HEADER TRANSFERASE 06-DEC-16 5WSC
TITLE CRYSTAL OF PYRUVATE KINASE (PYK) FROM MYCOBACTERIUM TUBERCULOSIS IN
TITLE 2 COMPLEX WITH OXALATE, SOAKED WITH ALLOSTERIC ACTIVATORS AMP AND
TITLE 3 GLUCOSE 6-PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PK;
COMPND 5 EC: 2.7.1.40;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: PYK, PYKA, RV1617, MTCY01B2.09;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PYUB28B-TEV
KEYWDS PYRUVATE KINASE, GLYCOLYSIS, TETRAMER, ALLOSTERY, SYNERGISM, PHOSPHO
KEYWDS 2 TRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.ZHONG,Q.CAI,A.EL SAHILI,J.LESCAR,P.C.DEDON
REVDAT 4 08-NOV-23 5WSC 1 HETSYN
REVDAT 3 29-JUL-20 5WSC 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 10-JAN-18 5WSC 1 JRNL
REVDAT 1 15-NOV-17 5WSC 0
JRNL AUTH W.ZHONG,L.CUI,B.C.GOH,Q.CAI,P.HO,Y.H.CHIONH,M.YUAN,
JRNL AUTH 2 A.E.SAHILI,L.A.FOTHERGILL-GILMORE,M.D.WALKINSHAW,J.LESCAR,
JRNL AUTH 3 P.C.DEDON
JRNL TITL ALLOSTERIC PYRUVATE KINASE-BASED "LOGIC GATE"
JRNL TITL 2 SYNERGISTICALLY SENSES ENERGY AND SUGAR LEVELS IN
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS.
JRNL REF NAT COMMUN V. 8 1986 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29215013
JRNL DOI 10.1038/S41467-017-02086-Y
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 92706
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4790
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6814
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.4250
REMARK 3 BIN FREE R VALUE SET COUNT : 313
REMARK 3 BIN FREE R VALUE : 0.4640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 195
REMARK 3 SOLVENT ATOMS : 335
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.11000
REMARK 3 B22 (A**2) : 10.11000
REMARK 3 B33 (A**2) : -20.23000
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): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.792
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14564 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 14068 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19804 ; 1.528 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 32420 ; 0.714 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1880 ; 6.659 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 592 ;32.666 ;23.243
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2448 ;17.274 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 148 ;20.432 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2380 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16168 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2808 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7532 ; 1.579 ; 1.976
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7531 ; 1.579 ; 1.976
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9408 ; 2.115 ; 2.962
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 9409 ; 2.114 ; 2.962
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7032 ; 1.589 ; 2.022
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7004 ; 1.583 ; 2.020
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 10361 ; 2.088 ; 3.011
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 61662 ; 2.773 ;38.063
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 61509 ; 2.771 ;38.057
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 472 B 2 472 29524 0.08 0.05
REMARK 3 2 A 2 472 C 2 472 29190 0.08 0.05
REMARK 3 3 A 2 472 D 2 472 29166 0.08 0.05
REMARK 3 4 B 2 472 C 2 472 29216 0.09 0.05
REMARK 3 5 B 2 472 D 2 472 29106 0.09 0.05
REMARK 3 6 C 2 472 D 2 472 29398 0.07 0.05
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 4
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.245
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -K, -H, -L
REMARK 3 TWIN FRACTION : 0.248
REMARK 3 TWIN DOMAIN : 3
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.254
REMARK 3 TWIN DOMAIN : 4
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.253
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 70
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8879 -52.5944 30.9786
REMARK 3 T TENSOR
REMARK 3 T11: 0.0878 T22: 0.0788
REMARK 3 T33: 0.1342 T12: 0.0335
REMARK 3 T13: -0.0231 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 0.4484 L22: 0.1862
REMARK 3 L33: 1.1627 L12: -0.1431
REMARK 3 L13: 0.4803 L23: -0.2711
REMARK 3 S TENSOR
REMARK 3 S11: 0.0756 S12: 0.0609 S13: -0.0379
REMARK 3 S21: -0.0237 S22: -0.1058 S23: -0.1182
REMARK 3 S31: 0.0661 S32: 0.1209 S33: 0.0301
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 71 A 167
REMARK 3 ORIGIN FOR THE GROUP (A): -28.4073 -72.3047 8.6781
REMARK 3 T TENSOR
REMARK 3 T11: 0.0716 T22: 0.0415
REMARK 3 T33: 0.0734 T12: 0.0096
REMARK 3 T13: -0.0124 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.0656 L22: 1.1113
REMARK 3 L33: 1.7526 L12: 0.1478
REMARK 3 L13: -0.2440 L23: -0.6852
REMARK 3 S TENSOR
REMARK 3 S11: 0.0644 S12: 0.1278 S13: 0.0521
REMARK 3 S21: -0.1213 S22: -0.0355 S23: 0.0619
REMARK 3 S31: 0.0783 S32: -0.0332 S33: -0.0288
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 168 A 344
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2505 -48.8801 19.8666
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.0280
REMARK 3 T33: 0.0058 T12: 0.0455
REMARK 3 T13: -0.0198 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.8700 L22: 0.7335
REMARK 3 L33: 0.8391 L12: 0.1021
REMARK 3 L13: -0.0340 L23: -0.1246
REMARK 3 S TENSOR
REMARK 3 S11: 0.0418 S12: 0.0086 S13: -0.0009
REMARK 3 S21: -0.0262 S22: -0.0330 S23: 0.0331
REMARK 3 S31: -0.0003 S32: -0.0383 S33: -0.0089
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 345 A 467
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6821 -27.8951 35.0214
REMARK 3 T TENSOR
REMARK 3 T11: 0.0919 T22: 0.0438
REMARK 3 T33: 0.0339 T12: 0.0332
REMARK 3 T13: 0.0016 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.6733 L22: 1.7102
REMARK 3 L33: 1.4595 L12: -0.5889
REMARK 3 L13: 0.1019 L23: -0.4422
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: -0.1165 S13: 0.0471
REMARK 3 S21: 0.0817 S22: 0.0082 S23: -0.0996
REMARK 3 S31: -0.0564 S32: 0.0367 S33: 0.0054
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 : B 2 B 70
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6341 -50.1469 -17.4578
REMARK 3 T TENSOR
REMARK 3 T11: 0.1029 T22: 0.0474
REMARK 3 T33: 0.1974 T12: 0.0493
REMARK 3 T13: 0.0422 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.1769 L22: 0.9532
REMARK 3 L33: 1.0358 L12: 0.2721
REMARK 3 L13: 0.0834 L23: 0.4121
REMARK 3 S TENSOR
REMARK 3 S11: -0.0282 S12: 0.0174 S13: -0.1556
REMARK 3 S21: 0.0825 S22: 0.0341 S23: -0.0668
REMARK 3 S31: 0.1521 S32: -0.0093 S33: -0.0059
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 71 B 167
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7354 -47.3914 4.6598
REMARK 3 T TENSOR
REMARK 3 T11: 0.0669 T22: 0.0697
REMARK 3 T33: 0.0553 T12: 0.0129
REMARK 3 T13: -0.0025 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.1447 L22: 0.8481
REMARK 3 L33: 1.5769 L12: -0.4320
REMARK 3 L13: -0.4828 L23: 0.1243
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: -0.1007 S13: 0.0598
REMARK 3 S21: 0.1392 S22: -0.0186 S23: 0.0300
REMARK 3 S31: -0.0300 S32: 0.0921 S33: 0.0259
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 168 B 344
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7238 -39.3330 -6.4861
REMARK 3 T TENSOR
REMARK 3 T11: 0.0819 T22: 0.0320
REMARK 3 T33: 0.0046 T12: 0.0502
REMARK 3 T13: -0.0102 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 1.0027 L22: 0.6515
REMARK 3 L33: 0.9897 L12: 0.0560
REMARK 3 L13: -0.1250 L23: -0.0158
REMARK 3 S TENSOR
REMARK 3 S11: -0.0261 S12: 0.0006 S13: 0.0267
REMARK 3 S21: 0.0498 S22: 0.0210 S23: -0.0453
REMARK 3 S31: -0.0302 S32: 0.0068 S33: 0.0051
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 345 B 467
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1571 -29.2684 -21.6698
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.0715
REMARK 3 T33: 0.0374 T12: 0.0441
REMARK 3 T13: -0.0010 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.7552 L22: 1.3394
REMARK 3 L33: 1.3456 L12: -0.6632
REMARK 3 L13: -0.2878 L23: 0.3366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: 0.0977 S13: -0.0404
REMARK 3 S21: -0.1014 S22: 0.0059 S23: 0.0822
REMARK 3 S31: -0.0288 S32: -0.0731 S33: -0.0174
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 : C 2 C 70
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8689 16.0084 31.0264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1452 T22: 0.0622
REMARK 3 T33: 0.0626 T12: 0.0345
REMARK 3 T13: 0.0212 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.4002 L22: 0.3074
REMARK 3 L33: 1.3152 L12: 0.1934
REMARK 3 L13: -0.6330 L23: 0.4307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: -0.0451 S13: 0.2258
REMARK 3 S21: 0.0215 S22: -0.0913 S23: 0.1045
REMARK 3 S31: -0.0963 S32: -0.1414 S33: 0.0335
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 : C 71 C 167
REMARK 3 ORIGIN FOR THE GROUP (A): -35.4090 35.5013 8.2508
REMARK 3 T TENSOR
REMARK 3 T11: 0.1123 T22: 0.1174
REMARK 3 T33: 0.1296 T12: 0.0131
REMARK 3 T13: 0.0216 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 0.4144 L22: 0.4374
REMARK 3 L33: 1.1120 L12: 0.2113
REMARK 3 L13: 0.6055 L23: 0.0585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: 0.0514 S13: -0.0697
REMARK 3 S21: 0.1343 S22: 0.0320 S23: -0.0140
REMARK 3 S31: -0.0429 S32: 0.1264 S33: -0.0630
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 168 C 344
REMARK 3 ORIGIN FOR THE GROUP (A): -36.8972 12.1939 19.6231
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.0299
REMARK 3 T33: 0.0554 T12: 0.0242
REMARK 3 T13: 0.0350 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.4607 L22: 0.3819
REMARK 3 L33: 1.0716 L12: -0.2889
REMARK 3 L13: 0.2429 L23: 0.0657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: -0.0110 S13: 0.0445
REMARK 3 S21: 0.0147 S22: -0.0024 S23: -0.0680
REMARK 3 S31: -0.0467 S32: 0.0864 S33: -0.0009
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 345 C 467
REMARK 3 ORIGIN FOR THE GROUP (A): -36.9840 -8.5806 35.1322
REMARK 3 T TENSOR
REMARK 3 T11: 0.1189 T22: 0.0408
REMARK 3 T33: 0.0234 T12: 0.0239
REMARK 3 T13: 0.0127 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.5236 L22: 1.7237
REMARK 3 L33: 1.0357 L12: -0.5575
REMARK 3 L13: 0.1823 L23: -0.0652
REMARK 3 S TENSOR
REMARK 3 S11: 0.0330 S12: -0.0835 S13: -0.0075
REMARK 3 S21: 0.1499 S22: 0.0067 S23: 0.0712
REMARK 3 S31: 0.0196 S32: -0.0225 S33: -0.0397
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 70
REMARK 3 ORIGIN FOR THE GROUP (A): -52.6772 12.6752 -17.5493
REMARK 3 T TENSOR
REMARK 3 T11: 0.1032 T22: 0.0768
REMARK 3 T33: 0.0658 T12: 0.0511
REMARK 3 T13: 0.0036 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.5000 L22: 0.9169
REMARK 3 L33: 1.4781 L12: 0.4514
REMARK 3 L13: 0.2510 L23: -0.5980
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: 0.0003 S13: 0.1628
REMARK 3 S21: 0.0422 S22: 0.0046 S23: 0.1598
REMARK 3 S31: -0.1620 S32: -0.0308 S33: 0.0538
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 71 D 167
REMARK 3 ORIGIN FOR THE GROUP (A): -75.3291 12.3672 5.1331
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.0983
REMARK 3 T33: 0.0941 T12: 0.0170
REMARK 3 T13: 0.0289 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.5221 L22: 0.6666
REMARK 3 L33: 1.4345 L12: 0.2442
REMARK 3 L13: 0.1312 L23: 0.6564
REMARK 3 S TENSOR
REMARK 3 S11: 0.0639 S12: 0.1627 S13: -0.0267
REMARK 3 S21: -0.0657 S22: 0.0102 S23: -0.0610
REMARK 3 S31: 0.1028 S32: -0.1383 S33: -0.0741
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 168 D 344
REMARK 3 ORIGIN FOR THE GROUP (A): -54.3156 2.1462 -6.1934
REMARK 3 T TENSOR
REMARK 3 T11: 0.0664 T22: 0.0489
REMARK 3 T33: 0.0388 T12: 0.0417
REMARK 3 T13: 0.0315 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.5652 L22: 0.8539
REMARK 3 L33: 0.9986 L12: 0.0665
REMARK 3 L13: 0.3284 L23: 0.0283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: 0.0028 S13: -0.0322
REMARK 3 S21: 0.0049 S22: -0.0017 S23: 0.0821
REMARK 3 S31: 0.0487 S32: -0.0882 S33: 0.0079
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 345 D 467
REMARK 3 ORIGIN FOR THE GROUP (A): -36.3014 -8.2793 -21.7471
REMARK 3 T TENSOR
REMARK 3 T11: 0.0898 T22: 0.0609
REMARK 3 T33: 0.0197 T12: 0.0495
REMARK 3 T13: 0.0045 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.1790 L22: 1.3331
REMARK 3 L33: 1.1522 L12: -0.7082
REMARK 3 L13: -0.0039 L23: -0.0835
REMARK 3 S TENSOR
REMARK 3 S11: 0.0456 S12: 0.1547 S13: 0.0625
REMARK 3 S21: -0.1242 S22: -0.0336 S23: -0.0605
REMARK 3 S31: -0.0288 S32: 0.0389 S33: -0.0121
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5WSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1300002281.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95370
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 97539
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 53.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: 5WRP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 8000, 20% GLYCEROL, 50 MM
REMARK 280 TRIETHANOLAMINE-HCL (TEA) BUFFER PH 7.2, 100 MM KCL, 50 MM MGCL2,
REMARK 280 5 MM OXALATE, 5 MM ATP, 5 MM AMP, 5 MM D-GLUCOSE 6-PHOSPHATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.06400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 96.12800
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY C -2
REMARK 465 GLY C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLY D -2
REMARK 465 GLY D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 622 O HOH C 648 1.56
REMARK 500 O HOH B 655 O HOH B 671 1.61
REMARK 500 O HOH D 652 O HOH D 672 1.87
REMARK 500 OE1 GLU A 334 O HOH A 601 1.94
REMARK 500 NH1 ARG C 74 O1 PO4 C 505 1.96
REMARK 500 NE2 HIS C 38 O4 PO4 C 505 1.98
REMARK 500 O HOH B 671 O HOH B 677 2.01
REMARK 500 OG SER D 432 O HOH D 601 2.07
REMARK 500 O HOH C 644 O HOH C 672 2.13
REMARK 500 O4 OXL D 504 O HOH D 602 2.13
REMARK 500 O HOH D 621 O HOH D 627 2.18
REMARK 500 OE2 GLU B 223 O HOH B 601 2.18
REMARK 500 NZ LYS D 72 O HOH D 603 2.19
REMARK 500 NH2 ARG D 50 O HOH D 604 2.19
REMARK 500 OD1 ASP D 173 O HOH D 605 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 655 O HOH D 618 1545 1.56
REMARK 500 NZ LYS A 45 OE2 GLU B 99 2445 2.13
REMARK 500 O ASP B 18 NH1 ARG C 17 3444 2.15
REMARK 500 OD2 ASP B 19 NH1 ARG C 17 3444 2.16
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 ARG A 359 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 194 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 359 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 211 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 211 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG D 359 NE - CZ - NH2 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 PRO A 13 -39.46 -39.89
REMARK 500 ALA A 82 143.27 -170.16
REMARK 500 GLU A 220 26.23 -155.14
REMARK 500 ALA A 241 79.75 -100.91
REMARK 500 THR A 276 121.80 99.48
REMARK 500 SER A 310 -85.86 -110.55
REMARK 500 HIS A 387 145.47 47.89
REMARK 500 THR A 459 118.36 -37.32
REMARK 500 ASN A 460 15.46 -158.76
REMARK 500 ASP A 470 57.97 -91.03
REMARK 500 GLU B 220 24.71 -153.83
REMARK 500 ALA B 241 79.96 -101.17
REMARK 500 THR B 276 121.80 96.86
REMARK 500 SER B 310 -86.81 -110.34
REMARK 500 HIS B 387 147.09 48.88
REMARK 500 THR B 459 118.81 -37.40
REMARK 500 ASN B 460 13.76 -157.43
REMARK 500 ASP B 470 58.85 -92.42
REMARK 500 ALA C 166 149.93 -177.13
REMARK 500 GLU C 220 27.18 -154.71
REMARK 500 THR C 276 122.70 98.97
REMARK 500 SER C 310 -86.25 -110.17
REMARK 500 HIS C 387 151.46 44.77
REMARK 500 ASN C 460 14.47 -157.52
REMARK 500 ALA D 79 33.79 -90.52
REMARK 500 ASP D 126 25.44 49.25
REMARK 500 GLU D 220 28.21 -153.66
REMARK 500 THR D 276 124.62 98.83
REMARK 500 SER D 310 -86.76 -112.23
REMARK 500 HIS D 387 149.94 45.69
REMARK 500 THR D 459 119.48 -37.14
REMARK 500 ASN D 460 13.28 -157.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 2 ARG B 3 -149.83
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 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 220 OE1
REMARK 620 2 ASP A 244 OD2 93.1
REMARK 620 3 OXL A 504 O3 85.1 83.9
REMARK 620 4 OXL A 504 O4 95.7 157.6 76.4
REMARK 620 5 HOH A 604 O 85.7 117.1 157.5 84.1
REMARK 620 6 HOH A 629 O 165.9 78.2 83.0 88.8 108.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 505 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 35 OD1
REMARK 620 2 SER B 37 OG 65.6
REMARK 620 3 ASP B 67 OD1 101.1 146.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 220 OE1
REMARK 620 2 ASP B 244 OD2 96.6
REMARK 620 3 OXL B 504 O3 89.3 98.2
REMARK 620 4 OXL B 504 O4 93.2 169.1 77.1
REMARK 620 5 HOH B 629 O 80.2 88.8 168.0 97.5
REMARK 620 6 HOH B 664 O 173.3 90.1 90.4 80.2 99.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 220 OE1
REMARK 620 2 ASP C 244 OD2 108.8
REMARK 620 3 OXL C 504 O1 84.2 99.3
REMARK 620 4 OXL C 504 O2 96.2 150.6 67.4
REMARK 620 5 HOH C 604 O 80.5 104.2 155.1 94.8
REMARK 620 6 HOH C 613 O 160.7 90.2 89.6 64.6 98.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 220 OE1
REMARK 620 2 ASP D 244 OD2 102.3
REMARK 620 3 OXL D 504 O1 82.5 86.9
REMARK 620 4 OXL D 504 O4 90.8 153.2 71.5
REMARK 620 5 HOH D 602 O 89.6 143.5 129.1 58.4
REMARK 620 6 HOH D 633 O 158.5 90.1 80.6 71.2 90.7
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5WRP RELATED DB: PDB
REMARK 900 RELATED ID: 5WS8 RELATED DB: PDB
REMARK 900 RELATED ID: 5WS9 RELATED DB: PDB
REMARK 900 RELATED ID: 5WSA RELATED DB: PDB
REMARK 900 RELATED ID: 5WSB RELATED DB: PDB
DBREF 5WSC A 1 472 UNP P9WKE5 KPYK_MYCTU 1 472
DBREF 5WSC B 1 472 UNP P9WKE5 KPYK_MYCTU 1 472
DBREF 5WSC C 1 472 UNP P9WKE5 KPYK_MYCTU 1 472
DBREF 5WSC D 1 472 UNP P9WKE5 KPYK_MYCTU 1 472
SEQADV 5WSC GLY A -2 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC GLY A -1 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC HIS A 0 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC GLY B -2 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC GLY B -1 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC HIS B 0 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC GLY C -2 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC GLY C -1 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC HIS C 0 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC GLY D -2 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC GLY D -1 UNP P9WKE5 EXPRESSION TAG
SEQADV 5WSC HIS D 0 UNP P9WKE5 EXPRESSION TAG
SEQRES 1 A 475 GLY GLY HIS MET THR ARG ARG GLY LYS ILE VAL CYS THR
SEQRES 2 A 475 LEU GLY PRO ALA THR GLN ARG ASP ASP LEU VAL ARG ALA
SEQRES 3 A 475 LEU VAL GLU ALA GLY MET ASP VAL ALA ARG MET ASN PHE
SEQRES 4 A 475 SER HIS GLY ASP TYR ASP ASP HIS LYS VAL ALA TYR GLU
SEQRES 5 A 475 ARG VAL ARG VAL ALA SER ASP ALA THR GLY ARG ALA VAL
SEQRES 6 A 475 GLY VAL LEU ALA ASP LEU GLN GLY PRO LYS ILE ARG LEU
SEQRES 7 A 475 GLY ARG PHE ALA SER GLY ALA THR HIS TRP ALA GLU GLY
SEQRES 8 A 475 GLU THR VAL ARG ILE THR VAL GLY ALA CYS GLU GLY SER
SEQRES 9 A 475 HIS ASP ARG VAL SER THR THR TYR LYS ARG LEU ALA GLN
SEQRES 10 A 475 ASP ALA VAL ALA GLY ASP ARG VAL LEU VAL ASP ASP GLY
SEQRES 11 A 475 LYS VAL ALA LEU VAL VAL ASP ALA VAL GLU GLY ASP ASP
SEQRES 12 A 475 VAL VAL CYS THR VAL VAL GLU GLY GLY PRO VAL SER ASP
SEQRES 13 A 475 ASN LYS GLY ILE SER LEU PRO GLY MET ASN VAL THR ALA
SEQRES 14 A 475 PRO ALA LEU SER GLU LYS ASP ILE GLU ASP LEU THR PHE
SEQRES 15 A 475 ALA LEU ASN LEU GLY VAL ASP MET VAL ALA LEU SER PHE
SEQRES 16 A 475 VAL ARG SER PRO ALA ASP VAL GLU LEU VAL HIS GLU VAL
SEQRES 17 A 475 MET ASP ARG ILE GLY ARG ARG VAL PRO VAL ILE ALA LYS
SEQRES 18 A 475 LEU GLU LYS PRO GLU ALA ILE ASP ASN LEU GLU ALA ILE
SEQRES 19 A 475 VAL LEU ALA PHE ASP ALA VAL MET VAL ALA ARG GLY ASP
SEQRES 20 A 475 LEU GLY VAL GLU LEU PRO LEU GLU GLU VAL PRO LEU VAL
SEQRES 21 A 475 GLN LYS ARG ALA ILE GLN MET ALA ARG GLU ASN ALA LYS
SEQRES 22 A 475 PRO VAL ILE VAL ALA THR GLN MET LEU ASP SER MET ILE
SEQRES 23 A 475 GLU ASN SER ARG PRO THR ARG ALA GLU ALA SER ASP VAL
SEQRES 24 A 475 ALA ASN ALA VAL LEU ASP GLY ALA ASP ALA LEU MET LEU
SEQRES 25 A 475 SER GLY GLU THR SER VAL GLY LYS TYR PRO LEU ALA ALA
SEQRES 26 A 475 VAL ARG THR MET SER ARG ILE ILE CYS ALA VAL GLU GLU
SEQRES 27 A 475 ASN SER THR ALA ALA PRO PRO LEU THR HIS ILE PRO ARG
SEQRES 28 A 475 THR LYS ARG GLY VAL ILE SER TYR ALA ALA ARG ASP ILE
SEQRES 29 A 475 GLY GLU ARG LEU ASP ALA LYS ALA LEU VAL ALA PHE THR
SEQRES 30 A 475 GLN SER GLY ASP THR VAL ARG ARG LEU ALA ARG LEU HIS
SEQRES 31 A 475 THR PRO LEU PRO LEU LEU ALA PHE THR ALA TRP PRO GLU
SEQRES 32 A 475 VAL ARG SER GLN LEU ALA MET THR TRP GLY THR GLU THR
SEQRES 33 A 475 PHE ILE VAL PRO LYS MET GLN SER THR ASP GLY MET ILE
SEQRES 34 A 475 ARG GLN VAL ASP LYS SER LEU LEU GLU LEU ALA ARG TYR
SEQRES 35 A 475 LYS ARG GLY ASP LEU VAL VAL ILE VAL ALA GLY ALA PRO
SEQRES 36 A 475 PRO GLY THR VAL GLY SER THR ASN LEU ILE HIS VAL HIS
SEQRES 37 A 475 ARG ILE GLY GLU ASP ASP VAL
SEQRES 1 B 475 GLY GLY HIS MET THR ARG ARG GLY LYS ILE VAL CYS THR
SEQRES 2 B 475 LEU GLY PRO ALA THR GLN ARG ASP ASP LEU VAL ARG ALA
SEQRES 3 B 475 LEU VAL GLU ALA GLY MET ASP VAL ALA ARG MET ASN PHE
SEQRES 4 B 475 SER HIS GLY ASP TYR ASP ASP HIS LYS VAL ALA TYR GLU
SEQRES 5 B 475 ARG VAL ARG VAL ALA SER ASP ALA THR GLY ARG ALA VAL
SEQRES 6 B 475 GLY VAL LEU ALA ASP LEU GLN GLY PRO LYS ILE ARG LEU
SEQRES 7 B 475 GLY ARG PHE ALA SER GLY ALA THR HIS TRP ALA GLU GLY
SEQRES 8 B 475 GLU THR VAL ARG ILE THR VAL GLY ALA CYS GLU GLY SER
SEQRES 9 B 475 HIS ASP ARG VAL SER THR THR TYR LYS ARG LEU ALA GLN
SEQRES 10 B 475 ASP ALA VAL ALA GLY ASP ARG VAL LEU VAL ASP ASP GLY
SEQRES 11 B 475 LYS VAL ALA LEU VAL VAL ASP ALA VAL GLU GLY ASP ASP
SEQRES 12 B 475 VAL VAL CYS THR VAL VAL GLU GLY GLY PRO VAL SER ASP
SEQRES 13 B 475 ASN LYS GLY ILE SER LEU PRO GLY MET ASN VAL THR ALA
SEQRES 14 B 475 PRO ALA LEU SER GLU LYS ASP ILE GLU ASP LEU THR PHE
SEQRES 15 B 475 ALA LEU ASN LEU GLY VAL ASP MET VAL ALA LEU SER PHE
SEQRES 16 B 475 VAL ARG SER PRO ALA ASP VAL GLU LEU VAL HIS GLU VAL
SEQRES 17 B 475 MET ASP ARG ILE GLY ARG ARG VAL PRO VAL ILE ALA LYS
SEQRES 18 B 475 LEU GLU LYS PRO GLU ALA ILE ASP ASN LEU GLU ALA ILE
SEQRES 19 B 475 VAL LEU ALA PHE ASP ALA VAL MET VAL ALA ARG GLY ASP
SEQRES 20 B 475 LEU GLY VAL GLU LEU PRO LEU GLU GLU VAL PRO LEU VAL
SEQRES 21 B 475 GLN LYS ARG ALA ILE GLN MET ALA ARG GLU ASN ALA LYS
SEQRES 22 B 475 PRO VAL ILE VAL ALA THR GLN MET LEU ASP SER MET ILE
SEQRES 23 B 475 GLU ASN SER ARG PRO THR ARG ALA GLU ALA SER ASP VAL
SEQRES 24 B 475 ALA ASN ALA VAL LEU ASP GLY ALA ASP ALA LEU MET LEU
SEQRES 25 B 475 SER GLY GLU THR SER VAL GLY LYS TYR PRO LEU ALA ALA
SEQRES 26 B 475 VAL ARG THR MET SER ARG ILE ILE CYS ALA VAL GLU GLU
SEQRES 27 B 475 ASN SER THR ALA ALA PRO PRO LEU THR HIS ILE PRO ARG
SEQRES 28 B 475 THR LYS ARG GLY VAL ILE SER TYR ALA ALA ARG ASP ILE
SEQRES 29 B 475 GLY GLU ARG LEU ASP ALA LYS ALA LEU VAL ALA PHE THR
SEQRES 30 B 475 GLN SER GLY ASP THR VAL ARG ARG LEU ALA ARG LEU HIS
SEQRES 31 B 475 THR PRO LEU PRO LEU LEU ALA PHE THR ALA TRP PRO GLU
SEQRES 32 B 475 VAL ARG SER GLN LEU ALA MET THR TRP GLY THR GLU THR
SEQRES 33 B 475 PHE ILE VAL PRO LYS MET GLN SER THR ASP GLY MET ILE
SEQRES 34 B 475 ARG GLN VAL ASP LYS SER LEU LEU GLU LEU ALA ARG TYR
SEQRES 35 B 475 LYS ARG GLY ASP LEU VAL VAL ILE VAL ALA GLY ALA PRO
SEQRES 36 B 475 PRO GLY THR VAL GLY SER THR ASN LEU ILE HIS VAL HIS
SEQRES 37 B 475 ARG ILE GLY GLU ASP ASP VAL
SEQRES 1 C 475 GLY GLY HIS MET THR ARG ARG GLY LYS ILE VAL CYS THR
SEQRES 2 C 475 LEU GLY PRO ALA THR GLN ARG ASP ASP LEU VAL ARG ALA
SEQRES 3 C 475 LEU VAL GLU ALA GLY MET ASP VAL ALA ARG MET ASN PHE
SEQRES 4 C 475 SER HIS GLY ASP TYR ASP ASP HIS LYS VAL ALA TYR GLU
SEQRES 5 C 475 ARG VAL ARG VAL ALA SER ASP ALA THR GLY ARG ALA VAL
SEQRES 6 C 475 GLY VAL LEU ALA ASP LEU GLN GLY PRO LYS ILE ARG LEU
SEQRES 7 C 475 GLY ARG PHE ALA SER GLY ALA THR HIS TRP ALA GLU GLY
SEQRES 8 C 475 GLU THR VAL ARG ILE THR VAL GLY ALA CYS GLU GLY SER
SEQRES 9 C 475 HIS ASP ARG VAL SER THR THR TYR LYS ARG LEU ALA GLN
SEQRES 10 C 475 ASP ALA VAL ALA GLY ASP ARG VAL LEU VAL ASP ASP GLY
SEQRES 11 C 475 LYS VAL ALA LEU VAL VAL ASP ALA VAL GLU GLY ASP ASP
SEQRES 12 C 475 VAL VAL CYS THR VAL VAL GLU GLY GLY PRO VAL SER ASP
SEQRES 13 C 475 ASN LYS GLY ILE SER LEU PRO GLY MET ASN VAL THR ALA
SEQRES 14 C 475 PRO ALA LEU SER GLU LYS ASP ILE GLU ASP LEU THR PHE
SEQRES 15 C 475 ALA LEU ASN LEU GLY VAL ASP MET VAL ALA LEU SER PHE
SEQRES 16 C 475 VAL ARG SER PRO ALA ASP VAL GLU LEU VAL HIS GLU VAL
SEQRES 17 C 475 MET ASP ARG ILE GLY ARG ARG VAL PRO VAL ILE ALA LYS
SEQRES 18 C 475 LEU GLU LYS PRO GLU ALA ILE ASP ASN LEU GLU ALA ILE
SEQRES 19 C 475 VAL LEU ALA PHE ASP ALA VAL MET VAL ALA ARG GLY ASP
SEQRES 20 C 475 LEU GLY VAL GLU LEU PRO LEU GLU GLU VAL PRO LEU VAL
SEQRES 21 C 475 GLN LYS ARG ALA ILE GLN MET ALA ARG GLU ASN ALA LYS
SEQRES 22 C 475 PRO VAL ILE VAL ALA THR GLN MET LEU ASP SER MET ILE
SEQRES 23 C 475 GLU ASN SER ARG PRO THR ARG ALA GLU ALA SER ASP VAL
SEQRES 24 C 475 ALA ASN ALA VAL LEU ASP GLY ALA ASP ALA LEU MET LEU
SEQRES 25 C 475 SER GLY GLU THR SER VAL GLY LYS TYR PRO LEU ALA ALA
SEQRES 26 C 475 VAL ARG THR MET SER ARG ILE ILE CYS ALA VAL GLU GLU
SEQRES 27 C 475 ASN SER THR ALA ALA PRO PRO LEU THR HIS ILE PRO ARG
SEQRES 28 C 475 THR LYS ARG GLY VAL ILE SER TYR ALA ALA ARG ASP ILE
SEQRES 29 C 475 GLY GLU ARG LEU ASP ALA LYS ALA LEU VAL ALA PHE THR
SEQRES 30 C 475 GLN SER GLY ASP THR VAL ARG ARG LEU ALA ARG LEU HIS
SEQRES 31 C 475 THR PRO LEU PRO LEU LEU ALA PHE THR ALA TRP PRO GLU
SEQRES 32 C 475 VAL ARG SER GLN LEU ALA MET THR TRP GLY THR GLU THR
SEQRES 33 C 475 PHE ILE VAL PRO LYS MET GLN SER THR ASP GLY MET ILE
SEQRES 34 C 475 ARG GLN VAL ASP LYS SER LEU LEU GLU LEU ALA ARG TYR
SEQRES 35 C 475 LYS ARG GLY ASP LEU VAL VAL ILE VAL ALA GLY ALA PRO
SEQRES 36 C 475 PRO GLY THR VAL GLY SER THR ASN LEU ILE HIS VAL HIS
SEQRES 37 C 475 ARG ILE GLY GLU ASP ASP VAL
SEQRES 1 D 475 GLY GLY HIS MET THR ARG ARG GLY LYS ILE VAL CYS THR
SEQRES 2 D 475 LEU GLY PRO ALA THR GLN ARG ASP ASP LEU VAL ARG ALA
SEQRES 3 D 475 LEU VAL GLU ALA GLY MET ASP VAL ALA ARG MET ASN PHE
SEQRES 4 D 475 SER HIS GLY ASP TYR ASP ASP HIS LYS VAL ALA TYR GLU
SEQRES 5 D 475 ARG VAL ARG VAL ALA SER ASP ALA THR GLY ARG ALA VAL
SEQRES 6 D 475 GLY VAL LEU ALA ASP LEU GLN GLY PRO LYS ILE ARG LEU
SEQRES 7 D 475 GLY ARG PHE ALA SER GLY ALA THR HIS TRP ALA GLU GLY
SEQRES 8 D 475 GLU THR VAL ARG ILE THR VAL GLY ALA CYS GLU GLY SER
SEQRES 9 D 475 HIS ASP ARG VAL SER THR THR TYR LYS ARG LEU ALA GLN
SEQRES 10 D 475 ASP ALA VAL ALA GLY ASP ARG VAL LEU VAL ASP ASP GLY
SEQRES 11 D 475 LYS VAL ALA LEU VAL VAL ASP ALA VAL GLU GLY ASP ASP
SEQRES 12 D 475 VAL VAL CYS THR VAL VAL GLU GLY GLY PRO VAL SER ASP
SEQRES 13 D 475 ASN LYS GLY ILE SER LEU PRO GLY MET ASN VAL THR ALA
SEQRES 14 D 475 PRO ALA LEU SER GLU LYS ASP ILE GLU ASP LEU THR PHE
SEQRES 15 D 475 ALA LEU ASN LEU GLY VAL ASP MET VAL ALA LEU SER PHE
SEQRES 16 D 475 VAL ARG SER PRO ALA ASP VAL GLU LEU VAL HIS GLU VAL
SEQRES 17 D 475 MET ASP ARG ILE GLY ARG ARG VAL PRO VAL ILE ALA LYS
SEQRES 18 D 475 LEU GLU LYS PRO GLU ALA ILE ASP ASN LEU GLU ALA ILE
SEQRES 19 D 475 VAL LEU ALA PHE ASP ALA VAL MET VAL ALA ARG GLY ASP
SEQRES 20 D 475 LEU GLY VAL GLU LEU PRO LEU GLU GLU VAL PRO LEU VAL
SEQRES 21 D 475 GLN LYS ARG ALA ILE GLN MET ALA ARG GLU ASN ALA LYS
SEQRES 22 D 475 PRO VAL ILE VAL ALA THR GLN MET LEU ASP SER MET ILE
SEQRES 23 D 475 GLU ASN SER ARG PRO THR ARG ALA GLU ALA SER ASP VAL
SEQRES 24 D 475 ALA ASN ALA VAL LEU ASP GLY ALA ASP ALA LEU MET LEU
SEQRES 25 D 475 SER GLY GLU THR SER VAL GLY LYS TYR PRO LEU ALA ALA
SEQRES 26 D 475 VAL ARG THR MET SER ARG ILE ILE CYS ALA VAL GLU GLU
SEQRES 27 D 475 ASN SER THR ALA ALA PRO PRO LEU THR HIS ILE PRO ARG
SEQRES 28 D 475 THR LYS ARG GLY VAL ILE SER TYR ALA ALA ARG ASP ILE
SEQRES 29 D 475 GLY GLU ARG LEU ASP ALA LYS ALA LEU VAL ALA PHE THR
SEQRES 30 D 475 GLN SER GLY ASP THR VAL ARG ARG LEU ALA ARG LEU HIS
SEQRES 31 D 475 THR PRO LEU PRO LEU LEU ALA PHE THR ALA TRP PRO GLU
SEQRES 32 D 475 VAL ARG SER GLN LEU ALA MET THR TRP GLY THR GLU THR
SEQRES 33 D 475 PHE ILE VAL PRO LYS MET GLN SER THR ASP GLY MET ILE
SEQRES 34 D 475 ARG GLN VAL ASP LYS SER LEU LEU GLU LEU ALA ARG TYR
SEQRES 35 D 475 LYS ARG GLY ASP LEU VAL VAL ILE VAL ALA GLY ALA PRO
SEQRES 36 D 475 PRO GLY THR VAL GLY SER THR ASN LEU ILE HIS VAL HIS
SEQRES 37 D 475 ARG ILE GLY GLU ASP ASP VAL
HET AMP A 501 23
HET G6P A 502 16
HET MG A 503 1
HET OXL A 504 6
HET AMP B 501 23
HET G6P B 502 16
HET MG B 503 1
HET OXL B 504 6
HET K B 505 1
HET AMP C 501 23
HET G6P C 502 16
HET MG C 503 1
HET OXL C 504 6
HET PO4 C 505 5
HET AMP D 501 23
HET G6P D 502 16
HET MG D 503 1
HET OXL D 504 6
HET PO4 D 505 5
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM G6P 6-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE
HETNAM MG MAGNESIUM ION
HETNAM OXL OXALATE ION
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
HETSYN G6P ALPHA-D-GLUCOSE-6-PHOSPHATE; 6-O-PHOSPHONO-ALPHA-D-
HETSYN 2 G6P GLUCOSE; 6-O-PHOSPHONO-D-GLUCOSE; 6-O-PHOSPHONO-
HETSYN 3 G6P GLUCOSE
FORMUL 5 AMP 4(C10 H14 N5 O7 P)
FORMUL 6 G6P 4(C6 H13 O9 P)
FORMUL 7 MG 4(MG 2+)
FORMUL 8 OXL 4(C2 O4 2-)
FORMUL 13 K K 1+
FORMUL 18 PO4 2(O4 P 3-)
FORMUL 24 HOH *335(H2 O)
HELIX 1 AA1 GLY A 12 GLN A 16 5 5
HELIX 2 AA2 ASP A 19 GLY A 28 1 10
HELIX 3 AA3 ASP A 40 GLY A 59 1 20
HELIX 4 AA4 ARG A 111 ALA A 116 1 6
HELIX 5 AA5 SER A 170 GLY A 184 1 15
HELIX 6 AA6 ALA A 197 GLY A 210 1 14
HELIX 7 AA7 LYS A 221 ASN A 227 1 7
HELIX 8 AA8 ASN A 227 PHE A 235 1 9
HELIX 9 AA9 ARG A 242 LEU A 249 1 8
HELIX 10 AB1 PRO A 250 GLU A 252 5 3
HELIX 11 AB2 GLU A 253 ASN A 268 1 16
HELIX 12 AB3 LEU A 279 GLU A 284 5 6
HELIX 13 AB4 THR A 289 GLY A 303 1 15
HELIX 14 AB5 SER A 310 VAL A 315 1 6
HELIX 15 AB6 TYR A 318 SER A 337 1 20
HELIX 16 AB7 THR A 349 LEU A 365 1 17
HELIX 17 AB8 GLY A 377 ARG A 385 1 9
HELIX 18 AB9 TRP A 398 LEU A 405 1 8
HELIX 19 AC1 ALA A 406 THR A 408 5 3
HELIX 20 AC2 SER A 421 GLU A 435 1 15
HELIX 21 AC3 ASP B 19 GLY B 28 1 10
HELIX 22 AC4 ASP B 40 GLY B 59 1 20
HELIX 23 AC5 ARG B 111 ALA B 116 1 6
HELIX 24 AC6 ASP B 126 LYS B 128 5 3
HELIX 25 AC7 SER B 170 GLY B 184 1 15
HELIX 26 AC8 ALA B 197 GLY B 210 1 14
HELIX 27 AC9 LYS B 221 ASN B 227 1 7
HELIX 28 AD1 ASN B 227 PHE B 235 1 9
HELIX 29 AD2 ARG B 242 LEU B 249 1 8
HELIX 30 AD3 PRO B 250 GLU B 252 5 3
HELIX 31 AD4 GLU B 253 ASN B 268 1 16
HELIX 32 AD5 LEU B 279 GLU B 284 5 6
HELIX 33 AD6 THR B 289 GLY B 303 1 15
HELIX 34 AD7 SER B 310 VAL B 315 1 6
HELIX 35 AD8 TYR B 318 SER B 337 1 20
HELIX 36 AD9 THR B 349 LEU B 365 1 17
HELIX 37 AE1 GLY B 377 ARG B 385 1 9
HELIX 38 AE2 TRP B 398 LEU B 405 1 8
HELIX 39 AE3 ALA B 406 THR B 408 5 3
HELIX 40 AE4 SER B 421 GLU B 435 1 15
HELIX 41 AE5 GLY C 12 GLN C 16 5 5
HELIX 42 AE6 ASP C 19 GLY C 28 1 10
HELIX 43 AE7 ASP C 40 GLY C 59 1 20
HELIX 44 AE8 ARG C 111 ALA C 116 1 6
HELIX 45 AE9 ASP C 126 LYS C 128 5 3
HELIX 46 AF1 SER C 170 GLY C 184 1 15
HELIX 47 AF2 ALA C 197 GLY C 210 1 14
HELIX 48 AF3 LYS C 221 ASN C 227 1 7
HELIX 49 AF4 ASN C 227 PHE C 235 1 9
HELIX 50 AF5 ARG C 242 LEU C 249 1 8
HELIX 51 AF6 PRO C 250 GLU C 252 5 3
HELIX 52 AF7 GLU C 253 ASN C 268 1 16
HELIX 53 AF8 LEU C 279 GLU C 284 5 6
HELIX 54 AF9 THR C 289 GLY C 303 1 15
HELIX 55 AG1 SER C 310 VAL C 315 1 6
HELIX 56 AG2 TYR C 318 SER C 337 1 20
HELIX 57 AG3 THR C 349 LEU C 365 1 17
HELIX 58 AG4 GLY C 377 ARG C 385 1 9
HELIX 59 AG5 TRP C 398 LEU C 405 1 8
HELIX 60 AG6 ALA C 406 THR C 408 5 3
HELIX 61 AG7 SER C 421 GLU C 435 1 15
HELIX 62 AG8 ASP D 19 GLY D 28 1 10
HELIX 63 AG9 ASP D 40 GLY D 59 1 20
HELIX 64 AH1 ARG D 111 ALA D 116 1 6
HELIX 65 AH2 ASP D 126 LYS D 128 5 3
HELIX 66 AH3 SER D 170 GLY D 184 1 15
HELIX 67 AH4 ALA D 197 GLY D 210 1 14
HELIX 68 AH5 LYS D 221 ASN D 227 1 7
HELIX 69 AH6 ASN D 227 PHE D 235 1 9
HELIX 70 AH7 ARG D 242 LEU D 249 1 8
HELIX 71 AH8 PRO D 250 GLU D 252 5 3
HELIX 72 AH9 GLU D 253 ASN D 268 1 16
HELIX 73 AI1 LEU D 279 GLU D 284 5 6
HELIX 74 AI2 THR D 289 GLY D 303 1 15
HELIX 75 AI3 SER D 310 VAL D 315 1 6
HELIX 76 AI4 TYR D 318 SER D 337 1 20
HELIX 77 AI5 THR D 349 LEU D 365 1 17
HELIX 78 AI6 GLY D 377 ARG D 385 1 9
HELIX 79 AI7 TRP D 398 LEU D 405 1 8
HELIX 80 AI8 ALA D 406 THR D 408 5 3
HELIX 81 AI9 SER D 421 LEU D 434 1 14
SHEET 1 AA1 9 LYS A 6 THR A 10 0
SHEET 2 AA1 9 VAL A 31 ASN A 35 1 O ARG A 33 N CYS A 9
SHEET 3 AA1 9 GLY A 63 LEU A 68 1 O ASP A 67 N MET A 34
SHEET 4 AA1 9 MET A 187 LEU A 190 1 O ALA A 189 N ALA A 66
SHEET 5 AA1 9 VAL A 215 LEU A 219 1 O ILE A 216 N VAL A 188
SHEET 6 AA1 9 ALA A 237 ALA A 241 1 O MET A 239 N LEU A 219
SHEET 7 AA1 9 VAL A 272 ALA A 275 1 O ILE A 273 N VAL A 240
SHEET 8 AA1 9 ALA A 306 LEU A 309 1 O ALA A 306 N VAL A 274
SHEET 9 AA1 9 LYS A 6 THR A 10 1 N VAL A 8 O LEU A 307
SHEET 1 AA2 2 ALA A 82 TRP A 85 0
SHEET 2 AA2 2 GLY A 149 SER A 152 -1 O VAL A 151 N THR A 83
SHEET 1 AA3 6 ARG A 104 SER A 106 0
SHEET 2 AA3 6 THR A 90 THR A 94 1 N THR A 94 O VAL A 105
SHEET 3 AA3 6 ASP A 140 GLU A 147 -1 O CYS A 143 N VAL A 91
SHEET 4 AA3 6 VAL A 129 GLU A 137 -1 N ASP A 134 O VAL A 142
SHEET 5 AA3 6 ARG A 121 VAL A 124 -1 N VAL A 124 O VAL A 129
SHEET 6 AA3 6 ILE A 157 SER A 158 -1 O SER A 158 N LEU A 123
SHEET 1 AA410 THR A 411 ILE A 415 0
SHEET 2 AA410 LEU A 392 THR A 396 1 N ALA A 394 O PHE A 414
SHEET 3 AA410 ALA A 369 PHE A 373 1 N LEU A 370 O LEU A 393
SHEET 4 AA410 LEU A 444 GLY A 450 1 O VAL A 448 N VAL A 371
SHEET 5 AA410 THR A 459 ARG A 466 -1 O HIS A 465 N VAL A 445
SHEET 6 AA410 THR C 459 ARG C 466 -1 O VAL C 464 N ASN A 460
SHEET 7 AA410 LEU C 444 GLY C 450 -1 N VAL C 445 O HIS C 465
SHEET 8 AA410 ALA C 369 PHE C 373 1 N VAL C 371 O VAL C 448
SHEET 9 AA410 LEU C 392 THR C 396 1 O LEU C 393 N LEU C 370
SHEET 10 AA410 THR C 411 ILE C 415 1 O GLU C 412 N ALA C 394
SHEET 1 AA5 9 LYS B 6 THR B 10 0
SHEET 2 AA5 9 VAL B 31 ASN B 35 1 O ARG B 33 N CYS B 9
SHEET 3 AA5 9 GLY B 63 LEU B 68 1 O ASP B 67 N MET B 34
SHEET 4 AA5 9 MET B 187 LEU B 190 1 O ALA B 189 N ALA B 66
SHEET 5 AA5 9 VAL B 215 LEU B 219 1 O ILE B 216 N VAL B 188
SHEET 6 AA5 9 ALA B 237 ALA B 241 1 O MET B 239 N LEU B 219
SHEET 7 AA5 9 VAL B 272 ALA B 275 1 O ILE B 273 N VAL B 240
SHEET 8 AA5 9 ALA B 306 LEU B 309 1 O ALA B 306 N VAL B 274
SHEET 9 AA5 9 LYS B 6 THR B 10 1 N VAL B 8 O LEU B 307
SHEET 1 AA6 2 ARG B 77 PHE B 78 0
SHEET 2 AA6 2 GLU B 99 GLY B 100 1 O GLY B 100 N ARG B 77
SHEET 1 AA7 2 ALA B 82 TRP B 85 0
SHEET 2 AA7 2 GLY B 149 SER B 152 -1 O VAL B 151 N THR B 83
SHEET 1 AA8 6 ARG B 104 SER B 106 0
SHEET 2 AA8 6 THR B 90 THR B 94 1 N THR B 94 O VAL B 105
SHEET 3 AA8 6 ASP B 140 GLU B 147 -1 O CYS B 143 N VAL B 91
SHEET 4 AA8 6 ALA B 130 GLU B 137 -1 N ASP B 134 O VAL B 142
SHEET 5 AA8 6 ARG B 121 VAL B 124 -1 N VAL B 122 O LEU B 131
SHEET 6 AA8 6 ILE B 157 SER B 158 -1 O SER B 158 N LEU B 123
SHEET 1 AA910 THR B 411 ILE B 415 0
SHEET 2 AA910 LEU B 392 THR B 396 1 N ALA B 394 O GLU B 412
SHEET 3 AA910 ALA B 369 PHE B 373 1 N LEU B 370 O LEU B 393
SHEET 4 AA910 LEU B 444 GLY B 450 1 O VAL B 446 N VAL B 371
SHEET 5 AA910 THR B 459 ARG B 466 -1 O HIS B 465 N VAL B 445
SHEET 6 AA910 THR D 459 ARG D 466 -1 O ASN D 460 N VAL B 464
SHEET 7 AA910 LEU D 444 GLY D 450 -1 N VAL D 445 O HIS D 465
SHEET 8 AA910 ALA D 369 PHE D 373 1 N VAL D 371 O VAL D 446
SHEET 9 AA910 LEU D 392 THR D 396 1 O LEU D 393 N LEU D 370
SHEET 10 AA910 THR D 411 ILE D 415 1 O PHE D 414 N ALA D 394
SHEET 1 AB1 9 LYS C 6 THR C 10 0
SHEET 2 AB1 9 VAL C 31 ASN C 35 1 O ARG C 33 N CYS C 9
SHEET 3 AB1 9 GLY C 63 LEU C 68 1 O ASP C 67 N MET C 34
SHEET 4 AB1 9 MET C 187 LEU C 190 1 O ALA C 189 N ALA C 66
SHEET 5 AB1 9 VAL C 215 LEU C 219 1 O ILE C 216 N VAL C 188
SHEET 6 AB1 9 ALA C 237 ALA C 241 1 O MET C 239 N LEU C 219
SHEET 7 AB1 9 VAL C 272 ALA C 275 1 O ILE C 273 N VAL C 240
SHEET 8 AB1 9 ALA C 306 LEU C 309 1 O ALA C 306 N VAL C 274
SHEET 9 AB1 9 LYS C 6 THR C 10 1 N VAL C 8 O LEU C 307
SHEET 1 AB2 2 ALA C 82 TRP C 85 0
SHEET 2 AB2 2 GLY C 149 SER C 152 -1 O VAL C 151 N THR C 83
SHEET 1 AB3 6 ARG C 104 SER C 106 0
SHEET 2 AB3 6 THR C 90 THR C 94 1 N THR C 94 O VAL C 105
SHEET 3 AB3 6 ASP C 140 GLU C 147 -1 O CYS C 143 N VAL C 91
SHEET 4 AB3 6 ALA C 130 GLU C 137 -1 N ASP C 134 O VAL C 142
SHEET 5 AB3 6 ARG C 121 VAL C 124 -1 N VAL C 122 O LEU C 131
SHEET 6 AB3 6 ILE C 157 SER C 158 -1 O SER C 158 N LEU C 123
SHEET 1 AB4 9 LYS D 6 THR D 10 0
SHEET 2 AB4 9 VAL D 31 ASN D 35 1 O ARG D 33 N CYS D 9
SHEET 3 AB4 9 GLY D 63 LEU D 68 1 O ASP D 67 N MET D 34
SHEET 4 AB4 9 MET D 187 LEU D 190 1 O ALA D 189 N ALA D 66
SHEET 5 AB4 9 VAL D 215 LEU D 219 1 O ILE D 216 N VAL D 188
SHEET 6 AB4 9 ALA D 237 ALA D 241 1 O MET D 239 N LEU D 219
SHEET 7 AB4 9 VAL D 272 ALA D 275 1 O ILE D 273 N VAL D 240
SHEET 8 AB4 9 ALA D 306 LEU D 309 1 O MET D 308 N VAL D 274
SHEET 9 AB4 9 LYS D 6 THR D 10 1 N VAL D 8 O LEU D 307
SHEET 1 AB5 2 ALA D 82 TRP D 85 0
SHEET 2 AB5 2 GLY D 149 SER D 152 -1 O VAL D 151 N THR D 83
SHEET 1 AB6 6 ARG D 104 SER D 106 0
SHEET 2 AB6 6 THR D 90 THR D 94 1 N THR D 94 O VAL D 105
SHEET 3 AB6 6 ASP D 140 GLU D 147 -1 O CYS D 143 N VAL D 91
SHEET 4 AB6 6 ALA D 130 GLU D 137 -1 N ASP D 134 O VAL D 142
SHEET 5 AB6 6 ARG D 121 VAL D 124 -1 N VAL D 122 O LEU D 131
SHEET 6 AB6 6 ILE D 157 SER D 158 -1 O SER D 158 N LEU D 123
LINK OE1 GLU A 220 MG MG A 503 1555 1555 2.22
LINK OD2 ASP A 244 MG MG A 503 1555 1555 2.14
LINK MG MG A 503 O3 OXL A 504 1555 1555 2.16
LINK MG MG A 503 O4 OXL A 504 1555 1555 2.09
LINK MG MG A 503 O HOH A 604 1555 1555 2.22
LINK MG MG A 503 O HOH A 629 1555 1555 2.06
LINK OD1 ASN B 35 K K B 505 1555 1555 2.72
LINK OG SER B 37 K K B 505 1555 1555 3.03
LINK OD1 ASP B 67 K K B 505 1555 1555 3.04
LINK OE1 GLU B 220 MG MG B 503 1555 1555 2.21
LINK OD2 ASP B 244 MG MG B 503 1555 1555 2.02
LINK MG MG B 503 O3 OXL B 504 1555 1555 2.10
LINK MG MG B 503 O4 OXL B 504 1555 1555 2.06
LINK MG MG B 503 O HOH B 629 1555 1555 1.99
LINK MG MG B 503 O HOH B 664 1555 1555 2.29
LINK OE1 GLU C 220 MG MG C 503 1555 1555 2.08
LINK OD2 ASP C 244 MG MG C 503 1555 1555 1.75
LINK MG MG C 503 O1 OXL C 504 1555 1555 2.39
LINK MG MG C 503 O2 OXL C 504 1555 1555 2.50
LINK MG MG C 503 O HOH C 604 1555 1555 2.19
LINK MG MG C 503 O HOH C 613 1555 1555 2.03
LINK OE1 GLU D 220 MG MG D 503 1555 1555 2.17
LINK OD2 ASP D 244 MG MG D 503 1555 1555 1.84
LINK MG MG D 503 O1 OXL D 504 1555 1555 2.14
LINK MG MG D 503 O4 OXL D 504 1555 1555 2.38
LINK MG MG D 503 O HOH D 602 1555 1555 1.91
LINK MG MG D 503 O HOH D 633 1555 1555 2.20
CISPEP 1 ALA A 451 PRO A 452 0 -1.03
CISPEP 2 ALA B 451 PRO B 452 0 1.40
CISPEP 3 ALA C 451 PRO C 452 0 2.92
CISPEP 4 ALA D 451 PRO D 452 0 5.34
CRYST1 124.370 124.370 144.192 90.00 90.00 120.00 P 31 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008041 0.004642 0.000000 0.00000
SCALE2 0.000000 0.009284 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006935 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
