HEADER ISOMERASE 21-MAY-09 3HJB
TITLE 1.5 ANGSTROM CRYSTAL STRUCTURE OF GLUCOSE-6-PHOSPHATE ISOMERASE FROM
TITLE 2 VIBRIO CHOLERAE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE-6-PHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GPI, PHOSPHOGLUCOSE ISOMERASE, PGI, PHOSPHOHEXOSE ISOMERASE,
COMPND 5 PHI;
COMPND 6 EC: 5.3.1.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 STRAIN: O1 BIOVAR EL TOR STR. N16961;
SOURCE 5 GENE: PGI, VC_0374;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS GLUCOSE-6-PHOSPHATE ISOMERASE, PGI, IDP01329, GLUCONEOGENESIS,
KEYWDS 2 GLYCOLYSIS, ISOMERASE, STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS OF INFECTIOUS DISEASES, CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,A.HALAVATY,L.SHUVALOVA,I.DUBROVSKA,J.WINSOR,L.PAPAZISI,
AUTHOR 2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 5 06-SEP-23 3HJB 1 REMARK
REVDAT 4 13-OCT-21 3HJB 1 REMARK SEQADV LINK
REVDAT 3 01-NOV-17 3HJB 1 REMARK
REVDAT 2 13-JUL-11 3HJB 1 VERSN
REVDAT 1 16-JUN-09 3HJB 0
JRNL AUTH G.MINASOV,A.HALAVATY,L.SHUVALOVA,I.DUBROVSKA,J.WINSOR,
JRNL AUTH 2 L.PAPAZISI,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL 1.5 ANGSTROM CRYSTAL STRUCTURE OF GLUCOSE-6-PHOSPHATE
JRNL TITL 2 ISOMERASE FROM VIBRIO CHOLERAE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0044
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 351339
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) : 0.128
REMARK 3 R VALUE (WORKING SET) : 0.127
REMARK 3 FREE R VALUE : 0.151
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 18596
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 23057
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.1840
REMARK 3 BIN FREE R VALUE SET COUNT : 1306
REMARK 3 BIN FREE R VALUE : 0.2150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17164
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 4071
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 11.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 6.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -0.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.057
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.905
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 18786 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 12238 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 25663 ; 1.370 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): 30059 ; 0.909 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2443 ; 3.761 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 906 ;32.605 ;25.276
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3063 ; 9.827 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;11.701 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2781 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21834 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3851 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 11654 ; 0.954 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4725 ; 0.321 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18856 ; 1.620 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7132 ; 2.623 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6794 ; 4.277 ; 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 0 A 97
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0965 -32.9700 36.0300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0320 T22: 0.0276
REMARK 3 T33: 0.0446 T12: 0.0236
REMARK 3 T13: 0.0021 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.4750 L22: 0.5824
REMARK 3 L33: 0.7499 L12: 0.2480
REMARK 3 L13: -0.1822 L23: -0.1386
REMARK 3 S TENSOR
REMARK 3 S11: -0.0377 S12: 0.0298 S13: -0.0629
REMARK 3 S21: -0.0516 S22: 0.0166 S23: -0.0666
REMARK 3 S31: 0.0960 S32: 0.0702 S33: 0.0211
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 98 A 177
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9832 -4.8202 56.3448
REMARK 3 T TENSOR
REMARK 3 T11: 0.0472 T22: 0.0207
REMARK 3 T33: 0.0178 T12: -0.0185
REMARK 3 T13: -0.0042 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.3867 L22: 0.5766
REMARK 3 L33: 0.5983 L12: -0.0901
REMARK 3 L13: -0.0199 L23: 0.0843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: -0.0525 S13: 0.0714
REMARK 3 S21: 0.0668 S22: 0.0010 S23: -0.0323
REMARK 3 S31: -0.1046 S32: 0.0656 S33: -0.0105
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 178 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3132 -2.8978 54.7387
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.0498
REMARK 3 T33: 0.1029 T12: -0.0163
REMARK 3 T13: 0.0270 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 1.4958 L22: 0.4413
REMARK 3 L33: 7.4197 L12: -0.4780
REMARK 3 L13: 2.2988 L23: -1.5840
REMARK 3 S TENSOR
REMARK 3 S11: 0.0359 S12: 0.0123 S13: -0.0840
REMARK 3 S21: 0.0740 S22: 0.0587 S23: 0.1025
REMARK 3 S31: 0.0432 S32: -0.3269 S33: -0.0946
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 183 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3287 7.7687 49.4766
REMARK 3 T TENSOR
REMARK 3 T11: 0.0785 T22: 0.0067
REMARK 3 T33: 0.0616 T12: 0.0113
REMARK 3 T13: 0.0084 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.9804 L22: 0.6154
REMARK 3 L33: 1.5445 L12: 0.1472
REMARK 3 L13: 0.7045 L23: 0.1408
REMARK 3 S TENSOR
REMARK 3 S11: -0.0242 S12: -0.0041 S13: 0.1672
REMARK 3 S21: 0.0216 S22: -0.0037 S23: 0.0361
REMARK 3 S31: -0.1597 S32: -0.0520 S33: 0.0279
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 235 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): 50.4645 8.4098 50.5372
REMARK 3 T TENSOR
REMARK 3 T11: 0.0966 T22: 0.0317
REMARK 3 T33: 0.0928 T12: -0.0291
REMARK 3 T13: 0.0021 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.3357 L22: 1.8843
REMARK 3 L33: 0.5528 L12: -0.9978
REMARK 3 L13: -0.3754 L23: 0.3516
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: 0.0264 S13: 0.2581
REMARK 3 S21: -0.0383 S22: 0.0211 S23: -0.2339
REMARK 3 S31: -0.1346 S32: 0.0891 S33: -0.0504
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 267 A 436
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3599 -23.9648 44.2850
REMARK 3 T TENSOR
REMARK 3 T11: 0.0082 T22: 0.0020
REMARK 3 T33: 0.0014 T12: 0.0038
REMARK 3 T13: -0.0023 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.3250 L22: 0.2788
REMARK 3 L33: 0.4027 L12: 0.0577
REMARK 3 L13: -0.0336 L23: -0.0050
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: -0.0045 S13: -0.0105
REMARK 3 S21: 0.0112 S22: 0.0064 S23: -0.0059
REMARK 3 S31: 0.0182 S32: 0.0071 S33: -0.0170
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 437 A 450
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8160 -49.7705 42.3251
REMARK 3 T TENSOR
REMARK 3 T11: 0.1035 T22: 0.0491
REMARK 3 T33: 0.0899 T12: -0.0625
REMARK 3 T13: -0.0380 T23: 0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 10.4189 L22: 3.3941
REMARK 3 L33: 2.8911 L12: 0.8900
REMARK 3 L13: -1.6433 L23: 0.0402
REMARK 3 S TENSOR
REMARK 3 S11: 0.2177 S12: -0.3424 S13: -0.6345
REMARK 3 S21: 0.1603 S22: -0.1644 S23: -0.0822
REMARK 3 S31: 0.1906 S32: -0.1646 S33: -0.0533
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 451 A 511
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1665 -27.9264 40.6330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0125 T22: 0.0017
REMARK 3 T33: 0.0066 T12: 0.0007
REMARK 3 T13: -0.0010 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.4833 L22: 0.2631
REMARK 3 L33: 0.3160 L12: 0.0915
REMARK 3 L13: -0.0138 L23: -0.0496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: 0.0079 S13: -0.0287
REMARK 3 S21: -0.0024 S22: 0.0104 S23: 0.0242
REMARK 3 S31: 0.0459 S32: -0.0120 S33: -0.0149
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 512 A 524
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7664 4.9282 25.9851
REMARK 3 T TENSOR
REMARK 3 T11: 0.0476 T22: 0.0163
REMARK 3 T33: 0.0791 T12: -0.0072
REMARK 3 T13: 0.0207 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 3.8177 L22: 8.2721
REMARK 3 L33: 1.9281 L12: -4.8345
REMARK 3 L13: -0.6030 L23: 1.4230
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: 0.0294 S13: 0.4681
REMARK 3 S21: -0.0974 S22: 0.0827 S23: -0.4853
REMARK 3 S31: -0.2289 S32: 0.1235 S33: -0.0982
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 525 A 550
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6423 7.2467 23.1585
REMARK 3 T TENSOR
REMARK 3 T11: 0.0903 T22: 0.0293
REMARK 3 T33: 0.0579 T12: 0.0429
REMARK 3 T13: 0.0244 T23: 0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 1.6553 L22: 1.8609
REMARK 3 L33: 2.1675 L12: 0.4644
REMARK 3 L13: -0.1444 L23: 0.0937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: 0.0715 S13: 0.2405
REMARK 3 S21: -0.0221 S22: -0.0074 S23: 0.0027
REMARK 3 S31: -0.3502 S32: -0.1371 S33: -0.0693
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 : B 0 B 103
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9018 -18.8217 20.1030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0287 T22: 0.0829
REMARK 3 T33: 0.0232 T12: 0.0040
REMARK 3 T13: -0.0160 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.3522 L22: 0.4989
REMARK 3 L33: 0.5232 L12: 0.0226
REMARK 3 L13: -0.2815 L23: 0.0147
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: 0.0979 S13: -0.0208
REMARK 3 S21: -0.0773 S22: 0.0173 S23: 0.0186
REMARK 3 S31: 0.0259 S32: -0.1154 S33: -0.0028
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 : B 104 B 137
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4222 -14.1108 47.9464
REMARK 3 T TENSOR
REMARK 3 T11: 0.0153 T22: 0.0819
REMARK 3 T33: 0.0567 T12: 0.0143
REMARK 3 T13: 0.0137 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.3698 L22: 1.2029
REMARK 3 L33: 2.4118 L12: 0.1904
REMARK 3 L13: 0.4868 L23: 0.7529
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: -0.0493 S13: -0.0648
REMARK 3 S21: 0.0539 S22: -0.0573 S23: 0.1431
REMARK 3 S31: 0.0826 S32: -0.2829 S33: 0.0575
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 : B 138 B 178
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8032 -8.5187 57.5140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0276 T22: 0.0316
REMARK 3 T33: 0.0149 T12: 0.0118
REMARK 3 T13: 0.0064 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.5647 L22: 0.4643
REMARK 3 L33: 1.3142 L12: -0.0987
REMARK 3 L13: -0.1609 L23: -0.2084
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: -0.0570 S13: 0.0603
REMARK 3 S21: 0.0810 S22: 0.0058 S23: -0.0051
REMARK 3 S31: -0.1272 S32: -0.0407 S33: -0.0285
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 : B 179 B 183
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5126 -13.8819 56.2289
REMARK 3 T TENSOR
REMARK 3 T11: 0.0554 T22: 0.0535
REMARK 3 T33: 0.0522 T12: 0.0051
REMARK 3 T13: 0.0082 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 2.8872 L22: 5.6903
REMARK 3 L33: 2.2418 L12: -2.9014
REMARK 3 L13: -1.4253 L23: 3.2321
REMARK 3 S TENSOR
REMARK 3 S11: 0.1410 S12: 0.0560 S13: -0.0115
REMARK 3 S21: -0.1205 S22: -0.0138 S23: -0.1793
REMARK 3 S31: -0.1617 S32: -0.0134 S33: -0.1272
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 : B 184 B 227
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8799 -20.5923 63.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.0248 T22: 0.0299
REMARK 3 T33: 0.0106 T12: 0.0019
REMARK 3 T13: -0.0011 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 2.2790 L22: 1.4120
REMARK 3 L33: 0.6424 L12: -1.5371
REMARK 3 L13: -0.3640 L23: -0.0218
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: -0.0879 S13: -0.0745
REMARK 3 S21: 0.0197 S22: 0.0460 S23: 0.0530
REMARK 3 S31: 0.0157 S32: -0.0169 S33: -0.0454
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 : B 228 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6068 -22.0943 63.8025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0545 T22: 0.0942
REMARK 3 T33: 0.0565 T12: -0.0112
REMARK 3 T13: 0.0090 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 0.5854 L22: 0.2496
REMARK 3 L33: 3.8521 L12: -0.1372
REMARK 3 L13: 0.8710 L23: 0.1678
REMARK 3 S TENSOR
REMARK 3 S11: 0.0599 S12: -0.1526 S13: -0.1274
REMARK 3 S21: 0.0639 S22: -0.0036 S23: 0.0456
REMARK 3 S31: 0.2373 S32: -0.2724 S33: -0.0563
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 : B 267 B 354
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3771 -14.0748 35.0053
REMARK 3 T TENSOR
REMARK 3 T11: 0.0048 T22: 0.0336
REMARK 3 T33: 0.0050 T12: 0.0090
REMARK 3 T13: 0.0015 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.2419 L22: 0.2364
REMARK 3 L33: 0.3881 L12: -0.0605
REMARK 3 L13: -0.1919 L23: 0.1303
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: 0.0549 S13: 0.0229
REMARK 3 S21: -0.0132 S22: 0.0064 S23: 0.0143
REMARK 3 S31: -0.0231 S32: -0.0880 S33: -0.0251
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 : B 355 B 509
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5916 -11.4377 28.2708
REMARK 3 T TENSOR
REMARK 3 T11: 0.0097 T22: 0.0118
REMARK 3 T33: 0.0110 T12: 0.0071
REMARK 3 T13: 0.0019 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.5506 L22: 0.2240
REMARK 3 L33: 0.3188 L12: 0.1561
REMARK 3 L13: -0.0810 L23: -0.0634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: 0.0561 S13: 0.0207
REMARK 3 S21: 0.0033 S22: 0.0119 S23: -0.0342
REMARK 3 S31: -0.0313 S32: -0.0158 S33: -0.0132
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 : B 510 B 524
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4025 -39.9629 52.7282
REMARK 3 T TENSOR
REMARK 3 T11: 0.0246 T22: 0.0344
REMARK 3 T33: 0.0175 T12: -0.0104
REMARK 3 T13: 0.0057 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 1.6089 L22: 1.2590
REMARK 3 L33: 10.1740 L12: -0.1462
REMARK 3 L13: 3.1955 L23: -0.7364
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.2198 S13: -0.0620
REMARK 3 S21: -0.0010 S22: 0.0255 S23: 0.0739
REMARK 3 S31: 0.3021 S32: -0.5404 S33: -0.0312
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 : B 525 B 550
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0211 -41.7124 58.7711
REMARK 3 T TENSOR
REMARK 3 T11: 0.0712 T22: 0.0128
REMARK 3 T33: 0.0140 T12: 0.0091
REMARK 3 T13: -0.0024 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.5279 L22: 1.8164
REMARK 3 L33: 2.8961 L12: -0.0353
REMARK 3 L13: -0.3493 L23: 0.2815
REMARK 3 S TENSOR
REMARK 3 S11: -0.0251 S12: -0.1081 S13: -0.0830
REMARK 3 S21: 0.1445 S22: 0.0030 S23: -0.0381
REMARK 3 S31: 0.2405 S32: -0.0343 S33: 0.0221
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 : C 0 C 23
REMARK 3 ORIGIN FOR THE GROUP (A): 79.5550 25.1906 48.6474
REMARK 3 T TENSOR
REMARK 3 T11: 0.0617 T22: 0.0837
REMARK 3 T33: 0.0235 T12: 0.0240
REMARK 3 T13: 0.0177 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.5368 L22: 1.3086
REMARK 3 L33: 1.7028 L12: -0.4800
REMARK 3 L13: 1.2439 L23: -0.5693
REMARK 3 S TENSOR
REMARK 3 S11: -0.1116 S12: -0.1234 S13: 0.1067
REMARK 3 S21: 0.1209 S22: 0.0368 S23: -0.0138
REMARK 3 S31: -0.1768 S32: -0.1786 S33: 0.0748
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 : C 24 C 100
REMARK 3 ORIGIN FOR THE GROUP (A): 77.5658 10.6650 42.6827
REMARK 3 T TENSOR
REMARK 3 T11: 0.0241 T22: 0.0783
REMARK 3 T33: 0.0225 T12: -0.0125
REMARK 3 T13: 0.0167 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.4872 L22: 0.6435
REMARK 3 L33: 0.4877 L12: -0.1553
REMARK 3 L13: 0.3266 L23: -0.0107
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -0.0962 S13: 0.0047
REMARK 3 S21: 0.0647 S22: 0.0146 S23: 0.0196
REMARK 3 S31: 0.0164 S32: -0.1206 S33: -0.0165
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 : C 101 C 137
REMARK 3 ORIGIN FOR THE GROUP (A): 60.2367 9.8566 16.2406
REMARK 3 T TENSOR
REMARK 3 T11: 0.0109 T22: 0.0756
REMARK 3 T33: 0.0448 T12: -0.0118
REMARK 3 T13: -0.0114 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.1088 L22: 1.0734
REMARK 3 L33: 2.1374 L12: 0.0201
REMARK 3 L13: -0.2062 L23: 0.6028
REMARK 3 S TENSOR
REMARK 3 S11: -0.0080 S12: 0.0381 S13: 0.0457
REMARK 3 S21: -0.0388 S22: -0.0634 S23: 0.1438
REMARK 3 S31: -0.0580 S32: -0.2633 S33: 0.0714
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 : C 138 C 178
REMARK 3 ORIGIN FOR THE GROUP (A): 77.0786 4.1025 6.4067
REMARK 3 T TENSOR
REMARK 3 T11: 0.0237 T22: 0.0313
REMARK 3 T33: 0.0173 T12: -0.0125
REMARK 3 T13: -0.0033 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.5701 L22: 0.5042
REMARK 3 L33: 1.3056 L12: 0.0539
REMARK 3 L13: 0.1782 L23: -0.2816
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.0494 S13: -0.0630
REMARK 3 S21: -0.0728 S22: 0.0011 S23: -0.0050
REMARK 3 S31: 0.1246 S32: -0.0115 S33: -0.0245
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 : C 179 C 192
REMARK 3 ORIGIN FOR THE GROUP (A): 87.4561 13.4664 4.9118
REMARK 3 T TENSOR
REMARK 3 T11: 0.0327 T22: 0.0212
REMARK 3 T33: 0.0344 T12: 0.0068
REMARK 3 T13: -0.0085 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.6845 L22: 0.8020
REMARK 3 L33: 1.0650 L12: 1.1521
REMARK 3 L13: 0.5324 L23: 0.4638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0146 S12: -0.0029 S13: -0.1114
REMARK 3 S21: 0.0083 S22: -0.0078 S23: -0.0669
REMARK 3 S31: 0.0515 S32: -0.0057 S33: -0.0068
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 : C 193 C 226
REMARK 3 ORIGIN FOR THE GROUP (A): 79.3182 16.5179 0.1528
REMARK 3 T TENSOR
REMARK 3 T11: 0.0174 T22: 0.0392
REMARK 3 T33: 0.0168 T12: -0.0044
REMARK 3 T13: -0.0011 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 2.3161 L22: 2.2383
REMARK 3 L33: 1.2738 L12: 1.3664
REMARK 3 L13: 0.0566 L23: 0.0108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: 0.0844 S13: 0.1559
REMARK 3 S21: -0.0359 S22: 0.0321 S23: 0.0524
REMARK 3 S31: -0.0706 S32: 0.0106 S33: -0.0427
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 : C 227 C 264
REMARK 3 ORIGIN FOR THE GROUP (A): 69.2424 17.1943 -1.7634
REMARK 3 T TENSOR
REMARK 3 T11: 0.0295 T22: 0.0761
REMARK 3 T33: 0.0351 T12: 0.0078
REMARK 3 T13: -0.0091 T23: 0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 1.1654 L22: 0.6942
REMARK 3 L33: 4.1649 L12: 0.2609
REMARK 3 L13: -1.0128 L23: 0.1642
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: 0.1688 S13: 0.1687
REMARK 3 S21: -0.0676 S22: 0.0263 S23: 0.0892
REMARK 3 S31: -0.2302 S32: -0.2840 S33: -0.0765
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 : C 265 C 354
REMARK 3 ORIGIN FOR THE GROUP (A): 77.2030 10.0402 28.2792
REMARK 3 T TENSOR
REMARK 3 T11: 0.0037 T22: 0.0317
REMARK 3 T33: 0.0046 T12: -0.0072
REMARK 3 T13: -0.0005 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.3220 L22: 0.2315
REMARK 3 L33: 0.4229 L12: 0.0879
REMARK 3 L13: 0.2115 L23: 0.1246
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.0504 S13: -0.0094
REMARK 3 S21: 0.0088 S22: 0.0075 S23: 0.0188
REMARK 3 S31: 0.0158 S32: -0.0815 S33: -0.0146
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 : C 355 C 511
REMARK 3 ORIGIN FOR THE GROUP (A): 92.2746 7.2683 34.9904
REMARK 3 T TENSOR
REMARK 3 T11: 0.0140 T22: 0.0129
REMARK 3 T33: 0.0120 T12: -0.0086
REMARK 3 T13: -0.0005 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.5148 L22: 0.2007
REMARK 3 L33: 0.3457 L12: -0.1247
REMARK 3 L13: 0.0882 L23: -0.0657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.0481 S13: -0.0214
REMARK 3 S21: -0.0001 S22: 0.0106 S23: -0.0335
REMARK 3 S31: 0.0316 S32: -0.0145 S33: -0.0145
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 : C 512 C 550
REMARK 3 ORIGIN FOR THE GROUP (A): 95.4375 36.7636 6.9523
REMARK 3 T TENSOR
REMARK 3 T11: 0.0718 T22: 0.0154
REMARK 3 T33: 0.0205 T12: 0.0019
REMARK 3 T13: -0.0008 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.9925 L22: 1.1190
REMARK 3 L33: 1.5954 L12: 0.1190
REMARK 3 L13: -0.0716 L23: -0.1310
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.0962 S13: 0.0822
REMARK 3 S21: -0.0885 S22: 0.0277 S23: 0.0353
REMARK 3 S31: -0.1554 S32: -0.0973 S33: -0.0081
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 : D 0 D 45
REMARK 3 ORIGIN FOR THE GROUP (A): 110.4054 34.4554 30.5957
REMARK 3 T TENSOR
REMARK 3 T11: 0.0776 T22: 0.0337
REMARK 3 T33: 0.0762 T12: -0.0322
REMARK 3 T13: -0.0006 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.7918 L22: 0.8265
REMARK 3 L33: 1.0818 L12: -0.5157
REMARK 3 L13: 0.4320 L23: -0.3204
REMARK 3 S TENSOR
REMARK 3 S11: -0.0705 S12: -0.0650 S13: 0.0683
REMARK 3 S21: 0.0934 S22: 0.0512 S23: -0.0369
REMARK 3 S31: -0.1860 S32: -0.0014 S33: 0.0193
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 : D 46 D 132
REMARK 3 ORIGIN FOR THE GROUP (A): 120.3837 14.6845 19.5772
REMARK 3 T TENSOR
REMARK 3 T11: 0.0145 T22: 0.0454
REMARK 3 T33: 0.0375 T12: 0.0009
REMARK 3 T13: 0.0042 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.3379 L22: 0.3791
REMARK 3 L33: 0.5547 L12: -0.1712
REMARK 3 L13: 0.0238 L23: 0.1030
REMARK 3 S TENSOR
REMARK 3 S11: -0.0043 S12: 0.0212 S13: 0.0016
REMARK 3 S21: 0.0098 S22: 0.0163 S23: -0.0819
REMARK 3 S31: 0.0451 S32: 0.1343 S33: -0.0120
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 : D 133 D 178
REMARK 3 ORIGIN FOR THE GROUP (A): 103.9529 -2.3054 3.8542
REMARK 3 T TENSOR
REMARK 3 T11: 0.0507 T22: 0.0165
REMARK 3 T33: 0.0173 T12: 0.0018
REMARK 3 T13: -0.0106 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 0.4745 L22: 1.1755
REMARK 3 L33: 0.7632 L12: -0.0667
REMARK 3 L13: -0.2107 L23: 0.0118
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: 0.0716 S13: -0.0779
REMARK 3 S21: -0.1575 S22: -0.0121 S23: 0.0468
REMARK 3 S31: 0.1115 S32: -0.0047 S33: 0.0050
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 : D 179 D 227
REMARK 3 ORIGIN FOR THE GROUP (A): 99.4498 -9.9789 14.3834
REMARK 3 T TENSOR
REMARK 3 T11: 0.0616 T22: 0.0081
REMARK 3 T33: 0.0466 T12: -0.0082
REMARK 3 T13: -0.0060 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.0464 L22: 0.7288
REMARK 3 L33: 1.5709 L12: -0.0150
REMARK 3 L13: -0.8205 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0105 S12: -0.0066 S13: -0.1300
REMARK 3 S21: -0.0256 S22: -0.0053 S23: 0.0201
REMARK 3 S31: 0.1082 S32: -0.0511 S33: 0.0158
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 : D 228 D 266
REMARK 3 ORIGIN FOR THE GROUP (A): 111.0481 -14.6487 12.2858
REMARK 3 T TENSOR
REMARK 3 T11: 0.0986 T22: 0.0124
REMARK 3 T33: 0.0778 T12: 0.0249
REMARK 3 T13: 0.0003 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.4503 L22: 2.1844
REMARK 3 L33: 1.0340 L12: 1.0515
REMARK 3 L13: 0.3991 L23: 0.6043
REMARK 3 S TENSOR
REMARK 3 S11: 0.0426 S12: -0.0115 S13: -0.2726
REMARK 3 S21: 0.0364 S22: 0.0028 S23: -0.1883
REMARK 3 S31: 0.2160 S32: 0.0752 S33: -0.0455
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 : D 267 D 435
REMARK 3 ORIGIN FOR THE GROUP (A): 103.9580 19.1785 19.3628
REMARK 3 T TENSOR
REMARK 3 T11: 0.0073 T22: 0.0022
REMARK 3 T33: 0.0022 T12: -0.0031
REMARK 3 T13: 0.0033 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.3107 L22: 0.2489
REMARK 3 L33: 0.3604 L12: -0.0697
REMARK 3 L13: 0.0294 L23: -0.0051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0134 S12: 0.0094 S13: 0.0082
REMARK 3 S21: -0.0172 S22: 0.0075 S23: -0.0104
REMARK 3 S31: -0.0150 S32: 0.0143 S33: -0.0209
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 : D 436 D 450
REMARK 3 ORIGIN FOR THE GROUP (A): 77.4970 44.9152 21.3374
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.0400
REMARK 3 T33: 0.0712 T12: 0.0481
REMARK 3 T13: 0.0360 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 10.0983 L22: 2.9001
REMARK 3 L33: 2.6166 L12: -3.1914
REMARK 3 L13: 0.5246 L23: 0.0167
REMARK 3 S TENSOR
REMARK 3 S11: 0.2909 S12: 0.4612 S13: 0.5182
REMARK 3 S21: -0.1999 S22: -0.2129 S23: -0.0853
REMARK 3 S31: -0.1761 S32: -0.1328 S33: -0.0780
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 : D 451 D 509
REMARK 3 ORIGIN FOR THE GROUP (A): 101.2673 23.9339 22.6332
REMARK 3 T TENSOR
REMARK 3 T11: 0.0114 T22: 0.0011
REMARK 3 T33: 0.0062 T12: -0.0002
REMARK 3 T13: 0.0026 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.4634 L22: 0.3272
REMARK 3 L33: 0.3196 L12: -0.1234
REMARK 3 L13: 0.0106 L23: -0.0517
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: 0.0015 S13: 0.0309
REMARK 3 S21: 0.0005 S22: 0.0092 S23: 0.0242
REMARK 3 S31: -0.0516 S32: -0.0080 S33: -0.0119
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 : D 510 D 524
REMARK 3 ORIGIN FOR THE GROUP (A): 100.9079 -8.6202 37.3452
REMARK 3 T TENSOR
REMARK 3 T11: 0.0536 T22: 0.0268
REMARK 3 T33: 0.0698 T12: 0.0235
REMARK 3 T13: -0.0049 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 4.5322 L22: 9.9961
REMARK 3 L33: 1.3724 L12: 6.0432
REMARK 3 L13: 0.8915 L23: 1.0031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.0267 S13: -0.4971
REMARK 3 S21: 0.0768 S22: 0.0922 S23: -0.5959
REMARK 3 S31: 0.2061 S32: 0.1140 S33: -0.0866
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 : D 525 D 550
REMARK 3 ORIGIN FOR THE GROUP (A): 86.6277 -11.9990 40.5582
REMARK 3 T TENSOR
REMARK 3 T11: 0.0941 T22: 0.0330
REMARK 3 T33: 0.0591 T12: -0.0402
REMARK 3 T13: -0.0221 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 2.7843 L22: 2.7610
REMARK 3 L33: 2.6763 L12: -0.2171
REMARK 3 L13: 0.6503 L23: 0.4165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0820 S12: -0.0241 S13: -0.3329
REMARK 3 S21: 0.0211 S22: 0.0269 S23: -0.0218
REMARK 3 S31: 0.3600 S32: -0.0714 S33: -0.1089
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 : 1.30
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 3HJB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 370201
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.33500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1GZD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 7.7 MG/ML PROTEIN,
REMARK 280 0.01M TRIS-HCL, 0.25M SODIUM CLORIDE, SCREEN SOLUTION (PACT II,
REMARK 280 DROP B11): 0.2M CALCIUM CHLORIDE, 0.1M MES PH 6.0, 25% W/V PEG
REMARK 280 6000., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 37.54700
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -235.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -218.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 MET B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 MET C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 SER C -16
REMARK 465 SER C -15
REMARK 465 GLY C -14
REMARK 465 VAL C -13
REMARK 465 ASP C -12
REMARK 465 LEU C -11
REMARK 465 GLY C -10
REMARK 465 THR C -9
REMARK 465 GLU C -8
REMARK 465 ASN C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 PHE C -4
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 MET D -23
REMARK 465 HIS D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 SER D -16
REMARK 465 SER D -15
REMARK 465 GLY D -14
REMARK 465 VAL D -13
REMARK 465 ASP D -12
REMARK 465 LEU D -11
REMARK 465 GLY D -10
REMARK 465 THR D -9
REMARK 465 GLU D -8
REMARK 465 ASN D -7
REMARK 465 LEU D -6
REMARK 465 TYR D -5
REMARK 465 PHE D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 ASN D -1
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 LYS A 56 42.50 -86.20
REMARK 500 ASP A 160 -51.10 -124.65
REMARK 500 SER A 183 -39.22 -138.11
REMARK 500 SER A 208 114.86 -161.14
REMARK 500 ASP A 340 112.40 -169.36
REMARK 500 THR A 373 -136.97 -108.48
REMARK 500 ALA A 388 -60.15 -105.38
REMARK 500 GLN A 508 58.34 -162.35
REMARK 500 HIS A 534 -166.43 -118.13
REMARK 500 LYS B 56 38.99 -88.97
REMARK 500 ASP B 160 -50.90 -129.29
REMARK 500 SER B 183 -42.49 -140.00
REMARK 500 SER B 208 115.28 -165.59
REMARK 500 SER B 276 -161.97 -100.40
REMARK 500 ASP B 340 110.87 -168.35
REMARK 500 THR B 373 -138.88 -109.23
REMARK 500 ALA B 388 -60.88 -105.48
REMARK 500 GLN B 508 60.46 -160.08
REMARK 500 HIS B 534 -167.56 -122.12
REMARK 500 LYS C 56 38.82 -88.89
REMARK 500 ASP C 160 -50.92 -128.00
REMARK 500 SER C 183 -42.86 -139.50
REMARK 500 SER C 208 113.37 -165.13
REMARK 500 THR C 213 108.62 -54.80
REMARK 500 SER C 276 -162.53 -100.77
REMARK 500 ASP C 340 113.34 -167.69
REMARK 500 THR C 373 -140.25 -108.56
REMARK 500 ALA C 388 -61.12 -103.97
REMARK 500 GLN C 508 59.97 -161.03
REMARK 500 HIS C 534 -166.52 -123.59
REMARK 500 LYS D 56 42.61 -87.26
REMARK 500 ASP D 160 -50.73 -126.25
REMARK 500 SER D 183 -37.20 -139.14
REMARK 500 SER D 276 -163.02 -100.76
REMARK 500 ASP D 340 112.38 -167.70
REMARK 500 THR D 373 -136.63 -108.53
REMARK 500 ALA D 388 -60.89 -108.17
REMARK 500 GLN D 508 58.57 -162.55
REMARK 500 HIS D 534 -167.73 -118.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH D 1197
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 CA A 551 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 62 OE1
REMARK 620 2 GLU A 62 OE2 52.6
REMARK 620 3 HOH A 812 O 121.3 78.7
REMARK 620 4 HOH A 921 O 72.5 89.7 77.4
REMARK 620 5 HOH A2078 O 145.5 152.9 74.3 82.9
REMARK 620 6 HOH A2216 O 77.6 128.0 150.2 88.5 77.9
REMARK 620 7 HOH A3413 O 77.4 84.4 133.4 145.9 115.7 69.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 552 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 168 OE1
REMARK 620 2 GLU A 168 OE2 50.1
REMARK 620 3 HOH A1387 O 121.3 77.1
REMARK 620 4 HOH A2765 O 83.5 98.4 80.5
REMARK 620 5 HOH A2918 O 154.4 153.7 83.5 95.6
REMARK 620 6 HOH A3926 O 74.4 75.6 120.1 155.5 99.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 553 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 253 O
REMARK 620 2 HOH A3373 O 78.4
REMARK 620 3 HOH A3833 O 84.6 66.5
REMARK 620 4 HOH A3984 O 158.3 81.6 79.7
REMARK 620 5 HOH A4115 O 111.9 134.6 70.5 76.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 552 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 330 O
REMARK 620 2 HOH A3970 O 84.1
REMARK 620 3 HOH A3971 O 92.5 85.5
REMARK 620 4 GLU B 332 OE2 84.7 154.4 117.9
REMARK 620 5 HOH B4111 O 149.8 83.4 113.7 95.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 554 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 332 OE2
REMARK 620 2 HOH A3970 O 97.0
REMARK 620 3 GLY B 330 O 83.2 153.0
REMARK 620 4 HOH B4111 O 163.6 86.9 86.1
REMARK 620 5 HOH B4114 O 105.8 110.8 94.8 87.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 551 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 62 OE1
REMARK 620 2 GLU B 62 OE2 53.4
REMARK 620 3 HOH B 638 O 121.1 76.8
REMARK 620 4 HOH B 651 O 77.0 95.9 79.5
REMARK 620 5 HOH B1182 O 77.0 129.4 148.4 80.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 560 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 720 O
REMARK 620 2 HOH B1465 O 81.9
REMARK 620 3 HOH B1875 O 162.6 85.8
REMARK 620 4 HOH B2002 O 75.3 78.1 90.3
REMARK 620 5 HOH B3986 O 91.3 67.4 95.2 144.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 551 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 62 OE1
REMARK 620 2 GLU C 62 OE2 54.0
REMARK 620 3 HOH C 617 O 121.9 77.8
REMARK 620 4 HOH C 734 O 76.7 97.1 79.6
REMARK 620 5 HOH C1246 O 75.9 128.8 147.8 79.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 557 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 651 O
REMARK 620 2 HOH C1214 O 84.9
REMARK 620 3 HOH C1811 O 76.9 76.2
REMARK 620 4 HOH C3215 O 161.3 82.5 86.7
REMARK 620 5 HOH C3913 O 92.0 68.6 143.9 96.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 551 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 62 OE1
REMARK 620 2 GLU D 62 OE2 52.4
REMARK 620 3 HOH D 811 O 121.2 77.2
REMARK 620 4 HOH D 830 O 74.3 89.9 77.9
REMARK 620 5 HOH D2011 O 150.0 152.9 75.9 87.0
REMARK 620 6 HOH D2302 O 78.4 129.1 150.7 88.2 77.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 552 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 168 OE1
REMARK 620 2 GLU D 168 OE2 50.7
REMARK 620 3 HOH D1444 O 121.9 77.6
REMARK 620 4 HOH D2839 O 86.9 100.2 77.0
REMARK 620 5 HOH D3928 O 157.7 148.3 80.3 96.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 553 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 253 O
REMARK 620 2 HOH D2802 O 77.1
REMARK 620 3 HOH D3337 O 83.1 66.3
REMARK 620 4 HOH D3881 O 114.8 131.0 68.3
REMARK 620 5 HOH D3985 O 153.6 82.5 73.3 67.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 557
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 558
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 559
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 560
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 561
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 562
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 553
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 554
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 557
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 558
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 559
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 560
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 561
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 553
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 554
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 557
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 558
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 559
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 560
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 553
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 554
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 557
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 558
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 559
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 560
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 561
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP01329 RELATED DB: TARGETDB
DBREF 3HJB A 1 550 UNP Q9KUY4 G6PI_VIBCH 1 550
DBREF 3HJB B 1 550 UNP Q9KUY4 G6PI_VIBCH 1 550
DBREF 3HJB C 1 550 UNP Q9KUY4 G6PI_VIBCH 1 550
DBREF 3HJB D 1 550 UNP Q9KUY4 G6PI_VIBCH 1 550
SEQADV 3HJB MET A -23 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS A -22 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS A -21 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS A -20 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS A -19 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS A -18 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS A -17 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER A -16 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER A -15 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY A -14 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL A -13 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASP A -12 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU A -11 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY A -10 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB THR A -9 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLU A -8 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN A -7 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU A -6 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB TYR A -5 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB PHE A -4 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY A -3 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER A -2 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN A -1 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ALA A 0 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL A 179 UNP Q9KUY4 MET 179 ENGINEERED MUTATION
SEQADV 3HJB MET B -23 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS B -22 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS B -21 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS B -20 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS B -19 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS B -18 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS B -17 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER B -16 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER B -15 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY B -14 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL B -13 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASP B -12 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU B -11 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY B -10 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB THR B -9 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLU B -8 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN B -7 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU B -6 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB TYR B -5 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB PHE B -4 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY B -3 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER B -2 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN B -1 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ALA B 0 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL B 179 UNP Q9KUY4 MET 179 ENGINEERED MUTATION
SEQADV 3HJB MET C -23 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS C -22 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS C -21 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS C -20 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS C -19 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS C -18 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS C -17 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER C -16 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER C -15 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY C -14 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL C -13 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASP C -12 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU C -11 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY C -10 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB THR C -9 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLU C -8 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN C -7 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU C -6 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB TYR C -5 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB PHE C -4 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY C -3 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER C -2 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN C -1 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ALA C 0 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL C 179 UNP Q9KUY4 MET 179 ENGINEERED MUTATION
SEQADV 3HJB MET D -23 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS D -22 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS D -21 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS D -20 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS D -19 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS D -18 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB HIS D -17 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER D -16 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER D -15 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY D -14 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL D -13 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASP D -12 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU D -11 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY D -10 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB THR D -9 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLU D -8 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN D -7 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB LEU D -6 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB TYR D -5 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB PHE D -4 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB GLY D -3 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB SER D -2 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ASN D -1 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB ALA D 0 UNP Q9KUY4 EXPRESSION TAG
SEQADV 3HJB VAL D 179 UNP Q9KUY4 MET 179 ENGINEERED MUTATION
SEQRES 1 A 574 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 574 GLY THR GLU ASN LEU TYR PHE GLY SER ASN ALA MET LEU
SEQRES 3 A 574 LYS ASN ILE ASN PRO THR GLN THR GLN ALA TRP LYS ALA
SEQRES 4 A 574 LEU THR ALA HIS PHE GLU SER ALA GLN ASP MET ASP LEU
SEQRES 5 A 574 LYS ALA LEU PHE ALA GLN ASP SER GLU ARG PHE ALA LYS
SEQRES 6 A 574 TYR SER ALA ARG PHE GLY GLN ASP ILE LEU VAL ASP TYR
SEQRES 7 A 574 SER LYS ASN LEU VAL ASN ALA GLU THR MET GLN HIS LEU
SEQRES 8 A 574 PHE ALA LEU ALA LYS GLU THR ASP LEU GLN SER ALA ILE
SEQRES 9 A 574 THR ALA MET PHE LYS GLY GLU ALA ILE ASN GLN THR GLU
SEQRES 10 A 574 ASP ARG ALA VAL LEU HIS THR ALA LEU ARG ASN ARG SER
SEQRES 11 A 574 ASN SER PRO VAL LEU VAL ASN GLY GLU ASP VAL MET PRO
SEQRES 12 A 574 ALA VAL ASN ALA VAL LEU ALA LYS MET LYS ALA PHE SER
SEQRES 13 A 574 GLU ARG VAL ILE GLY GLY GLU TRP LYS GLY PHE THR GLY
SEQRES 14 A 574 LYS ALA ILE THR ASP VAL VAL ASN ILE GLY ILE GLY GLY
SEQRES 15 A 574 SER ASP LEU GLY PRO TYR MET VAL THR GLU ALA LEU VAL
SEQRES 16 A 574 PRO TYR LYS ASN HIS LEU THR VAL HIS PHE VAL SER ASN
SEQRES 17 A 574 VAL ASP GLY THR HIS MET ALA GLU THR LEU LYS ASN VAL
SEQRES 18 A 574 ASP PRO GLU THR THR LEU PHE LEU VAL ALA SER LYS THR
SEQRES 19 A 574 PHE THR THR GLN GLU THR MET THR ASN ALA HIS THR ALA
SEQRES 20 A 574 ARG ASP TRP PHE LEU LYS ALA ALA GLY ASP GLU ALA HIS
SEQRES 21 A 574 VAL ALA LYS HIS PHE ALA ALA LEU SER THR ASN GLY LYS
SEQRES 22 A 574 ALA VAL ALA GLU PHE GLY ILE ASP THR ASP ASN MET PHE
SEQRES 23 A 574 GLU PHE TRP ASP TRP VAL GLY GLY ARG TYR SER LEU TRP
SEQRES 24 A 574 SER ALA ILE GLY LEU SER ILE ILE LEU SER ILE GLY TYR
SEQRES 25 A 574 ASP ASN PHE VAL GLU LEU LEU ALA GLY ALA HIS GLU MET
SEQRES 26 A 574 ASP GLN HIS PHE VAL ASN THR PRO PHE GLU SER ASN ILE
SEQRES 27 A 574 PRO VAL ILE LEU ALA LEU ILE GLY ILE TRP TYR ASN ASN
SEQRES 28 A 574 PHE HIS GLY ALA GLU SER GLU ALA ILE LEU PRO TYR ASP
SEQRES 29 A 574 GLN TYR LEU HIS ARG PHE ALA ALA TYR PHE GLN GLN GLY
SEQRES 30 A 574 ASN MET GLU SER ASN GLY LYS TYR VAL ASP ARG ASN GLY
SEQRES 31 A 574 ASN PRO VAL THR TYR GLN THR GLY PRO ILE ILE TRP GLY
SEQRES 32 A 574 GLU PRO GLY THR ASN GLY GLN HIS ALA PHE TYR GLN LEU
SEQRES 33 A 574 ILE HIS GLN GLY THR LYS LEU ILE PRO CYS ASP PHE ILE
SEQRES 34 A 574 ALA PRO ALA VAL SER HIS ASN LEU VAL GLY ASP HIS HIS
SEQRES 35 A 574 GLN LYS LEU MET SER ASN PHE PHE ALA GLN THR GLU ALA
SEQRES 36 A 574 LEU ALA PHE GLY LYS SER ALA GLN ALA VAL GLN ALA GLU
SEQRES 37 A 574 LEU GLU LYS ALA GLY LYS SER ALA ALA GLU ILE ALA ALA
SEQRES 38 A 574 LEU VAL PRO PHE LYS VAL PHE GLU GLY ASN ARG PRO THR
SEQRES 39 A 574 ASN SER ILE LEU VAL LYS GLN ILE THR PRO ARG THR LEU
SEQRES 40 A 574 GLY ASN LEU ILE ALA MET TYR GLU HIS LYS ILE PHE VAL
SEQRES 41 A 574 GLN GLY VAL ILE TRP ASN ILE PHE SER PHE ASP GLN TRP
SEQRES 42 A 574 GLY VAL GLU LEU GLY LYS GLN LEU ALA ASN GLN ILE LEU
SEQRES 43 A 574 PRO GLU LEU ALA ASP SER ALA ALA VAL THR SER HIS ASP
SEQRES 44 A 574 SER SER THR ASN GLY LEU ILE ASN ALA PHE LYS ALA PHE
SEQRES 45 A 574 ARG ALA
SEQRES 1 B 574 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 574 GLY THR GLU ASN LEU TYR PHE GLY SER ASN ALA MET LEU
SEQRES 3 B 574 LYS ASN ILE ASN PRO THR GLN THR GLN ALA TRP LYS ALA
SEQRES 4 B 574 LEU THR ALA HIS PHE GLU SER ALA GLN ASP MET ASP LEU
SEQRES 5 B 574 LYS ALA LEU PHE ALA GLN ASP SER GLU ARG PHE ALA LYS
SEQRES 6 B 574 TYR SER ALA ARG PHE GLY GLN ASP ILE LEU VAL ASP TYR
SEQRES 7 B 574 SER LYS ASN LEU VAL ASN ALA GLU THR MET GLN HIS LEU
SEQRES 8 B 574 PHE ALA LEU ALA LYS GLU THR ASP LEU GLN SER ALA ILE
SEQRES 9 B 574 THR ALA MET PHE LYS GLY GLU ALA ILE ASN GLN THR GLU
SEQRES 10 B 574 ASP ARG ALA VAL LEU HIS THR ALA LEU ARG ASN ARG SER
SEQRES 11 B 574 ASN SER PRO VAL LEU VAL ASN GLY GLU ASP VAL MET PRO
SEQRES 12 B 574 ALA VAL ASN ALA VAL LEU ALA LYS MET LYS ALA PHE SER
SEQRES 13 B 574 GLU ARG VAL ILE GLY GLY GLU TRP LYS GLY PHE THR GLY
SEQRES 14 B 574 LYS ALA ILE THR ASP VAL VAL ASN ILE GLY ILE GLY GLY
SEQRES 15 B 574 SER ASP LEU GLY PRO TYR MET VAL THR GLU ALA LEU VAL
SEQRES 16 B 574 PRO TYR LYS ASN HIS LEU THR VAL HIS PHE VAL SER ASN
SEQRES 17 B 574 VAL ASP GLY THR HIS MET ALA GLU THR LEU LYS ASN VAL
SEQRES 18 B 574 ASP PRO GLU THR THR LEU PHE LEU VAL ALA SER LYS THR
SEQRES 19 B 574 PHE THR THR GLN GLU THR MET THR ASN ALA HIS THR ALA
SEQRES 20 B 574 ARG ASP TRP PHE LEU LYS ALA ALA GLY ASP GLU ALA HIS
SEQRES 21 B 574 VAL ALA LYS HIS PHE ALA ALA LEU SER THR ASN GLY LYS
SEQRES 22 B 574 ALA VAL ALA GLU PHE GLY ILE ASP THR ASP ASN MET PHE
SEQRES 23 B 574 GLU PHE TRP ASP TRP VAL GLY GLY ARG TYR SER LEU TRP
SEQRES 24 B 574 SER ALA ILE GLY LEU SER ILE ILE LEU SER ILE GLY TYR
SEQRES 25 B 574 ASP ASN PHE VAL GLU LEU LEU ALA GLY ALA HIS GLU MET
SEQRES 26 B 574 ASP GLN HIS PHE VAL ASN THR PRO PHE GLU SER ASN ILE
SEQRES 27 B 574 PRO VAL ILE LEU ALA LEU ILE GLY ILE TRP TYR ASN ASN
SEQRES 28 B 574 PHE HIS GLY ALA GLU SER GLU ALA ILE LEU PRO TYR ASP
SEQRES 29 B 574 GLN TYR LEU HIS ARG PHE ALA ALA TYR PHE GLN GLN GLY
SEQRES 30 B 574 ASN MET GLU SER ASN GLY LYS TYR VAL ASP ARG ASN GLY
SEQRES 31 B 574 ASN PRO VAL THR TYR GLN THR GLY PRO ILE ILE TRP GLY
SEQRES 32 B 574 GLU PRO GLY THR ASN GLY GLN HIS ALA PHE TYR GLN LEU
SEQRES 33 B 574 ILE HIS GLN GLY THR LYS LEU ILE PRO CYS ASP PHE ILE
SEQRES 34 B 574 ALA PRO ALA VAL SER HIS ASN LEU VAL GLY ASP HIS HIS
SEQRES 35 B 574 GLN LYS LEU MET SER ASN PHE PHE ALA GLN THR GLU ALA
SEQRES 36 B 574 LEU ALA PHE GLY LYS SER ALA GLN ALA VAL GLN ALA GLU
SEQRES 37 B 574 LEU GLU LYS ALA GLY LYS SER ALA ALA GLU ILE ALA ALA
SEQRES 38 B 574 LEU VAL PRO PHE LYS VAL PHE GLU GLY ASN ARG PRO THR
SEQRES 39 B 574 ASN SER ILE LEU VAL LYS GLN ILE THR PRO ARG THR LEU
SEQRES 40 B 574 GLY ASN LEU ILE ALA MET TYR GLU HIS LYS ILE PHE VAL
SEQRES 41 B 574 GLN GLY VAL ILE TRP ASN ILE PHE SER PHE ASP GLN TRP
SEQRES 42 B 574 GLY VAL GLU LEU GLY LYS GLN LEU ALA ASN GLN ILE LEU
SEQRES 43 B 574 PRO GLU LEU ALA ASP SER ALA ALA VAL THR SER HIS ASP
SEQRES 44 B 574 SER SER THR ASN GLY LEU ILE ASN ALA PHE LYS ALA PHE
SEQRES 45 B 574 ARG ALA
SEQRES 1 C 574 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 574 GLY THR GLU ASN LEU TYR PHE GLY SER ASN ALA MET LEU
SEQRES 3 C 574 LYS ASN ILE ASN PRO THR GLN THR GLN ALA TRP LYS ALA
SEQRES 4 C 574 LEU THR ALA HIS PHE GLU SER ALA GLN ASP MET ASP LEU
SEQRES 5 C 574 LYS ALA LEU PHE ALA GLN ASP SER GLU ARG PHE ALA LYS
SEQRES 6 C 574 TYR SER ALA ARG PHE GLY GLN ASP ILE LEU VAL ASP TYR
SEQRES 7 C 574 SER LYS ASN LEU VAL ASN ALA GLU THR MET GLN HIS LEU
SEQRES 8 C 574 PHE ALA LEU ALA LYS GLU THR ASP LEU GLN SER ALA ILE
SEQRES 9 C 574 THR ALA MET PHE LYS GLY GLU ALA ILE ASN GLN THR GLU
SEQRES 10 C 574 ASP ARG ALA VAL LEU HIS THR ALA LEU ARG ASN ARG SER
SEQRES 11 C 574 ASN SER PRO VAL LEU VAL ASN GLY GLU ASP VAL MET PRO
SEQRES 12 C 574 ALA VAL ASN ALA VAL LEU ALA LYS MET LYS ALA PHE SER
SEQRES 13 C 574 GLU ARG VAL ILE GLY GLY GLU TRP LYS GLY PHE THR GLY
SEQRES 14 C 574 LYS ALA ILE THR ASP VAL VAL ASN ILE GLY ILE GLY GLY
SEQRES 15 C 574 SER ASP LEU GLY PRO TYR MET VAL THR GLU ALA LEU VAL
SEQRES 16 C 574 PRO TYR LYS ASN HIS LEU THR VAL HIS PHE VAL SER ASN
SEQRES 17 C 574 VAL ASP GLY THR HIS MET ALA GLU THR LEU LYS ASN VAL
SEQRES 18 C 574 ASP PRO GLU THR THR LEU PHE LEU VAL ALA SER LYS THR
SEQRES 19 C 574 PHE THR THR GLN GLU THR MET THR ASN ALA HIS THR ALA
SEQRES 20 C 574 ARG ASP TRP PHE LEU LYS ALA ALA GLY ASP GLU ALA HIS
SEQRES 21 C 574 VAL ALA LYS HIS PHE ALA ALA LEU SER THR ASN GLY LYS
SEQRES 22 C 574 ALA VAL ALA GLU PHE GLY ILE ASP THR ASP ASN MET PHE
SEQRES 23 C 574 GLU PHE TRP ASP TRP VAL GLY GLY ARG TYR SER LEU TRP
SEQRES 24 C 574 SER ALA ILE GLY LEU SER ILE ILE LEU SER ILE GLY TYR
SEQRES 25 C 574 ASP ASN PHE VAL GLU LEU LEU ALA GLY ALA HIS GLU MET
SEQRES 26 C 574 ASP GLN HIS PHE VAL ASN THR PRO PHE GLU SER ASN ILE
SEQRES 27 C 574 PRO VAL ILE LEU ALA LEU ILE GLY ILE TRP TYR ASN ASN
SEQRES 28 C 574 PHE HIS GLY ALA GLU SER GLU ALA ILE LEU PRO TYR ASP
SEQRES 29 C 574 GLN TYR LEU HIS ARG PHE ALA ALA TYR PHE GLN GLN GLY
SEQRES 30 C 574 ASN MET GLU SER ASN GLY LYS TYR VAL ASP ARG ASN GLY
SEQRES 31 C 574 ASN PRO VAL THR TYR GLN THR GLY PRO ILE ILE TRP GLY
SEQRES 32 C 574 GLU PRO GLY THR ASN GLY GLN HIS ALA PHE TYR GLN LEU
SEQRES 33 C 574 ILE HIS GLN GLY THR LYS LEU ILE PRO CYS ASP PHE ILE
SEQRES 34 C 574 ALA PRO ALA VAL SER HIS ASN LEU VAL GLY ASP HIS HIS
SEQRES 35 C 574 GLN LYS LEU MET SER ASN PHE PHE ALA GLN THR GLU ALA
SEQRES 36 C 574 LEU ALA PHE GLY LYS SER ALA GLN ALA VAL GLN ALA GLU
SEQRES 37 C 574 LEU GLU LYS ALA GLY LYS SER ALA ALA GLU ILE ALA ALA
SEQRES 38 C 574 LEU VAL PRO PHE LYS VAL PHE GLU GLY ASN ARG PRO THR
SEQRES 39 C 574 ASN SER ILE LEU VAL LYS GLN ILE THR PRO ARG THR LEU
SEQRES 40 C 574 GLY ASN LEU ILE ALA MET TYR GLU HIS LYS ILE PHE VAL
SEQRES 41 C 574 GLN GLY VAL ILE TRP ASN ILE PHE SER PHE ASP GLN TRP
SEQRES 42 C 574 GLY VAL GLU LEU GLY LYS GLN LEU ALA ASN GLN ILE LEU
SEQRES 43 C 574 PRO GLU LEU ALA ASP SER ALA ALA VAL THR SER HIS ASP
SEQRES 44 C 574 SER SER THR ASN GLY LEU ILE ASN ALA PHE LYS ALA PHE
SEQRES 45 C 574 ARG ALA
SEQRES 1 D 574 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 574 GLY THR GLU ASN LEU TYR PHE GLY SER ASN ALA MET LEU
SEQRES 3 D 574 LYS ASN ILE ASN PRO THR GLN THR GLN ALA TRP LYS ALA
SEQRES 4 D 574 LEU THR ALA HIS PHE GLU SER ALA GLN ASP MET ASP LEU
SEQRES 5 D 574 LYS ALA LEU PHE ALA GLN ASP SER GLU ARG PHE ALA LYS
SEQRES 6 D 574 TYR SER ALA ARG PHE GLY GLN ASP ILE LEU VAL ASP TYR
SEQRES 7 D 574 SER LYS ASN LEU VAL ASN ALA GLU THR MET GLN HIS LEU
SEQRES 8 D 574 PHE ALA LEU ALA LYS GLU THR ASP LEU GLN SER ALA ILE
SEQRES 9 D 574 THR ALA MET PHE LYS GLY GLU ALA ILE ASN GLN THR GLU
SEQRES 10 D 574 ASP ARG ALA VAL LEU HIS THR ALA LEU ARG ASN ARG SER
SEQRES 11 D 574 ASN SER PRO VAL LEU VAL ASN GLY GLU ASP VAL MET PRO
SEQRES 12 D 574 ALA VAL ASN ALA VAL LEU ALA LYS MET LYS ALA PHE SER
SEQRES 13 D 574 GLU ARG VAL ILE GLY GLY GLU TRP LYS GLY PHE THR GLY
SEQRES 14 D 574 LYS ALA ILE THR ASP VAL VAL ASN ILE GLY ILE GLY GLY
SEQRES 15 D 574 SER ASP LEU GLY PRO TYR MET VAL THR GLU ALA LEU VAL
SEQRES 16 D 574 PRO TYR LYS ASN HIS LEU THR VAL HIS PHE VAL SER ASN
SEQRES 17 D 574 VAL ASP GLY THR HIS MET ALA GLU THR LEU LYS ASN VAL
SEQRES 18 D 574 ASP PRO GLU THR THR LEU PHE LEU VAL ALA SER LYS THR
SEQRES 19 D 574 PHE THR THR GLN GLU THR MET THR ASN ALA HIS THR ALA
SEQRES 20 D 574 ARG ASP TRP PHE LEU LYS ALA ALA GLY ASP GLU ALA HIS
SEQRES 21 D 574 VAL ALA LYS HIS PHE ALA ALA LEU SER THR ASN GLY LYS
SEQRES 22 D 574 ALA VAL ALA GLU PHE GLY ILE ASP THR ASP ASN MET PHE
SEQRES 23 D 574 GLU PHE TRP ASP TRP VAL GLY GLY ARG TYR SER LEU TRP
SEQRES 24 D 574 SER ALA ILE GLY LEU SER ILE ILE LEU SER ILE GLY TYR
SEQRES 25 D 574 ASP ASN PHE VAL GLU LEU LEU ALA GLY ALA HIS GLU MET
SEQRES 26 D 574 ASP GLN HIS PHE VAL ASN THR PRO PHE GLU SER ASN ILE
SEQRES 27 D 574 PRO VAL ILE LEU ALA LEU ILE GLY ILE TRP TYR ASN ASN
SEQRES 28 D 574 PHE HIS GLY ALA GLU SER GLU ALA ILE LEU PRO TYR ASP
SEQRES 29 D 574 GLN TYR LEU HIS ARG PHE ALA ALA TYR PHE GLN GLN GLY
SEQRES 30 D 574 ASN MET GLU SER ASN GLY LYS TYR VAL ASP ARG ASN GLY
SEQRES 31 D 574 ASN PRO VAL THR TYR GLN THR GLY PRO ILE ILE TRP GLY
SEQRES 32 D 574 GLU PRO GLY THR ASN GLY GLN HIS ALA PHE TYR GLN LEU
SEQRES 33 D 574 ILE HIS GLN GLY THR LYS LEU ILE PRO CYS ASP PHE ILE
SEQRES 34 D 574 ALA PRO ALA VAL SER HIS ASN LEU VAL GLY ASP HIS HIS
SEQRES 35 D 574 GLN LYS LEU MET SER ASN PHE PHE ALA GLN THR GLU ALA
SEQRES 36 D 574 LEU ALA PHE GLY LYS SER ALA GLN ALA VAL GLN ALA GLU
SEQRES 37 D 574 LEU GLU LYS ALA GLY LYS SER ALA ALA GLU ILE ALA ALA
SEQRES 38 D 574 LEU VAL PRO PHE LYS VAL PHE GLU GLY ASN ARG PRO THR
SEQRES 39 D 574 ASN SER ILE LEU VAL LYS GLN ILE THR PRO ARG THR LEU
SEQRES 40 D 574 GLY ASN LEU ILE ALA MET TYR GLU HIS LYS ILE PHE VAL
SEQRES 41 D 574 GLN GLY VAL ILE TRP ASN ILE PHE SER PHE ASP GLN TRP
SEQRES 42 D 574 GLY VAL GLU LEU GLY LYS GLN LEU ALA ASN GLN ILE LEU
SEQRES 43 D 574 PRO GLU LEU ALA ASP SER ALA ALA VAL THR SER HIS ASP
SEQRES 44 D 574 SER SER THR ASN GLY LEU ILE ASN ALA PHE LYS ALA PHE
SEQRES 45 D 574 ARG ALA
HET CA A 551 1
HET CA A 552 1
HET CA A 553 1
HET CA A 554 1
HET CL A 555 1
HET CL A 556 1
HET CL A 557 1
HET CL A 558 1
HET CL A 559 1
HET CL A 560 1
HET CL A 561 1
HET PG4 A 562 13
HET CA B 551 1
HET CA B 552 1
HET CL B 553 1
HET CL B 554 1
HET CL B 555 1
HET CL B 556 2
HET CL B 557 1
HET CL B 558 1
HET CL B 559 1
HET NA B 560 1
HET PEG B 561 7
HET CA C 551 1
HET CL C 552 1
HET CL C 553 1
HET CL C 554 1
HET CL C 555 1
HET CL C 556 1
HET NA C 557 1
HET PEG C 558 7
HET PEG C 559 7
HET PEG C 560 7
HET CA D 551 1
HET CA D 552 1
HET CA D 553 1
HET CL D 554 1
HET CL D 555 1
HET CL D 556 1
HET CL D 557 1
HET CL D 558 1
HET CL D 559 1
HET CL D 560 1
HET PG4 D 561 13
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 5 CA 10(CA 2+)
FORMUL 9 CL 26(CL 1-)
FORMUL 16 PG4 2(C8 H18 O5)
FORMUL 26 NA 2(NA 1+)
FORMUL 27 PEG 4(C4 H10 O3)
FORMUL 49 HOH *4071(H2 O)
HELIX 1 1 ASN A 6 GLN A 9 5 4
HELIX 2 2 THR A 10 GLN A 24 1 15
HELIX 3 3 ASP A 27 GLN A 34 1 8
HELIX 4 4 GLU A 37 TYR A 42 1 6
HELIX 5 5 ASN A 60 THR A 74 1 15
HELIX 6 6 ASP A 75 GLY A 86 1 12
HELIX 7 7 LEU A 98 ARG A 103 1 6
HELIX 8 8 VAL A 117 GLY A 138 1 22
HELIX 9 9 ILE A 156 SER A 159 5 4
HELIX 10 10 ASP A 160 LEU A 170 1 11
HELIX 11 11 VAL A 171 LYS A 174 5 4
HELIX 12 12 ASP A 186 LYS A 195 1 10
HELIX 13 13 ASN A 196 VAL A 197 5 2
HELIX 14 14 ASP A 198 GLU A 200 5 3
HELIX 15 15 THR A 213 GLY A 232 1 20
HELIX 16 16 ASP A 233 LYS A 239 5 7
HELIX 17 17 ASN A 247 GLY A 255 1 9
HELIX 18 18 ASP A 257 ASP A 259 5 3
HELIX 19 19 GLY A 269 SER A 273 5 5
HELIX 20 20 SER A 276 ILE A 278 5 3
HELIX 21 21 GLY A 279 GLY A 287 1 9
HELIX 22 22 GLY A 287 THR A 308 1 22
HELIX 23 23 PRO A 309 SER A 312 5 4
HELIX 24 24 ASN A 313 PHE A 328 1 16
HELIX 25 25 ASP A 340 HIS A 344 5 5
HELIX 26 26 ARG A 345 GLY A 359 1 15
HELIX 27 27 GLY A 385 GLY A 396 1 12
HELIX 28 28 ASP A 416 GLY A 435 1 20
HELIX 29 29 SER A 437 ALA A 448 1 12
HELIX 30 30 SER A 451 VAL A 463 1 13
HELIX 31 31 THR A 479 TRP A 501 1 23
HELIX 32 32 GLN A 508 GLY A 510 5 3
HELIX 33 33 VAL A 511 LEU A 522 1 12
HELIX 34 34 PRO A 523 ALA A 526 5 4
HELIX 35 35 ASP A 535 ALA A 550 1 16
HELIX 36 36 ASN B 6 GLN B 9 5 4
HELIX 37 37 THR B 10 GLN B 24 1 15
HELIX 38 38 ASP B 27 GLN B 34 1 8
HELIX 39 39 GLU B 37 TYR B 42 1 6
HELIX 40 40 ASN B 60 THR B 74 1 15
HELIX 41 41 ASP B 75 GLY B 86 1 12
HELIX 42 42 LEU B 98 ARG B 103 1 6
HELIX 43 43 VAL B 117 GLY B 137 1 21
HELIX 44 44 ILE B 156 SER B 159 5 4
HELIX 45 45 ASP B 160 LEU B 170 1 11
HELIX 46 46 VAL B 171 LYS B 174 5 4
HELIX 47 47 ASP B 186 LYS B 195 1 10
HELIX 48 48 ASN B 196 VAL B 197 5 2
HELIX 49 49 ASP B 198 GLU B 200 5 3
HELIX 50 50 THR B 213 GLY B 232 1 20
HELIX 51 51 ASP B 233 LYS B 239 5 7
HELIX 52 52 ASN B 247 GLY B 255 1 9
HELIX 53 53 ASP B 257 ASP B 259 5 3
HELIX 54 54 GLY B 269 SER B 273 5 5
HELIX 55 55 SER B 276 ILE B 278 5 3
HELIX 56 56 GLY B 279 GLY B 287 1 9
HELIX 57 57 GLY B 287 THR B 308 1 22
HELIX 58 58 PRO B 309 SER B 312 5 4
HELIX 59 59 ASN B 313 PHE B 328 1 16
HELIX 60 60 ASP B 340 HIS B 344 5 5
HELIX 61 61 ARG B 345 GLY B 359 1 15
HELIX 62 62 GLY B 385 GLY B 396 1 12
HELIX 63 63 ASP B 416 GLY B 435 1 20
HELIX 64 64 SER B 437 ALA B 448 1 12
HELIX 65 65 SER B 451 VAL B 463 1 13
HELIX 66 66 THR B 479 TRP B 501 1 23
HELIX 67 67 GLN B 508 GLY B 510 5 3
HELIX 68 68 VAL B 511 LEU B 522 1 12
HELIX 69 69 PRO B 523 ALA B 526 5 4
HELIX 70 70 ASP B 535 ALA B 550 1 16
HELIX 71 71 ASN C 6 GLN C 9 5 4
HELIX 72 72 THR C 10 GLN C 24 1 15
HELIX 73 73 ASP C 27 GLN C 34 1 8
HELIX 74 74 GLU C 37 TYR C 42 1 6
HELIX 75 75 ASN C 60 THR C 74 1 15
HELIX 76 76 ASP C 75 GLY C 86 1 12
HELIX 77 77 LEU C 98 ARG C 103 1 6
HELIX 78 78 VAL C 117 GLY C 137 1 21
HELIX 79 79 ILE C 156 SER C 159 5 4
HELIX 80 80 ASP C 160 LEU C 170 1 11
HELIX 81 81 VAL C 171 LYS C 174 5 4
HELIX 82 82 ASP C 186 LYS C 195 1 10
HELIX 83 83 ASN C 196 VAL C 197 5 2
HELIX 84 84 ASP C 198 GLU C 200 5 3
HELIX 85 85 THR C 213 GLY C 232 1 20
HELIX 86 86 ASP C 233 LYS C 239 5 7
HELIX 87 87 ASN C 247 GLY C 255 1 9
HELIX 88 88 ASP C 257 ASP C 259 5 3
HELIX 89 89 GLY C 269 SER C 273 5 5
HELIX 90 90 SER C 276 ILE C 278 5 3
HELIX 91 91 GLY C 279 GLY C 287 1 9
HELIX 92 92 GLY C 287 THR C 308 1 22
HELIX 93 93 PRO C 309 SER C 312 5 4
HELIX 94 94 ASN C 313 PHE C 328 1 16
HELIX 95 95 ASP C 340 HIS C 344 5 5
HELIX 96 96 ARG C 345 GLY C 359 1 15
HELIX 97 97 GLY C 385 GLY C 396 1 12
HELIX 98 98 ASP C 416 GLY C 435 1 20
HELIX 99 99 SER C 437 ALA C 448 1 12
HELIX 100 100 SER C 451 VAL C 463 1 13
HELIX 101 101 THR C 479 TRP C 501 1 23
HELIX 102 102 GLN C 508 GLY C 510 5 3
HELIX 103 103 VAL C 511 LEU C 522 1 12
HELIX 104 104 PRO C 523 ALA C 526 5 4
HELIX 105 105 ASP C 535 ALA C 550 1 16
HELIX 106 106 ASN D 6 GLN D 9 5 4
HELIX 107 107 THR D 10 GLN D 24 1 15
HELIX 108 108 ASP D 27 ASP D 35 1 9
HELIX 109 109 GLU D 37 TYR D 42 1 6
HELIX 110 110 ASN D 60 THR D 74 1 15
HELIX 111 111 ASP D 75 GLY D 86 1 12
HELIX 112 112 LEU D 98 ARG D 103 1 6
HELIX 113 113 VAL D 117 GLY D 138 1 22
HELIX 114 114 ILE D 156 SER D 159 5 4
HELIX 115 115 ASP D 160 LEU D 170 1 11
HELIX 116 116 VAL D 171 LYS D 174 5 4
HELIX 117 117 ASP D 186 LYS D 195 1 10
HELIX 118 118 ASN D 196 VAL D 197 5 2
HELIX 119 119 ASP D 198 GLU D 200 5 3
HELIX 120 120 THR D 213 GLY D 232 1 20
HELIX 121 121 ASP D 233 LYS D 239 5 7
HELIX 122 122 ASN D 247 GLY D 255 1 9
HELIX 123 123 ASP D 257 ASP D 259 5 3
HELIX 124 124 GLY D 269 SER D 273 5 5
HELIX 125 125 SER D 276 ILE D 278 5 3
HELIX 126 126 GLY D 279 GLY D 287 1 9
HELIX 127 127 GLY D 287 THR D 308 1 22
HELIX 128 128 PRO D 309 SER D 312 5 4
HELIX 129 129 ASN D 313 PHE D 328 1 16
HELIX 130 130 ASP D 340 HIS D 344 5 5
HELIX 131 131 ARG D 345 GLY D 359 1 15
HELIX 132 132 GLY D 385 GLY D 396 1 12
HELIX 133 133 ASP D 416 GLY D 435 1 20
HELIX 134 134 SER D 437 ALA D 448 1 12
HELIX 135 135 SER D 451 VAL D 463 1 13
HELIX 136 136 THR D 479 TRP D 501 1 23
HELIX 137 137 GLN D 508 GLY D 510 5 3
HELIX 138 138 VAL D 511 LEU D 522 1 12
HELIX 139 139 PRO D 523 ALA D 526 5 4
HELIX 140 140 ASP D 535 ALA D 550 1 16
SHEET 1 A 6 SER A 43 PHE A 46 0
SHEET 2 A 6 ILE A 50 ASP A 53 -1 O VAL A 52 N ALA A 44
SHEET 3 A 6 THR A 470 VAL A 475 -1 O SER A 472 N ASP A 53
SHEET 4 A 6 CYS A 402 PRO A 407 1 N PHE A 404 O ILE A 473
SHEET 5 A 6 SER A 333 PRO A 338 1 N LEU A 337 O ASP A 403
SHEET 6 A 6 ILE A 376 TRP A 378 1 O ILE A 376 N GLU A 334
SHEET 1 B 2 LEU A 111 VAL A 112 0
SHEET 2 B 2 GLU A 115 ASP A 116 -1 O GLU A 115 N VAL A 112
SHEET 1 C 5 THR A 178 VAL A 182 0
SHEET 2 C 5 ASP A 150 ILE A 154 1 N ASN A 153 O HIS A 180
SHEET 3 C 5 THR A 202 ALA A 207 1 O ALA A 207 N ILE A 154
SHEET 4 C 5 PHE A 241 LEU A 244 1 O ALA A 242 N VAL A 206
SHEET 5 C 5 MET A 261 PHE A 262 1 O PHE A 262 N ALA A 243
SHEET 1 D 6 SER B 43 PHE B 46 0
SHEET 2 D 6 ILE B 50 ASP B 53 -1 O VAL B 52 N ALA B 44
SHEET 3 D 6 THR B 470 VAL B 475 -1 O SER B 472 N ASP B 53
SHEET 4 D 6 CYS B 402 PRO B 407 1 N PHE B 404 O ILE B 473
SHEET 5 D 6 SER B 333 PRO B 338 1 N LEU B 337 O ASP B 403
SHEET 6 D 6 ILE B 376 TRP B 378 1 O TRP B 378 N ILE B 336
SHEET 1 E 2 LEU B 111 VAL B 112 0
SHEET 2 E 2 GLU B 115 ASP B 116 -1 O GLU B 115 N VAL B 112
SHEET 1 F 5 THR B 178 VAL B 182 0
SHEET 2 F 5 ASP B 150 ILE B 154 1 N ASN B 153 O HIS B 180
SHEET 3 F 5 THR B 202 ALA B 207 1 O ALA B 207 N ILE B 154
SHEET 4 F 5 PHE B 241 LEU B 244 1 O ALA B 242 N VAL B 206
SHEET 5 F 5 MET B 261 PHE B 262 1 O PHE B 262 N ALA B 243
SHEET 1 G 6 SER C 43 PHE C 46 0
SHEET 2 G 6 ILE C 50 ASP C 53 -1 O VAL C 52 N ALA C 44
SHEET 3 G 6 THR C 470 VAL C 475 -1 O SER C 472 N ASP C 53
SHEET 4 G 6 CYS C 402 PRO C 407 1 N PHE C 404 O ASN C 471
SHEET 5 G 6 SER C 333 PRO C 338 1 N LEU C 337 O ASP C 403
SHEET 6 G 6 ILE C 376 TRP C 378 1 O ILE C 376 N GLU C 334
SHEET 1 H 2 LEU C 111 VAL C 112 0
SHEET 2 H 2 GLU C 115 ASP C 116 -1 O GLU C 115 N VAL C 112
SHEET 1 I 5 THR C 178 VAL C 182 0
SHEET 2 I 5 ASP C 150 ILE C 154 1 N ASN C 153 O HIS C 180
SHEET 3 I 5 THR C 202 ALA C 207 1 O ALA C 207 N ILE C 154
SHEET 4 I 5 PHE C 241 LEU C 244 1 O ALA C 242 N VAL C 206
SHEET 5 I 5 MET C 261 PHE C 262 1 O PHE C 262 N ALA C 243
SHEET 1 J 6 SER D 43 PHE D 46 0
SHEET 2 J 6 ILE D 50 ASP D 53 -1 O VAL D 52 N ALA D 44
SHEET 3 J 6 THR D 470 VAL D 475 -1 O SER D 472 N ASP D 53
SHEET 4 J 6 CYS D 402 PRO D 407 1 N PHE D 404 O ILE D 473
SHEET 5 J 6 SER D 333 PRO D 338 1 N LEU D 337 O ASP D 403
SHEET 6 J 6 ILE D 376 TRP D 378 1 O ILE D 376 N GLU D 334
SHEET 1 K 2 LEU D 111 VAL D 112 0
SHEET 2 K 2 GLU D 115 ASP D 116 -1 O GLU D 115 N VAL D 112
SHEET 1 L 5 THR D 178 VAL D 182 0
SHEET 2 L 5 ASP D 150 ILE D 154 1 N ASN D 153 O HIS D 180
SHEET 3 L 5 THR D 202 ALA D 207 1 O ALA D 207 N ILE D 154
SHEET 4 L 5 PHE D 241 LEU D 244 1 O ALA D 242 N VAL D 206
SHEET 5 L 5 MET D 261 PHE D 262 1 O PHE D 262 N ALA D 243
LINK OE1 GLU A 62 CA CA A 551 1555 1555 2.53
LINK OE2 GLU A 62 CA CA A 551 1555 1555 2.39
LINK OE1 GLU A 168 CA CA A 552 1555 1555 2.51
LINK OE2 GLU A 168 CA CA A 552 1555 1555 2.64
LINK O GLU A 253 CA B CA A 553 1555 1555 2.51
LINK O GLY A 330 CA A CA B 552 1555 1555 2.38
LINK OE2 GLU A 332 CA B CA A 554 1555 1555 2.26
LINK CA CA A 551 O HOH A 812 1555 1555 2.45
LINK CA CA A 551 O HOH A 921 1555 1555 2.59
LINK CA CA A 551 O HOH A2078 1555 1555 2.47
LINK CA CA A 551 O HOH A2216 1555 1555 2.40
LINK CA CA A 551 O HOH A3413 1555 1555 2.68
LINK CA CA A 552 O HOH A1387 1555 1555 2.38
LINK CA CA A 552 O HOH A2765 1555 1555 2.33
LINK CA CA A 552 O HOH A2918 1555 1555 2.30
LINK CA CA A 552 O HOH A3926 1555 1555 2.29
LINK CA B CA A 553 O HOH A3373 1555 1555 2.67
LINK CA B CA A 553 O HOH A3833 1555 1555 2.15
LINK CA B CA A 553 O HOH A3984 1555 1555 2.48
LINK CA B CA A 553 O BHOH A4115 1555 1555 2.39
LINK CA B CA A 554 O BHOH A3970 1555 1555 2.41
LINK CA B CA A 554 O GLY B 330 1555 1555 2.35
LINK CA B CA A 554 O BHOH B4111 1555 1555 2.58
LINK CA B CA A 554 O HOH B4114 1555 1555 2.22
LINK O AHOH A3970 CA A CA B 552 1555 1555 2.64
LINK O HOH A3971 CA A CA B 552 1555 1555 2.05
LINK OE1 GLU B 62 CA CA B 551 1555 1555 2.46
LINK OE2 GLU B 62 CA CA B 551 1555 1555 2.41
LINK OE2 GLU B 332 CA A CA B 552 1555 1555 2.16
LINK CA CA B 551 O HOH B 638 1555 1555 2.52
LINK CA CA B 551 O HOH B 651 1555 1555 2.51
LINK CA CA B 551 O HOH B1182 1555 1555 2.35
LINK CA A CA B 552 O AHOH B4111 1555 1555 2.39
LINK NA NA B 560 O HOH B 720 1555 1555 2.51
LINK NA NA B 560 O HOH B1465 1555 1555 2.36
LINK NA NA B 560 O HOH B1875 1555 1555 2.41
LINK NA NA B 560 O HOH B2002 1555 1555 2.53
LINK NA NA B 560 O HOH B3986 1555 1555 2.40
LINK OE1 GLU C 62 CA CA C 551 1555 1555 2.44
LINK OE2 GLU C 62 CA CA C 551 1555 1555 2.39
LINK CA CA C 551 O HOH C 617 1555 1555 2.50
LINK CA CA C 551 O HOH C 734 1555 1555 2.49
LINK CA CA C 551 O HOH C1246 1555 1555 2.42
LINK NA NA C 557 O HOH C 651 1555 1555 2.47
LINK NA NA C 557 O HOH C1214 1555 1555 2.36
LINK NA NA C 557 O HOH C1811 1555 1555 2.59
LINK NA NA C 557 O HOH C3215 1555 1555 2.31
LINK NA NA C 557 O HOH C3913 1555 1555 2.42
LINK OE1 GLU D 62 CA CA D 551 1555 1555 2.50
LINK OE2 GLU D 62 CA CA D 551 1555 1555 2.43
LINK OE1 GLU D 168 CA B CA D 552 1555 1555 2.48
LINK OE2 GLU D 168 CA B CA D 552 1555 1555 2.62
LINK O GLU D 253 CA B CA D 553 1555 1555 2.50
LINK CA CA D 551 O HOH D 811 1555 1555 2.52
LINK CA CA D 551 O HOH D 830 1555 1555 2.56
LINK CA CA D 551 O HOH D2011 1555 1555 2.36
LINK CA CA D 551 O HOH D2302 1555 1555 2.36
LINK CA B CA D 552 O HOH D1444 1555 1555 2.36
LINK CA B CA D 552 O HOH D2839 1555 1555 2.36
LINK CA B CA D 552 O HOH D3928 1555 1555 2.32
LINK CA B CA D 553 O HOH D2802 1555 1555 2.59
LINK CA B CA D 553 O HOH D3337 1555 1555 2.25
LINK CA B CA D 553 O BHOH D3881 1555 1555 2.41
LINK CA B CA D 553 O HOH D3985 1555 1555 2.71
CISPEP 1 GLY A 382 THR A 383 0 1.45
CISPEP 2 GLY B 382 THR B 383 0 1.41
CISPEP 3 GLY C 382 THR C 383 0 0.97
CISPEP 4 GLY D 382 THR D 383 0 2.10
SITE 1 AC1 7 GLU A 62 HOH A 812 HOH A 921 HOH A2078
SITE 2 AC1 7 HOH A2216 HOH A3413 HOH C2469
SITE 1 AC2 5 GLU A 168 HOH A1387 HOH A2765 HOH A2918
SITE 2 AC2 5 HOH A3926
SITE 1 AC3 5 GLU A 253 HOH A3373 HOH A3833 HOH A3984
SITE 2 AC3 5 HOH A4115
SITE 1 AC4 6 GLU A 332 HOH A3970 GLY B 330 CA B 552
SITE 2 AC4 6 HOH B4111 HOH B4114
SITE 1 AC5 4 ARG A 95 ALA A 96 HOH A1640 HOH A2031
SITE 1 AC6 5 ASN A 327 TYR A 371 GLN A 372 HOH A1459
SITE 2 AC6 5 HOH A1928
SITE 1 AC7 4 LYS A 127 MET A 261 GLU A 263 HOH A1040
SITE 1 AC8 3 GLN A 419 HOH A 598 ARG B 549
SITE 1 AC9 4 ASN A 175 GLY A 287 HOH A1053 HOH A1302
SITE 1 BC1 4 MET A 26 ASP A 27 HOH A2211 HOH A2711
SITE 1 BC2 2 ALA A 452 HOH A2855
SITE 1 BC3 13 GLN A 24 ASP A 25 GLY A 396 THR A 397
SITE 2 BC3 13 LYS A 398 LEU A 399 ASN A 467 ARG A 468
SITE 3 BC3 13 HOH A2008 HOH A2467 HOH A2504 HOH A3493
SITE 4 BC3 13 PEG B 561
SITE 1 BC4 4 GLU B 62 HOH B 638 HOH B 651 HOH B1182
SITE 1 BC5 6 GLY A 330 CA A 554 HOH A3970 HOH A3971
SITE 2 BC5 6 GLU B 332 HOH B4111
SITE 1 BC6 5 ARG B 95 ALA B 96 TRP B 267 HOH B1188
SITE 2 BC6 5 HOH B1869
SITE 1 BC7 4 ASN B 175 GLY B 287 HOH B 731 HOH B1657
SITE 1 BC8 4 ASN B 327 TYR B 371 GLN B 372 HOH B2282
SITE 1 BC9 5 ASP B 266 HOH B1729 HOH B1869 HOH B3152
SITE 2 BC9 5 HOH B3651
SITE 1 CC1 6 ASN B 104 ASN B 107 MET B 118 ASN B 122
SITE 2 CC1 6 HOH B 596 HOH B3987
SITE 1 CC2 6 LYS B 72 LEU B 76 GLN B 77 PHE B 310
SITE 2 CC2 6 HOH B1482 HOH B2632
SITE 1 CC3 6 PHE A 32 HOH A 890 ASP B 535 SER B 536
SITE 2 CC3 6 HOH B 658 HOH B1354
SITE 1 CC4 5 HOH B 720 HOH B1465 HOH B1875 HOH B2002
SITE 2 CC4 5 HOH B3986
SITE 1 CC5 4 PG4 A 562 TYR B 371 GLN B 372 HOH B1094
SITE 1 CC6 4 GLU C 62 HOH C 617 HOH C 734 HOH C1246
SITE 1 CC7 4 ARG C 95 ALA C 96 TRP C 267 HOH C1993
SITE 1 CC8 3 ASN C 175 GLY C 287 HOH C 636
SITE 1 CC9 4 ARG C 549 GLN D 419 HOH D 580 HOH D 714
SITE 1 DC1 4 ASN C 327 TYR C 371 GLN C 372 HOH C1846
SITE 1 DC2 5 SER C 410 ASN C 412 HOH C 624 HOH C1255
SITE 2 DC2 5 GLY D 187
SITE 1 DC3 5 HOH C 651 HOH C1214 HOH C1811 HOH C3215
SITE 2 DC3 5 HOH C3913
SITE 1 DC4 6 ARG B 105 SER B 106 ASN B 107 LYS C 450
SITE 2 DC4 6 HOH C1379 HOH C2803
SITE 1 DC5 10 ALA B 448 LYS B 450 HOH B1842 ARG C 105
SITE 2 DC5 10 SER C 106 ASN C 107 HOH C1326 HOH C2774
SITE 3 DC5 10 HOH C2888 HOH C3994
SITE 1 DC6 6 VAL C 369 TYR C 371 GLN C 372 HOH C 818
SITE 2 DC6 6 THR D 397 PG4 D 561
SITE 1 DC7 6 HOH B2124 GLU D 62 HOH D 811 HOH D 830
SITE 2 DC7 6 HOH D2011 HOH D2302
SITE 1 DC8 6 GLU D 168 HOH D1444 HOH D1506 HOH D2839
SITE 2 DC8 6 HOH D3927 HOH D3928
SITE 1 DC9 6 GLU D 253 HOH D2802 HOH D3337 HOH D3881
SITE 2 DC9 6 HOH D3930 HOH D3985
SITE 1 EC1 4 ARG D 95 ALA D 96 HOH D1885 HOH D2032
SITE 1 EC2 5 ASN D 327 TYR D 371 GLN D 372 HOH D1477
SITE 2 EC2 5 HOH D1656
SITE 1 EC3 5 ASN D 175 GLY D 287 HOH D1031 HOH D1418
SITE 2 EC3 5 HOH D3873
SITE 1 EC4 3 LYS D 127 MET D 261 GLU D 263
SITE 1 EC5 5 MET D 26 ASP D 27 HOH D2120 HOH D3226
SITE 2 EC5 5 HOH D3709
SITE 1 EC6 4 ILE D 89 PHE D 506 HOH D 565 HOH D 574
SITE 1 EC7 2 ALA D 452 HOH D2046
SITE 1 EC8 12 PEG C 560 GLN D 24 GLY D 396 THR D 397
SITE 2 EC8 12 LEU D 399 ASN D 467 ARG D 468 HOH D1814
SITE 3 EC8 12 HOH D1882 HOH D2122 HOH D2505 HOH D3887
CRYST1 125.661 75.094 127.456 90.00 90.21 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 0.007958 0.000000 0.000029 0.00000
SCALE2 0.000000 0.013317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
