HEADER LYASE 07-DEC-05 2FAF
TITLE THE STRUCTURE OF CHICKEN MITOCHONDRIAL PEPCK.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOENOLPYRUVATE CARBOXYLASE, PEPCK-M;
COMPND 5 EC: 4.1.1.32
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 OTHER_DETAILS: LIVER MITOCHONDRIAL IOSZYME
KEYWDS PHOSPHOENOLPYRUVATE CARBOXYKINASE, PEPCK, KINASE, PHOSPHORYL
KEYWDS 2 TRANSFER, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HOLYOAK,S.M.SULLIVAN,T.NOWAK
REVDAT 7 30-AUG-23 2FAF 1 HETSYN
REVDAT 6 29-JUL-20 2FAF 1 COMPND REMARK SEQADV HET
REVDAT 6 2 1 HETNAM HETSYN FORMUL LINK
REVDAT 6 3 1 SITE ATOM
REVDAT 5 18-OCT-17 2FAF 1 REMARK
REVDAT 4 13-JUL-11 2FAF 1 VERSN
REVDAT 3 24-FEB-09 2FAF 1 VERSN
REVDAT 2 18-JUL-06 2FAF 1 JRNL
REVDAT 1 27-JUN-06 2FAF 0
JRNL AUTH T.HOLYOAK,S.M.SULLIVAN,T.NOWAK
JRNL TITL STRUCTURAL INSIGHTS INTO THE MECHANISM OF PEPCK CATALYSIS
JRNL REF BIOCHEMISTRY V. 45 8254 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16819824
JRNL DOI 10.1021/BI060269G
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 123906
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6219
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7895
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 433
REMARK 3 BIN FREE R VALUE : 0.2280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9306
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.648
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9908 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13511 ; 1.332 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1258 ; 5.845 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 455 ;28.655 ;22.242
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1545 ;12.770 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;16.796 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1393 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7818 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4628 ; 0.197 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6667 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 862 ; 0.127 ; 0.200
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): 80 ; 0.203 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.187 ; 0.200
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): 6231 ; 0.717 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9820 ; 1.058 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4223 ; 1.753 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3656 ; 2.731 ; 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 : 40
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 34 A 52
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9490 -36.1700 69.5750
REMARK 3 T TENSOR
REMARK 3 T11: -0.0002 T22: -0.0570
REMARK 3 T33: -0.0193 T12: 0.0191
REMARK 3 T13: 0.0059 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.7675 L22: 1.2012
REMARK 3 L33: 3.0777 L12: -0.3185
REMARK 3 L13: 0.6776 L23: -1.4801
REMARK 3 S TENSOR
REMARK 3 S11: -0.0291 S12: 0.2087 S13: -0.0494
REMARK 3 S21: -0.2511 S22: 0.0558 S23: 0.1207
REMARK 3 S31: 0.2943 S32: 0.0004 S33: -0.0267
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 53 A 61
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2090 -36.4760 75.3430
REMARK 3 T TENSOR
REMARK 3 T11: -0.0428 T22: -0.0415
REMARK 3 T33: -0.0120 T12: 0.0390
REMARK 3 T13: 0.0272 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 6.1201 L22: 3.2823
REMARK 3 L33: 2.1661 L12: 1.6901
REMARK 3 L13: 1.0354 L23: -0.2031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: 0.0810 S13: 0.1496
REMARK 3 S21: -0.0260 S22: 0.0732 S23: 0.1522
REMARK 3 S31: -0.0183 S32: -0.1144 S33: -0.0729
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 62 A 80
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7820 -34.6170 81.8200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0008 T22: -0.0896
REMARK 3 T33: -0.0292 T12: 0.0137
REMARK 3 T13: -0.0090 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.7585 L22: 5.4369
REMARK 3 L33: 2.2480 L12: 1.1461
REMARK 3 L13: -0.0874 L23: -2.7383
REMARK 3 S TENSOR
REMARK 3 S11: -0.1659 S12: -0.0317 S13: 0.2132
REMARK 3 S21: -0.0396 S22: 0.1722 S23: 0.1603
REMARK 3 S31: -0.0254 S32: -0.1188 S33: -0.0063
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 81 A 105
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1020 -51.8050 82.6440
REMARK 3 T TENSOR
REMARK 3 T11: -0.0046 T22: -0.0827
REMARK 3 T33: -0.0251 T12: 0.0082
REMARK 3 T13: 0.0020 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.8343 L22: 0.7720
REMARK 3 L33: 0.7742 L12: 0.2261
REMARK 3 L13: 0.2950 L23: 0.0415
REMARK 3 S TENSOR
REMARK 3 S11: -0.0306 S12: -0.0443 S13: -0.0593
REMARK 3 S21: 0.0260 S22: 0.0085 S23: 0.0451
REMARK 3 S31: 0.0301 S32: -0.0226 S33: 0.0221
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 106 A 117
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2970 -49.1730 60.3580
REMARK 3 T TENSOR
REMARK 3 T11: -0.0642 T22: -0.0247
REMARK 3 T33: -0.0281 T12: -0.0116
REMARK 3 T13: 0.0024 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 2.2432 L22: 0.6175
REMARK 3 L33: 6.5363 L12: -0.1979
REMARK 3 L13: -0.4320 L23: -0.4345
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: 0.1362 S13: -0.0505
REMARK 3 S21: -0.0512 S22: -0.2017 S23: -0.0165
REMARK 3 S31: 0.0030 S32: 0.0787 S33: 0.1846
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 : A 118 A 143
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3460 -53.9430 49.0960
REMARK 3 T TENSOR
REMARK 3 T11: -0.0338 T22: -0.0072
REMARK 3 T33: -0.0184 T12: -0.0026
REMARK 3 T13: 0.0070 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.3319 L22: 1.0447
REMARK 3 L33: 0.8782 L12: -0.2160
REMARK 3 L13: -0.4612 L23: 0.4775
REMARK 3 S TENSOR
REMARK 3 S11: 0.0499 S12: 0.0822 S13: -0.0440
REMARK 3 S21: -0.0979 S22: -0.0473 S23: -0.1409
REMARK 3 S31: 0.0294 S32: -0.2280 S33: -0.0026
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 : A 144 A 196
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7780 -40.8400 76.0780
REMARK 3 T TENSOR
REMARK 3 T11: -0.0042 T22: -0.0572
REMARK 3 T33: -0.0175 T12: 0.0051
REMARK 3 T13: 0.0052 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 1.2921 L22: 0.0820
REMARK 3 L33: 0.4904 L12: -0.2158
REMARK 3 L13: -0.0122 L23: 0.0883
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.0179 S13: 0.0231
REMARK 3 S21: 0.0710 S22: 0.0121 S23: 0.0060
REMARK 3 S31: -0.0530 S32: -0.0220 S33: -0.0128
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 : A 197 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): -18.6400 -41.1200 72.0210
REMARK 3 T TENSOR
REMARK 3 T11: -0.0218 T22: -0.0371
REMARK 3 T33: -0.0246 T12: 0.0076
REMARK 3 T13: 0.0065 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 2.1792 L22: 1.3551
REMARK 3 L33: 2.5266 L12: 0.8194
REMARK 3 L13: -1.2302 L23: -1.3998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0947 S12: 0.1756 S13: -0.0301
REMARK 3 S21: -0.0048 S22: 0.1641 S23: 0.0469
REMARK 3 S31: -0.0091 S32: -0.2669 S33: -0.0694
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 : A 226 A 262
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4020 -48.1090 72.1900
REMARK 3 T TENSOR
REMARK 3 T11: -0.0253 T22: -0.0537
REMARK 3 T33: -0.0064 T12: 0.0004
REMARK 3 T13: -0.0018 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.9304 L22: 0.1743
REMARK 3 L33: 2.2797 L12: 0.1017
REMARK 3 L13: -0.0846 L23: 0.0144
REMARK 3 S TENSOR
REMARK 3 S11: -0.0226 S12: 0.0749 S13: -0.0451
REMARK 3 S21: 0.0262 S22: 0.0375 S23: 0.0332
REMARK 3 S31: 0.0696 S32: 0.0227 S33: -0.0149
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 : A 263 A 281
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6460 -43.4230 62.4700
REMARK 3 T TENSOR
REMARK 3 T11: -0.0455 T22: -0.0248
REMARK 3 T33: -0.0144 T12: -0.0146
REMARK 3 T13: -0.0020 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 2.9099 L22: 1.9261
REMARK 3 L33: 2.1332 L12: 0.7050
REMARK 3 L13: -1.6659 L23: -0.9876
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: -0.1463 S13: -0.0539
REMARK 3 S21: 0.0549 S22: -0.1017 S23: 0.0792
REMARK 3 S31: -0.0589 S32: 0.1047 S33: 0.1163
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 : A 282 A 308
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8690 -43.1540 61.2150
REMARK 3 T TENSOR
REMARK 3 T11: -0.0495 T22: -0.0194
REMARK 3 T33: -0.0072 T12: -0.0261
REMARK 3 T13: -0.0037 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 3.8568 L22: 0.7893
REMARK 3 L33: 1.3486 L12: 0.7191
REMARK 3 L13: 0.5324 L23: 1.0133
REMARK 3 S TENSOR
REMARK 3 S11: -0.1545 S12: 0.0772 S13: 0.0366
REMARK 3 S21: -0.0603 S22: 0.0461 S23: -0.1022
REMARK 3 S31: -0.0706 S32: 0.0554 S33: 0.1084
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 : A 309 A 324
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7520 -38.3980 63.4170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0300 T22: 0.0558
REMARK 3 T33: 0.0360 T12: -0.0161
REMARK 3 T13: 0.0645 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 6.7869 L22: 1.8538
REMARK 3 L33: 3.7855 L12: -0.5008
REMARK 3 L13: -2.7510 L23: 0.6975
REMARK 3 S TENSOR
REMARK 3 S11: 0.4840 S12: 0.0909 S13: 0.4688
REMARK 3 S21: -0.2705 S22: 0.0292 S23: -0.4985
REMARK 3 S31: -0.6400 S32: 0.3359 S33: -0.5133
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 : A 325 A 350
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3280 -40.3410 66.7760
REMARK 3 T TENSOR
REMARK 3 T11: -0.0418 T22: -0.0272
REMARK 3 T33: -0.0140 T12: -0.0228
REMARK 3 T13: -0.0019 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 0.5870 L22: 0.7005
REMARK 3 L33: 2.7923 L12: -0.3140
REMARK 3 L13: -0.1277 L23: -0.0296
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: -0.0237 S13: 0.0775
REMARK 3 S21: 0.0550 S22: -0.0111 S23: -0.0486
REMARK 3 S31: -0.0582 S32: -0.1642 S33: 0.0091
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 : A 351 A 431
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2500 -47.0250 81.0520
REMARK 3 T TENSOR
REMARK 3 T11: -0.0194 T22: -0.0819
REMARK 3 T33: -0.0292 T12: 0.0155
REMARK 3 T13: -0.0116 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.0415 L22: 1.4790
REMARK 3 L33: 1.5680 L12: 0.7124
REMARK 3 L13: 0.0263 L23: -0.5422
REMARK 3 S TENSOR
REMARK 3 S11: -0.0635 S12: 0.0729 S13: 0.0930
REMARK 3 S21: -0.0636 S22: 0.0992 S23: 0.0956
REMARK 3 S31: -0.0352 S32: 0.0131 S33: -0.0357
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 : A 432 A 495
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3450 -46.6960 55.0920
REMARK 3 T TENSOR
REMARK 3 T11: -0.0664 T22: -0.0442
REMARK 3 T33: 0.0165 T12: -0.0143
REMARK 3 T13: 0.0259 T23: 0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 0.7454 L22: 0.7591
REMARK 3 L33: 0.9932 L12: -0.2533
REMARK 3 L13: -0.0646 L23: 0.3680
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: -0.0113 S13: -0.0565
REMARK 3 S21: -0.0834 S22: -0.0718 S23: -0.1371
REMARK 3 S31: -0.0138 S32: 0.1136 S33: 0.0456
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 : A 496 A 521
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2900 -48.4590 54.7400
REMARK 3 T TENSOR
REMARK 3 T11: -0.0335 T22: -0.0333
REMARK 3 T33: -0.0156 T12: -0.0056
REMARK 3 T13: 0.0064 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 0.7596 L22: 1.7141
REMARK 3 L33: 1.1362 L12: -0.1051
REMARK 3 L13: -0.5215 L23: -0.0517
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: -0.0284 S13: -0.0393
REMARK 3 S21: 0.0116 S22: -0.0396 S23: -0.0083
REMARK 3 S31: -0.0259 S32: -0.0192 S33: 0.0893
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 522 A 546
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7870 -52.4610 55.7010
REMARK 3 T TENSOR
REMARK 3 T11: -0.0990 T22: -0.0614
REMARK 3 T33: -0.0211 T12: 0.0062
REMARK 3 T13: 0.0359 T23: 0.0506
REMARK 3 L TENSOR
REMARK 3 L11: 2.0094 L22: 8.5963
REMARK 3 L33: 3.3700 L12: -1.9168
REMARK 3 L13: 1.5356 L23: -2.6996
REMARK 3 S TENSOR
REMARK 3 S11: -0.0688 S12: -0.0867 S13: -0.1412
REMARK 3 S21: -0.1905 S22: 0.1664 S23: -0.0468
REMARK 3 S31: -0.0729 S32: -0.0600 S33: -0.0976
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 547 A 577
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1520 -56.8820 52.3860
REMARK 3 T TENSOR
REMARK 3 T11: -0.1194 T22: -0.0771
REMARK 3 T33: 0.0283 T12: -0.0108
REMARK 3 T13: 0.0439 T23: 0.0689
REMARK 3 L TENSOR
REMARK 3 L11: 1.2010 L22: 3.0515
REMARK 3 L33: 4.1309 L12: -0.5445
REMARK 3 L13: -0.2009 L23: 0.8761
REMARK 3 S TENSOR
REMARK 3 S11: -0.0325 S12: 0.0131 S13: -0.1228
REMARK 3 S21: -0.1747 S22: -0.0594 S23: -0.1769
REMARK 3 S31: 0.2698 S32: -0.0846 S33: 0.0919
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 578 A 606
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1930 -64.2480 45.8110
REMARK 3 T TENSOR
REMARK 3 T11: -0.0442 T22: -0.0837
REMARK 3 T33: 0.0867 T12: -0.0166
REMARK 3 T13: 0.0146 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 2.8241 L22: 2.0579
REMARK 3 L33: 2.9765 L12: 0.6974
REMARK 3 L13: 1.5359 L23: 1.3264
REMARK 3 S TENSOR
REMARK 3 S11: -0.2241 S12: -0.0787 S13: -0.2473
REMARK 3 S21: -0.3522 S22: -0.1717 S23: 0.2071
REMARK 3 S31: 0.1212 S32: -0.3110 S33: 0.3958
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 607 A 641
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3070 -55.5810 46.5860
REMARK 3 T TENSOR
REMARK 3 T11: -0.0359 T22: -0.0514
REMARK 3 T33: -0.0262 T12: -0.0151
REMARK 3 T13: 0.0200 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.9140 L22: 1.3733
REMARK 3 L33: 0.8573 L12: -0.8528
REMARK 3 L13: -0.5656 L23: 0.2217
REMARK 3 S TENSOR
REMARK 3 S11: -0.0404 S12: 0.0467 S13: -0.0833
REMARK 3 S21: -0.1030 S22: -0.0651 S23: -0.0396
REMARK 3 S31: 0.0137 S32: -0.1538 S33: 0.1056
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 34 B 69
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5650 -67.1510 -9.6400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0047 T22: -0.0628
REMARK 3 T33: -0.1045 T12: -0.0142
REMARK 3 T13: -0.0307 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 3.8141 L22: 2.1041
REMARK 3 L33: 2.6301 L12: -0.7211
REMARK 3 L13: 0.1405 L23: -0.8719
REMARK 3 S TENSOR
REMARK 3 S11: -0.0360 S12: 0.0098 S13: 0.1145
REMARK 3 S21: -0.1805 S22: -0.0193 S23: -0.2753
REMARK 3 S31: 0.4387 S32: 0.1765 S33: 0.0553
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 70 B 106
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0810 -56.2350 -14.2500
REMARK 3 T TENSOR
REMARK 3 T11: -0.0014 T22: -0.0215
REMARK 3 T33: -0.0911 T12: 0.0077
REMARK 3 T13: -0.0134 T23: 0.0701
REMARK 3 L TENSOR
REMARK 3 L11: 0.5815 L22: 0.9692
REMARK 3 L33: 2.4006 L12: 0.5679
REMARK 3 L13: -0.3751 L23: -0.1366
REMARK 3 S TENSOR
REMARK 3 S11: -0.0286 S12: 0.1194 S13: 0.0664
REMARK 3 S21: -0.2108 S22: 0.0509 S23: -0.0383
REMARK 3 S31: 0.1339 S32: 0.0030 S33: -0.0223
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 107 B 149
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5800 -50.8170 0.4670
REMARK 3 T TENSOR
REMARK 3 T11: -0.1119 T22: 0.0531
REMARK 3 T33: -0.0761 T12: 0.0469
REMARK 3 T13: -0.0035 T23: 0.1207
REMARK 3 L TENSOR
REMARK 3 L11: 1.5415 L22: 0.6672
REMARK 3 L33: 6.4983 L12: -0.4198
REMARK 3 L13: -0.5017 L23: 0.1241
REMARK 3 S TENSOR
REMARK 3 S11: 0.0699 S12: 0.1652 S13: 0.1851
REMARK 3 S21: -0.0844 S22: 0.0934 S23: 0.0835
REMARK 3 S31: -0.2575 S32: -0.2038 S33: -0.1633
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 150 B 199
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5050 -59.3260 -2.2240
REMARK 3 T TENSOR
REMARK 3 T11: -0.0042 T22: -0.0313
REMARK 3 T33: -0.0630 T12: -0.0166
REMARK 3 T13: -0.0221 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 0.8001 L22: 0.2421
REMARK 3 L33: 1.9746 L12: -0.0833
REMARK 3 L13: -0.4098 L23: -0.1507
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: 0.0018 S13: 0.0484
REMARK 3 S21: -0.0478 S22: 0.0241 S23: -0.0221
REMARK 3 S31: 0.0986 S32: 0.0830 S33: -0.0465
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 200 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2490 -60.8140 -10.2800
REMARK 3 T TENSOR
REMARK 3 T11: -0.0595 T22: 0.0111
REMARK 3 T33: -0.0956 T12: -0.0387
REMARK 3 T13: -0.0445 T23: 0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 1.4314 L22: 3.6763
REMARK 3 L33: 4.9356 L12: 0.0606
REMARK 3 L13: -0.2792 L23: -2.5297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0209 S12: 0.1489 S13: 0.0498
REMARK 3 S21: -0.0107 S22: 0.1433 S23: 0.1027
REMARK 3 S31: 0.0439 S32: -0.4865 S33: -0.1224
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 224 B 251
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0490 -53.9090 -4.9600
REMARK 3 T TENSOR
REMARK 3 T11: -0.0610 T22: 0.0174
REMARK 3 T33: -0.0744 T12: 0.0054
REMARK 3 T13: -0.0448 T23: 0.0864
REMARK 3 L TENSOR
REMARK 3 L11: 1.7708 L22: 1.7399
REMARK 3 L33: 3.2082 L12: 0.1206
REMARK 3 L13: -1.8857 L23: -0.7997
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: -0.1094 S13: 0.0193
REMARK 3 S21: -0.0066 S22: 0.0535 S23: -0.0394
REMARK 3 S31: 0.0475 S32: -0.1032 S33: -0.0622
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 252 B 279
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8570 -55.8610 0.6380
REMARK 3 T TENSOR
REMARK 3 T11: -0.0214 T22: 0.0138
REMARK 3 T33: -0.0224 T12: 0.0082
REMARK 3 T13: -0.0229 T23: 0.0625
REMARK 3 L TENSOR
REMARK 3 L11: 1.0755 L22: 0.3675
REMARK 3 L33: 5.2371 L12: -0.0425
REMARK 3 L13: -0.8121 L23: -1.2684
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: 0.0788 S13: 0.0527
REMARK 3 S21: -0.0256 S22: -0.0277 S23: 0.0120
REMARK 3 S31: -0.0010 S32: -0.1402 S33: -0.0022
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 280 B 308
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4190 -61.1940 19.5350
REMARK 3 T TENSOR
REMARK 3 T11: -0.0202 T22: -0.0179
REMARK 3 T33: -0.0336 T12: 0.0004
REMARK 3 T13: -0.0057 T23: 0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 0.9481 L22: 0.4428
REMARK 3 L33: 2.4068 L12: -0.3155
REMARK 3 L13: 0.8765 L23: 0.3094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0420 S12: -0.0615 S13: 0.0171
REMARK 3 S21: 0.0778 S22: 0.0387 S23: -0.0231
REMARK 3 S31: 0.0172 S32: -0.0214 S33: -0.0807
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 309 B 320
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6770 -60.4590 27.1760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0052 T22: 0.0474
REMARK 3 T33: -0.0040 T12: -0.0223
REMARK 3 T13: -0.0101 T23: -0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 3.8291 L22: 4.0261
REMARK 3 L33: 9.3307 L12: -1.3920
REMARK 3 L13: 3.4590 L23: -2.4850
REMARK 3 S TENSOR
REMARK 3 S11: 0.0931 S12: -0.0167 S13: -0.1633
REMARK 3 S21: 0.4229 S22: -0.0326 S23: -0.2363
REMARK 3 S31: 0.3193 S32: 0.5743 S33: -0.0605
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 321 B 334
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9220 -61.3930 13.5310
REMARK 3 T TENSOR
REMARK 3 T11: -0.0136 T22: -0.0282
REMARK 3 T33: -0.0340 T12: 0.0071
REMARK 3 T13: -0.0211 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 0.5397 L22: 0.5524
REMARK 3 L33: 3.4356 L12: -0.5410
REMARK 3 L13: 0.4397 L23: -0.2651
REMARK 3 S TENSOR
REMARK 3 S11: 0.0830 S12: 0.0256 S13: 0.0478
REMARK 3 S21: -0.0678 S22: -0.0268 S23: -0.0191
REMARK 3 S31: 0.0913 S32: -0.1164 S33: -0.0562
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 335 B 357
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7710 -59.2140 9.2510
REMARK 3 T TENSOR
REMARK 3 T11: -0.0022 T22: -0.0503
REMARK 3 T33: -0.0476 T12: 0.0268
REMARK 3 T13: -0.0120 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 1.1456 L22: 0.7421
REMARK 3 L33: 3.6032 L12: 0.4282
REMARK 3 L13: -0.5619 L23: -1.5298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: 0.0718 S13: -0.0445
REMARK 3 S21: 0.1098 S22: 0.0458 S23: 0.0121
REMARK 3 S31: 0.0057 S32: -0.0847 S33: -0.0350
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 358 B 376
REMARK 3 ORIGIN FOR THE GROUP (A): 36.4810 -55.4610 -9.0930
REMARK 3 T TENSOR
REMARK 3 T11: 0.0459 T22: 0.1008
REMARK 3 T33: -0.0276 T12: 0.0198
REMARK 3 T13: -0.0605 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 2.9939 L22: 3.4342
REMARK 3 L33: 9.3172 L12: -0.3202
REMARK 3 L13: 2.5677 L23: -1.1456
REMARK 3 S TENSOR
REMARK 3 S11: 0.0538 S12: 0.3476 S13: -0.0056
REMARK 3 S21: -0.6028 S22: -0.1070 S23: 0.3421
REMARK 3 S31: 0.2477 S32: -0.4967 S33: 0.0532
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 377 B 424
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6180 -60.3540 4.5620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0870 T22: 0.1226
REMARK 3 T33: 0.0036 T12: -0.0619
REMARK 3 T13: 0.1705 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 4.2054 L22: 1.3436
REMARK 3 L33: 2.3047 L12: 0.6419
REMARK 3 L13: 0.0738 L23: -0.5154
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: -0.3622 S13: -0.4673
REMARK 3 S21: 0.4339 S22: -0.0259 S23: 0.1925
REMARK 3 S31: 0.1682 S32: -0.6634 S33: -0.0283
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 425 B 443
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9280 -54.1720 -3.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0304 T22: -0.0088
REMARK 3 T33: 0.0035 T12: 0.0305
REMARK 3 T13: -0.0388 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 1.2549 L22: 0.9087
REMARK 3 L33: 2.5671 L12: 0.0595
REMARK 3 L13: 0.2478 L23: -0.0701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: 0.1470 S13: 0.2323
REMARK 3 S21: -0.2271 S22: 0.0004 S23: 0.1611
REMARK 3 S31: -0.1486 S32: -0.2169 S33: -0.0085
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 444 B 464
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6830 -57.8520 27.2990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0054 T22: -0.0405
REMARK 3 T33: -0.0366 T12: -0.0053
REMARK 3 T13: -0.0173 T23: 0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 0.5332 L22: 5.3854
REMARK 3 L33: 1.9122 L12: 0.3439
REMARK 3 L13: -0.1393 L23: 2.0619
REMARK 3 S TENSOR
REMARK 3 S11: 0.1340 S12: 0.0391 S13: 0.0786
REMARK 3 S21: 0.3563 S22: -0.0220 S23: -0.0881
REMARK 3 S31: 0.2140 S32: 0.0695 S33: -0.1120
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 465 B 526
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4530 -54.0900 29.6700
REMARK 3 T TENSOR
REMARK 3 T11: -0.0462 T22: -0.0415
REMARK 3 T33: -0.0374 T12: -0.0122
REMARK 3 T13: 0.0236 T23: 0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 1.5298 L22: 0.7337
REMARK 3 L33: 3.7791 L12: -0.1476
REMARK 3 L13: -0.1792 L23: 0.3161
REMARK 3 S TENSOR
REMARK 3 S11: 0.0432 S12: -0.1062 S13: 0.0658
REMARK 3 S21: 0.0971 S22: -0.0232 S23: 0.0082
REMARK 3 S31: -0.0450 S32: 0.0613 S33: -0.0200
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 527 B 565
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8600 -57.1270 31.5030
REMARK 3 T TENSOR
REMARK 3 T11: -0.0184 T22: -0.0547
REMARK 3 T33: -0.0442 T12: -0.0191
REMARK 3 T13: 0.0095 T23: 0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 2.0944 L22: 1.7063
REMARK 3 L33: 1.2602 L12: -1.1094
REMARK 3 L13: 0.1488 L23: 0.6577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0515 S12: -0.0577 S13: -0.0854
REMARK 3 S21: 0.0314 S22: 0.0184 S23: 0.0753
REMARK 3 S31: 0.1240 S32: 0.0106 S33: -0.0698
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 566 B 609
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8600 -49.6830 38.0650
REMARK 3 T TENSOR
REMARK 3 T11: -0.0265 T22: -0.0709
REMARK 3 T33: 0.0186 T12: 0.0004
REMARK 3 T13: 0.0549 T23: 0.0667
REMARK 3 L TENSOR
REMARK 3 L11: 1.7099 L22: 1.5323
REMARK 3 L33: 0.7908 L12: -1.0200
REMARK 3 L13: -0.5515 L23: 0.2814
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: -0.1258 S13: -0.0483
REMARK 3 S21: 0.2194 S22: 0.1011 S23: 0.2489
REMARK 3 S31: -0.0797 S32: 0.0084 S33: -0.1120
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 610 B 628
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1740 -49.1140 26.7530
REMARK 3 T TENSOR
REMARK 3 T11: -0.0720 T22: -0.0281
REMARK 3 T33: -0.0448 T12: 0.0389
REMARK 3 T13: 0.0309 T23: 0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 1.7686 L22: 2.7670
REMARK 3 L33: 3.4655 L12: -0.1321
REMARK 3 L13: -0.5201 L23: 0.8725
REMARK 3 S TENSOR
REMARK 3 S11: 0.1302 S12: 0.0729 S13: 0.1250
REMARK 3 S21: 0.1156 S22: -0.1045 S23: -0.0550
REMARK 3 S31: -0.0184 S32: -0.3942 S33: -0.0257
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 629 B 641
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8310 -47.8470 35.5080
REMARK 3 T TENSOR
REMARK 3 T11: -0.0265 T22: -0.0426
REMARK 3 T33: -0.0149 T12: 0.0082
REMARK 3 T13: 0.0592 T23: 0.0625
REMARK 3 L TENSOR
REMARK 3 L11: 3.6980 L22: 3.1120
REMARK 3 L33: 3.3126 L12: 0.0443
REMARK 3 L13: -1.0757 L23: 0.1765
REMARK 3 S TENSOR
REMARK 3 S11: 0.1174 S12: 0.2338 S13: 0.0538
REMARK 3 S21: 0.0060 S22: -0.0204 S23: 0.0710
REMARK 3 S31: 0.0537 S32: -0.1075 S33: -0.0970
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 2FAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : UNKNOWN
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123916
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1KHG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 6000, HEPES PH 7.4, N-OCTANOYL
REMARK 280 SUCROSE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 23.86850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 GLU A 482
REMARK 465 ALA A 483
REMARK 465 THR A 484
REMARK 465 ALA A 485
REMARK 465 ALA A 486
REMARK 465 ALA A 487
REMARK 465 GLU A 488
REMARK 465 HIS A 489
REMARK 465 LYS A 490
REMARK 465 GLY A 491
REMARK 465 GLY A 492
REMARK 465 ARG A 493
REMARK 465 GLU B 482
REMARK 465 ALA B 483
REMARK 465 THR B 484
REMARK 465 ALA B 485
REMARK 465 ALA B 486
REMARK 465 ALA B 487
REMARK 465 GLU B 488
REMARK 465 HIS B 489
REMARK 465 LYS B 490
REMARK 465 GLY B 491
REMARK 465 GLY B 492
REMARK 465 ARG B 493
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 A 1949 O HOH B 1937 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS B 411 CE LYS B 411 NZ 0.285
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 B 195 CG - CD - NE ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG B 195 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG B 195 NE - CZ - NH1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ARG B 195 NE - CZ - NH2 ANGL. DEV. = 8.3 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 ASP A 205 -146.49 -137.01
REMARK 500 LYS A 263 -41.81 -130.86
REMARK 500 SER A 305 9.62 52.74
REMARK 500 ASP A 330 -52.27 -148.29
REMARK 500 ASN A 363 74.85 -154.20
REMARK 500 ASN A 540 33.55 -74.90
REMARK 500 PHE A 549 -130.74 49.89
REMARK 500 ASP B 205 -142.26 -131.65
REMARK 500 LYS B 263 -40.03 -133.60
REMARK 500 ASP B 330 -51.07 -151.94
REMARK 500 ASN B 363 65.09 -161.17
REMARK 500 PHE B 499 18.47 59.24
REMARK 500 PHE B 549 -128.23 53.62
REMARK 500 LEU B 588 74.37 -115.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1701 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 263 NZ
REMARK 620 2 HIS A 283 NE2 94.5
REMARK 620 3 CYS A 307 SG 113.7 112.2
REMARK 620 4 ASP A 330 OD1 105.4 95.5 128.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1702 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 263 NZ
REMARK 620 2 HIS B 283 NE2 103.8
REMARK 620 3 CYS B 307 SG 112.0 114.9
REMARK 620 4 ASP B 330 OD1 101.4 98.2 123.9
REMARK 620 N 1 2 3
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CHANGES IN THE PROTEIN SEQUENCE REPRESENT ERRORS
REMARK 999 IN THE ORIGINAL PUBLISHED SEQUENCE. THESE CHANGES WERE
REMARK 999 VERIFIED BY RESEQUENCING OF THE GENE AND MASS SPECTROMETRY
REMARK 999 ANALYSIS.
DBREF 2FAF A 34 641 UNP P21642 PPCKM_CHICK 34 640
DBREF 2FAF B 34 641 UNP P21642 PPCKM_CHICK 34 640
SEQADV 2FAF GLY A 129 UNP P21642 129 INSERTION
SEQADV 2FAF PRO A 130 UNP P21642 SER 129 SEE REMARK 999
SEQADV 2FAF PRO A 233 UNP P21642 ARG 232 SEE REMARK 999
SEQADV 2FAF ARG A 268 UNP P21642 ALA 267 SEE REMARK 999
SEQADV 2FAF GLU A 339 UNP P21642 ARG 338 SEE REMARK 999
SEQADV 2FAF ARG A 502 UNP P21642 SER 501 SEE REMARK 999
SEQADV 2FAF GLY B 129 UNP P21642 129 INSERTION
SEQADV 2FAF PRO B 130 UNP P21642 SER 129 SEE REMARK 999
SEQADV 2FAF PRO B 233 UNP P21642 ARG 232 SEE REMARK 999
SEQADV 2FAF ARG B 268 UNP P21642 ALA 267 SEE REMARK 999
SEQADV 2FAF GLU B 339 UNP P21642 ARG 338 SEE REMARK 999
SEQADV 2FAF ARG B 502 UNP P21642 SER 501 SEE REMARK 999
SEQRES 1 A 608 LEU SER THR SER LEU SER ALA LEU PRO ALA ALA ALA ARG
SEQRES 2 A 608 ASP PHE VAL GLU GLU ALA VAL ARG LEU CYS ARG PRO ARG
SEQRES 3 A 608 GLU VAL LEU LEU CYS ASP GLY SER GLU GLU GLU GLY LYS
SEQRES 4 A 608 GLU LEU LEU ARG GLY LEU GLN ASP ASP GLY VAL LEU HIS
SEQRES 5 A 608 PRO LEU PRO LYS TYR ASP ASN CYS TRP LEU ALA ARG THR
SEQRES 6 A 608 ASP PRO ARG ASP VAL ALA ARG VAL GLU SER LYS THR VAL
SEQRES 7 A 608 LEU VAL THR PRO GLU GLN SER ASP ALA VAL PRO PRO PRO
SEQRES 8 A 608 PRO PRO SER GLY GLY PRO PRO GLN LEU GLY ASN TRP MET
SEQRES 9 A 608 SER PRO ASN ALA PHE GLN ALA ALA VAL GLN GLU ARG PHE
SEQRES 10 A 608 PRO GLY CYS MET ALA GLY ARG PRO LEU TYR VAL ILE PRO
SEQRES 11 A 608 PHE SER MET GLY PRO PRO THR SER PRO LEU ALA LYS LEU
SEQRES 12 A 608 GLY VAL GLN VAL THR ASP SER PRO TYR VAL VAL LEU SER
SEQRES 13 A 608 MET ARG ILE MET THR ARG VAL GLY PRO ALA VAL LEU GLN
SEQRES 14 A 608 ARG LEU ASP ASP ASP PHE VAL ARG CYS LEU HIS SER VAL
SEQRES 15 A 608 GLY ARG PRO LEU PRO LEU THR GLU PRO LEU VAL SER SER
SEQRES 16 A 608 TRP PRO CYS ASP PRO SER ARG VAL LEU VAL ALA HIS ILE
SEQRES 17 A 608 PRO SER GLU ARG ARG ILE VAL SER PHE GLY SER GLY TYR
SEQRES 18 A 608 GLY GLY ASN SER LEU LEU GLY LYS LYS CYS PHE ALA LEU
SEQRES 19 A 608 ARG ILE ALA SER ARG MET ALA GLN GLN GLN GLY TRP LEU
SEQRES 20 A 608 ALA GLU HIS MET LEU ILE LEU GLY VAL THR SER PRO SER
SEQRES 21 A 608 GLY GLU LYS ARG TYR MET ALA ALA ALA PHE PRO SER ALA
SEQRES 22 A 608 CYS GLY LYS THR ASN LEU ALA MET MET THR PRO SER LEU
SEQRES 23 A 608 PRO GLY TRP ARG ILE HIS CYS VAL GLY ASP ASP ILE ALA
SEQRES 24 A 608 TRP MET LYS PHE ASP ASP GLU GLY ARG LEU ARG ALA ILE
SEQRES 25 A 608 ASN PRO GLU ARG GLY PHE PHE GLY VAL ALA PRO GLY THR
SEQRES 26 A 608 SER SER ARG THR ASN PRO ASN ALA MET ALA THR ILE ALA
SEQRES 27 A 608 ARG ASN THR ILE PHE THR ASN VAL GLY LEU ARG SER ASP
SEQRES 28 A 608 GLY GLY VAL TYR TRP ASP GLY LEU ASP GLU PRO THR GLU
SEQRES 29 A 608 PRO GLY VAL THR TYR THR SER TRP LEU GLY LYS PRO TRP
SEQRES 30 A 608 LYS HIS GLY ASP PRO GLU PRO CYS ALA HIS PRO ASN SER
SEQRES 31 A 608 ARG PHE CYS ALA PRO ALA ASP GLN CYS PRO ILE MET ASP
SEQRES 32 A 608 PRO ARG TRP ASP ASP PRO GLU GLY VAL PRO ILE ASP ALA
SEQRES 33 A 608 ILE ILE PHE GLY GLY ARG ARG PRO ARG GLY VAL PRO LEU
SEQRES 34 A 608 VAL VAL GLU ALA PHE GLY TRP ARG HIS GLY VAL PHE MET
SEQRES 35 A 608 GLY SER ALA MET ARG SER GLU ALA THR ALA ALA ALA GLU
SEQRES 36 A 608 HIS LYS GLY GLY ARG LEU MET HIS ASP PRO PHE ALA MET
SEQRES 37 A 608 ARG PRO PHE PHE GLY TYR ASN ALA GLY ARG TYR LEU GLU
SEQRES 38 A 608 HIS TRP LEU SER THR GLY LEU ARG SER ASN ALA ARG LEU
SEQRES 39 A 608 PRO ARG LEU PHE HIS VAL ASN TRP PHE LEU ARG ASP ASN
SEQRES 40 A 608 GLU GLY ARG PHE VAL TRP PRO GLY PHE GLY HIS ASN ALA
SEQRES 41 A 608 ARG VAL LEU ALA TRP ILE PHE GLY ARG ILE GLN GLY ARG
SEQRES 42 A 608 ASP THR ALA ARG PRO THR PRO ILE GLY TRP VAL PRO LYS
SEQRES 43 A 608 GLU GLY ASP LEU ASP LEU GLY GLY LEU PRO GLY VAL ASP
SEQRES 44 A 608 TYR SER GLN LEU PHE PRO MET GLU LYS GLY PHE TRP GLU
SEQRES 45 A 608 GLU GLU CYS ARG GLN LEU ARG GLU TYR TYR GLY GLU ASN
SEQRES 46 A 608 PHE GLY ALA ASP LEU PRO ARG ASP VAL MET ALA GLU LEU
SEQRES 47 A 608 GLU GLY LEU GLU GLU ARG VAL ARG LYS MET
SEQRES 1 B 608 LEU SER THR SER LEU SER ALA LEU PRO ALA ALA ALA ARG
SEQRES 2 B 608 ASP PHE VAL GLU GLU ALA VAL ARG LEU CYS ARG PRO ARG
SEQRES 3 B 608 GLU VAL LEU LEU CYS ASP GLY SER GLU GLU GLU GLY LYS
SEQRES 4 B 608 GLU LEU LEU ARG GLY LEU GLN ASP ASP GLY VAL LEU HIS
SEQRES 5 B 608 PRO LEU PRO LYS TYR ASP ASN CYS TRP LEU ALA ARG THR
SEQRES 6 B 608 ASP PRO ARG ASP VAL ALA ARG VAL GLU SER LYS THR VAL
SEQRES 7 B 608 LEU VAL THR PRO GLU GLN SER ASP ALA VAL PRO PRO PRO
SEQRES 8 B 608 PRO PRO SER GLY GLY PRO PRO GLN LEU GLY ASN TRP MET
SEQRES 9 B 608 SER PRO ASN ALA PHE GLN ALA ALA VAL GLN GLU ARG PHE
SEQRES 10 B 608 PRO GLY CYS MET ALA GLY ARG PRO LEU TYR VAL ILE PRO
SEQRES 11 B 608 PHE SER MET GLY PRO PRO THR SER PRO LEU ALA LYS LEU
SEQRES 12 B 608 GLY VAL GLN VAL THR ASP SER PRO TYR VAL VAL LEU SER
SEQRES 13 B 608 MET ARG ILE MET THR ARG VAL GLY PRO ALA VAL LEU GLN
SEQRES 14 B 608 ARG LEU ASP ASP ASP PHE VAL ARG CYS LEU HIS SER VAL
SEQRES 15 B 608 GLY ARG PRO LEU PRO LEU THR GLU PRO LEU VAL SER SER
SEQRES 16 B 608 TRP PRO CYS ASP PRO SER ARG VAL LEU VAL ALA HIS ILE
SEQRES 17 B 608 PRO SER GLU ARG ARG ILE VAL SER PHE GLY SER GLY TYR
SEQRES 18 B 608 GLY GLY ASN SER LEU LEU GLY LYS LYS CYS PHE ALA LEU
SEQRES 19 B 608 ARG ILE ALA SER ARG MET ALA GLN GLN GLN GLY TRP LEU
SEQRES 20 B 608 ALA GLU HIS MET LEU ILE LEU GLY VAL THR SER PRO SER
SEQRES 21 B 608 GLY GLU LYS ARG TYR MET ALA ALA ALA PHE PRO SER ALA
SEQRES 22 B 608 CYS GLY LYS THR ASN LEU ALA MET MET THR PRO SER LEU
SEQRES 23 B 608 PRO GLY TRP ARG ILE HIS CYS VAL GLY ASP ASP ILE ALA
SEQRES 24 B 608 TRP MET LYS PHE ASP ASP GLU GLY ARG LEU ARG ALA ILE
SEQRES 25 B 608 ASN PRO GLU ARG GLY PHE PHE GLY VAL ALA PRO GLY THR
SEQRES 26 B 608 SER SER ARG THR ASN PRO ASN ALA MET ALA THR ILE ALA
SEQRES 27 B 608 ARG ASN THR ILE PHE THR ASN VAL GLY LEU ARG SER ASP
SEQRES 28 B 608 GLY GLY VAL TYR TRP ASP GLY LEU ASP GLU PRO THR GLU
SEQRES 29 B 608 PRO GLY VAL THR TYR THR SER TRP LEU GLY LYS PRO TRP
SEQRES 30 B 608 LYS HIS GLY ASP PRO GLU PRO CYS ALA HIS PRO ASN SER
SEQRES 31 B 608 ARG PHE CYS ALA PRO ALA ASP GLN CYS PRO ILE MET ASP
SEQRES 32 B 608 PRO ARG TRP ASP ASP PRO GLU GLY VAL PRO ILE ASP ALA
SEQRES 33 B 608 ILE ILE PHE GLY GLY ARG ARG PRO ARG GLY VAL PRO LEU
SEQRES 34 B 608 VAL VAL GLU ALA PHE GLY TRP ARG HIS GLY VAL PHE MET
SEQRES 35 B 608 GLY SER ALA MET ARG SER GLU ALA THR ALA ALA ALA GLU
SEQRES 36 B 608 HIS LYS GLY GLY ARG LEU MET HIS ASP PRO PHE ALA MET
SEQRES 37 B 608 ARG PRO PHE PHE GLY TYR ASN ALA GLY ARG TYR LEU GLU
SEQRES 38 B 608 HIS TRP LEU SER THR GLY LEU ARG SER ASN ALA ARG LEU
SEQRES 39 B 608 PRO ARG LEU PHE HIS VAL ASN TRP PHE LEU ARG ASP ASN
SEQRES 40 B 608 GLU GLY ARG PHE VAL TRP PRO GLY PHE GLY HIS ASN ALA
SEQRES 41 B 608 ARG VAL LEU ALA TRP ILE PHE GLY ARG ILE GLN GLY ARG
SEQRES 42 B 608 ASP THR ALA ARG PRO THR PRO ILE GLY TRP VAL PRO LYS
SEQRES 43 B 608 GLU GLY ASP LEU ASP LEU GLY GLY LEU PRO GLY VAL ASP
SEQRES 44 B 608 TYR SER GLN LEU PHE PRO MET GLU LYS GLY PHE TRP GLU
SEQRES 45 B 608 GLU GLU CYS ARG GLN LEU ARG GLU TYR TYR GLY GLU ASN
SEQRES 46 B 608 PHE GLY ALA ASP LEU PRO ARG ASP VAL MET ALA GLU LEU
SEQRES 47 B 608 GLU GLY LEU GLU GLU ARG VAL ARG LYS MET
HET TQY C 1 20
HET FRU C 2 12
HET EPE A1002 15
HET 1PE A1262 32
HET MN A1701 1
HET MN B1702 1
HETNAM TQY 6-O-OCTANOYL-ALPHA-D-GLUCOPYRANOSE
HETNAM FRU BETA-D-FRUCTOFURANOSE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM MN MANGANESE (II) ION
HETSYN FRU BETA-D-FRUCTOSE; D-FRUCTOSE; FRUCTOSE
HETSYN EPE HEPES
HETSYN 1PE PEG400
FORMUL 3 TQY C14 H26 O7
FORMUL 3 FRU C6 H12 O6
FORMUL 4 EPE C8 H18 N2 O4 S
FORMUL 5 1PE C10 H22 O6
FORMUL 6 MN 2(MN 2+)
FORMUL 8 HOH *980(H2 O)
HELIX 1 1 PRO A 42 ARG A 57 1 16
HELIX 2 2 SER A 67 ASP A 81 1 15
HELIX 3 3 VAL A 106 SER A 108 5 3
HELIX 4 4 GLU A 116 ALA A 120 5 5
HELIX 5 5 SER A 138 PHE A 150 1 13
HELIX 6 6 SER A 183 THR A 194 1 12
HELIX 7 7 GLY A 197 GLN A 202 1 6
HELIX 8 8 ASP A 232 VAL A 236 5 5
HELIX 9 9 PRO A 242 GLU A 244 5 3
HELIX 10 10 TYR A 254 LEU A 259 1 6
HELIX 11 11 LEU A 267 GLY A 278 1 12
HELIX 12 12 ASN A 311 MET A 315 5 5
HELIX 13 13 ASN A 363 ILE A 370 1 8
HELIX 14 14 ASP A 430 CYS A 432 5 3
HELIX 15 15 GLY A 468 ALA A 478 1 11
HELIX 16 16 ASP A 497 PHE A 505 5 9
HELIX 17 17 ASN A 508 GLY A 520 1 13
HELIX 18 18 GLY A 548 GLY A 550 5 3
HELIX 19 19 HIS A 551 GLN A 564 1 14
HELIX 20 20 ASP A 592 PHE A 597 1 6
HELIX 21 21 GLU A 600 PHE A 619 1 20
HELIX 22 22 GLY A 620 LEU A 623 5 4
HELIX 23 23 PRO A 624 LYS A 640 1 17
HELIX 24 24 PRO B 42 ARG B 57 1 16
HELIX 25 25 SER B 67 ASP B 81 1 15
HELIX 26 26 VAL B 106 SER B 108 5 3
HELIX 27 27 GLU B 116 VAL B 121 1 6
HELIX 28 28 SER B 138 PHE B 150 1 13
HELIX 29 29 SER B 183 THR B 194 1 12
HELIX 30 30 GLY B 197 GLN B 202 1 6
HELIX 31 31 ASP B 232 VAL B 236 5 5
HELIX 32 32 PRO B 242 GLU B 244 5 3
HELIX 33 33 TYR B 254 LEU B 259 1 6
HELIX 34 34 LEU B 267 GLY B 278 1 12
HELIX 35 35 ASN B 311 MET B 315 5 5
HELIX 36 36 ASN B 363 ILE B 370 1 8
HELIX 37 37 ASP B 430 CYS B 432 5 3
HELIX 38 38 GLY B 468 ALA B 478 1 11
HELIX 39 39 ASP B 497 PHE B 505 5 9
HELIX 40 40 ASN B 508 GLY B 520 1 13
HELIX 41 41 GLY B 548 GLY B 550 5 3
HELIX 42 42 HIS B 551 GLN B 564 1 14
HELIX 43 43 ASP B 592 PHE B 597 1 6
HELIX 44 44 GLU B 600 PHE B 619 1 20
HELIX 45 45 GLY B 620 LEU B 623 5 4
HELIX 46 46 PRO B 624 MET B 641 1 18
SHEET 1 A 8 GLU A 60 LEU A 63 0
SHEET 2 A 8 PRO A 158 MET A 166 1 O VAL A 161 N LEU A 62
SHEET 3 A 8 LYS A 175 THR A 181 -1 O THR A 181 N TYR A 160
SHEET 4 A 8 VAL A 209 SER A 214 1 O CYS A 211 N VAL A 178
SHEET 5 A 8 ARG A 246 PHE A 250 1 O SER A 249 N LEU A 212
SHEET 6 A 8 LEU A 237 ILE A 241 -1 N ALA A 239 O VAL A 248
SHEET 7 A 8 THR A 110 VAL A 113 1 N VAL A 113 O HIS A 240
SHEET 8 A 8 TRP A 136 MET A 137 1 O MET A 137 N LEU A 112
SHEET 1 B 3 GLU A 60 LEU A 63 0
SHEET 2 B 3 PRO A 158 MET A 166 1 O VAL A 161 N LEU A 62
SHEET 3 B 3 ARG A 195 VAL A 196 -1 O ARG A 195 N SER A 165
SHEET 1 C 5 LEU A 84 PRO A 86 0
SHEET 2 C 5 TRP A 94 ALA A 96 -1 O LEU A 95 N HIS A 85
SHEET 3 C 5 ILE A 375 THR A 377 1 O PHE A 376 N TRP A 94
SHEET 4 C 5 ARG A 424 PRO A 428 -1 O ARG A 424 N THR A 377
SHEET 5 C 5 GLY A 350 VAL A 354 -1 N PHE A 351 O ALA A 427
SHEET 1 D 7 LEU A 280 GLU A 282 0
SHEET 2 D 7 ALA A 332 PHE A 336 -1 O ALA A 332 N GLU A 282
SHEET 3 D 7 LEU A 342 ILE A 345 -1 O ILE A 345 N TRP A 333
SHEET 4 D 7 VAL A 445 GLY A 454 -1 O ILE A 447 N LEU A 342
SHEET 5 D 7 LYS A 296 ALA A 302 1 N ALA A 302 O ILE A 451
SHEET 6 D 7 LEU A 285 THR A 290 -1 N VAL A 289 O ARG A 297
SHEET 7 D 7 ARG A 323 GLY A 328 -1 O ARG A 323 N THR A 290
SHEET 1 E 6 LEU A 280 GLU A 282 0
SHEET 2 E 6 ALA A 332 PHE A 336 -1 O ALA A 332 N GLU A 282
SHEET 3 E 6 LEU A 342 ILE A 345 -1 O ILE A 345 N TRP A 333
SHEET 4 E 6 VAL A 445 GLY A 454 -1 O ILE A 447 N LEU A 342
SHEET 5 E 6 ARG A 529 ASN A 534 1 O PHE A 531 N PHE A 452
SHEET 6 E 6 VAL A 463 GLU A 465 -1 N VAL A 464 O HIS A 532
SHEET 1 F 4 VAL A 387 TYR A 388 0
SHEET 2 F 4 GLY A 380 ARG A 382 -1 N GLY A 380 O TYR A 388
SHEET 3 F 4 TYR A 402 THR A 403 -1 O THR A 403 N LEU A 381
SHEET 4 F 4 PRO A 409 TRP A 410 -1 O TRP A 410 N TYR A 402
SHEET 1 G 2 ALA A 569 THR A 572 0
SHEET 2 G 2 GLY A 575 PRO A 578 -1 O VAL A 577 N ARG A 570
SHEET 1 H 8 GLU B 60 LEU B 63 0
SHEET 2 H 8 PRO B 158 MET B 166 1 O VAL B 161 N LEU B 62
SHEET 3 H 8 LYS B 175 THR B 181 -1 O THR B 181 N TYR B 160
SHEET 4 H 8 VAL B 209 SER B 214 1 O CYS B 211 N VAL B 180
SHEET 5 H 8 ARG B 246 PHE B 250 1 O SER B 249 N LEU B 212
SHEET 6 H 8 LEU B 237 ILE B 241 -1 N ALA B 239 O VAL B 248
SHEET 7 H 8 THR B 110 VAL B 113 1 N VAL B 113 O HIS B 240
SHEET 8 H 8 TRP B 136 MET B 137 1 O MET B 137 N LEU B 112
SHEET 1 I 5 LEU B 84 PRO B 86 0
SHEET 2 I 5 TRP B 94 ALA B 96 -1 O LEU B 95 N HIS B 85
SHEET 3 I 5 ILE B 375 THR B 377 1 O PHE B 376 N TRP B 94
SHEET 4 I 5 ARG B 424 PRO B 428 -1 O ARG B 424 N THR B 377
SHEET 5 I 5 GLY B 350 VAL B 354 -1 N PHE B 351 O ALA B 427
SHEET 1 J 7 LEU B 280 GLU B 282 0
SHEET 2 J 7 ALA B 332 PHE B 336 -1 O ALA B 332 N GLU B 282
SHEET 3 J 7 LEU B 342 ILE B 345 -1 O ARG B 343 N LYS B 335
SHEET 4 J 7 VAL B 445 GLY B 454 -1 O ILE B 447 N LEU B 342
SHEET 5 J 7 LYS B 296 ALA B 302 1 N ALA B 300 O ILE B 451
SHEET 6 J 7 LEU B 285 THR B 290 -1 N VAL B 289 O ARG B 297
SHEET 7 J 7 ARG B 323 GLY B 328 -1 O VAL B 327 N ILE B 286
SHEET 1 K 6 LEU B 280 GLU B 282 0
SHEET 2 K 6 ALA B 332 PHE B 336 -1 O ALA B 332 N GLU B 282
SHEET 3 K 6 LEU B 342 ILE B 345 -1 O ARG B 343 N LYS B 335
SHEET 4 K 6 VAL B 445 GLY B 454 -1 O ILE B 447 N LEU B 342
SHEET 5 K 6 ARG B 529 ASN B 534 1 O PHE B 531 N PHE B 452
SHEET 6 K 6 VAL B 463 GLU B 465 -1 N VAL B 464 O HIS B 532
SHEET 1 L 4 VAL B 387 TYR B 388 0
SHEET 2 L 4 GLY B 380 ARG B 382 -1 N GLY B 380 O TYR B 388
SHEET 3 L 4 TYR B 402 THR B 403 -1 O THR B 403 N LEU B 381
SHEET 4 L 4 PRO B 409 TRP B 410 -1 O TRP B 410 N TYR B 402
SHEET 1 M 2 ALA B 569 THR B 572 0
SHEET 2 M 2 GLY B 575 PRO B 578 -1 O VAL B 577 N ARG B 570
LINK C1 TQY C 1 O2 FRU C 2 1555 1555 1.44
LINK NZ LYS A 263 MN MN A1701 1555 1555 1.97
LINK NE2 HIS A 283 MN MN A1701 1555 1555 2.01
LINK SG CYS A 307 MN MN A1701 1555 1555 2.29
LINK OD1 ASP A 330 MN MN A1701 1555 1555 1.94
LINK NZ LYS B 263 MN MN B1702 1555 1555 1.97
LINK NE2 HIS B 283 MN MN B1702 1555 1555 2.00
LINK SG CYS B 307 MN MN B1702 1555 1555 2.29
LINK OD1 ASP B 330 MN MN B1702 1555 1555 1.94
CISPEP 1 LEU A 219 PRO A 220 0 1.48
CISPEP 2 LEU B 219 PRO B 220 0 0.42
CRYST1 110.807 47.737 127.205 90.00 111.31 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009030 0.000000 0.003520 0.00000
SCALE2 0.000000 0.020950 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008440 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
