HEADER TRANSLATION 19-MAY-10 2XEX
TITLE CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS ELONGATION FACTOR G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR G;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RIBOSOMAL ELONGATION FACTOR G, EF-G, 85 KDA VITRONECTIN-
COMPND 5 BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GTPASE, TRANSLATION, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.CHEN,R.K.KORIPELLA,S.SANYAL,M.SELMER
REVDAT 5 20-DEC-23 2XEX 1 REMARK LINK
REVDAT 4 13-JUL-11 2XEX 1 VERSN
REVDAT 3 24-NOV-10 2XEX 1 JRNL FORMUL
REVDAT 2 01-SEP-10 2XEX 1 JRNL
REVDAT 1 14-JUL-10 2XEX 0
JRNL AUTH Y.CHEN,R.K.KORIPELLA,S.SANYAL,M.SELMER
JRNL TITL STAPHYLOCOCCUS AUREUS ELONGATION FACTOR G - STRUCTURE AND
JRNL TITL 2 ANALYSIS OF A TARGET FOR FUSIDIC ACID.
JRNL REF FEBS J. V. 277 3789 2010
JRNL REFN ISSN 1742-464X
JRNL PMID 20718859
JRNL DOI 10.1111/J.1742-4658.2010.07780.X
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 110987
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4777
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6536
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 300
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10352
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 509
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.13000
REMARK 3 B22 (A**2) : -1.87000
REMARK 3 B33 (A**2) : -1.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.19000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.144
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.506
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10533 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14237 ; 1.527 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1330 ; 6.042 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 484 ;33.891 ;24.855
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1851 ;16.870 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;19.641 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1595 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7960 ; 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): 6627 ; 0.945 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10684 ; 1.672 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3906 ; 2.685 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3553 ; 4.360 ; 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 : 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 2 A 280
REMARK 3 ORIGIN FOR THE GROUP (A): 35.1632 -2.3913 65.8257
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: 0.0037
REMARK 3 T33: 0.0281 T12: -0.0068
REMARK 3 T13: -0.0381 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.0175 L22: 2.1561
REMARK 3 L33: 1.4188 L12: 0.7134
REMARK 3 L13: 0.5392 L23: 0.3033
REMARK 3 S TENSOR
REMARK 3 S11: 0.1799 S12: -0.0567 S13: -0.1563
REMARK 3 S21: 0.0883 S22: -0.0292 S23: -0.0949
REMARK 3 S31: 0.2680 S32: -0.0073 S33: -0.1507
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 288 A 400
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9338 25.3349 63.6284
REMARK 3 T TENSOR
REMARK 3 T11: 0.0434 T22: 0.1011
REMARK 3 T33: 0.1157 T12: -0.0234
REMARK 3 T13: 0.0329 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 0.9433 L22: 2.5715
REMARK 3 L33: 2.4830 L12: -0.0487
REMARK 3 L13: 0.4012 L23: 0.0165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0281 S12: 0.0330 S13: 0.1237
REMARK 3 S21: 0.0796 S22: -0.0616 S23: -0.1475
REMARK 3 S31: -0.2416 S32: 0.0476 S33: 0.0335
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 405 A 482
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4721 36.0364 59.5039
REMARK 3 T TENSOR
REMARK 3 T11: 0.0897 T22: 0.1540
REMARK 3 T33: 0.1254 T12: 0.0410
REMARK 3 T13: 0.0159 T23: -0.0911
REMARK 3 L TENSOR
REMARK 3 L11: 3.3657 L22: 2.9211
REMARK 3 L33: 6.6184 L12: -0.2804
REMARK 3 L13: 1.5759 L23: 0.3893
REMARK 3 S TENSOR
REMARK 3 S11: -0.2371 S12: -0.6009 S13: 0.4490
REMARK 3 S21: 0.3477 S22: 0.0954 S23: 0.0248
REMARK 3 S31: -0.3373 S32: -0.4153 S33: 0.1416
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 483 A 605
REMARK 3 RESIDUE RANGE : A 674 A 691
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5313 51.0329 31.2062
REMARK 3 T TENSOR
REMARK 3 T11: 0.2554 T22: 0.0706
REMARK 3 T33: 0.0667 T12: -0.0607
REMARK 3 T13: -0.0645 T23: 0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 1.1346 L22: 4.3879
REMARK 3 L33: 1.5761 L12: 1.5252
REMARK 3 L13: -0.7748 L23: -2.5792
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: -0.0375 S13: 0.0453
REMARK 3 S21: 0.2797 S22: -0.0936 S23: -0.0525
REMARK 3 S31: -0.2535 S32: 0.0983 S33: 0.0911
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 606 A 673
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5003 13.7933 42.3481
REMARK 3 T TENSOR
REMARK 3 T11: 0.0116 T22: 0.0742
REMARK 3 T33: 0.0566 T12: -0.0110
REMARK 3 T13: 0.0171 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.4774 L22: 1.9529
REMARK 3 L33: 0.8648 L12: 0.1408
REMARK 3 L13: 0.2298 L23: 0.1904
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.0035 S13: 0.0143
REMARK 3 S21: -0.0462 S22: -0.0046 S23: -0.0235
REMARK 3 S31: -0.0632 S32: 0.0700 S33: -0.0064
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 2 B 280
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6584 17.7553 0.1063
REMARK 3 T TENSOR
REMARK 3 T11: 0.0323 T22: 0.0432
REMARK 3 T33: 0.0220 T12: 0.0254
REMARK 3 T13: 0.0095 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.6196 L22: 1.8868
REMARK 3 L33: 1.5707 L12: -0.2134
REMARK 3 L13: 0.1276 L23: -0.0790
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: 0.0435 S13: 0.0146
REMARK 3 S21: 0.0234 S22: 0.0418 S23: -0.0324
REMARK 3 S31: -0.1372 S32: -0.0056 S33: -0.0301
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 288 B 400
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3681 -9.6061 -4.0398
REMARK 3 T TENSOR
REMARK 3 T11: 0.1043 T22: 0.1154
REMARK 3 T33: 0.1357 T12: 0.0759
REMARK 3 T13: 0.0241 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 0.4775 L22: 3.1104
REMARK 3 L33: 3.3215 L12: -0.1557
REMARK 3 L13: 0.6895 L23: 0.1686
REMARK 3 S TENSOR
REMARK 3 S11: 0.0536 S12: 0.0077 S13: -0.0883
REMARK 3 S21: -0.0938 S22: -0.0292 S23: -0.2154
REMARK 3 S31: 0.4314 S32: 0.1548 S33: -0.0244
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 405 B 482
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1061 -20.6075 13.0412
REMARK 3 T TENSOR
REMARK 3 T11: 0.1675 T22: 0.0771
REMARK 3 T33: 0.1045 T12: -0.0710
REMARK 3 T13: -0.0494 T23: -0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 3.0791 L22: 3.0306
REMARK 3 L33: 3.9596 L12: 2.0588
REMARK 3 L13: 0.4305 L23: 0.8513
REMARK 3 S TENSOR
REMARK 3 S11: -0.1579 S12: 0.2975 S13: -0.2775
REMARK 3 S21: -0.3878 S22: 0.1730 S23: 0.0955
REMARK 3 S31: 0.4972 S32: -0.3428 S33: -0.0151
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 483 B 605
REMARK 3 RESIDUE RANGE : B 674 B 691
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8822 -35.3027 33.3222
REMARK 3 T TENSOR
REMARK 3 T11: 0.1909 T22: 0.0444
REMARK 3 T33: 0.0240 T12: 0.0293
REMARK 3 T13: -0.0229 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 1.7039 L22: 4.1670
REMARK 3 L33: 0.3242 L12: -2.3030
REMARK 3 L13: 0.2632 L23: -0.6852
REMARK 3 S TENSOR
REMARK 3 S11: 0.0975 S12: 0.0352 S13: -0.0558
REMARK 3 S21: -0.2244 S22: -0.0310 S23: 0.2129
REMARK 3 S31: 0.2092 S32: -0.0001 S33: -0.0665
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 606 B 673
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0672 1.5769 28.0960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0150 T22: 0.0559
REMARK 3 T33: 0.0466 T12: 0.0034
REMARK 3 T13: 0.0086 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.2389 L22: 2.2983
REMARK 3 L33: 1.3796 L12: -0.1283
REMARK 3 L13: 0.2221 L23: 0.1086
REMARK 3 S TENSOR
REMARK 3 S11: 0.0203 S12: 0.0402 S13: -0.0477
REMARK 3 S21: -0.0976 S22: -0.0616 S23: 0.0153
REMARK 3 S31: -0.0308 S32: -0.0229 S33: 0.0413
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 U VALUES RESIDUAL ONLY
REMARK 4
REMARK 4 2XEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1290043574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 193
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110987
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 46.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 3.710
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.56
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1FNM
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 68.67000
REMARK 290 SMTRY3 2 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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 MET A 1
REMARK 465 LYS A 39
REMARK 465 ILE A 40
REMARK 465 GLY A 41
REMARK 465 GLU A 42
REMARK 465 THR A 43
REMARK 465 HIS A 44
REMARK 465 GLU A 45
REMARK 465 GLY A 46
REMARK 465 ALA A 47
REMARK 465 SER A 48
REMARK 465 GLN A 49
REMARK 465 MET A 50
REMARK 465 ASP A 51
REMARK 465 TRP A 52
REMARK 465 MET A 53
REMARK 465 GLU A 54
REMARK 465 GLN A 55
REMARK 465 GLU A 56
REMARK 465 GLN A 57
REMARK 465 ASP A 58
REMARK 465 ARG A 59
REMARK 465 GLY A 60
REMARK 465 ILE A 61
REMARK 465 THR A 62
REMARK 465 ILE A 63
REMARK 465 ASP A 442
REMARK 465 GLU A 443
REMARK 465 GLU A 444
REMARK 465 MET B 1
REMARK 465 GLU B 42
REMARK 465 THR B 43
REMARK 465 HIS B 44
REMARK 465 GLU B 45
REMARK 465 GLN B 57
REMARK 465 ASP B 58
REMARK 465 ARG B 59
REMARK 465 GLY B 60
REMARK 465 ILE B 61
REMARK 465 THR B 62
REMARK 465 ILE B 63
REMARK 465 THR B 64
REMARK 465 ASP B 442
REMARK 465 GLU B 443
REMARK 465 GLU B 444
REMARK 465 THR B 445
REMARK 465 GLY B 446
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 ALA A 418 CB
REMARK 470 GLU A 693 CA C O CB CG CD OE1
REMARK 470 GLU A 693 OE2
REMARK 470 ALA B 418 CB
REMARK 470 GLU B 693 CA C O CB CG CD OE1
REMARK 470 GLU B 693 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 TYR A 254 CE2 TYR A 254 CD2 0.095
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 ASP A 272 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 629 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 659 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 659 NE - CZ - NH1 ANGL. DEV. = 3.0 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 GLU A 169 -135.77 60.09
REMARK 500 ASP A 202 0.28 -68.10
REMARK 500 ASP A 304 106.43 -169.53
REMARK 500 ASP A 395 39.38 -146.45
REMARK 500 ALA A 555 20.91 -143.59
REMARK 500 ASP A 673 -53.71 -121.85
REMARK 500 LYS B 9 32.50 -98.44
REMARK 500 GLU B 169 -136.19 62.80
REMARK 500 GLU B 173 -20.16 -143.40
REMARK 500 ASP B 304 105.53 -177.07
REMARK 500 ASP B 382 52.15 -153.35
REMARK 500 ARG B 498 -169.79 -126.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1694 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 78 OD1
REMARK 620 2 ASP A 373 OD1 118.7
REMARK 620 3 ILE A 374 N 84.1 96.7
REMARK 620 4 HOH A2018 O 81.6 158.1 93.1
REMARK 620 5 HOH A2141 O 125.9 58.7 147.0 103.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1694 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 78 OD1
REMARK 620 2 ASP B 373 OD1 114.2
REMARK 620 3 ILE B 374 N 82.9 93.7
REMARK 620 4 HOH B2016 O 84.4 160.5 94.6
REMARK 620 5 HOH B2021 O 122.4 61.1 149.0 104.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1694
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1694
DBREF 2XEX A 1 693 UNP P68790 EFG_STAAU 1 693
DBREF 2XEX B 1 693 UNP P68790 EFG_STAAU 1 693
SEQRES 1 A 693 MET ALA ARG GLU PHE SER LEU GLU LYS THR ARG ASN ILE
SEQRES 2 A 693 GLY ILE MET ALA HIS ILE ASP ALA GLY LYS THR THR THR
SEQRES 3 A 693 THR GLU ARG ILE LEU TYR TYR THR GLY ARG ILE HIS LYS
SEQRES 4 A 693 ILE GLY GLU THR HIS GLU GLY ALA SER GLN MET ASP TRP
SEQRES 5 A 693 MET GLU GLN GLU GLN ASP ARG GLY ILE THR ILE THR SER
SEQRES 6 A 693 ALA ALA THR THR ALA ALA TRP GLU GLY HIS ARG VAL ASN
SEQRES 7 A 693 ILE ILE ASP THR PRO GLY HIS VAL ASP PHE THR VAL GLU
SEQRES 8 A 693 VAL GLU ARG SER LEU ARG VAL LEU ASP GLY ALA VAL THR
SEQRES 9 A 693 VAL LEU ASP ALA GLN SER GLY VAL GLU PRO GLN THR GLU
SEQRES 10 A 693 THR VAL TRP ARG GLN ALA THR THR TYR GLY VAL PRO ARG
SEQRES 11 A 693 ILE VAL PHE VAL ASN LYS MET ASP LYS LEU GLY ALA ASN
SEQRES 12 A 693 PHE GLU TYR SER VAL SER THR LEU HIS ASP ARG LEU GLN
SEQRES 13 A 693 ALA ASN ALA ALA PRO ILE GLN LEU PRO ILE GLY ALA GLU
SEQRES 14 A 693 ASP GLU PHE GLU ALA ILE ILE ASP LEU VAL GLU MET LYS
SEQRES 15 A 693 CYS PHE LYS TYR THR ASN ASP LEU GLY THR GLU ILE GLU
SEQRES 16 A 693 GLU ILE GLU ILE PRO GLU ASP HIS LEU ASP ARG ALA GLU
SEQRES 17 A 693 GLU ALA ARG ALA SER LEU ILE GLU ALA VAL ALA GLU THR
SEQRES 18 A 693 SER ASP GLU LEU MET GLU LYS TYR LEU GLY ASP GLU GLU
SEQRES 19 A 693 ILE SER VAL SER GLU LEU LYS GLU ALA ILE ARG GLN ALA
SEQRES 20 A 693 THR THR ASN VAL GLU PHE TYR PRO VAL LEU CYS GLY THR
SEQRES 21 A 693 ALA PHE LYS ASN LYS GLY VAL GLN LEU MET LEU ASP ALA
SEQRES 22 A 693 VAL ILE ASP TYR LEU PRO SER PRO LEU ASP VAL LYS PRO
SEQRES 23 A 693 ILE ILE GLY HIS ARG ALA SER ASN PRO GLU GLU GLU VAL
SEQRES 24 A 693 ILE ALA LYS ALA ASP ASP SER ALA GLU PHE ALA ALA LEU
SEQRES 25 A 693 ALA PHE LYS VAL MET THR ASP PRO TYR VAL GLY LYS LEU
SEQRES 26 A 693 THR PHE PHE ARG VAL TYR SER GLY THR MET THR SER GLY
SEQRES 27 A 693 SER TYR VAL LYS ASN SER THR LYS GLY LYS ARG GLU ARG
SEQRES 28 A 693 VAL GLY ARG LEU LEU GLN MET HIS ALA ASN SER ARG GLN
SEQRES 29 A 693 GLU ILE ASP THR VAL TYR SER GLY ASP ILE ALA ALA ALA
SEQRES 30 A 693 VAL GLY LEU LYS ASP THR GLY THR GLY ASP THR LEU CYS
SEQRES 31 A 693 GLY GLU LYS ASN ASP ILE ILE LEU GLU SER MET GLU PHE
SEQRES 32 A 693 PRO GLU PRO VAL ILE HIS LEU SER VAL GLU PRO LYS SER
SEQRES 33 A 693 LYS ALA ASP GLN ASP LYS MET THR GLN ALA LEU VAL LYS
SEQRES 34 A 693 LEU GLN GLU GLU ASP PRO THR PHE HIS ALA HIS THR ASP
SEQRES 35 A 693 GLU GLU THR GLY GLN VAL ILE ILE GLY GLY MET GLY GLU
SEQRES 36 A 693 LEU HIS LEU ASP ILE LEU VAL ASP ARG MET LYS LYS GLU
SEQRES 37 A 693 PHE ASN VAL GLU CYS ASN VAL GLY ALA PRO MET VAL SER
SEQRES 38 A 693 TYR ARG GLU THR PHE LYS SER SER ALA GLN VAL GLN GLY
SEQRES 39 A 693 LYS PHE SER ARG GLN SER GLY GLY ARG GLY GLN TYR GLY
SEQRES 40 A 693 ASP VAL HIS ILE GLU PHE THR PRO ASN GLU THR GLY ALA
SEQRES 41 A 693 GLY PHE GLU PHE GLU ASN ALA ILE VAL GLY GLY VAL VAL
SEQRES 42 A 693 PRO ARG GLU TYR ILE PRO SER VAL GLU ALA GLY LEU LYS
SEQRES 43 A 693 ASP ALA MET GLU ASN GLY VAL LEU ALA GLY TYR PRO LEU
SEQRES 44 A 693 ILE ASP VAL LYS ALA LYS LEU TYR ASP GLY SER TYR HIS
SEQRES 45 A 693 ASP VAL ASP SER SER GLU MET ALA PHE LYS ILE ALA ALA
SEQRES 46 A 693 SER LEU ALA LEU LYS GLU ALA ALA LYS LYS CYS ASP PRO
SEQRES 47 A 693 VAL ILE LEU GLU PRO MET MET LYS VAL THR ILE GLU MET
SEQRES 48 A 693 PRO GLU GLU TYR MET GLY ASP ILE MET GLY ASP VAL THR
SEQRES 49 A 693 SER ARG ARG GLY ARG VAL ASP GLY MET GLU PRO ARG GLY
SEQRES 50 A 693 ASN ALA GLN VAL VAL ASN ALA TYR VAL PRO LEU SER GLU
SEQRES 51 A 693 MET PHE GLY TYR ALA THR SER LEU ARG SER ASN THR GLN
SEQRES 52 A 693 GLY ARG GLY THR TYR THR MET TYR PHE ASP HIS TYR ALA
SEQRES 53 A 693 GLU VAL PRO LYS SER ILE ALA GLU ASP ILE ILE LYS LYS
SEQRES 54 A 693 ASN LYS GLY GLU
SEQRES 1 B 693 MET ALA ARG GLU PHE SER LEU GLU LYS THR ARG ASN ILE
SEQRES 2 B 693 GLY ILE MET ALA HIS ILE ASP ALA GLY LYS THR THR THR
SEQRES 3 B 693 THR GLU ARG ILE LEU TYR TYR THR GLY ARG ILE HIS LYS
SEQRES 4 B 693 ILE GLY GLU THR HIS GLU GLY ALA SER GLN MET ASP TRP
SEQRES 5 B 693 MET GLU GLN GLU GLN ASP ARG GLY ILE THR ILE THR SER
SEQRES 6 B 693 ALA ALA THR THR ALA ALA TRP GLU GLY HIS ARG VAL ASN
SEQRES 7 B 693 ILE ILE ASP THR PRO GLY HIS VAL ASP PHE THR VAL GLU
SEQRES 8 B 693 VAL GLU ARG SER LEU ARG VAL LEU ASP GLY ALA VAL THR
SEQRES 9 B 693 VAL LEU ASP ALA GLN SER GLY VAL GLU PRO GLN THR GLU
SEQRES 10 B 693 THR VAL TRP ARG GLN ALA THR THR TYR GLY VAL PRO ARG
SEQRES 11 B 693 ILE VAL PHE VAL ASN LYS MET ASP LYS LEU GLY ALA ASN
SEQRES 12 B 693 PHE GLU TYR SER VAL SER THR LEU HIS ASP ARG LEU GLN
SEQRES 13 B 693 ALA ASN ALA ALA PRO ILE GLN LEU PRO ILE GLY ALA GLU
SEQRES 14 B 693 ASP GLU PHE GLU ALA ILE ILE ASP LEU VAL GLU MET LYS
SEQRES 15 B 693 CYS PHE LYS TYR THR ASN ASP LEU GLY THR GLU ILE GLU
SEQRES 16 B 693 GLU ILE GLU ILE PRO GLU ASP HIS LEU ASP ARG ALA GLU
SEQRES 17 B 693 GLU ALA ARG ALA SER LEU ILE GLU ALA VAL ALA GLU THR
SEQRES 18 B 693 SER ASP GLU LEU MET GLU LYS TYR LEU GLY ASP GLU GLU
SEQRES 19 B 693 ILE SER VAL SER GLU LEU LYS GLU ALA ILE ARG GLN ALA
SEQRES 20 B 693 THR THR ASN VAL GLU PHE TYR PRO VAL LEU CYS GLY THR
SEQRES 21 B 693 ALA PHE LYS ASN LYS GLY VAL GLN LEU MET LEU ASP ALA
SEQRES 22 B 693 VAL ILE ASP TYR LEU PRO SER PRO LEU ASP VAL LYS PRO
SEQRES 23 B 693 ILE ILE GLY HIS ARG ALA SER ASN PRO GLU GLU GLU VAL
SEQRES 24 B 693 ILE ALA LYS ALA ASP ASP SER ALA GLU PHE ALA ALA LEU
SEQRES 25 B 693 ALA PHE LYS VAL MET THR ASP PRO TYR VAL GLY LYS LEU
SEQRES 26 B 693 THR PHE PHE ARG VAL TYR SER GLY THR MET THR SER GLY
SEQRES 27 B 693 SER TYR VAL LYS ASN SER THR LYS GLY LYS ARG GLU ARG
SEQRES 28 B 693 VAL GLY ARG LEU LEU GLN MET HIS ALA ASN SER ARG GLN
SEQRES 29 B 693 GLU ILE ASP THR VAL TYR SER GLY ASP ILE ALA ALA ALA
SEQRES 30 B 693 VAL GLY LEU LYS ASP THR GLY THR GLY ASP THR LEU CYS
SEQRES 31 B 693 GLY GLU LYS ASN ASP ILE ILE LEU GLU SER MET GLU PHE
SEQRES 32 B 693 PRO GLU PRO VAL ILE HIS LEU SER VAL GLU PRO LYS SER
SEQRES 33 B 693 LYS ALA ASP GLN ASP LYS MET THR GLN ALA LEU VAL LYS
SEQRES 34 B 693 LEU GLN GLU GLU ASP PRO THR PHE HIS ALA HIS THR ASP
SEQRES 35 B 693 GLU GLU THR GLY GLN VAL ILE ILE GLY GLY MET GLY GLU
SEQRES 36 B 693 LEU HIS LEU ASP ILE LEU VAL ASP ARG MET LYS LYS GLU
SEQRES 37 B 693 PHE ASN VAL GLU CYS ASN VAL GLY ALA PRO MET VAL SER
SEQRES 38 B 693 TYR ARG GLU THR PHE LYS SER SER ALA GLN VAL GLN GLY
SEQRES 39 B 693 LYS PHE SER ARG GLN SER GLY GLY ARG GLY GLN TYR GLY
SEQRES 40 B 693 ASP VAL HIS ILE GLU PHE THR PRO ASN GLU THR GLY ALA
SEQRES 41 B 693 GLY PHE GLU PHE GLU ASN ALA ILE VAL GLY GLY VAL VAL
SEQRES 42 B 693 PRO ARG GLU TYR ILE PRO SER VAL GLU ALA GLY LEU LYS
SEQRES 43 B 693 ASP ALA MET GLU ASN GLY VAL LEU ALA GLY TYR PRO LEU
SEQRES 44 B 693 ILE ASP VAL LYS ALA LYS LEU TYR ASP GLY SER TYR HIS
SEQRES 45 B 693 ASP VAL ASP SER SER GLU MET ALA PHE LYS ILE ALA ALA
SEQRES 46 B 693 SER LEU ALA LEU LYS GLU ALA ALA LYS LYS CYS ASP PRO
SEQRES 47 B 693 VAL ILE LEU GLU PRO MET MET LYS VAL THR ILE GLU MET
SEQRES 48 B 693 PRO GLU GLU TYR MET GLY ASP ILE MET GLY ASP VAL THR
SEQRES 49 B 693 SER ARG ARG GLY ARG VAL ASP GLY MET GLU PRO ARG GLY
SEQRES 50 B 693 ASN ALA GLN VAL VAL ASN ALA TYR VAL PRO LEU SER GLU
SEQRES 51 B 693 MET PHE GLY TYR ALA THR SER LEU ARG SER ASN THR GLN
SEQRES 52 B 693 GLY ARG GLY THR TYR THR MET TYR PHE ASP HIS TYR ALA
SEQRES 53 B 693 GLU VAL PRO LYS SER ILE ALA GLU ASP ILE ILE LYS LYS
SEQRES 54 B 693 ASN LYS GLY GLU
HET K A1694 1
HET CL A1693 1
HET K B1694 1
HET CL B1693 1
HETNAM K POTASSIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 K 2(K 1+)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *509(H2 O)
HELIX 1 1 HIS A 18 ALA A 21 5 4
HELIX 2 2 GLY A 22 GLY A 35 1 14
HELIX 3 3 THR A 89 LEU A 99 1 11
HELIX 4 4 GLU A 113 TYR A 126 1 14
HELIX 5 5 ASN A 143 GLN A 156 1 14
HELIX 6 6 ALA A 168 PHE A 172 5 5
HELIX 7 7 PRO A 200 ASP A 202 5 3
HELIX 8 8 HIS A 203 GLU A 220 1 18
HELIX 9 9 SER A 222 GLY A 231 1 10
HELIX 10 10 SER A 236 ASN A 250 1 15
HELIX 11 11 GLY A 266 LEU A 278 1 13
HELIX 12 12 SER A 280 VAL A 284 5 5
HELIX 13 13 SER A 416 ASP A 434 1 19
HELIX 14 14 GLY A 454 PHE A 469 1 16
HELIX 15 15 PRO A 534 GLU A 536 5 3
HELIX 16 16 TYR A 537 ASN A 551 1 15
HELIX 17 17 SER A 577 LYS A 594 1 18
HELIX 18 18 TYR A 615 ARG A 626 1 12
HELIX 19 19 SER A 649 MET A 651 5 3
HELIX 20 20 GLY A 653 THR A 662 1 10
HELIX 21 21 PRO A 679 LYS A 691 1 13
HELIX 22 22 ILE B 19 ALA B 21 5 3
HELIX 23 23 GLY B 22 THR B 34 1 13
HELIX 24 24 GLY B 46 ASP B 51 5 6
HELIX 25 25 THR B 89 LEU B 99 1 11
HELIX 26 26 GLU B 113 TYR B 126 1 14
HELIX 27 27 ASN B 143 GLN B 156 1 14
HELIX 28 28 ALA B 168 PHE B 172 5 5
HELIX 29 29 PRO B 200 GLU B 220 1 21
HELIX 30 30 SER B 222 GLY B 231 1 10
HELIX 31 31 SER B 236 ASN B 250 1 15
HELIX 32 32 GLY B 266 LEU B 278 1 13
HELIX 33 33 SER B 416 ASP B 434 1 19
HELIX 34 34 GLY B 454 GLU B 468 1 15
HELIX 35 35 PRO B 534 GLU B 536 5 3
HELIX 36 36 TYR B 537 ASN B 551 1 15
HELIX 37 37 SER B 577 LYS B 594 1 18
HELIX 38 38 TYR B 615 ARG B 626 1 12
HELIX 39 39 SER B 649 MET B 651 5 3
HELIX 40 40 GLY B 653 THR B 662 1 10
HELIX 41 41 PRO B 679 LYS B 691 1 13
SHEET 1 AA 7 ALA A 67 TRP A 72 0
SHEET 2 AA 7 HIS A 75 ILE A 80 -1 O HIS A 75 N TRP A 72
SHEET 3 AA 7 THR A 10 MET A 16 1 O ARG A 11 N ASN A 78
SHEET 4 AA 7 GLY A 101 ASP A 107 1 O GLY A 101 N GLY A 14
SHEET 5 AA 7 ARG A 130 ASN A 135 1 O ILE A 131 N THR A 104
SHEET 6 AA 7 TYR A 254 CYS A 258 1 O PRO A 255 N VAL A 132
SHEET 7 AA 7 ALA A 159 PRO A 161 1 O ALA A 160 N VAL A 256
SHEET 1 AB 4 GLN A 163 ILE A 166 0
SHEET 2 AB 4 ALA A 174 ASP A 177 -1 O ALA A 174 N ILE A 166
SHEET 3 AB 4 LYS A 182 LYS A 185 -1 O LYS A 182 N ASP A 177
SHEET 4 AB 4 GLU A 195 ILE A 197 -1 O GLU A 195 N LYS A 185
SHEET 1 AC 3 ASN A 294 ALA A 301 0
SHEET 2 AC 3 ILE A 287 ARG A 291 -1 O ILE A 287 N ALA A 301
SHEET 3 AC 3 ILE A 396 ILE A 397 -1 O ILE A 397 N HIS A 290
SHEET 1 AD 8 LYS A 348 VAL A 352 0
SHEET 2 AD 8 SER A 339 ASN A 343 -1 O SER A 339 N VAL A 352
SHEET 3 AD 8 THR A 388 GLY A 391 -1 O CYS A 390 N LYS A 342
SHEET 4 AD 8 ALA A 310 ASP A 319 -1 O ALA A 311 N LEU A 389
SHEET 5 AD 8 GLY A 323 SER A 332 -1 O GLY A 323 N ASP A 319
SHEET 6 AD 8 ILE A 374 VAL A 378 -1 O ALA A 375 N PHE A 328
SHEET 7 AD 8 LEU A 355 MET A 358 -1 O LEU A 356 N ALA A 376
SHEET 8 AD 8 ARG A 363 GLU A 365 -1 O GLN A 364 N GLN A 357
SHEET 1 AE 2 THR A 334 THR A 336 0
SHEET 2 AE 2 THR A 368 TYR A 370 -1 O VAL A 369 N MET A 335
SHEET 1 AF 4 HIS A 438 HIS A 440 0
SHEET 2 AF 4 VAL A 448 GLY A 452 -1 O ILE A 449 N HIS A 440
SHEET 3 AF 4 ILE A 408 PRO A 414 -1 O ILE A 408 N GLY A 452
SHEET 4 AF 4 CYS A 473 VAL A 475 -1 O ASN A 474 N GLU A 413
SHEET 1 AG 4 HIS A 438 HIS A 440 0
SHEET 2 AG 4 VAL A 448 GLY A 452 -1 O ILE A 449 N HIS A 440
SHEET 3 AG 4 ILE A 408 PRO A 414 -1 O ILE A 408 N GLY A 452
SHEET 4 AG 4 MET A 479 VAL A 480 -1 O MET A 479 N HIS A 409
SHEET 1 AH 2 CYS A 473 VAL A 475 0
SHEET 2 AH 2 ILE A 408 PRO A 414 -1 O GLU A 413 N ASN A 474
SHEET 1 AI 2 ARG A 483 PHE A 486 0
SHEET 2 AI 2 PRO A 598 PRO A 612 1 O VAL A 599 N THR A 485
SHEET 1 AJ 4 ARG A 629 ARG A 636 0
SHEET 2 AJ 4 ALA A 639 PRO A 647 -1 O ALA A 639 N ARG A 636
SHEET 3 AJ 4 PRO A 598 PRO A 612 -1 O MET A 605 N VAL A 646
SHEET 4 AJ 4 THR A 667 GLU A 677 -1 O THR A 667 N GLU A 610
SHEET 1 AK 4 ARG A 629 ARG A 636 0
SHEET 2 AK 4 ALA A 639 PRO A 647 -1 O ALA A 639 N ARG A 636
SHEET 3 AK 4 PRO A 598 PRO A 612 -1 O MET A 605 N VAL A 646
SHEET 4 AK 4 ARG A 483 PHE A 486 1 O ARG A 483 N LEU A 601
SHEET 1 AL 2 THR A 667 GLU A 677 0
SHEET 2 AL 2 PRO A 598 PRO A 612 -1 O GLU A 602 N ALA A 676
SHEET 1 AM 4 ALA A 490 ARG A 498 0
SHEET 2 AM 4 GLN A 505 PRO A 515 -1 O GLN A 505 N ARG A 498
SHEET 3 AM 4 VAL A 562 SER A 570 -1 O LYS A 563 N THR A 514
SHEET 4 AM 4 GLU A 523 ASN A 526 1 O GLU A 523 N ALA A 564
SHEET 1 BA 7 ALA B 67 TRP B 72 0
SHEET 2 BA 7 HIS B 75 ILE B 80 -1 O HIS B 75 N TRP B 72
SHEET 3 BA 7 THR B 10 ALA B 17 1 O ARG B 11 N ASN B 78
SHEET 4 BA 7 GLY B 101 ASP B 107 1 O GLY B 101 N GLY B 14
SHEET 5 BA 7 ARG B 130 ASN B 135 1 O ILE B 131 N THR B 104
SHEET 6 BA 7 TYR B 254 CYS B 258 1 O PRO B 255 N VAL B 132
SHEET 7 BA 7 ALA B 159 PRO B 161 1 O ALA B 160 N VAL B 256
SHEET 1 BB 4 GLN B 163 ILE B 166 0
SHEET 2 BB 4 ALA B 174 ASP B 177 -1 O ALA B 174 N ILE B 166
SHEET 3 BB 4 LYS B 182 LYS B 185 -1 O LYS B 182 N ASP B 177
SHEET 4 BB 4 GLU B 195 ILE B 197 -1 O GLU B 195 N LYS B 185
SHEET 1 BC 2 ILE B 287 HIS B 290 0
SHEET 2 BC 2 GLU B 298 ALA B 301 -1 O VAL B 299 N GLY B 289
SHEET 1 BD 8 LYS B 348 ARG B 351 0
SHEET 2 BD 8 TYR B 340 ASN B 343 -1 O VAL B 341 N GLU B 350
SHEET 3 BD 8 THR B 388 CYS B 390 -1 O CYS B 390 N LYS B 342
SHEET 4 BD 8 ALA B 310 ASP B 319 -1 O ALA B 311 N LEU B 389
SHEET 5 BD 8 GLY B 323 SER B 332 -1 O GLY B 323 N ASP B 319
SHEET 6 BD 8 ILE B 374 VAL B 378 -1 O ALA B 375 N PHE B 328
SHEET 7 BD 8 LEU B 355 HIS B 359 -1 O LEU B 356 N ALA B 376
SHEET 8 BD 8 SER B 362 GLU B 365 -1 O SER B 362 N HIS B 359
SHEET 1 BE 2 THR B 334 THR B 336 0
SHEET 2 BE 2 THR B 368 TYR B 370 -1 O VAL B 369 N MET B 335
SHEET 1 BF 4 HIS B 438 HIS B 440 0
SHEET 2 BF 4 VAL B 448 GLY B 452 -1 O ILE B 449 N HIS B 440
SHEET 3 BF 4 ILE B 408 PRO B 414 -1 O ILE B 408 N GLY B 452
SHEET 4 BF 4 CYS B 473 VAL B 475 -1 O ASN B 474 N GLU B 413
SHEET 1 BG 4 HIS B 438 HIS B 440 0
SHEET 2 BG 4 VAL B 448 GLY B 452 -1 O ILE B 449 N HIS B 440
SHEET 3 BG 4 ILE B 408 PRO B 414 -1 O ILE B 408 N GLY B 452
SHEET 4 BG 4 MET B 479 VAL B 480 -1 O MET B 479 N HIS B 409
SHEET 1 BH 2 CYS B 473 VAL B 475 0
SHEET 2 BH 2 ILE B 408 PRO B 414 -1 O GLU B 413 N ASN B 474
SHEET 1 BI 2 ARG B 483 PHE B 486 0
SHEET 2 BI 2 PRO B 598 PRO B 612 1 O VAL B 599 N THR B 485
SHEET 1 BJ 4 ARG B 629 ARG B 636 0
SHEET 2 BJ 4 ALA B 639 PRO B 647 -1 O ALA B 639 N ARG B 636
SHEET 3 BJ 4 PRO B 598 PRO B 612 -1 O MET B 605 N VAL B 646
SHEET 4 BJ 4 THR B 667 GLU B 677 -1 O THR B 667 N GLU B 610
SHEET 1 BK 4 ARG B 629 ARG B 636 0
SHEET 2 BK 4 ALA B 639 PRO B 647 -1 O ALA B 639 N ARG B 636
SHEET 3 BK 4 PRO B 598 PRO B 612 -1 O MET B 605 N VAL B 646
SHEET 4 BK 4 ARG B 483 PHE B 486 1 O ARG B 483 N LEU B 601
SHEET 1 BL 2 THR B 667 GLU B 677 0
SHEET 2 BL 2 PRO B 598 PRO B 612 -1 O GLU B 602 N ALA B 676
SHEET 1 BM 4 ALA B 490 ARG B 498 0
SHEET 2 BM 4 GLN B 505 PRO B 515 -1 O GLN B 505 N ARG B 498
SHEET 3 BM 4 VAL B 562 SER B 570 -1 O LYS B 563 N THR B 514
SHEET 4 BM 4 GLU B 523 ASN B 526 1 O GLU B 523 N ALA B 564
LINK OD1 ASN A 78 K K A1694 1555 1555 3.07
LINK OD1 ASP A 373 K K A1694 1555 1555 2.85
LINK N ILE A 374 K K A1694 1555 1555 3.05
LINK K K A1694 O HOH A2018 1555 1555 2.93
LINK K K A1694 O HOH A2141 1555 1555 3.06
LINK OD1 ASN B 78 K K B1694 1555 1555 3.14
LINK OD1 ASP B 373 K K B1694 1555 1555 2.96
LINK N ILE B 374 K K B1694 1555 1555 3.16
LINK K K B1694 O HOH B2016 1555 1555 2.84
LINK K K B1694 O HOH B2021 1555 1555 3.16
CISPEP 1 SER A 500 GLY A 501 0 -4.12
CISPEP 2 SER B 500 GLY B 501 0 -1.91
SITE 1 AC1 4 TYR A 186 GLY A 266 GLN A 268 LEU A 269
SITE 1 AC2 4 TYR B 186 GLY B 266 GLN B 268 LEU B 269
SITE 1 AC3 6 ASN A 78 GLN A 357 ASP A 373 ILE A 374
SITE 2 AC3 6 HOH A2018 HOH A2141
SITE 1 AC4 5 ASN B 78 GLN B 357 ASP B 373 ILE B 374
SITE 2 AC4 5 HOH B2016
CRYST1 47.160 137.340 125.360 90.00 94.93 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 0.021204 0.000000 0.001829 0.00000
SCALE2 0.000000 0.007281 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008007 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
