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HEADER HYDROLASE 09-MAY-18 6GI0
TITLE CRYSTAL STRUCTURE OF THE FERRIC ENTEROBACTIN ESTERASE (PFEE) FROM
TITLE 2 PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERRIC ENTEROBACTIN ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 5 / 1C / PRS 101 / PAO1;
SOURCE 6 GENE: PA2689;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PFEE, PA2689, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.MOYNIE,J.H.NAISMITH
REVDAT 1 20-JUN-18 6GI0 0
JRNL AUTH L.MOYNIE,J.H.NAISMITH,I.SCHALK
JRNL TITL A KEY ROLE FOR PFEE ESTERASE IN IRON ACQUISITION VIA THE
JRNL TITL 2 SIDEROPHORE ENTEROBACTIN IN P. AERUGINOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 28603
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1555
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1667
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.29000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.210
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.557
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4075 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3850 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5539 ; 1.334 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8826 ; 0.709 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 513 ; 6.937 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;33.643 ;21.390
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 617 ;14.991 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;20.822 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 594 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4627 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 914 ; 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): 2067 ; 1.756 ; 2.028
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2066 ; 1.755 ; 2.028
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2575 ; 2.537 ; 3.027
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2576 ; 2.536 ; 3.027
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2008 ; 2.190 ; 2.325
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2003 ; 2.185 ; 2.323
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2959 ; 3.389 ; 3.375
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4409 ; 4.665 ;23.866
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4392 ; 4.660 ;23.782
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 12 275 B 12 275 15128 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
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 12 A 27
REMARK 3 ORIGIN FOR THE GROUP (A): 41.1814 37.7675 32.7561
REMARK 3 T TENSOR
REMARK 3 T11: 0.1690 T22: 0.1075
REMARK 3 T33: 0.1001 T12: 0.0018
REMARK 3 T13: 0.0046 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 12.3526 L22: 5.7764
REMARK 3 L33: 3.8964 L12: -5.1619
REMARK 3 L13: 2.0923 L23: -0.1954
REMARK 3 S TENSOR
REMARK 3 S11: -0.2666 S12: 0.2264 S13: 0.8869
REMARK 3 S21: 0.0928 S22: 0.0682 S23: -0.0999
REMARK 3 S31: -0.7037 S32: -0.2355 S33: 0.1984
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 28 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2676 29.5305 29.0900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0451 T22: 0.0323
REMARK 3 T33: 0.0170 T12: -0.0141
REMARK 3 T13: 0.0091 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 3.3864 L22: 2.3065
REMARK 3 L33: 2.3470 L12: -0.6812
REMARK 3 L13: 0.7865 L23: -0.1883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0384 S12: -0.1189 S13: 0.2159
REMARK 3 S21: 0.0750 S22: -0.0013 S23: -0.0287
REMARK 3 S31: -0.1338 S32: -0.1869 S33: 0.0397
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 76 A 88
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2822 29.4619 28.5217
REMARK 3 T TENSOR
REMARK 3 T11: 0.0597 T22: 0.0963
REMARK 3 T33: 0.0509 T12: -0.0196
REMARK 3 T13: -0.0033 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 12.8539 L22: 3.8044
REMARK 3 L33: 5.8625 L12: -0.1410
REMARK 3 L13: -4.9624 L23: 0.2977
REMARK 3 S TENSOR
REMARK 3 S11: 0.0443 S12: -0.0936 S13: 0.4600
REMARK 3 S21: -0.0115 S22: -0.0060 S23: 0.3378
REMARK 3 S31: -0.1286 S32: -0.5056 S33: -0.0382
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 89 A 138
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4575 16.5830 22.0402
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.0440
REMARK 3 T33: 0.0905 T12: 0.0210
REMARK 3 T13: -0.0162 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 4.0357 L22: 2.9673
REMARK 3 L33: 9.6135 L12: -0.9520
REMARK 3 L13: -3.9243 L23: 2.0119
REMARK 3 S TENSOR
REMARK 3 S11: 0.0061 S12: 0.1298 S13: -0.1142
REMARK 3 S21: -0.1061 S22: 0.0126 S23: -0.2772
REMARK 3 S31: 0.1720 S32: 0.1625 S33: -0.0187
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 139 A 190
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3907 18.0453 20.5644
REMARK 3 T TENSOR
REMARK 3 T11: 0.0784 T22: 0.0198
REMARK 3 T33: 0.0559 T12: -0.0091
REMARK 3 T13: 0.0069 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.2843 L22: 1.5220
REMARK 3 L33: 4.9476 L12: -0.0180
REMARK 3 L13: -0.3567 L23: 1.1500
REMARK 3 S TENSOR
REMARK 3 S11: -0.0065 S12: -0.0764 S13: -0.2372
REMARK 3 S21: 0.1053 S22: -0.0428 S23: 0.0133
REMARK 3 S31: 0.5921 S32: 0.0064 S33: 0.0493
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 191 A 240
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2090 14.7928 8.4119
REMARK 3 T TENSOR
REMARK 3 T11: 0.1664 T22: 0.1404
REMARK 3 T33: 0.1637 T12: -0.0182
REMARK 3 T13: 0.0245 T23: -0.1024
REMARK 3 L TENSOR
REMARK 3 L11: 2.3115 L22: 4.7331
REMARK 3 L33: 3.8062 L12: -0.3866
REMARK 3 L13: 1.1331 L23: -0.7454
REMARK 3 S TENSOR
REMARK 3 S11: 0.0278 S12: 0.4899 S13: -0.5031
REMARK 3 S21: -0.4087 S22: -0.0611 S23: -0.0285
REMARK 3 S31: 0.6333 S32: 0.1301 S33: 0.0333
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 241 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8980 24.7567 12.4135
REMARK 3 T TENSOR
REMARK 3 T11: 0.0448 T22: 0.0510
REMARK 3 T33: 0.0366 T12: -0.0195
REMARK 3 T13: -0.0134 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 4.7043 L22: 4.8171
REMARK 3 L33: 3.9062 L12: 1.4112
REMARK 3 L13: 0.5680 L23: -0.2008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0157 S12: 0.2551 S13: -0.1642
REMARK 3 S21: -0.1917 S22: 0.0556 S23: 0.3186
REMARK 3 S31: 0.3275 S32: -0.3079 S33: -0.0399
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 6 B 59
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0748 36.0310 -3.0337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0799 T22: 0.0558
REMARK 3 T33: 0.0301 T12: 0.0164
REMARK 3 T13: 0.0118 T23: -0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 2.3301 L22: 5.1503
REMARK 3 L33: 4.0086 L12: 1.0395
REMARK 3 L13: 0.2887 L23: -1.2997
REMARK 3 S TENSOR
REMARK 3 S11: 0.0199 S12: -0.0039 S13: -0.1952
REMARK 3 S21: -0.4363 S22: -0.1384 S23: -0.0999
REMARK 3 S31: 0.4998 S32: 0.0279 S33: 0.1185
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 : B 60 B 96
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2436 35.4734 0.1399
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.0416
REMARK 3 T33: 0.0508 T12: 0.0241
REMARK 3 T13: -0.0069 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 4.4227 L22: 7.5241
REMARK 3 L33: 5.6243 L12: -0.4926
REMARK 3 L13: 1.0948 L23: -3.7323
REMARK 3 S TENSOR
REMARK 3 S11: 0.0876 S12: 0.0891 S13: -0.0598
REMARK 3 S21: -0.2315 S22: -0.2156 S23: -0.2099
REMARK 3 S31: 0.2947 S32: 0.2433 S33: 0.1280
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 97 B 137
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7869 55.7689 -4.4866
REMARK 3 T TENSOR
REMARK 3 T11: 0.1462 T22: 0.0297
REMARK 3 T33: 0.0784 T12: 0.0074
REMARK 3 T13: -0.0300 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 7.7576 L22: 3.9453
REMARK 3 L33: 3.1024 L12: 2.1839
REMARK 3 L13: -1.5840 L23: -0.5638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0920 S12: -0.0595 S13: 0.3984
REMARK 3 S21: -0.0875 S22: -0.1420 S23: -0.1023
REMARK 3 S31: -0.5002 S32: 0.1450 S33: 0.0500
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 138 B 204
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9162 51.9135 7.3364
REMARK 3 T TENSOR
REMARK 3 T11: 0.0853 T22: 0.0440
REMARK 3 T33: 0.1343 T12: 0.0229
REMARK 3 T13: -0.0195 T23: -0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 2.0923 L22: 3.2076
REMARK 3 L33: 3.4804 L12: 0.6100
REMARK 3 L13: 0.9719 L23: 0.9481
REMARK 3 S TENSOR
REMARK 3 S11: -0.0769 S12: -0.2480 S13: 0.5070
REMARK 3 S21: 0.0849 S22: -0.2204 S23: 0.1766
REMARK 3 S31: -0.4737 S32: -0.2374 S33: 0.2973
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 205 B 235
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7494 49.7815 13.5541
REMARK 3 T TENSOR
REMARK 3 T11: 0.1440 T22: 0.0512
REMARK 3 T33: 0.0750 T12: -0.0147
REMARK 3 T13: -0.0526 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 5.1992 L22: 7.1998
REMARK 3 L33: 6.2286 L12: -3.1181
REMARK 3 L13: 0.1669 L23: 2.4416
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: 0.1636 S13: 0.4935
REMARK 3 S21: 0.2358 S22: 0.0588 S23: -0.5013
REMARK 3 S31: -0.3006 S32: 0.3865 S33: -0.0727
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 236 B 256
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6520 50.0470 18.4656
REMARK 3 T TENSOR
REMARK 3 T11: 0.1466 T22: 0.1357
REMARK 3 T33: 0.1167 T12: -0.0059
REMARK 3 T13: -0.0307 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 10.4293 L22: 3.8452
REMARK 3 L33: 4.8055 L12: -3.9235
REMARK 3 L13: -2.3102 L23: 2.1424
REMARK 3 S TENSOR
REMARK 3 S11: -0.1557 S12: -0.7218 S13: 0.6813
REMARK 3 S21: 0.4001 S22: 0.1533 S23: -0.3029
REMARK 3 S31: -0.3461 S32: 0.1280 S33: 0.0024
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 257 B 275
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5753 38.5284 9.5790
REMARK 3 T TENSOR
REMARK 3 T11: 0.0466 T22: 0.0227
REMARK 3 T33: 0.0303 T12: 0.0094
REMARK 3 T13: -0.0230 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 10.1434 L22: 8.8292
REMARK 3 L33: 5.8035 L12: 4.5151
REMARK 3 L13: -0.3470 L23: -2.9766
REMARK 3 S TENSOR
REMARK 3 S11: 0.2862 S12: -0.2523 S13: 0.1193
REMARK 3 S21: 0.3164 S22: -0.1882 S23: 0.0759
REMARK 3 S31: -0.1968 S32: -0.1704 S33: -0.0980
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6GI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200009975.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30184
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 55.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.20900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2GZR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, SODIUM ACETATE,
REMARK 280 POTASSIUM NITRATE, VAPOR DIFFUSION, TEMPERATURE 294K
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 55.55000
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
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 ALA A -1
REMARK 465 MET A 0
REMARK 465 ASN A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 PRO A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 THR A 7
REMARK 465 MET A 8
REMARK 465 ASP A 9
REMARK 465 ARG A 10
REMARK 465 SER A 11
REMARK 465 PRO A 91
REMARK 465 LEU A 92
REMARK 465 ARG A 93
REMARK 465 ILE A 94
REMARK 465 ALA A 111
REMARK 465 ASP A 112
REMARK 465 ARG A 277
REMARK 465 GLN A 278
REMARK 465 ARG A 279
REMARK 465 GLY B -2
REMARK 465 ALA B -1
REMARK 465 MET B 0
REMARK 465 ASN B 1
REMARK 465 PRO B 2
REMARK 465 ASP B 3
REMARK 465 PRO B 4
REMARK 465 GLU B 5
REMARK 465 GLY B 109
REMARK 465 GLN B 110
REMARK 465 ALA B 111
REMARK 465 SER B 220
REMARK 465 PRO B 221
REMARK 465 ARG B 222
REMARK 465 GLY B 223
REMARK 465 SER B 224
REMARK 465 LEU B 225
REMARK 465 LYS B 226
REMARK 465 ALA B 227
REMARK 465 GLU B 228
REMARK 465 GLU B 276
REMARK 465 ARG B 277
REMARK 465 GLN B 278
REMARK 465 ARG B 279
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 ARG B 10 NE2 GLN B 14 1.84
REMARK 500 OD2 ASP A 59 O HOH A 401 2.01
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 170 NE - CZ - NH2 ANGL. DEV. = -3.5 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 SER A 157 -119.92 69.40
REMARK 500 ARG A 170 57.41 -143.02
REMARK 500 SER B 157 -119.97 70.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 302
DBREF 6GI0 A 2 279 UNP Q9I0F2 Q9I0F2_PSEAE 27 304
DBREF 6GI0 B 2 279 UNP Q9I0F2 Q9I0F2_PSEAE 27 304
SEQADV 6GI0 GLY A -2 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI0 ALA A -1 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI0 MET A 0 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI0 ASN A 1 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI0 GLY B -2 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI0 ALA B -1 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI0 MET B 0 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI0 ASN B 1 UNP Q9I0F2 EXPRESSION TAG
SEQRES 1 A 282 GLY ALA MET ASN PRO ASP PRO GLU ALA THR MET ASP ARG
SEQRES 2 A 282 SER LEU LEU GLN ARG GLN ASP LEU PRO TYR ARG PHE SER
SEQRES 3 A 282 ALA VAL ASP LEU ASP SER VAL ASP GLY GLN ARG HIS TYR
SEQRES 4 A 282 ARG LEU TRP LEU GLY ARG PRO LEU GLN ALA PRO PRO ALA
SEQRES 5 A 282 ALA GLY TYR PRO VAL VAL TRP MET LEU ASP GLY ASN ALA
SEQRES 6 A 282 ALA VAL GLY ALA LEU ASP GLU SER THR LEU ARG ARG LEU
SEQRES 7 A 282 ALA ASP GLY ASP ALA PRO LEU LEU VAL ALA ILE GLY TYR
SEQRES 8 A 282 ARG THR PRO LEU ARG ILE ASP ARG ALA GLY ARG THR PHE
SEQRES 9 A 282 ASP TYR THR PRO ALA SER PRO GLY GLN ALA ASP GLN ARG
SEQRES 10 A 282 ASP PRO LEU ASN GLY LEU PRO SER GLY GLY ALA ASP ALA
SEQRES 11 A 282 PHE LEU ASP LEU LEU ARG ASP GLY MET ARG PRO ALA VAL
SEQRES 12 A 282 ALA ALA GLN ALA PRO LEU ASP THR ALA ARG GLN THR LEU
SEQRES 13 A 282 TRP GLY HIS SER TYR GLY GLY LEU LEU VAL LEU HIS ALA
SEQRES 14 A 282 LEU PHE THR ARG PRO GLY GLU PHE ALA ARG TYR ALA ALA
SEQRES 15 A 282 ALA SER PRO SER LEU TRP TRP ARG ASP GLY ALA ILE LEU
SEQRES 16 A 282 GLY GLU ARG ALA GLY LEU GLU GLN ARG LEU ARG GLY LYS
SEQRES 17 A 282 ARG ALA GLU LEU LEU LEU TRP ARG GLY SER ALA GLU PRO
SEQRES 18 A 282 ALA SER PRO ARG GLY SER LEU LYS ALA GLU PRO GLY GLN
SEQRES 19 A 282 ALA MET ALA ARG LEU VAL ASP ASP LEU ARG ARG VAL ALA
SEQRES 20 A 282 GLY LEU THR LEU ASP PHE GLN PRO LEU ASP GLY LEU GLY
SEQRES 21 A 282 HIS GLY GLU THR LEU GLY ALA SER LEU ARG LEU LEU LEU
SEQRES 22 A 282 ALA ARG PRO ALA VAL GLU ARG GLN ARG
SEQRES 1 B 282 GLY ALA MET ASN PRO ASP PRO GLU ALA THR MET ASP ARG
SEQRES 2 B 282 SER LEU LEU GLN ARG GLN ASP LEU PRO TYR ARG PHE SER
SEQRES 3 B 282 ALA VAL ASP LEU ASP SER VAL ASP GLY GLN ARG HIS TYR
SEQRES 4 B 282 ARG LEU TRP LEU GLY ARG PRO LEU GLN ALA PRO PRO ALA
SEQRES 5 B 282 ALA GLY TYR PRO VAL VAL TRP MET LEU ASP GLY ASN ALA
SEQRES 6 B 282 ALA VAL GLY ALA LEU ASP GLU SER THR LEU ARG ARG LEU
SEQRES 7 B 282 ALA ASP GLY ASP ALA PRO LEU LEU VAL ALA ILE GLY TYR
SEQRES 8 B 282 ARG THR PRO LEU ARG ILE ASP ARG ALA GLY ARG THR PHE
SEQRES 9 B 282 ASP TYR THR PRO ALA SER PRO GLY GLN ALA ASP GLN ARG
SEQRES 10 B 282 ASP PRO LEU ASN GLY LEU PRO SER GLY GLY ALA ASP ALA
SEQRES 11 B 282 PHE LEU ASP LEU LEU ARG ASP GLY MET ARG PRO ALA VAL
SEQRES 12 B 282 ALA ALA GLN ALA PRO LEU ASP THR ALA ARG GLN THR LEU
SEQRES 13 B 282 TRP GLY HIS SER TYR GLY GLY LEU LEU VAL LEU HIS ALA
SEQRES 14 B 282 LEU PHE THR ARG PRO GLY GLU PHE ALA ARG TYR ALA ALA
SEQRES 15 B 282 ALA SER PRO SER LEU TRP TRP ARG ASP GLY ALA ILE LEU
SEQRES 16 B 282 GLY GLU ARG ALA GLY LEU GLU GLN ARG LEU ARG GLY LYS
SEQRES 17 B 282 ARG ALA GLU LEU LEU LEU TRP ARG GLY SER ALA GLU PRO
SEQRES 18 B 282 ALA SER PRO ARG GLY SER LEU LYS ALA GLU PRO GLY GLN
SEQRES 19 B 282 ALA MET ALA ARG LEU VAL ASP ASP LEU ARG ARG VAL ALA
SEQRES 20 B 282 GLY LEU THR LEU ASP PHE GLN PRO LEU ASP GLY LEU GLY
SEQRES 21 B 282 HIS GLY GLU THR LEU GLY ALA SER LEU ARG LEU LEU LEU
SEQRES 22 B 282 ALA ARG PRO ALA VAL GLU ARG GLN ARG
HET NO3 A 301 4
HET NO3 A 302 4
HETNAM NO3 NITRATE ION
FORMUL 3 NO3 2(N O3 1-)
FORMUL 5 HOH *123(H2 O)
HELIX 1 AA1 ASP A 59 ALA A 66 1 8
HELIX 2 AA2 ASP A 68 ALA A 76 1 9
HELIX 3 AA3 ARG A 96 THR A 104 1 9
HELIX 4 AA4 GLY A 124 GLY A 135 1 12
HELIX 5 AA5 GLY A 135 ALA A 142 1 8
HELIX 6 AA6 SER A 157 ARG A 170 1 14
HELIX 7 AA7 TRP A 185 GLU A 194 1 10
HELIX 8 AA8 GLY A 197 ARG A 203 1 7
HELIX 9 AA9 GLY A 230 ARG A 241 1 12
HELIX 10 AB1 GLU A 260 ARG A 272 1 13
HELIX 11 AB2 ASP B 9 LEU B 13 5 5
HELIX 12 AB3 ASP B 59 ALA B 66 1 8
HELIX 13 AB4 ASP B 68 ALA B 76 1 9
HELIX 14 AB5 ASP B 95 TYR B 103 1 9
HELIX 15 AB6 GLY B 124 GLY B 135 1 12
HELIX 16 AB7 GLY B 135 ALA B 142 1 8
HELIX 17 AB8 SER B 157 ARG B 170 1 14
HELIX 18 AB9 TRP B 185 GLU B 194 1 10
HELIX 19 AC1 GLY B 197 LEU B 202 1 6
HELIX 20 AC2 GLY B 230 ARG B 241 1 12
HELIX 21 AC3 GLU B 260 ARG B 272 1 13
SHEET 1 AA1 8 TYR A 20 ASP A 28 0
SHEET 2 AA1 8 HIS A 35 PRO A 43 -1 O LEU A 40 N SER A 23
SHEET 3 AA1 8 LEU A 82 TYR A 88 -1 O ALA A 85 N TRP A 39
SHEET 4 AA1 8 TYR A 52 MET A 57 1 N MET A 57 O VAL A 84
SHEET 5 AA1 8 LEU A 146 HIS A 156 1 O THR A 152 N TRP A 56
SHEET 6 AA1 8 ARG A 176 ALA A 180 1 O ALA A 178 N LEU A 153
SHEET 7 AA1 8 ALA A 207 GLY A 214 1 O LEU A 210 N ALA A 179
SHEET 8 AA1 8 LEU A 246 LEU A 253 1 O THR A 247 N LEU A 209
SHEET 1 AA2 8 TYR B 20 ASP B 28 0
SHEET 2 AA2 8 HIS B 35 PRO B 43 -1 O LEU B 40 N SER B 23
SHEET 3 AA2 8 LEU B 82 TYR B 88 -1 O ALA B 85 N TRP B 39
SHEET 4 AA2 8 TYR B 52 MET B 57 1 N MET B 57 O ILE B 86
SHEET 5 AA2 8 LEU B 146 HIS B 156 1 O THR B 152 N TRP B 56
SHEET 6 AA2 8 ARG B 176 ALA B 180 1 O ALA B 178 N LEU B 153
SHEET 7 AA2 8 ALA B 207 GLY B 214 1 O GLU B 208 N TYR B 177
SHEET 8 AA2 8 LEU B 246 LEU B 253 1 O THR B 247 N LEU B 209
SITE 1 AC1 6 ALA A 264 ARG A 267 LEU A 268 ALA B 264
SITE 2 AC1 6 ARG B 267 LEU B 268
SITE 1 AC2 6 ASP A 59 GLY A 60 ASN A 61 ALA A 62
SITE 2 AC2 6 GLY A 87 TYR A 88
CRYST1 45.340 111.100 48.500 90.00 105.47 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 0.022056 0.000000 0.006104 0.00000
SCALE2 0.000000 0.009001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021394 0.00000
TER 1982 GLU A 276
TER 3978 VAL B 275
MASTER 601 0 2 21 16 0 4 6 4093 2 8 44
END |