HEADER TRANSFERASE 03-JUL-12 4FXJ
TITLE STRUCTURE OF M2 PYRUVATE KINASE IN COMPLEX WITH PHENYLALANINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE ISOZYMES M1/M2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CYTOSOLIC THYROID HORMONE-BINDING PROTEIN, CTHBP, OPA-
COMPND 5 INTERACTING PROTEIN 3, OIP-3, PYRUVATE KINASE 2/3, PYRUVATE KINASE
COMPND 6 MUSCLE ISOZYME, THYROID HORMONE-BINDING PROTEIN 1, THBP1, TUMOR M2-
COMPND 7 PK, P58;
COMPND 8 EC: 2.7.1.40;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: OIP3, PK2, PK3, PKM, PKM2, PYRUVATE KINASE M2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A_M2
KEYWDS TIM BARREL, TRANSFERASE, PHENYLALANINE BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.WALKINSHAW,H.P.MORGAN
REVDAT 3 13-SEP-23 4FXJ 1 REMARK SEQADV
REVDAT 2 24-APR-13 4FXJ 1 JRNL
REVDAT 1 27-MAR-13 4FXJ 0
JRNL AUTH H.P.MORGAN,F.J.O'REILLY,M.A.WEAR,J.R.O'NEILL,
JRNL AUTH 2 L.A.FOTHERGILL-GILMORE,T.HUPP,M.D.WALKINSHAW
JRNL TITL M2 PYRUVATE KINASE PROVIDES A MECHANISM FOR NUTRIENT SENSING
JRNL TITL 2 AND REGULATION OF CELL PROLIFERATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 5881 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23530218
JRNL DOI 10.1073/PNAS.1217157110
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 41633
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2211
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3011
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14721
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.86000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : -1.12000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.76000
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): 0.545
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.442
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.835
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.886
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.830
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15025 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20296 ; 0.773 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1915 ; 3.539 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 624 ;34.865 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2704 ;13.788 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 119 ;13.375 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2332 ; 0.047 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11139 ; 0.002 ; 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): 9576 ; 0.129 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15452 ; 0.231 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5449 ; 0.062 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4844 ; 0.114 ; 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 : 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 28 A 116
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2926 -22.0777 36.3986
REMARK 3 T TENSOR
REMARK 3 T11: 0.3407 T22: 0.1466
REMARK 3 T33: 0.0320 T12: 0.0597
REMARK 3 T13: -0.0861 T23: -0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.5362 L22: 0.9537
REMARK 3 L33: 1.4880 L12: -0.1425
REMARK 3 L13: -0.7282 L23: -0.4567
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: 0.1025 S13: -0.0631
REMARK 3 S21: -0.0440 S22: -0.0696 S23: -0.0107
REMARK 3 S31: 0.1534 S32: -0.0645 S33: 0.0806
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 117 A 214
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2142 -18.1874 68.3835
REMARK 3 T TENSOR
REMARK 3 T11: 0.2564 T22: 0.1522
REMARK 3 T33: 0.0258 T12: 0.0580
REMARK 3 T13: -0.0519 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 1.4019 L22: 6.3429
REMARK 3 L33: 5.5479 L12: -0.5024
REMARK 3 L13: -1.2098 L23: -1.5159
REMARK 3 S TENSOR
REMARK 3 S11: -0.1158 S12: -0.1291 S13: -0.0185
REMARK 3 S21: -0.1167 S22: 0.0034 S23: -0.1752
REMARK 3 S31: 0.3700 S32: 0.1361 S33: 0.1124
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 215 A 390
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0534 -11.7848 47.7143
REMARK 3 T TENSOR
REMARK 3 T11: 0.3351 T22: 0.1361
REMARK 3 T33: 0.0268 T12: 0.0216
REMARK 3 T13: -0.0759 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.7664 L22: 1.0570
REMARK 3 L33: 1.0719 L12: -0.0534
REMARK 3 L13: -0.2285 L23: 0.0435
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.1421 S13: 0.0876
REMARK 3 S21: 0.0717 S22: -0.0585 S23: -0.0176
REMARK 3 S31: 0.0994 S32: 0.1209 S33: 0.0147
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 391 A 531
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1623 -6.7137 25.2009
REMARK 3 T TENSOR
REMARK 3 T11: 0.3518 T22: 0.1375
REMARK 3 T33: 0.0227 T12: 0.0291
REMARK 3 T13: -0.0711 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.6333 L22: 1.7936
REMARK 3 L33: 1.8536 L12: -0.1182
REMARK 3 L13: 0.8568 L23: 0.2247
REMARK 3 S TENSOR
REMARK 3 S11: -0.0916 S12: 0.0050 S13: 0.0911
REMARK 3 S21: -0.0547 S22: -0.0139 S23: -0.0308
REMARK 3 S31: -0.0592 S32: -0.0508 S33: 0.1055
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 23 B 113
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9709 24.4259 10.0666
REMARK 3 T TENSOR
REMARK 3 T11: 0.3784 T22: 0.1123
REMARK 3 T33: 0.0529 T12: -0.0427
REMARK 3 T13: -0.0814 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 0.3693 L22: 0.5395
REMARK 3 L33: 2.2438 L12: -0.3377
REMARK 3 L13: -0.3559 L23: 0.1682
REMARK 3 S TENSOR
REMARK 3 S11: 0.0970 S12: -0.1187 S13: 0.0895
REMARK 3 S21: -0.0807 S22: -0.0090 S23: -0.0884
REMARK 3 S31: -0.0420 S32: 0.0382 S33: -0.0880
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 114 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2127 12.9483 3.2641
REMARK 3 T TENSOR
REMARK 3 T11: 0.5076 T22: 1.4470
REMARK 3 T33: 0.8757 T12: -0.0637
REMARK 3 T13: -0.0793 T23: -0.4732
REMARK 3 L TENSOR
REMARK 3 L11: 89.0544 L22: 2.7316
REMARK 3 L33: 1.6492 L12: -15.4425
REMARK 3 L13: 12.0141 L23: -2.1088
REMARK 3 S TENSOR
REMARK 3 S11: 1.0254 S12: -3.2677 S13: -0.4056
REMARK 3 S21: -0.2918 S22: -0.2549 S23: 0.1978
REMARK 3 S31: 0.2261 S32: -0.3387 S33: -0.7705
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 216 B 391
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5518 14.3369 13.5048
REMARK 3 T TENSOR
REMARK 3 T11: 0.3758 T22: 0.1438
REMARK 3 T33: 0.0494 T12: -0.0057
REMARK 3 T13: -0.0856 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.8150 L22: 1.1801
REMARK 3 L33: 1.2791 L12: -0.3279
REMARK 3 L13: -0.2185 L23: 0.3606
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: -0.0432 S13: -0.0495
REMARK 3 S21: 0.0039 S22: -0.0094 S23: 0.1840
REMARK 3 S31: 0.0354 S32: -0.2340 S33: 0.0497
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 392 B 531
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0995 9.3175 16.0041
REMARK 3 T TENSOR
REMARK 3 T11: 0.3728 T22: 0.1143
REMARK 3 T33: 0.0242 T12: -0.0153
REMARK 3 T13: -0.0851 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 2.4381 L22: 1.8672
REMARK 3 L33: 0.9329 L12: -0.6692
REMARK 3 L13: -0.1420 L23: 0.3451
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: -0.1061 S13: -0.0370
REMARK 3 S21: 0.0762 S22: 0.0223 S23: -0.0072
REMARK 3 S31: 0.0785 S32: 0.0836 S33: 0.0331
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 29 C 116
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3361 23.5151 47.0242
REMARK 3 T TENSOR
REMARK 3 T11: 0.3264 T22: 0.2627
REMARK 3 T33: 0.0775 T12: -0.0070
REMARK 3 T13: -0.0936 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.6693 L22: 0.1677
REMARK 3 L33: 1.7274 L12: -0.5237
REMARK 3 L13: -1.4810 L23: 0.4867
REMARK 3 S TENSOR
REMARK 3 S11: -0.1235 S12: 0.0314 S13: -0.2463
REMARK 3 S21: 0.0173 S22: -0.0342 S23: 0.0826
REMARK 3 S31: 0.1982 S32: -0.3480 S33: 0.1576
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 117 C 214
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8559 53.1233 30.1305
REMARK 3 T TENSOR
REMARK 3 T11: 0.3601 T22: 0.2102
REMARK 3 T33: 0.0420 T12: 0.0587
REMARK 3 T13: -0.0159 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 3.8842 L22: 3.6921
REMARK 3 L33: 2.7673 L12: -1.1884
REMARK 3 L13: 0.6089 L23: -2.2083
REMARK 3 S TENSOR
REMARK 3 S11: 0.0567 S12: 0.3411 S13: 0.3937
REMARK 3 S21: -0.1300 S22: -0.0819 S23: -0.0722
REMARK 3 S31: -0.1423 S32: -0.0365 S33: 0.0253
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 215 C 392
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9347 29.9629 43.5438
REMARK 3 T TENSOR
REMARK 3 T11: 0.3150 T22: 0.1683
REMARK 3 T33: 0.0177 T12: 0.0303
REMARK 3 T13: -0.0585 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.9199 L22: 0.8382
REMARK 3 L33: 1.2412 L12: -0.2807
REMARK 3 L13: -0.3744 L23: 0.3695
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: -0.0003 S13: 0.0309
REMARK 3 S21: -0.0408 S22: 0.0454 S23: -0.0290
REMARK 3 S31: -0.0841 S32: -0.1419 S33: -0.0724
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 393 C 531
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9519 8.8337 58.9244
REMARK 3 T TENSOR
REMARK 3 T11: 0.3006 T22: 0.1222
REMARK 3 T33: 0.0440 T12: 0.0218
REMARK 3 T13: -0.0688 T23: 0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 2.5250 L22: 2.8021
REMARK 3 L33: 3.5951 L12: -0.6357
REMARK 3 L13: -0.2469 L23: -0.0799
REMARK 3 S TENSOR
REMARK 3 S11: -0.0342 S12: -0.0849 S13: -0.2127
REMARK 3 S21: 0.0804 S22: 0.1759 S23: 0.0109
REMARK 3 S31: 0.2040 S32: 0.0376 S33: -0.1417
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 26 D 59
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7625 -10.9848 67.7641
REMARK 3 T TENSOR
REMARK 3 T11: 0.3633 T22: 0.2080
REMARK 3 T33: 0.0155 T12: 0.0607
REMARK 3 T13: -0.0570 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.0934 L22: 0.3010
REMARK 3 L33: 2.8662 L12: 0.5690
REMARK 3 L13: -1.7698 L23: -0.9184
REMARK 3 S TENSOR
REMARK 3 S11: 0.1145 S12: -0.0159 S13: 0.0497
REMARK 3 S21: 0.0971 S22: -0.0245 S23: 0.0179
REMARK 3 S31: -0.1777 S32: 0.0171 S33: -0.0899
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 60 D 204
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5175 -41.2744 66.1939
REMARK 3 T TENSOR
REMARK 3 T11: 0.3884 T22: 0.1657
REMARK 3 T33: 0.1032 T12: 0.0818
REMARK 3 T13: -0.0515 T23: 0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 0.7756 L22: 1.8016
REMARK 3 L33: 1.0446 L12: -0.2661
REMARK 3 L13: 0.0974 L23: 0.9436
REMARK 3 S TENSOR
REMARK 3 S11: 0.0617 S12: -0.0856 S13: -0.2078
REMARK 3 S21: 0.0013 S22: 0.0272 S23: -0.1604
REMARK 3 S31: 0.1209 S32: 0.2576 S33: -0.0889
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 205 D 391
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8763 -27.5871 63.4393
REMARK 3 T TENSOR
REMARK 3 T11: 0.3448 T22: 0.1190
REMARK 3 T33: 0.0312 T12: 0.0132
REMARK 3 T13: -0.0575 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.4734 L22: 1.4273
REMARK 3 L33: 0.8971 L12: 0.3962
REMARK 3 L13: -0.3831 L23: -0.1960
REMARK 3 S TENSOR
REMARK 3 S11: -0.0545 S12: -0.0378 S13: -0.1397
REMARK 3 S21: -0.0650 S22: -0.0368 S23: 0.0039
REMARK 3 S31: 0.0260 S32: 0.0351 S33: 0.0913
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 392 D 531
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5578 -5.3654 68.7758
REMARK 3 T TENSOR
REMARK 3 T11: 0.3164 T22: 0.1293
REMARK 3 T33: 0.0316 T12: 0.0000
REMARK 3 T13: -0.0671 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 1.7738 L22: 2.1663
REMARK 3 L33: 2.7474 L12: -1.2198
REMARK 3 L13: -0.5030 L23: -0.5762
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: 0.0267 S13: -0.0182
REMARK 3 S21: 0.0367 S22: 0.0501 S23: 0.1480
REMARK 3 S31: -0.1102 S32: -0.1828 S33: -0.0733
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 4FXJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44252
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 80.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.16700
REMARK 200 R SYM (I) : 0.18900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.62700
REMARK 200 R SYM FOR SHELL (I) : 0.70000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3BJT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-16% PEG 3350, 100 MM SODIUM
REMARK 280 CACODYLATE, 50 MM MGCL2, 100 MM KCL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 290K, PH 7
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 35.30000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 PRO A 4
REMARK 465 HIS A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 GLY A 9
REMARK 465 THR A 10
REMARK 465 ALA A 11
REMARK 465 PHE A 12
REMARK 465 ILE A 13
REMARK 465 GLN A 14
REMARK 465 THR A 15
REMARK 465 GLN A 16
REMARK 465 GLN A 17
REMARK 465 LEU A 18
REMARK 465 HIS A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 MET A 22
REMARK 465 ALA A 23
REMARK 465 ASP A 24
REMARK 465 THR A 25
REMARK 465 PHE A 26
REMARK 465 LEU A 27
REMARK 465 SER A 127
REMARK 465 GLY A 128
REMARK 465 THR A 129
REMARK 465 ILE A 404
REMARK 465 THR A 405
REMARK 465 SER A 406
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 PRO B 4
REMARK 465 HIS B 5
REMARK 465 SER B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 GLY B 9
REMARK 465 THR B 10
REMARK 465 ALA B 11
REMARK 465 PHE B 12
REMARK 465 ILE B 13
REMARK 465 GLN B 14
REMARK 465 THR B 15
REMARK 465 GLN B 16
REMARK 465 GLN B 17
REMARK 465 LEU B 18
REMARK 465 HIS B 19
REMARK 465 ALA B 20
REMARK 465 ALA B 21
REMARK 465 MET B 22
REMARK 465 ARG B 120
REMARK 465 THR B 121
REMARK 465 GLY B 122
REMARK 465 LEU B 123
REMARK 465 ILE B 124
REMARK 465 LYS B 125
REMARK 465 GLY B 126
REMARK 465 SER B 127
REMARK 465 GLY B 128
REMARK 465 THR B 129
REMARK 465 ALA B 130
REMARK 465 GLU B 131
REMARK 465 VAL B 132
REMARK 465 GLU B 133
REMARK 465 LEU B 134
REMARK 465 LYS B 135
REMARK 465 LYS B 136
REMARK 465 GLY B 137
REMARK 465 ALA B 138
REMARK 465 THR B 139
REMARK 465 LEU B 140
REMARK 465 LYS B 141
REMARK 465 ILE B 142
REMARK 465 THR B 143
REMARK 465 LEU B 144
REMARK 465 ASP B 145
REMARK 465 ASN B 146
REMARK 465 ALA B 147
REMARK 465 TYR B 148
REMARK 465 MET B 149
REMARK 465 GLU B 150
REMARK 465 LYS B 151
REMARK 465 CYS B 152
REMARK 465 ASP B 153
REMARK 465 GLU B 154
REMARK 465 ASN B 155
REMARK 465 ILE B 156
REMARK 465 LEU B 157
REMARK 465 TRP B 158
REMARK 465 LEU B 159
REMARK 465 ASP B 160
REMARK 465 TYR B 161
REMARK 465 LYS B 162
REMARK 465 ASN B 163
REMARK 465 ILE B 164
REMARK 465 CYS B 165
REMARK 465 LYS B 166
REMARK 465 VAL B 167
REMARK 465 VAL B 168
REMARK 465 GLU B 169
REMARK 465 VAL B 170
REMARK 465 GLY B 171
REMARK 465 SER B 172
REMARK 465 LYS B 173
REMARK 465 ILE B 174
REMARK 465 TYR B 175
REMARK 465 VAL B 176
REMARK 465 ASP B 177
REMARK 465 ASP B 178
REMARK 465 GLY B 179
REMARK 465 LEU B 180
REMARK 465 ILE B 181
REMARK 465 SER B 182
REMARK 465 LEU B 183
REMARK 465 GLN B 184
REMARK 465 VAL B 185
REMARK 465 LYS B 186
REMARK 465 GLN B 187
REMARK 465 LYS B 188
REMARK 465 GLY B 189
REMARK 465 ALA B 190
REMARK 465 ASP B 191
REMARK 465 PHE B 192
REMARK 465 LEU B 193
REMARK 465 VAL B 194
REMARK 465 THR B 195
REMARK 465 GLU B 196
REMARK 465 VAL B 197
REMARK 465 GLU B 198
REMARK 465 ASN B 199
REMARK 465 GLY B 200
REMARK 465 GLY B 201
REMARK 465 SER B 202
REMARK 465 LEU B 203
REMARK 465 GLY B 204
REMARK 465 SER B 205
REMARK 465 LYS B 206
REMARK 465 LYS B 207
REMARK 465 GLY B 208
REMARK 465 VAL B 209
REMARK 465 ASN B 210
REMARK 465 LEU B 211
REMARK 465 PRO B 212
REMARK 465 GLY B 213
REMARK 465 ALA B 214
REMARK 465 ALA B 215
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 3
REMARK 465 PRO C 4
REMARK 465 HIS C 5
REMARK 465 SER C 6
REMARK 465 GLU C 7
REMARK 465 ALA C 8
REMARK 465 GLY C 9
REMARK 465 THR C 10
REMARK 465 ALA C 11
REMARK 465 PHE C 12
REMARK 465 ILE C 13
REMARK 465 GLN C 14
REMARK 465 THR C 15
REMARK 465 GLN C 16
REMARK 465 GLN C 17
REMARK 465 LEU C 18
REMARK 465 HIS C 19
REMARK 465 ALA C 20
REMARK 465 ALA C 21
REMARK 465 MET C 22
REMARK 465 ALA C 23
REMARK 465 SER C 127
REMARK 465 GLY C 128
REMARK 465 THR C 129
REMARK 465 ALA C 130
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 LYS D 3
REMARK 465 PRO D 4
REMARK 465 HIS D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 ALA D 8
REMARK 465 GLY D 9
REMARK 465 THR D 10
REMARK 465 ALA D 11
REMARK 465 PHE D 12
REMARK 465 ILE D 13
REMARK 465 GLN D 14
REMARK 465 THR D 15
REMARK 465 GLN D 16
REMARK 465 GLN D 17
REMARK 465 LEU D 18
REMARK 465 HIS D 19
REMARK 465 ALA D 20
REMARK 465 ALA D 21
REMARK 465 MET D 22
REMARK 465 ALA D 23
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 ARG A 489 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 489 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 489 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 489 CG CD NE CZ NH1 NH2
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 SER A 55 14.81 -144.12
REMARK 500 PRO A 117 80.55 -69.04
REMARK 500 ASP A 153 -154.70 -149.74
REMARK 500 ASP A 177 76.09 56.99
REMARK 500 ARG A 279 47.56 -109.06
REMARK 500 THR A 328 144.37 64.30
REMARK 500 MET A 330 -69.38 -92.67
REMARK 500 SER A 362 -95.19 -102.65
REMARK 500 CYS A 424 53.60 39.65
REMARK 500 ARG A 445 75.81 50.35
REMARK 500 PHE A 521 152.14 70.46
REMARK 500 THR A 522 69.81 -111.92
REMARK 500 THR B 328 140.57 70.58
REMARK 500 SER B 362 -101.70 -98.79
REMARK 500 ILE B 404 104.12 -52.55
REMARK 500 THR B 405 -141.73 41.90
REMARK 500 ARG B 445 70.56 53.16
REMARK 500 THR B 522 79.99 -101.02
REMARK 500 ILE C 40 41.81 -94.86
REMARK 500 ASP C 153 -155.29 -137.11
REMARK 500 ASN C 163 34.77 -95.93
REMARK 500 ASP C 177 87.11 58.95
REMARK 500 ASP C 178 15.71 55.30
REMARK 500 LYS C 206 70.59 51.12
REMARK 500 VAL C 216 105.92 -56.14
REMARK 500 GLU C 272 21.86 -143.03
REMARK 500 ARG C 279 45.96 -104.36
REMARK 500 THR C 328 148.76 63.33
REMARK 500 SER C 362 -105.36 -93.90
REMARK 500 ILE C 404 96.57 -67.10
REMARK 500 ARG C 445 79.00 53.33
REMARK 500 ASP D 153 -151.91 -143.37
REMARK 500 ASN D 163 41.54 -108.31
REMARK 500 ASP D 177 87.06 59.17
REMARK 500 ASP D 191 43.75 -144.03
REMARK 500 LYS D 206 73.16 47.88
REMARK 500 ARG D 279 42.99 -105.79
REMARK 500 THR D 328 156.01 68.19
REMARK 500 MET D 330 -76.34 -87.50
REMARK 500 SER D 362 -102.20 -103.34
REMARK 500 ARG D 445 76.51 48.02
REMARK 500 THR D 522 70.33 -102.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE D 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BJF RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITHOUT ATP
REMARK 900 RELATED ID: 4FXF RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 H379N SEQUENCE CONFLICT IN UNP ENTRY P14618
DBREF 4FXJ A 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4FXJ B 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4FXJ C 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4FXJ D 1 531 UNP P14618 KPYM_HUMAN 1 531
SEQADV 4FXJ MET A -19 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY A -18 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER A -17 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER A -16 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS A -15 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS A -14 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS A -13 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS A -12 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS A -11 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS A -10 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER A -9 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER A -8 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY A -7 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ LEU A -6 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ VAL A -5 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ PRO A -4 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ARG A -3 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY A -2 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER A -1 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS A 0 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ASN A 379 UNP P14618 HIS 379 SEE REMARK 999
SEQADV 4FXJ MET B -19 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY B -18 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER B -17 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER B -16 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS B -15 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS B -14 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS B -13 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS B -12 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS B -11 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS B -10 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER B -9 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER B -8 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY B -7 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ LEU B -6 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ VAL B -5 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ PRO B -4 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ARG B -3 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY B -2 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER B -1 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS B 0 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ASN B 379 UNP P14618 HIS 379 SEE REMARK 999
SEQADV 4FXJ MET C -19 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY C -18 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER C -17 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER C -16 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS C -15 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS C -14 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS C -13 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS C -12 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS C -11 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS C -10 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER C -9 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER C -8 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY C -7 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ LEU C -6 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ VAL C -5 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ PRO C -4 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ARG C -3 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY C -2 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER C -1 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS C 0 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ASN C 379 UNP P14618 HIS 379 SEE REMARK 999
SEQADV 4FXJ MET D -19 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY D -18 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER D -17 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER D -16 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS D -15 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS D -14 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS D -13 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS D -12 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS D -11 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS D -10 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER D -9 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER D -8 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY D -7 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ LEU D -6 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ VAL D -5 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ PRO D -4 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ARG D -3 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ GLY D -2 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ SER D -1 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ HIS D 0 UNP P14618 EXPRESSION TAG
SEQADV 4FXJ ASN D 379 UNP P14618 HIS 379 SEE REMARK 999
SEQRES 1 A 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 A 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 A 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 A 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 A 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 A 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 A 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 A 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 A 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 A 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 A 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 A 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 A 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 A 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 A 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 A 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 A 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 A 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 A 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 A 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 A 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 A 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 A 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 A 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 A 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 A 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 A 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 A 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 A 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 A 551 PRO LEU GLU ALA VAL ARG MET GLN ASN LEU ILE ALA ARG
SEQRES 32 A 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 A 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 A 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 A 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 A 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 A 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 A 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 A 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 A 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 A 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 A 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 A 551 VAL VAL PRO VAL PRO
SEQRES 1 B 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 B 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 B 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 B 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 B 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 B 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 B 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 B 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 B 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 B 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 B 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 B 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 B 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 B 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 B 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 B 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 B 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 B 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 B 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 B 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 B 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 B 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 B 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 B 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 B 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 B 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 B 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 B 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 B 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 B 551 PRO LEU GLU ALA VAL ARG MET GLN ASN LEU ILE ALA ARG
SEQRES 32 B 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 B 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 B 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 B 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 B 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 B 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 B 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 B 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 B 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 B 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 B 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 B 551 VAL VAL PRO VAL PRO
SEQRES 1 C 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 C 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 C 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 C 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 C 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 C 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 C 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 C 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 C 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 C 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 C 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 C 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 C 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 C 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 C 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 C 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 C 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 C 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 C 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 C 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 C 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 C 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 C 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 C 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 C 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 C 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 C 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 C 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 C 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 C 551 PRO LEU GLU ALA VAL ARG MET GLN ASN LEU ILE ALA ARG
SEQRES 32 C 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 C 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 C 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 C 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 C 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 C 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 C 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 C 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 C 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 C 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 C 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 C 551 VAL VAL PRO VAL PRO
SEQRES 1 D 551 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 551 LEU VAL PRO ARG GLY SER HIS MET SER LYS PRO HIS SER
SEQRES 3 D 551 GLU ALA GLY THR ALA PHE ILE GLN THR GLN GLN LEU HIS
SEQRES 4 D 551 ALA ALA MET ALA ASP THR PHE LEU GLU HIS MET CYS ARG
SEQRES 5 D 551 LEU ASP ILE ASP SER PRO PRO ILE THR ALA ARG ASN THR
SEQRES 6 D 551 GLY ILE ILE CYS THR ILE GLY PRO ALA SER ARG SER VAL
SEQRES 7 D 551 GLU THR LEU LYS GLU MET ILE LYS SER GLY MET ASN VAL
SEQRES 8 D 551 ALA ARG LEU ASN PHE SER HIS GLY THR HIS GLU TYR HIS
SEQRES 9 D 551 ALA GLU THR ILE LYS ASN VAL ARG THR ALA THR GLU SER
SEQRES 10 D 551 PHE ALA SER ASP PRO ILE LEU TYR ARG PRO VAL ALA VAL
SEQRES 11 D 551 ALA LEU ASP THR LYS GLY PRO GLU ILE ARG THR GLY LEU
SEQRES 12 D 551 ILE LYS GLY SER GLY THR ALA GLU VAL GLU LEU LYS LYS
SEQRES 13 D 551 GLY ALA THR LEU LYS ILE THR LEU ASP ASN ALA TYR MET
SEQRES 14 D 551 GLU LYS CYS ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS
SEQRES 15 D 551 ASN ILE CYS LYS VAL VAL GLU VAL GLY SER LYS ILE TYR
SEQRES 16 D 551 VAL ASP ASP GLY LEU ILE SER LEU GLN VAL LYS GLN LYS
SEQRES 17 D 551 GLY ALA ASP PHE LEU VAL THR GLU VAL GLU ASN GLY GLY
SEQRES 18 D 551 SER LEU GLY SER LYS LYS GLY VAL ASN LEU PRO GLY ALA
SEQRES 19 D 551 ALA VAL ASP LEU PRO ALA VAL SER GLU LYS ASP ILE GLN
SEQRES 20 D 551 ASP LEU LYS PHE GLY VAL GLU GLN ASP VAL ASP MET VAL
SEQRES 21 D 551 PHE ALA SER PHE ILE ARG LYS ALA SER ASP VAL HIS GLU
SEQRES 22 D 551 VAL ARG LYS VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS
SEQRES 23 D 551 ILE ILE SER LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG
SEQRES 24 D 551 PHE ASP GLU ILE LEU GLU ALA SER ASP GLY ILE MET VAL
SEQRES 25 D 551 ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS
SEQRES 26 D 551 VAL PHE LEU ALA GLN LYS MET MET ILE GLY ARG CYS ASN
SEQRES 27 D 551 ARG ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET LEU
SEQRES 28 D 551 GLU SER MET ILE LYS LYS PRO ARG PRO THR ARG ALA GLU
SEQRES 29 D 551 GLY SER ASP VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP
SEQRES 30 D 551 CYS ILE MET LEU SER GLY GLU THR ALA LYS GLY ASP TYR
SEQRES 31 D 551 PRO LEU GLU ALA VAL ARG MET GLN ASN LEU ILE ALA ARG
SEQRES 32 D 551 GLU ALA GLU ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU
SEQRES 33 D 551 GLU LEU ARG ARG LEU ALA PRO ILE THR SER ASP PRO THR
SEQRES 34 D 551 GLU ALA THR ALA VAL GLY ALA VAL GLU ALA SER PHE LYS
SEQRES 35 D 551 CYS CYS SER GLY ALA ILE ILE VAL LEU THR LYS SER GLY
SEQRES 36 D 551 ARG SER ALA HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA
SEQRES 37 D 551 PRO ILE ILE ALA VAL THR ARG ASN PRO GLN THR ALA ARG
SEQRES 38 D 551 GLN ALA HIS LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS
SEQRES 39 D 551 LYS ASP PRO VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP
SEQRES 40 D 551 LEU ARG VAL ASN PHE ALA MET ASN VAL GLY LYS ALA ARG
SEQRES 41 D 551 GLY PHE PHE LYS LYS GLY ASP VAL VAL ILE VAL LEU THR
SEQRES 42 D 551 GLY TRP ARG PRO GLY SER GLY PHE THR ASN THR MET ARG
SEQRES 43 D 551 VAL VAL PRO VAL PRO
HET PO4 A 601 5
HET PO4 A 602 5
HET PHE A 603 12
HET PO4 B 601 5
HET PHE B 602 12
HET PO4 C 601 5
HET PHE C 602 12
HET PO4 D 601 5
HET PHE D 602 12
HETNAM PO4 PHOSPHATE ION
HETNAM PHE PHENYLALANINE
FORMUL 5 PO4 5(O4 P 3-)
FORMUL 7 PHE 4(C9 H11 N O2)
FORMUL 14 HOH *103(H2 O)
HELIX 1 1 SER A 57 GLY A 68 1 12
HELIX 2 2 THR A 80 GLU A 96 1 17
HELIX 3 3 ASP A 145 MET A 149 5 5
HELIX 4 4 ASN A 163 VAL A 168 1 6
HELIX 5 5 SER A 222 GLN A 235 1 14
HELIX 6 6 LYS A 247 GLY A 259 1 13
HELIX 7 7 ASN A 273 ARG A 279 1 7
HELIX 8 8 ARG A 279 SER A 287 1 9
HELIX 9 9 ARG A 294 ILE A 301 1 8
HELIX 10 10 LYS A 305 GLY A 321 1 17
HELIX 11 11 LEU A 331 LYS A 336 5 6
HELIX 12 12 THR A 341 GLY A 355 1 15
HELIX 13 13 SER A 362 LYS A 367 1 6
HELIX 14 14 TYR A 370 GLU A 386 1 17
HELIX 15 15 ALA A 387 ILE A 389 5 3
HELIX 16 16 TYR A 390 LEU A 401 1 12
HELIX 17 17 PRO A 408 CYS A 423 1 16
HELIX 18 18 GLY A 435 TYR A 444 1 10
HELIX 19 19 ASN A 456 ALA A 463 1 8
HELIX 20 20 HIS A 464 TYR A 466 5 3
HELIX 21 21 ALA A 481 ARG A 500 1 20
HELIX 22 22 THR B 25 ARG B 32 1 8
HELIX 23 23 SER B 57 GLY B 68 1 12
HELIX 24 24 THR B 80 GLU B 96 1 17
HELIX 25 25 SER B 222 ASP B 236 1 15
HELIX 26 26 LYS B 247 GLY B 259 1 13
HELIX 27 27 ASN B 273 ARG B 279 1 7
HELIX 28 28 ARG B 279 SER B 287 1 9
HELIX 29 29 ARG B 294 ILE B 301 1 8
HELIX 30 30 PRO B 302 GLU B 304 5 3
HELIX 31 31 LYS B 305 GLY B 321 1 17
HELIX 32 32 LEU B 331 LYS B 336 5 6
HELIX 33 33 THR B 341 ASP B 354 1 14
HELIX 34 34 SER B 362 LYS B 367 1 6
HELIX 35 35 TYR B 370 ALA B 385 1 16
HELIX 36 36 TYR B 390 ALA B 402 1 13
HELIX 37 37 ASP B 407 CYS B 423 1 17
HELIX 38 38 GLY B 435 ARG B 443 1 9
HELIX 39 39 ASN B 456 ALA B 463 1 8
HELIX 40 40 HIS B 464 TYR B 466 5 3
HELIX 41 41 ALA B 481 GLY B 501 1 21
HELIX 42 42 THR C 25 ARG C 32 1 8
HELIX 43 43 SER C 57 GLY C 68 1 12
HELIX 44 44 THR C 80 GLU C 96 1 17
HELIX 45 45 SER C 97 ALA C 99 5 3
HELIX 46 46 ASP C 145 MET C 149 5 5
HELIX 47 47 SER C 222 GLN C 235 1 14
HELIX 48 48 LYS C 247 GLY C 259 1 13
HELIX 49 49 ASN C 273 ARG C 279 1 7
HELIX 50 50 ARG C 279 SER C 287 1 9
HELIX 51 51 ARG C 294 ILE C 301 1 8
HELIX 52 52 PRO C 302 GLU C 304 5 3
HELIX 53 53 LYS C 305 GLY C 321 1 17
HELIX 54 54 LEU C 331 LYS C 336 5 6
HELIX 55 55 THR C 341 GLY C 355 1 15
HELIX 56 56 SER C 362 LYS C 367 1 6
HELIX 57 57 TYR C 370 GLU C 386 1 17
HELIX 58 58 ALA C 387 ILE C 389 5 3
HELIX 59 59 TYR C 390 ALA C 402 1 13
HELIX 60 60 ASP C 407 CYS C 423 1 17
HELIX 61 61 GLY C 435 ARG C 443 1 9
HELIX 62 62 ASN C 456 ALA C 463 1 8
HELIX 63 63 HIS C 464 TYR C 466 5 3
HELIX 64 64 ALA C 481 ARG C 500 1 20
HELIX 65 65 THR D 25 ARG D 32 1 8
HELIX 66 66 SER D 57 GLY D 68 1 12
HELIX 67 67 THR D 80 GLU D 96 1 17
HELIX 68 68 SER D 97 ALA D 99 5 3
HELIX 69 69 ASP D 145 MET D 149 5 5
HELIX 70 70 SER D 222 GLN D 235 1 14
HELIX 71 71 LYS D 247 GLY D 259 1 13
HELIX 72 72 ASN D 273 ARG D 279 1 7
HELIX 73 73 ARG D 279 GLU D 285 1 7
HELIX 74 74 ARG D 294 ILE D 301 1 8
HELIX 75 75 PRO D 302 GLY D 321 1 20
HELIX 76 76 LEU D 331 LYS D 336 5 6
HELIX 77 77 THR D 341 GLY D 355 1 15
HELIX 78 78 SER D 362 LYS D 367 1 6
HELIX 79 79 TYR D 370 ILE D 389 1 20
HELIX 80 80 TYR D 390 LEU D 401 1 12
HELIX 81 81 ASP D 407 CYS D 423 1 17
HELIX 82 82 GLY D 435 ARG D 443 1 9
HELIX 83 83 ASN D 456 ALA D 463 1 8
HELIX 84 84 HIS D 464 TYR D 466 5 3
HELIX 85 85 ALA D 481 ARG D 500 1 20
SHEET 1 A 9 GLY A 46 THR A 50 0
SHEET 2 A 9 VAL A 71 ASN A 75 1 O VAL A 71 N CYS A 49
SHEET 3 A 9 ALA A 109 ASP A 113 1 O ALA A 111 N ALA A 72
SHEET 4 A 9 MET A 239 ALA A 242 1 O PHE A 241 N LEU A 112
SHEET 5 A 9 LYS A 266 ILE A 271 1 O LYS A 270 N ALA A 242
SHEET 6 A 9 GLY A 289 ALA A 293 1 O MET A 291 N SER A 269
SHEET 7 A 9 VAL A 324 ALA A 327 1 O ILE A 325 N VAL A 292
SHEET 8 A 9 CYS A 358 LEU A 361 1 O MET A 360 N CYS A 326
SHEET 9 A 9 GLY A 46 THR A 50 1 N ILE A 48 O LEU A 361
SHEET 1 B 2 VAL A 132 LEU A 134 0
SHEET 2 B 2 GLY A 201 LEU A 203 -1 O GLY A 201 N LEU A 134
SHEET 1 C 6 ILE A 156 TRP A 158 0
SHEET 2 C 6 THR A 139 THR A 143 1 N THR A 143 O LEU A 157
SHEET 3 C 6 PHE A 192 ASN A 199 -1 O LEU A 193 N ILE A 142
SHEET 4 C 6 ILE A 181 LYS A 188 -1 N GLN A 187 O VAL A 194
SHEET 5 C 6 LYS A 173 VAL A 176 -1 N VAL A 176 O ILE A 181
SHEET 6 C 6 VAL A 209 ASN A 210 -1 O ASN A 210 N TYR A 175
SHEET 1 D10 ILE A 469 LEU A 473 0
SHEET 2 D10 ILE A 450 THR A 454 1 N ILE A 450 O PHE A 470
SHEET 3 D10 ALA A 427 LEU A 431 1 N VAL A 430 O ILE A 451
SHEET 4 D10 VAL A 508 THR A 513 1 O LEU A 512 N ILE A 429
SHEET 5 D10 THR A 524 PRO A 529 -1 O ARG A 526 N VAL A 511
SHEET 6 D10 THR B 524 PRO B 529 -1 O MET B 525 N MET A 525
SHEET 7 D10 VAL B 508 THR B 513 -1 N VAL B 511 O ARG B 526
SHEET 8 D10 ILE B 428 LEU B 431 1 N ILE B 429 O LEU B 512
SHEET 9 D10 ILE B 450 THR B 454 1 O ILE B 451 N VAL B 430
SHEET 10 D10 ILE B 469 LEU B 473 1 O PHE B 470 N ILE B 450
SHEET 1 E 9 GLY B 46 THR B 50 0
SHEET 2 E 9 VAL B 71 ASN B 75 1 O ARG B 73 N CYS B 49
SHEET 3 E 9 ALA B 109 ASP B 113 1 O ALA B 111 N ALA B 72
SHEET 4 E 9 MET B 239 ALA B 242 1 O PHE B 241 N LEU B 112
SHEET 5 E 9 LYS B 266 ILE B 271 1 O ILE B 268 N VAL B 240
SHEET 6 E 9 GLY B 289 ALA B 293 1 O MET B 291 N SER B 269
SHEET 7 E 9 VAL B 324 ALA B 327 1 O ILE B 325 N VAL B 292
SHEET 8 E 9 CYS B 358 LEU B 361 1 O MET B 360 N CYS B 326
SHEET 9 E 9 GLY B 46 THR B 50 1 N ILE B 48 O LEU B 361
SHEET 1 F 9 GLY C 46 THR C 50 0
SHEET 2 F 9 MET C 69 ASN C 75 1 O ASN C 70 N ILE C 47
SHEET 3 F 9 ALA C 109 ASP C 113 1 O ALA C 111 N ALA C 72
SHEET 4 F 9 MET C 239 ALA C 242 1 O PHE C 241 N LEU C 112
SHEET 5 F 9 LYS C 266 ILE C 271 1 O ILE C 268 N VAL C 240
SHEET 6 F 9 GLY C 289 ALA C 293 1 O MET C 291 N ILE C 271
SHEET 7 F 9 VAL C 324 ALA C 327 1 O ILE C 325 N VAL C 292
SHEET 8 F 9 CYS C 358 LEU C 361 1 O MET C 360 N CYS C 326
SHEET 9 F 9 GLY C 46 THR C 50 1 N ILE C 48 O LEU C 361
SHEET 1 G 2 VAL C 132 LEU C 134 0
SHEET 2 G 2 GLY C 201 LEU C 203 -1 O LEU C 203 N VAL C 132
SHEET 1 H 6 ILE C 156 TRP C 158 0
SHEET 2 H 6 THR C 139 THR C 143 1 N THR C 143 O LEU C 157
SHEET 3 H 6 PHE C 192 ASN C 199 -1 O THR C 195 N LEU C 140
SHEET 4 H 6 ILE C 181 LYS C 188 -1 N LYS C 186 O VAL C 194
SHEET 5 H 6 LYS C 173 VAL C 176 -1 N VAL C 176 O ILE C 181
SHEET 6 H 6 VAL C 209 ASN C 210 -1 O ASN C 210 N TYR C 175
SHEET 1 I10 ILE C 469 LEU C 473 0
SHEET 2 I10 ILE C 450 THR C 454 1 N ILE C 450 O PHE C 470
SHEET 3 I10 ILE C 428 LEU C 431 1 N VAL C 430 O ILE C 451
SHEET 4 I10 VAL C 508 THR C 513 1 O LEU C 512 N ILE C 429
SHEET 5 I10 THR C 524 PRO C 529 -1 O THR C 524 N THR C 513
SHEET 6 I10 THR D 524 PRO D 529 -1 O MET D 525 N MET C 525
SHEET 7 I10 VAL D 508 THR D 513 -1 N VAL D 509 O VAL D 528
SHEET 8 I10 ILE D 428 LEU D 431 1 N ILE D 429 O ILE D 510
SHEET 9 I10 ILE D 450 THR D 454 1 O ILE D 451 N VAL D 430
SHEET 10 I10 ILE D 469 LEU D 473 1 O PHE D 470 N ILE D 450
SHEET 1 J 9 GLY D 46 THR D 50 0
SHEET 2 J 9 VAL D 71 ASN D 75 1 O ARG D 73 N CYS D 49
SHEET 3 J 9 ALA D 109 ASP D 113 1 O ALA D 111 N ALA D 72
SHEET 4 J 9 MET D 239 ALA D 242 1 O PHE D 241 N LEU D 112
SHEET 5 J 9 LYS D 266 ILE D 271 1 O ILE D 268 N VAL D 240
SHEET 6 J 9 GLY D 289 ALA D 293 1 O MET D 291 N SER D 269
SHEET 7 J 9 VAL D 324 ALA D 327 1 O ILE D 325 N VAL D 292
SHEET 8 J 9 CYS D 358 LEU D 361 1 O MET D 360 N CYS D 326
SHEET 9 J 9 GLY D 46 THR D 50 1 N ILE D 48 O LEU D 361
SHEET 1 K 7 ILE D 119 ARG D 120 0
SHEET 2 K 7 GLY D 208 ASN D 210 -1 O VAL D 209 N ILE D 119
SHEET 3 K 7 LYS D 173 VAL D 176 -1 N TYR D 175 O ASN D 210
SHEET 4 K 7 ILE D 181 LYS D 188 -1 O ILE D 181 N VAL D 176
SHEET 5 K 7 PHE D 192 VAL D 197 -1 O GLU D 196 N GLN D 184
SHEET 6 K 7 THR D 139 THR D 143 -1 N LEU D 140 O THR D 195
SHEET 7 K 7 ILE D 156 TRP D 158 1 O LEU D 157 N THR D 143
SHEET 1 L 2 VAL D 132 LEU D 134 0
SHEET 2 L 2 GLY D 201 LEU D 203 -1 O LEU D 203 N VAL D 132
CISPEP 1 THR B 405 SER B 406 0 -1.50
SITE 1 AC1 7 THR A 432 LYS A 433 SER A 434 GLY A 435
SITE 2 AC1 7 ARG A 436 SER A 437 THR A 522
SITE 1 AC2 3 ASN A 75 HIS A 78 ARG A 120
SITE 1 AC3 10 ARG A 43 ASN A 44 THR A 45 ASN A 70
SITE 2 AC3 10 ARG A 106 HIS A 464 GLY A 468 ILE A 469
SITE 3 AC3 10 PHE A 470 PRO A 471
SITE 1 AC4 7 THR B 432 LYS B 433 SER B 434 ARG B 436
SITE 2 AC4 7 SER B 437 THR B 522 HOH B 709
SITE 1 AC5 9 ARG B 43 ASN B 44 THR B 45 ASN B 70
SITE 2 AC5 9 ARG B 106 HIS B 464 GLY B 468 ILE B 469
SITE 3 AC5 9 PHE B 470
SITE 1 AC6 7 THR C 432 LYS C 433 SER C 434 GLY C 435
SITE 2 AC6 7 ARG C 436 SER C 437 THR C 522
SITE 1 AC7 8 ARG C 43 ASN C 44 ASN C 70 ARG C 106
SITE 2 AC7 8 HIS C 464 GLY C 468 ILE C 469 PHE C 470
SITE 1 AC8 6 THR D 432 LYS D 433 SER D 434 ARG D 436
SITE 2 AC8 6 SER D 437 HOH D 724
SITE 1 AC9 9 ARG D 43 ASN D 44 ASN D 70 ARG D 106
SITE 2 AC9 9 HIS D 464 GLY D 468 ILE D 469 PHE D 470
SITE 3 AC9 9 HOH D 722
CRYST1 97.260 70.600 167.600 90.00 105.72 90.00 P 1 21 1 8
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 0.010282 0.000000 0.002894 0.00000
SCALE2 0.000000 0.014164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
