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.489
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5996 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8087 ; 1.390 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 733 ; 6.312 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 298 ;38.547 ;25.973
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1120 ;16.118 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;15.219 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 899 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4502 ; 0.007 ; 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): 3658 ; 1.012 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5925 ; 1.940 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2338 ; 2.763 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2162 ; 4.501 ; 4.500
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 : 10
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 46
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3188 34.2877 27.3267
REMARK 3 T TENSOR
REMARK 3 T11: 0.3579 T22: 0.4027
REMARK 3 T33: 0.4216 T12: 0.0389
REMARK 3 T13: 0.0060 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 0.2084 L22: 0.6021
REMARK 3 L33: 0.6082 L12: 0.0928
REMARK 3 L13: 0.1260 L23: 0.1545
REMARK 3 S TENSOR
REMARK 3 S11: -0.0183 S12: 0.0607 S13: 0.1373
REMARK 3 S21: -0.0167 S22: -0.0560 S23: -0.0085
REMARK 3 S31: 0.0381 S32: 0.0860 S33: 0.0743
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 47 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1310 40.1882 22.0680
REMARK 3 T TENSOR
REMARK 3 T11: 0.3149 T22: 0.3917
REMARK 3 T33: 0.4665 T12: 0.0127
REMARK 3 T13: 0.0114 T23: 0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 0.9277 L22: 0.4218
REMARK 3 L33: 0.8361 L12: 0.4501
REMARK 3 L13: -0.0783 L23: -0.4482
REMARK 3 S TENSOR
REMARK 3 S11: -0.0594 S12: 0.1266 S13: 0.0477
REMARK 3 S21: 0.0183 S22: 0.0037 S23: -0.0110
REMARK 3 S31: -0.1147 S32: 0.1130 S33: 0.0556
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 101 A 149
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0969 20.1437 2.8346
REMARK 3 T TENSOR
REMARK 3 T11: 0.4125 T22: 0.9080
REMARK 3 T33: 0.2738 T12: 0.2052
REMARK 3 T13: -0.0029 T23: -0.0718
REMARK 3 L TENSOR
REMARK 3 L11: 0.9725 L22: 0.3736
REMARK 3 L33: 4.4945 L12: 0.3364
REMARK 3 L13: 2.0081 L23: 0.8202
REMARK 3 S TENSOR
REMARK 3 S11: 0.0129 S12: 0.5378 S13: -0.0700
REMARK 3 S21: -0.2103 S22: -0.0443 S23: 0.1590
REMARK 3 S31: -0.1684 S32: 1.3100 S33: 0.0314
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 150 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 58.1810 22.6802 -6.8122
REMARK 3 T TENSOR
REMARK 3 T11: 0.5643 T22: 0.7245
REMARK 3 T33: 0.1090 T12: 0.2198
REMARK 3 T13: 0.1293 T23: -0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 3.0839 L22: 8.0962
REMARK 3 L33: 12.0293 L12: 2.1900
REMARK 3 L13: 6.0176 L23: 3.2885
REMARK 3 S TENSOR
REMARK 3 S11: -0.2416 S12: 0.3466 S13: 0.2548
REMARK 3 S21: -1.3289 S22: -0.2711 S23: -0.1801
REMARK 3 S31: -0.1858 S32: 1.0466 S33: 0.5128
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 186 A 371
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4571 17.3381 16.0024
REMARK 3 T TENSOR
REMARK 3 T11: 0.4477 T22: 0.3763
REMARK 3 T33: 0.3379 T12: 0.0841
REMARK 3 T13: -0.0011 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.6478 L22: 0.1492
REMARK 3 L33: 0.6859 L12: 0.0055
REMARK 3 L13: -0.1764 L23: -0.1085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: 0.0773 S13: 0.0196
REMARK 3 S21: -0.0759 S22: -0.0378 S23: -0.0394
REMARK 3 S31: 0.1996 S32: 0.0328 S33: 0.0142
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 : B 1 B 103
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4118 38.6221 28.2700
REMARK 3 T TENSOR
REMARK 3 T11: 0.3573 T22: 0.4066
REMARK 3 T33: 0.4195 T12: 0.0651
REMARK 3 T13: -0.0078 T23: 0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 0.6954 L22: 0.5034
REMARK 3 L33: 0.6877 L12: 0.1938
REMARK 3 L13: -0.0891 L23: 0.0616
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0075 S13: 0.1477
REMARK 3 S21: 0.0010 S22: -0.0060 S23: 0.0152
REMARK 3 S31: 0.0215 S32: -0.1163 S33: -0.0285
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 104 B 185
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0304 28.3947 56.9423
REMARK 3 T TENSOR
REMARK 3 T11: 0.2813 T22: 0.6239
REMARK 3 T33: 0.2646 T12: 0.0775
REMARK 3 T13: 0.0556 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 0.4239 L22: 1.1255
REMARK 3 L33: 5.3106 L12: -0.4016
REMARK 3 L13: 0.8147 L23: -0.2317
REMARK 3 S TENSOR
REMARK 3 S11: -0.1028 S12: -0.1271 S13: -0.0352
REMARK 3 S21: 0.1566 S22: 0.2111 S23: 0.1492
REMARK 3 S31: -0.3595 S32: -0.0726 S33: -0.1083
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 186 B 217
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3509 18.1966 40.4929
REMARK 3 T TENSOR
REMARK 3 T11: 0.3933 T22: 0.4627
REMARK 3 T33: 0.3772 T12: -0.0242
REMARK 3 T13: -0.0321 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 0.8736 L22: 0.0165
REMARK 3 L33: 0.1303 L12: -0.0928
REMARK 3 L13: -0.3289 L23: 0.0291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: -0.0523 S13: 0.0135
REMARK 3 S21: -0.0199 S22: 0.0386 S23: 0.0399
REMARK 3 S31: 0.0320 S32: -0.0238 S33: -0.0277
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 218 B 366
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0178 20.8628 39.9828
REMARK 3 T TENSOR
REMARK 3 T11: 0.3975 T22: 0.3975
REMARK 3 T33: 0.3924 T12: 0.0226
REMARK 3 T13: -0.0230 T23: 0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.4526 L22: 0.0862
REMARK 3 L33: 0.6156 L12: 0.0927
REMARK 3 L13: -0.0129 L23: -0.1998
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: -0.0604 S13: -0.0147
REMARK 3 S21: -0.0341 S22: 0.0277 S23: -0.0122
REMARK 3 S31: 0.0541 S32: -0.0859 S33: -0.0580
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 367 B 372
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4383 19.6388 53.8210
REMARK 3 T TENSOR
REMARK 3 T11: 0.3559 T22: 0.4448
REMARK 3 T33: 0.4354 T12: 0.0295
REMARK 3 T13: 0.0307 T23: 0.0792
REMARK 3 L TENSOR
REMARK 3 L11: 6.1360 L22: 9.3099
REMARK 3 L33: 6.0690 L12: 6.8597
REMARK 3 L13: -0.7672 L23: -3.9863
REMARK 3 S TENSOR
REMARK 3 S11: 0.1969 S12: 0.0245 S13: 0.2468
REMARK 3 S21: 0.2217 S22: -0.2581 S23: 0.2402
REMARK 3 S31: 0.0441 S32: 0.5349 S33: 0.0612
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 3ORR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97951, 0.97937, 0.97196
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34628
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 45.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 28% W/V POLYETHYLENE
REMARK 280 GLYCOL MONOMETHYL ETHER 2,000, PH 6.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 26.66350
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A -2
REMARK 465 GLY A 153
REMARK 465 TYR A 154
REMARK 465 ASP A 155
REMARK 465 GLY A 156
REMARK 465 LYS A 157
REMARK 465 GLY A 372
REMARK 465 SER A 373
REMARK 465 ASN A 374
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 GLY B 153
REMARK 465 TYR B 154
REMARK 465 ASP B 155
REMARK 465 GLY B 156
REMARK 465 LYS B 157
REMARK 465 SER B 373
REMARK 465 ASN B 374
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 GLU A 79 56.32 -66.32
REMARK 500 LEU A 141 -78.08 -109.97
REMARK 500 ILE A 162 90.40 46.53
REMARK 500 LYS A 189 -71.99 -50.46
REMARK 500 ASP A 229 88.38 -69.34
REMARK 500 ASN A 266 -67.02 -106.70
REMARK 500 PRO A 270 47.84 -85.06
REMARK 500 ASN B 4 128.70 -38.25
REMARK 500 ASP B 39 142.25 -170.81
REMARK 500 ASN B 80 -54.31 -140.06
REMARK 500 LEU B 105 2.34 -69.72
REMARK 500 ASN B 164 -168.75 -165.28
REMARK 500 ASN B 202 14.33 57.37
REMARK 500 PRO B 270 52.17 -92.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ORQ RELATED DB: PDB
REMARK 900 RELATED ID: 3ORS RELATED DB: PDB
DBREF 3ORR A 1 374 UNP A6QFS4 A6QFS4_STAAE 1 374
DBREF 3ORR B 1 374 UNP A6QFS4 A6QFS4_STAAE 1 374
SEQADV 3ORR SER A -2 UNP A6QFS4 EXPRESSION TAG
SEQADV 3ORR ASN A -1 UNP A6QFS4 EXPRESSION TAG
SEQADV 3ORR ALA A 0 UNP A6QFS4 EXPRESSION TAG
SEQADV 3ORR SER B -2 UNP A6QFS4 EXPRESSION TAG
SEQADV 3ORR ASN B -1 UNP A6QFS4 EXPRESSION TAG
SEQADV 3ORR ALA B 0 UNP A6QFS4 EXPRESSION TAG
SEQRES 1 A 377 SER ASN ALA MSE ASN PHE ASN LYS LEU LYS PHE GLY ALA
SEQRES 2 A 377 THR ILE GLY ILE ILE GLY GLY GLY GLN LEU GLY LYS MSE
SEQRES 3 A 377 MSE ALA GLN SER ALA GLN LYS MSE GLY TYR LYS VAL VAL
SEQRES 4 A 377 VAL LEU ASP PRO SER GLU ASP CYS PRO CYS ARG TYR VAL
SEQRES 5 A 377 ALA HIS GLU PHE ILE GLN ALA LYS TYR ASP ASP GLU LYS
SEQRES 6 A 377 ALA LEU ASN GLN LEU GLY GLN LYS CYS ASP VAL ILE THR
SEQRES 7 A 377 TYR GLU PHE GLU ASN ILE SER ALA GLN GLN LEU LYS LEU
SEQRES 8 A 377 LEU CYS GLU LYS TYR ASN ILE PRO GLN GLY TYR GLN ALA
SEQRES 9 A 377 ILE GLN LEU LEU GLN ASP ARG LEU THR GLU LYS GLU THR
SEQRES 10 A 377 LEU LYS SER ALA GLY THR LYS VAL VAL PRO PHE ILE SER
SEQRES 11 A 377 VAL LYS GLU SER THR ASP ILE ASP LYS ALA ILE GLU THR
SEQRES 12 A 377 LEU GLY TYR PRO PHE ILE VAL LYS THR ARG PHE GLY GLY
SEQRES 13 A 377 TYR ASP GLY LYS GLY GLN VAL LEU ILE ASN ASN GLU LYS
SEQRES 14 A 377 ASP LEU GLN GLU GLY PHE LYS LEU ILE GLU THR SER GLU
SEQRES 15 A 377 CYS VAL ALA GLU LYS TYR LEU ASN ILE LYS LYS GLU VAL
SEQRES 16 A 377 SER LEU THR VAL THR ARG GLY ASN ASN ASN GLN ILE THR
SEQRES 17 A 377 PHE PHE PRO LEU GLN GLU ASN GLU HIS ARG ASN GLN ILE
SEQRES 18 A 377 LEU PHE LYS THR ILE VAL PRO ALA ARG ILE ASP LYS THR
SEQRES 19 A 377 ALA GLU ALA LYS GLU GLN VAL ASN LYS ILE ILE GLN SER
SEQRES 20 A 377 ILE HIS PHE ILE GLY THR PHE THR VAL GLU PHE PHE ILE
SEQRES 21 A 377 ASP SER ASN ASN GLN LEU TYR VAL ASN GLU ILE ALA PRO
SEQRES 22 A 377 ARG PRO HIS ASN SER GLY HIS TYR SER ILE GLU ALA CYS
SEQRES 23 A 377 ASP TYR SER GLN PHE ASP THR HIS ILE LEU ALA VAL THR
SEQRES 24 A 377 GLY GLN SER LEU PRO ASN SER ILE GLU LEU LEU LYS PRO
SEQRES 25 A 377 ALA VAL MSE MSE ASN LEU LEU GLY LYS ASP LEU ASP LEU
SEQRES 26 A 377 LEU GLU ASN GLU PHE ASN GLU HIS PRO GLU TRP HIS LEU
SEQRES 27 A 377 HIS ILE TYR GLY LYS SER GLU ARG LYS ASP SER ARG LYS
SEQRES 28 A 377 MSE GLY HIS MSE THR VAL LEU THR ASN ASP VAL ASN GLN
SEQRES 29 A 377 THR GLU GLN ASP MSE TYR ALA LYS PHE GLU GLY SER ASN
SEQRES 1 B 377 SER ASN ALA MSE ASN PHE ASN LYS LEU LYS PHE GLY ALA
SEQRES 2 B 377 THR ILE GLY ILE ILE GLY GLY GLY GLN LEU GLY LYS MSE
SEQRES 3 B 377 MSE ALA GLN SER ALA GLN LYS MSE GLY TYR LYS VAL VAL
SEQRES 4 B 377 VAL LEU ASP PRO SER GLU ASP CYS PRO CYS ARG TYR VAL
SEQRES 5 B 377 ALA HIS GLU PHE ILE GLN ALA LYS TYR ASP ASP GLU LYS
SEQRES 6 B 377 ALA LEU ASN GLN LEU GLY GLN LYS CYS ASP VAL ILE THR
SEQRES 7 B 377 TYR GLU PHE GLU ASN ILE SER ALA GLN GLN LEU LYS LEU
SEQRES 8 B 377 LEU CYS GLU LYS TYR ASN ILE PRO GLN GLY TYR GLN ALA
SEQRES 9 B 377 ILE GLN LEU LEU GLN ASP ARG LEU THR GLU LYS GLU THR
SEQRES 10 B 377 LEU LYS SER ALA GLY THR LYS VAL VAL PRO PHE ILE SER
SEQRES 11 B 377 VAL LYS GLU SER THR ASP ILE ASP LYS ALA ILE GLU THR
SEQRES 12 B 377 LEU GLY TYR PRO PHE ILE VAL LYS THR ARG PHE GLY GLY
SEQRES 13 B 377 TYR ASP GLY LYS GLY GLN VAL LEU ILE ASN ASN GLU LYS
SEQRES 14 B 377 ASP LEU GLN GLU GLY PHE LYS LEU ILE GLU THR SER GLU
SEQRES 15 B 377 CYS VAL ALA GLU LYS TYR LEU ASN ILE LYS LYS GLU VAL
SEQRES 16 B 377 SER LEU THR VAL THR ARG GLY ASN ASN ASN GLN ILE THR
SEQRES 17 B 377 PHE PHE PRO LEU GLN GLU ASN GLU HIS ARG ASN GLN ILE
SEQRES 18 B 377 LEU PHE LYS THR ILE VAL PRO ALA ARG ILE ASP LYS THR
SEQRES 19 B 377 ALA GLU ALA LYS GLU GLN VAL ASN LYS ILE ILE GLN SER
SEQRES 20 B 377 ILE HIS PHE ILE GLY THR PHE THR VAL GLU PHE PHE ILE
SEQRES 21 B 377 ASP SER ASN ASN GLN LEU TYR VAL ASN GLU ILE ALA PRO
SEQRES 22 B 377 ARG PRO HIS ASN SER GLY HIS TYR SER ILE GLU ALA CYS
SEQRES 23 B 377 ASP TYR SER GLN PHE ASP THR HIS ILE LEU ALA VAL THR
SEQRES 24 B 377 GLY GLN SER LEU PRO ASN SER ILE GLU LEU LEU LYS PRO
SEQRES 25 B 377 ALA VAL MSE MSE ASN LEU LEU GLY LYS ASP LEU ASP LEU
SEQRES 26 B 377 LEU GLU ASN GLU PHE ASN GLU HIS PRO GLU TRP HIS LEU
SEQRES 27 B 377 HIS ILE TYR GLY LYS SER GLU ARG LYS ASP SER ARG LYS
SEQRES 28 B 377 MSE GLY HIS MSE THR VAL LEU THR ASN ASP VAL ASN GLN
SEQRES 29 B 377 THR GLU GLN ASP MSE TYR ALA LYS PHE GLU GLY SER ASN
MODRES 3ORR MSE A 1 MET SELENOMETHIONINE
MODRES 3ORR MSE A 23 MET SELENOMETHIONINE
MODRES 3ORR MSE A 24 MET SELENOMETHIONINE
MODRES 3ORR MSE A 31 MET SELENOMETHIONINE
MODRES 3ORR MSE A 312 MET SELENOMETHIONINE
MODRES 3ORR MSE A 313 MET SELENOMETHIONINE
MODRES 3ORR MSE A 349 MET SELENOMETHIONINE
MODRES 3ORR MSE A 352 MET SELENOMETHIONINE
MODRES 3ORR MSE A 366 MET SELENOMETHIONINE
MODRES 3ORR MSE B 1 MET SELENOMETHIONINE
MODRES 3ORR MSE B 23 MET SELENOMETHIONINE
MODRES 3ORR MSE B 24 MET SELENOMETHIONINE
MODRES 3ORR MSE B 31 MET SELENOMETHIONINE
MODRES 3ORR MSE B 312 MET SELENOMETHIONINE
MODRES 3ORR MSE B 313 MET SELENOMETHIONINE
MODRES 3ORR MSE B 349 MET SELENOMETHIONINE
MODRES 3ORR MSE B 352 MET SELENOMETHIONINE
MODRES 3ORR MSE B 366 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 23 8
HET MSE A 24 8
HET MSE A 31 8
HET MSE A 312 8
HET MSE A 313 8
HET MSE A 349 8
HET MSE A 352 8
HET MSE A 366 8
HET MSE B 1 8
HET MSE B 23 8
HET MSE B 24 8
HET MSE B 31 8
HET MSE B 312 8
HET MSE B 313 8
HET MSE B 349 8
HET MSE B 352 8
HET MSE B 366 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 3 HOH *215(H2 O)
HELIX 1 1 GLY A 18 MSE A 31 1 14
HELIX 2 2 CYS A 46 ALA A 50 5 5
HELIX 3 3 ASP A 60 CYS A 71 1 12
HELIX 4 4 SER A 82 TYR A 93 1 12
HELIX 5 5 TYR A 99 GLN A 106 1 8
HELIX 6 6 ASP A 107 GLY A 119 1 13
HELIX 7 7 THR A 132 LEU A 141 1 10
HELIX 8 8 ASN A 164 LYS A 166 5 3
HELIX 9 9 ASP A 167 SER A 178 1 12
HELIX 10 10 ASN A 200 ASN A 202 5 3
HELIX 11 11 LYS A 230 ILE A 245 1 16
HELIX 12 12 HIS A 273 HIS A 277 5 5
HELIX 13 13 TYR A 278 CYS A 283 1 6
HELIX 14 14 SER A 286 THR A 296 1 11
HELIX 15 15 GLY A 317 GLU A 324 1 8
HELIX 16 16 ASN A 325 TRP A 333 5 9
HELIX 17 17 ASP A 358 GLU A 371 1 14
HELIX 18 18 GLY B 18 MSE B 31 1 14
HELIX 19 19 CYS B 46 ALA B 50 5 5
HELIX 20 20 ASP B 60 CYS B 71 1 12
HELIX 21 21 SER B 82 TYR B 93 1 12
HELIX 22 22 TYR B 99 LEU B 105 1 7
HELIX 23 23 ASP B 107 ALA B 118 1 12
HELIX 24 24 THR B 132 LEU B 141 1 10
HELIX 25 25 ASN B 164 LYS B 166 5 3
HELIX 26 26 ASP B 167 GLU B 176 1 10
HELIX 27 27 LYS B 230 ILE B 245 1 16
HELIX 28 28 HIS B 273 HIS B 277 5 5
HELIX 29 29 TYR B 278 CYS B 283 1 6
HELIX 30 30 SER B 286 THR B 296 1 11
HELIX 31 31 GLY B 317 GLU B 324 1 8
HELIX 32 32 ASN B 325 TRP B 333 5 9
HELIX 33 33 ASP B 358 GLU B 371 1 14
SHEET 1 A 4 GLU A 52 ILE A 54 0
SHEET 2 A 4 LYS A 34 LEU A 38 1 N VAL A 37 O ILE A 54
SHEET 3 A 4 THR A 11 ILE A 15 1 N ILE A 12 O LYS A 34
SHEET 4 A 4 VAL A 73 TYR A 76 1 O VAL A 73 N GLY A 13
SHEET 1 B 4 PHE A 125 VAL A 128 0
SHEET 2 B 4 CYS A 180 LYS A 184 -1 O ALA A 182 N ILE A 126
SHEET 3 B 4 PHE A 145 THR A 149 -1 N LYS A 148 O VAL A 181
SHEET 4 B 4 GLN A 159 VAL A 160 -1 O VAL A 160 N VAL A 147
SHEET 1 C 4 ILE A 204 PHE A 206 0
SHEET 2 C 4 ILE A 188 ARG A 198 -1 N THR A 197 O THR A 205
SHEET 3 C 4 GLY A 249 ASP A 258 -1 O GLY A 249 N ARG A 198
SHEET 4 C 4 LEU A 263 ALA A 269 -1 O GLU A 267 N GLU A 254
SHEET 1 D 7 ILE A 204 PHE A 206 0
SHEET 2 D 7 ILE A 188 ARG A 198 -1 N THR A 197 O THR A 205
SHEET 3 D 7 GLN A 210 ARG A 215 -1 O GLN A 210 N SER A 193
SHEET 4 D 7 ILE A 218 VAL A 224 -1 O LYS A 221 N GLU A 213
SHEET 5 D 7 ALA A 310 LEU A 316 -1 O MSE A 312 N THR A 222
SHEET 6 D 7 LYS A 348 LEU A 355 -1 O GLY A 350 N LEU A 315
SHEET 7 D 7 LEU A 335 ILE A 337 -1 N HIS A 336 O HIS A 351
SHEET 1 E 4 GLU B 52 GLN B 55 0
SHEET 2 E 4 LYS B 34 ASP B 39 1 N VAL B 37 O ILE B 54
SHEET 3 E 4 THR B 11 ILE B 15 1 N ILE B 12 O LYS B 34
SHEET 4 E 4 VAL B 73 TYR B 76 1 O VAL B 73 N GLY B 13
SHEET 1 F 4 PHE B 125 VAL B 128 0
SHEET 2 F 4 CYS B 180 LYS B 184 -1 O ALA B 182 N ILE B 126
SHEET 3 F 4 PHE B 145 THR B 149 -1 N ILE B 146 O GLU B 183
SHEET 4 F 4 GLN B 159 ILE B 162 -1 O ILE B 162 N PHE B 145
SHEET 1 G 4 ILE B 204 PHE B 206 0
SHEET 2 G 4 ILE B 188 ARG B 198 -1 N THR B 197 O THR B 205
SHEET 3 G 4 GLY B 249 ASP B 258 -1 O GLY B 249 N ARG B 198
SHEET 4 G 4 LEU B 263 ALA B 269 -1 O ALA B 269 N THR B 252
SHEET 1 H 7 ILE B 204 PHE B 206 0
SHEET 2 H 7 ILE B 188 ARG B 198 -1 N THR B 197 O THR B 205
SHEET 3 H 7 GLN B 210 ARG B 215 -1 O GLN B 210 N SER B 193
SHEET 4 H 7 ILE B 218 VAL B 224 -1 O LYS B 221 N GLU B 213
SHEET 5 H 7 ALA B 310 LEU B 316 -1 O MSE B 312 N THR B 222
SHEET 6 H 7 LYS B 348 LEU B 355 -1 O GLY B 350 N LEU B 315
SHEET 7 H 7 LEU B 335 ILE B 337 -1 N HIS B 336 O HIS B 351
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N ASN A 2 1555 1555 1.33
LINK C LYS A 22 N MSE A 23 1555 1555 1.31
LINK C MSE A 23 N MSE A 24 1555 1555 1.33
LINK C MSE A 24 N ALA A 25 1555 1555 1.34
LINK C LYS A 30 N MSE A 31 1555 1555 1.32
LINK C MSE A 31 N GLY A 32 1555 1555 1.32
LINK C VAL A 311 N MSE A 312 1555 1555 1.32
LINK C MSE A 312 N MSE A 313 1555 1555 1.33
LINK C MSE A 313 N ASN A 314 1555 1555 1.33
LINK C LYS A 348 N MSE A 349 1555 1555 1.33
LINK C MSE A 349 N GLY A 350 1555 1555 1.32
LINK C HIS A 351 N MSE A 352 1555 1555 1.31
LINK C MSE A 352 N THR A 353 1555 1555 1.34
LINK C ASP A 365 N MSE A 366 1555 1555 1.34
LINK C MSE A 366 N TYR A 367 1555 1555 1.33
LINK C MSE B 1 N ASN B 2 1555 1555 1.33
LINK C LYS B 22 N MSE B 23 1555 1555 1.33
LINK C MSE B 23 N MSE B 24 1555 1555 1.34
LINK C MSE B 24 N ALA B 25 1555 1555 1.33
LINK C LYS B 30 N MSE B 31 1555 1555 1.34
LINK C MSE B 31 N GLY B 32 1555 1555 1.32
LINK C VAL B 311 N MSE B 312 1555 1555 1.33
LINK C MSE B 312 N MSE B 313 1555 1555 1.33
LINK C MSE B 313 N ASN B 314 1555 1555 1.33
LINK C LYS B 348 N MSE B 349 1555 1555 1.35
LINK C MSE B 349 N GLY B 350 1555 1555 1.33
LINK C HIS B 351 N MSE B 352 1555 1555 1.32
LINK C MSE B 352 N THR B 353 1555 1555 1.32
LINK C ASP B 365 N MSE B 366 1555 1555 1.34
LINK C MSE B 366 N TYR B 367 1555 1555 1.34
CISPEP 1 GLY A 142 TYR A 143 0 4.07
CISPEP 2 TYR A 143 PRO A 144 0 -10.92
CISPEP 3 VAL A 224 PRO A 225 0 -0.34
CISPEP 4 TYR B 143 PRO B 144 0 -9.90
CISPEP 5 VAL B 224 PRO B 225 0 3.87
CRYST1 66.112 53.327 107.406 90.00 95.34 90.00 P 1 21 1 4
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 0.015126 0.000000 0.001414 0.00000
SCALE2 0.000000 0.018752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
