HEADER TRANSLATION 07-NOV-18 6N0I
TITLE 2.60 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF ELONGATION FACTOR G 2
TITLE 2 FROM PSEUDOMONAS PUTIDA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR G 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: EF-G 2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA (STRAIN ATCC 47054 / DSM
SOURCE 3 6125 / NCIMB 11950 / KT2440);
SOURCE 4 ORGANISM_TAXID: 160488;
SOURCE 5 STRAIN: ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440;
SOURCE 6 GENE: FUSB, FUSA-2, PP_4111;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-MAGIC;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 2 DISEASES, CSGID, ELONGATION FACTOR G 2, TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,L.SHUVALOVA,Z.WAWRZAK,A.CARDONA-CORREA,W.F.ANDERSON,
AUTHOR 2 K.J.F.SATCHELL,A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF
AUTHOR 3 INFECTIOUS DISEASES (CSGID)
REVDAT 2 11-OCT-23 6N0I 1 REMARK
REVDAT 1 14-NOV-18 6N0I 0
JRNL AUTH G.MINASOV,L.SHUVALOVA,Z.WAWRZAK,A.CARDONA-CORREA,
JRNL AUTH 2 W.F.ANDERSON,K.J.F.SATCHELL,A.JOACHIMIAK,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL 2.60 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF ELONGATION
JRNL TITL 2 FACTOR G 2 FROM PSEUDOMONAS PUTIDA.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 41967
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2120
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3006
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3570
REMARK 3 BIN FREE R VALUE SET COUNT : 168
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10509
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.06000
REMARK 3 B22 (A**2) : 4.46000
REMARK 3 B33 (A**2) : -2.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.351
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.327
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.051
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10709 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 10097 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14456 ; 1.168 ; 1.646
REMARK 3 BOND ANGLES OTHERS (DEGREES): 23417 ; 0.292 ; 1.578
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1349 ; 1.478 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 581 ;12.598 ;22.151
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1903 ; 6.857 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ; 7.327 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1416 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12059 ; 0.053 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2205 ; 0.049 ; 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): 5408 ; 2.426 ; 4.484
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5407 ; 2.425 ; 4.484
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6753 ; 4.034 ; 6.724
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6754 ; 4.034 ; 6.725
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5301 ; 2.708 ; 4.811
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5302 ; 2.708 ; 4.812
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7704 ; 4.425 ; 7.086
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11585 ; 7.091 ;52.986
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 11582 ; 7.084 ;52.976
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 1 701 B 1 701 19278 0.14 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 1 A 137
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7976 -10.5613 23.0402
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: 0.1639
REMARK 3 T33: 0.1686 T12: -0.0747
REMARK 3 T13: -0.0156 T23: 0.1096
REMARK 3 L TENSOR
REMARK 3 L11: 3.8986 L22: 3.9651
REMARK 3 L33: 5.1171 L12: -0.3473
REMARK 3 L13: 0.7603 L23: 0.1617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0976 S12: 0.0365 S13: -0.0115
REMARK 3 S21: 0.5546 S22: -0.0507 S23: 0.1157
REMARK 3 S31: 0.3597 S32: -0.6868 S33: -0.0469
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 138 A 241
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1259 7.8342 30.3973
REMARK 3 T TENSOR
REMARK 3 T11: 0.6903 T22: 0.2776
REMARK 3 T33: 0.4987 T12: 0.0753
REMARK 3 T13: 0.0591 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 3.2507 L22: 3.6563
REMARK 3 L33: 3.9542 L12: 1.3408
REMARK 3 L13: -1.8237 L23: 0.3835
REMARK 3 S TENSOR
REMARK 3 S11: 0.4129 S12: -0.3285 S13: 0.5850
REMARK 3 S21: 0.7053 S22: 0.0612 S23: -0.1125
REMARK 3 S31: -0.7776 S32: -0.4106 S33: -0.4741
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 242 A 407
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0373 -16.2164 13.0465
REMARK 3 T TENSOR
REMARK 3 T11: 0.2300 T22: 0.3439
REMARK 3 T33: 0.1667 T12: -0.0718
REMARK 3 T13: -0.0598 T23: 0.1244
REMARK 3 L TENSOR
REMARK 3 L11: 2.3492 L22: 4.6716
REMARK 3 L33: 3.2255 L12: -0.5625
REMARK 3 L13: -1.3134 L23: 0.8521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0118 S12: 0.3718 S13: 0.1351
REMARK 3 S21: -0.2622 S22: -0.1130 S23: 0.3794
REMARK 3 S31: 0.1814 S32: -0.7296 S33: 0.1248
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 408 A 486
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2664 -41.4315 29.7704
REMARK 3 T TENSOR
REMARK 3 T11: 0.0194 T22: 0.0515
REMARK 3 T33: 0.1193 T12: -0.0139
REMARK 3 T13: -0.0194 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 8.7699 L22: 2.4075
REMARK 3 L33: 3.1425 L12: 0.0852
REMARK 3 L13: 1.3085 L23: 0.2415
REMARK 3 S TENSOR
REMARK 3 S11: 0.1285 S12: -0.0590 S13: -0.7228
REMARK 3 S21: -0.1770 S22: 0.1541 S23: -0.0020
REMARK 3 S31: 0.1114 S32: 0.0353 S33: -0.2826
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 487 A 608
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2956 -52.5087 11.0189
REMARK 3 T TENSOR
REMARK 3 T11: 0.1517 T22: 0.2116
REMARK 3 T33: 0.1537 T12: 0.0173
REMARK 3 T13: 0.0137 T23: -0.1511
REMARK 3 L TENSOR
REMARK 3 L11: 0.8457 L22: 4.0613
REMARK 3 L33: 7.3723 L12: -1.6091
REMARK 3 L13: -2.2916 L23: 4.3615
REMARK 3 S TENSOR
REMARK 3 S11: -0.1499 S12: -0.2471 S13: 0.1024
REMARK 3 S21: -0.0460 S22: 0.4033 S23: -0.1810
REMARK 3 S31: 0.4352 S32: 0.7123 S33: -0.2534
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 609 A 702
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3697 -29.1868 39.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0876 T22: 0.0907
REMARK 3 T33: 0.0502 T12: 0.0004
REMARK 3 T13: -0.0625 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 3.7488 L22: 3.2505
REMARK 3 L33: 6.5087 L12: -0.1969
REMARK 3 L13: 0.7826 L23: 1.4969
REMARK 3 S TENSOR
REMARK 3 S11: -0.2601 S12: 0.3524 S13: 0.1520
REMARK 3 S21: -0.0045 S22: 0.0693 S23: 0.0108
REMARK 3 S31: -0.4445 S32: -0.0916 S33: 0.1908
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 0 B 96
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4392 -9.0127 70.5608
REMARK 3 T TENSOR
REMARK 3 T11: 0.1804 T22: 0.2718
REMARK 3 T33: 0.2035 T12: 0.0358
REMARK 3 T13: 0.0433 T23: -0.1333
REMARK 3 L TENSOR
REMARK 3 L11: 3.8614 L22: 5.6622
REMARK 3 L33: 3.3771 L12: 1.6369
REMARK 3 L13: 0.0138 L23: -0.7620
REMARK 3 S TENSOR
REMARK 3 S11: -0.0283 S12: -0.0132 S13: -0.0540
REMARK 3 S21: -0.7110 S22: -0.0651 S23: -0.7214
REMARK 3 S31: -0.1546 S32: 0.0161 S33: 0.0934
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 97 B 297
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5289 4.3325 65.7534
REMARK 3 T TENSOR
REMARK 3 T11: 0.5218 T22: 0.3135
REMARK 3 T33: 0.2028 T12: 0.0117
REMARK 3 T13: -0.1239 T23: -0.1168
REMARK 3 L TENSOR
REMARK 3 L11: 0.9731 L22: 3.9657
REMARK 3 L33: 1.7292 L12: -0.2605
REMARK 3 L13: -0.1583 L23: -0.7031
REMARK 3 S TENSOR
REMARK 3 S11: -0.1027 S12: 0.1811 S13: 0.2825
REMARK 3 S21: -0.9305 S22: 0.0463 S23: 0.0820
REMARK 3 S31: -0.4357 S32: -0.2136 S33: 0.0564
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 298 B 409
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1923 -25.4490 80.1011
REMARK 3 T TENSOR
REMARK 3 T11: 0.0758 T22: 0.4110
REMARK 3 T33: 0.0561 T12: 0.0051
REMARK 3 T13: -0.0122 T23: -0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 3.7531 L22: 1.6963
REMARK 3 L33: 3.8013 L12: -0.0411
REMARK 3 L13: -1.3576 L23: 1.1115
REMARK 3 S TENSOR
REMARK 3 S11: -0.1218 S12: -0.5280 S13: -0.1392
REMARK 3 S21: 0.1696 S22: -0.0464 S23: 0.0108
REMARK 3 S31: 0.3744 S32: 0.3378 S33: 0.1682
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 410 B 491
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7933 -39.8443 58.2539
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.2026
REMARK 3 T33: 0.0335 T12: 0.0296
REMARK 3 T13: -0.0108 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 7.5382 L22: 1.7782
REMARK 3 L33: 2.1298 L12: 0.5402
REMARK 3 L13: 1.5962 L23: -0.8522
REMARK 3 S TENSOR
REMARK 3 S11: 0.0286 S12: -0.2226 S13: -0.4755
REMARK 3 S21: -0.0788 S22: 0.0803 S23: -0.0388
REMARK 3 S31: 0.2428 S32: -0.2299 S33: -0.1089
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 492 B 607
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2881 -50.9110 82.2838
REMARK 3 T TENSOR
REMARK 3 T11: 0.0645 T22: 0.5527
REMARK 3 T33: 0.1445 T12: 0.1503
REMARK 3 T13: 0.0077 T23: 0.1766
REMARK 3 L TENSOR
REMARK 3 L11: 2.4540 L22: 3.3581
REMARK 3 L33: 8.1190 L12: 0.2824
REMARK 3 L13: 1.2537 L23: -4.4988
REMARK 3 S TENSOR
REMARK 3 S11: -0.1717 S12: -0.0710 S13: 0.2806
REMARK 3 S21: 0.2575 S22: 0.4407 S23: 0.0933
REMARK 3 S31: -0.5038 S32: -1.0828 S33: -0.2690
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 608 B 701
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7331 -31.8734 49.8961
REMARK 3 T TENSOR
REMARK 3 T11: 0.0520 T22: 0.3051
REMARK 3 T33: 0.0864 T12: -0.0545
REMARK 3 T13: -0.0157 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 5.9007 L22: 2.6642
REMARK 3 L33: 5.0960 L12: -1.2742
REMARK 3 L13: 0.2990 L23: -1.7145
REMARK 3 S TENSOR
REMARK 3 S11: 0.1527 S12: -0.5042 S13: 0.2902
REMARK 3 S21: -0.2376 S22: 0.0986 S23: -0.0118
REMARK 3 S31: -0.0722 S32: 0.1531 S33: -0.2512
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 6N0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000237966.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 : BE
REMARK 200 OPTICS : C(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44241
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.80400
REMARK 200 R SYM FOR SHELL (I) : 0.80400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: 4FN5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 9.5 MG/ML, 0.01M TRIS HCL (PH
REMARK 280 8.3); SCREEN: PACT (C10), 0.2M MAGNESIUM CHLORIDE, 0.1M HEPES
REMARK 280 (PH 7.0), 20% (W/V) PEG 6000., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
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 39.98400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 ASN A 37
REMARK 465 HIS A 38
REMARK 465 LYS A 39
REMARK 465 MET A 40
REMARK 465 GLY A 41
REMARK 465 GLU A 42
REMARK 465 VAL A 43
REMARK 465 HIS A 44
REMARK 465 ASP A 45
REMARK 465 GLY A 46
REMARK 465 ALA A 47
REMARK 465 ALA A 48
REMARK 465 THR A 49
REMARK 465 MET A 50
REMARK 465 ASP A 51
REMARK 465 TRP A 52
REMARK 465 MET A 53
REMARK 465 ALA A 54
REMARK 465 GLN A 55
REMARK 465 GLU A 56
REMARK 465 GLN A 57
REMARK 465 GLU A 58
REMARK 465 ARG A 59
REMARK 465 GLY A 60
REMARK 465 ILE A 61
REMARK 465 THR A 62
REMARK 465 ILE A 63
REMARK 465 THR A 64
REMARK 465 GLU A 703
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 HIS B 38
REMARK 465 LYS B 39
REMARK 465 MET B 40
REMARK 465 GLY B 41
REMARK 465 GLU B 42
REMARK 465 VAL B 43
REMARK 465 HIS B 44
REMARK 465 ASP B 45
REMARK 465 GLY B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 THR B 49
REMARK 465 MET B 50
REMARK 465 ASP B 51
REMARK 465 TRP B 52
REMARK 465 MET B 53
REMARK 465 ALA B 54
REMARK 465 GLN B 55
REMARK 465 GLU B 56
REMARK 465 GLN B 57
REMARK 465 GLU B 58
REMARK 465 ARG B 59
REMARK 465 GLY B 60
REMARK 465 GLY B 702
REMARK 465 GLU B 703
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 HIS A 18 CB - CA - C ANGL. DEV. = 19.5 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 VAL A 19 126.23 -36.13
REMARK 500 ASP A 20 44.12 71.78
REMARK 500 ASP A 95 -59.98 -26.88
REMARK 500 HIS A 135 56.82 37.75
REMARK 500 GLU A 177 -135.94 58.82
REMARK 500 ASN A 273 62.41 62.80
REMARK 500 PRO A 290 -9.83 -56.07
REMARK 500 ARG A 372 75.32 -151.47
REMARK 500 MET A 410 -134.54 55.83
REMARK 500 ASP A 411 -8.95 62.79
REMARK 500 ARG A 496 -26.71 -142.74
REMARK 500 GLN A 508 34.71 -154.62
REMARK 500 SER A 509 93.47 -65.55
REMARK 500 ILE A 538 46.77 -99.81
REMARK 500 VAL A 563 -30.52 -140.29
REMARK 500 LEU A 564 -61.07 -93.81
REMARK 500 GLN A 604 -60.24 -90.07
REMARK 500 GLU A 623 -36.66 -39.99
REMARK 500 ARG A 636 30.29 -83.69
REMARK 500 PRO A 647 106.92 -47.60
REMARK 500 ALA A 693 -70.35 -41.47
REMARK 500 SER A 700 -47.34 -132.60
REMARK 500 ASP B 20 48.73 72.85
REMARK 500 HIS B 135 57.52 37.12
REMARK 500 GLU B 177 -136.05 58.24
REMARK 500 ASN B 273 62.20 62.61
REMARK 500 PRO B 290 -8.92 -56.28
REMARK 500 ASP B 411 -4.13 -55.65
REMARK 500 ASP B 451 104.06 -59.70
REMARK 500 GLU B 452 -19.34 -49.68
REMARK 500 ARG B 496 -25.13 -143.62
REMARK 500 SER B 509 5.74 -65.39
REMARK 500 ILE B 538 41.66 -100.71
REMARK 500 VAL B 563 -30.52 -139.40
REMARK 500 LEU B 564 -61.32 -94.18
REMARK 500 GLN B 604 -62.32 -91.54
REMARK 500 GLU B 623 -37.13 -39.30
REMARK 500 ARG B 636 30.32 -83.45
REMARK 500 ALA B 693 -70.27 -41.01
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 SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP07336 RELATED DB: TARGETTRACK
DBREF 6N0I A 1 703 UNP Q88FI4 EFG2_PSEPK 1 703
DBREF 6N0I B 1 703 UNP Q88FI4 EFG2_PSEPK 1 703
SEQADV 6N0I SER A -2 UNP Q88FI4 EXPRESSION TAG
SEQADV 6N0I ASN A -1 UNP Q88FI4 EXPRESSION TAG
SEQADV 6N0I ALA A 0 UNP Q88FI4 EXPRESSION TAG
SEQADV 6N0I SER B -2 UNP Q88FI4 EXPRESSION TAG
SEQADV 6N0I ASN B -1 UNP Q88FI4 EXPRESSION TAG
SEQADV 6N0I ALA B 0 UNP Q88FI4 EXPRESSION TAG
SEQRES 1 A 706 SER ASN ALA MET ALA ARG THR THR PRO ILE GLU LEU TYR
SEQRES 2 A 706 ARG ASN ILE GLY ILE VAL ALA HIS VAL ASP ALA GLY LYS
SEQRES 3 A 706 THR THR THR THR GLU ARG ILE LEU PHE TYR THR GLY VAL
SEQRES 4 A 706 ASN HIS LYS MET GLY GLU VAL HIS ASP GLY ALA ALA THR
SEQRES 5 A 706 MET ASP TRP MET ALA GLN GLU GLN GLU ARG GLY ILE THR
SEQRES 6 A 706 ILE THR SER ALA ALA THR THR ALA PHE TRP GLN GLY SER
SEQRES 7 A 706 THR LYS GLN PHE ALA HIS LYS TYR ARG PHE ASN ILE ILE
SEQRES 8 A 706 ASP THR PRO GLY HIS VAL ASP PHE THR ILE GLU VAL GLU
SEQRES 9 A 706 ARG SER LEU ARG VAL LEU ASP GLY ALA VAL VAL VAL PHE
SEQRES 10 A 706 SER GLY ALA ASP GLY VAL GLU PRO GLN SER GLU THR VAL
SEQRES 11 A 706 TRP ARG GLN ALA ASN LYS TYR HIS VAL PRO ARG LEU ALA
SEQRES 12 A 706 TYR ILE ASN LYS MET ASP ARG GLN GLY ALA ASP PHE LEU
SEQRES 13 A 706 ARG VAL VAL LYS GLN ILE ASP GLN ARG LEU GLY HIS HIS
SEQRES 14 A 706 PRO VAL PRO ILE GLN LEU ALA ILE GLY SER GLU GLU ASN
SEQRES 15 A 706 PHE MET GLY GLN ILE ASP LEU VAL LYS MET LYS ALA ILE
SEQRES 16 A 706 TYR TRP ASN ASP ALA ASP GLN GLY THR SER TYR ARG GLU
SEQRES 17 A 706 GLU GLU ILE PRO ALA GLU LEU LYS ALA LEU ALA ASP GLU
SEQRES 18 A 706 TRP ARG ALA HIS MET ILE GLU ALA ALA ALA GLU ALA ASN
SEQRES 19 A 706 ASP GLU LEU THR MET LYS PHE LEU ASP GLY GLU GLU LEU
SEQRES 20 A 706 SER ILE GLU GLU ILE LYS ALA GLY LEU ARG GLN ARG THR
SEQRES 21 A 706 ILE ALA ASN GLU ILE VAL PRO THR ILE LEU GLY SER SER
SEQRES 22 A 706 PHE LYS ASN LYS GLY VAL PRO LEU MET LEU ASP ALA VAL
SEQRES 23 A 706 ILE ASP TYR LEU PRO ALA PRO SER GLU ILE PRO ALA ILE
SEQRES 24 A 706 ARG GLY THR ASP PRO ASP ASP GLU GLU LYS HIS LEU GLU
SEQRES 25 A 706 ARG HIS ALA ASP ASP LYS GLU PRO PHE SER ALA LEU ALA
SEQRES 26 A 706 PHE LYS ILE ALA THR ASP PRO PHE VAL GLY THR LEU THR
SEQRES 27 A 706 PHE ALA ARG VAL TYR SER GLY VAL LEU SER SER GLY ASN
SEQRES 28 A 706 ALA VAL LEU ASN SER VAL LYS GLY LYS LYS GLU ARG ILE
SEQRES 29 A 706 GLY ARG MET VAL GLN MET HIS ALA ASN GLN ARG ALA GLU
SEQRES 30 A 706 ILE LYS ASP VAL CYS ALA GLY ASP ILE ALA ALA LEU ILE
SEQRES 31 A 706 GLY MET LYS ASP VAL THR THR GLY ASP THR LEU CYS ASP
SEQRES 32 A 706 MET ASP LYS PRO ILE ILE LEU GLU ARG MET ASP PHE PRO
SEQRES 33 A 706 ASP PRO VAL ILE SER VAL ALA VAL GLU PRO LYS THR LYS
SEQRES 34 A 706 ALA ASP GLN GLU LYS MET GLY ILE ALA LEU GLY LYS LEU
SEQRES 35 A 706 ALA GLN GLU ASP PRO SER PHE ARG VAL ARG THR ASP GLU
SEQRES 36 A 706 GLU THR GLY GLN THR ILE ILE SER GLY MET GLY GLU LEU
SEQRES 37 A 706 HIS LEU ASP ILE ILE VAL ASP ARG MET ARG ARG GLU PHE
SEQRES 38 A 706 ASN VAL GLU ALA ASN ILE GLY LYS PRO GLN VAL ALA TYR
SEQRES 39 A 706 ARG GLU LYS ILE ARG ASN THR CYS GLU ILE GLU GLY ARG
SEQRES 40 A 706 PHE VAL ARG GLN SER GLY GLY ARG GLY GLN TYR GLY HIS
SEQRES 41 A 706 CYS TRP ILE ARG PHE ALA PRO GLY ASP GLU GLY LYS GLU
SEQRES 42 A 706 GLY LEU GLU PHE ILE ASN GLU ILE VAL GLY GLY VAL VAL
SEQRES 43 A 706 PRO ARG GLU TYR ILE PRO ALA ILE GLN LYS GLY ILE GLU
SEQRES 44 A 706 GLU GLN MET LYS ASN GLY VAL LEU ALA GLY TYR PRO LEU
SEQRES 45 A 706 ILE ASN LEU LYS ALA ALA VAL PHE ASP GLY SER TYR HIS
SEQRES 46 A 706 ASP VAL ASP SER ASN GLU MET ALA TYR LYS ILE ALA ALA
SEQRES 47 A 706 SER MET ALA THR LYS GLN LEU SER GLN LYS GLY GLY ALA
SEQRES 48 A 706 VAL LEU LEU GLU PRO VAL MET LYS VAL GLU VAL VAL THR
SEQRES 49 A 706 PRO GLU GLU TYR GLN GLY ASP ILE LEU GLY ASP LEU SER
SEQRES 50 A 706 ARG ARG ARG GLY MET ILE GLN ASP GLY ASP GLU THR PRO
SEQRES 51 A 706 ALA GLY LYS VAL ILE ARG ALA GLU VAL PRO LEU GLY GLU
SEQRES 52 A 706 MET PHE GLY TYR ALA THR SER MET ARG SER MET THR GLN
SEQRES 53 A 706 GLY ARG ALA SER PHE SER MET GLU PHE THR ARG TYR ALA
SEQRES 54 A 706 GLU ALA PRO ALA SER ILE ALA ASP GLY ILE VAL LYS LYS
SEQRES 55 A 706 SER ARG GLY GLU
SEQRES 1 B 706 SER ASN ALA MET ALA ARG THR THR PRO ILE GLU LEU TYR
SEQRES 2 B 706 ARG ASN ILE GLY ILE VAL ALA HIS VAL ASP ALA GLY LYS
SEQRES 3 B 706 THR THR THR THR GLU ARG ILE LEU PHE TYR THR GLY VAL
SEQRES 4 B 706 ASN HIS LYS MET GLY GLU VAL HIS ASP GLY ALA ALA THR
SEQRES 5 B 706 MET ASP TRP MET ALA GLN GLU GLN GLU ARG GLY ILE THR
SEQRES 6 B 706 ILE THR SER ALA ALA THR THR ALA PHE TRP GLN GLY SER
SEQRES 7 B 706 THR LYS GLN PHE ALA HIS LYS TYR ARG PHE ASN ILE ILE
SEQRES 8 B 706 ASP THR PRO GLY HIS VAL ASP PHE THR ILE GLU VAL GLU
SEQRES 9 B 706 ARG SER LEU ARG VAL LEU ASP GLY ALA VAL VAL VAL PHE
SEQRES 10 B 706 SER GLY ALA ASP GLY VAL GLU PRO GLN SER GLU THR VAL
SEQRES 11 B 706 TRP ARG GLN ALA ASN LYS TYR HIS VAL PRO ARG LEU ALA
SEQRES 12 B 706 TYR ILE ASN LYS MET ASP ARG GLN GLY ALA ASP PHE LEU
SEQRES 13 B 706 ARG VAL VAL LYS GLN ILE ASP GLN ARG LEU GLY HIS HIS
SEQRES 14 B 706 PRO VAL PRO ILE GLN LEU ALA ILE GLY SER GLU GLU ASN
SEQRES 15 B 706 PHE MET GLY GLN ILE ASP LEU VAL LYS MET LYS ALA ILE
SEQRES 16 B 706 TYR TRP ASN ASP ALA ASP GLN GLY THR SER TYR ARG GLU
SEQRES 17 B 706 GLU GLU ILE PRO ALA GLU LEU LYS ALA LEU ALA ASP GLU
SEQRES 18 B 706 TRP ARG ALA HIS MET ILE GLU ALA ALA ALA GLU ALA ASN
SEQRES 19 B 706 ASP GLU LEU THR MET LYS PHE LEU ASP GLY GLU GLU LEU
SEQRES 20 B 706 SER ILE GLU GLU ILE LYS ALA GLY LEU ARG GLN ARG THR
SEQRES 21 B 706 ILE ALA ASN GLU ILE VAL PRO THR ILE LEU GLY SER SER
SEQRES 22 B 706 PHE LYS ASN LYS GLY VAL PRO LEU MET LEU ASP ALA VAL
SEQRES 23 B 706 ILE ASP TYR LEU PRO ALA PRO SER GLU ILE PRO ALA ILE
SEQRES 24 B 706 ARG GLY THR ASP PRO ASP ASP GLU GLU LYS HIS LEU GLU
SEQRES 25 B 706 ARG HIS ALA ASP ASP LYS GLU PRO PHE SER ALA LEU ALA
SEQRES 26 B 706 PHE LYS ILE ALA THR ASP PRO PHE VAL GLY THR LEU THR
SEQRES 27 B 706 PHE ALA ARG VAL TYR SER GLY VAL LEU SER SER GLY ASN
SEQRES 28 B 706 ALA VAL LEU ASN SER VAL LYS GLY LYS LYS GLU ARG ILE
SEQRES 29 B 706 GLY ARG MET VAL GLN MET HIS ALA ASN GLN ARG ALA GLU
SEQRES 30 B 706 ILE LYS ASP VAL CYS ALA GLY ASP ILE ALA ALA LEU ILE
SEQRES 31 B 706 GLY MET LYS ASP VAL THR THR GLY ASP THR LEU CYS ASP
SEQRES 32 B 706 MET ASP LYS PRO ILE ILE LEU GLU ARG MET ASP PHE PRO
SEQRES 33 B 706 ASP PRO VAL ILE SER VAL ALA VAL GLU PRO LYS THR LYS
SEQRES 34 B 706 ALA ASP GLN GLU LYS MET GLY ILE ALA LEU GLY LYS LEU
SEQRES 35 B 706 ALA GLN GLU ASP PRO SER PHE ARG VAL ARG THR ASP GLU
SEQRES 36 B 706 GLU THR GLY GLN THR ILE ILE SER GLY MET GLY GLU LEU
SEQRES 37 B 706 HIS LEU ASP ILE ILE VAL ASP ARG MET ARG ARG GLU PHE
SEQRES 38 B 706 ASN VAL GLU ALA ASN ILE GLY LYS PRO GLN VAL ALA TYR
SEQRES 39 B 706 ARG GLU LYS ILE ARG ASN THR CYS GLU ILE GLU GLY ARG
SEQRES 40 B 706 PHE VAL ARG GLN SER GLY GLY ARG GLY GLN TYR GLY HIS
SEQRES 41 B 706 CYS TRP ILE ARG PHE ALA PRO GLY ASP GLU GLY LYS GLU
SEQRES 42 B 706 GLY LEU GLU PHE ILE ASN GLU ILE VAL GLY GLY VAL VAL
SEQRES 43 B 706 PRO ARG GLU TYR ILE PRO ALA ILE GLN LYS GLY ILE GLU
SEQRES 44 B 706 GLU GLN MET LYS ASN GLY VAL LEU ALA GLY TYR PRO LEU
SEQRES 45 B 706 ILE ASN LEU LYS ALA ALA VAL PHE ASP GLY SER TYR HIS
SEQRES 46 B 706 ASP VAL ASP SER ASN GLU MET ALA TYR LYS ILE ALA ALA
SEQRES 47 B 706 SER MET ALA THR LYS GLN LEU SER GLN LYS GLY GLY ALA
SEQRES 48 B 706 VAL LEU LEU GLU PRO VAL MET LYS VAL GLU VAL VAL THR
SEQRES 49 B 706 PRO GLU GLU TYR GLN GLY ASP ILE LEU GLY ASP LEU SER
SEQRES 50 B 706 ARG ARG ARG GLY MET ILE GLN ASP GLY ASP GLU THR PRO
SEQRES 51 B 706 ALA GLY LYS VAL ILE ARG ALA GLU VAL PRO LEU GLY GLU
SEQRES 52 B 706 MET PHE GLY TYR ALA THR SER MET ARG SER MET THR GLN
SEQRES 53 B 706 GLY ARG ALA SER PHE SER MET GLU PHE THR ARG TYR ALA
SEQRES 54 B 706 GLU ALA PRO ALA SER ILE ALA ASP GLY ILE VAL LYS LYS
SEQRES 55 B 706 SER ARG GLY GLU
HET SO4 A 801 5
HET SO4 B 801 5
HET PEG B 802 7
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 PEG C4 H10 O3
FORMUL 6 HOH *116(H2 O)
HELIX 1 AA1 PRO A 6 GLU A 8 5 3
HELIX 2 AA2 GLY A 22 VAL A 36 1 15
HELIX 3 AA3 PHE A 96 LEU A 107 1 12
HELIX 4 AA4 GLU A 121 TYR A 134 1 14
HELIX 5 AA5 ASP A 151 ARG A 162 1 12
HELIX 6 AA6 SER A 176 PHE A 180 5 5
HELIX 7 AA7 ASP A 196 GLN A 199 5 4
HELIX 8 AA8 PRO A 209 GLU A 229 1 21
HELIX 9 AA9 ASN A 231 ASP A 240 1 10
HELIX 10 AB1 SER A 245 ALA A 259 1 15
HELIX 11 AB2 GLY A 275 LEU A 287 1 13
HELIX 12 AB3 THR A 425 ASP A 443 1 19
HELIX 13 AB4 GLY A 463 GLU A 477 1 15
HELIX 14 AB5 PRO A 544 GLU A 546 5 3
HELIX 15 AB6 TYR A 547 GLY A 562 1 16
HELIX 16 AB7 ASN A 587 GLN A 601 1 15
HELIX 17 AB8 GLN A 601 GLY A 606 1 6
HELIX 18 AB9 PRO A 622 GLU A 624 5 3
HELIX 19 AC1 TYR A 625 ARG A 636 1 12
HELIX 20 AC2 GLY A 659 MET A 661 5 3
HELIX 21 AC3 GLY A 663 GLN A 673 1 11
HELIX 22 AC4 PRO A 689 LYS A 698 1 10
HELIX 23 AC5 PRO B 6 GLU B 8 5 3
HELIX 24 AC6 GLY B 22 ASN B 37 1 16
HELIX 25 AC7 THR B 97 LEU B 107 1 11
HELIX 26 AC8 GLU B 121 TYR B 134 1 14
HELIX 27 AC9 ASP B 151 ARG B 162 1 12
HELIX 28 AD1 SER B 176 PHE B 180 5 5
HELIX 29 AD2 ASP B 196 GLN B 199 5 4
HELIX 30 AD3 PRO B 209 GLU B 229 1 21
HELIX 31 AD4 ASN B 231 ASP B 240 1 10
HELIX 32 AD5 SER B 245 ALA B 259 1 15
HELIX 33 AD6 GLY B 275 LEU B 287 1 13
HELIX 34 AD7 THR B 425 ALA B 427 5 3
HELIX 35 AD8 ASP B 428 ASP B 443 1 16
HELIX 36 AD9 GLY B 463 GLU B 477 1 15
HELIX 37 AE1 PRO B 544 GLU B 546 5 3
HELIX 38 AE2 TYR B 547 GLY B 562 1 16
HELIX 39 AE3 ASN B 587 GLN B 601 1 15
HELIX 40 AE4 LEU B 602 GLN B 604 5 3
HELIX 41 AE5 PRO B 622 GLU B 624 5 3
HELIX 42 AE6 TYR B 625 ARG B 636 1 12
HELIX 43 AE7 GLY B 659 MET B 661 5 3
HELIX 44 AE8 GLY B 663 GLN B 673 1 11
HELIX 45 AE9 PRO B 689 ARG B 701 1 13
SHEET 1 AA1 7 ALA A 67 TRP A 72 0
SHEET 2 AA1 7 TYR A 83 ILE A 88 -1 O PHE A 85 N ALA A 70
SHEET 3 AA1 7 TYR A 10 ALA A 17 1 N ILE A 13 O ILE A 88
SHEET 4 AA1 7 GLY A 109 SER A 115 1 O VAL A 113 N VAL A 16
SHEET 5 AA1 7 ARG A 138 ASN A 143 1 O TYR A 141 N VAL A 112
SHEET 6 AA1 7 VAL A 263 LEU A 267 1 O ILE A 266 N ALA A 140
SHEET 7 AA1 7 PRO A 167 PRO A 169 1 N VAL A 168 O VAL A 263
SHEET 1 AA2 4 GLN A 171 ILE A 174 0
SHEET 2 AA2 4 GLY A 182 ASP A 185 -1 O GLY A 182 N ILE A 174
SHEET 3 AA2 4 ALA A 191 TRP A 194 -1 O ILE A 192 N GLN A 183
SHEET 4 AA2 4 TYR A 203 GLU A 206 -1 O ARG A 204 N TYR A 193
SHEET 1 AA3 2 ILE A 296 ASP A 300 0
SHEET 2 AA3 2 ASP A 303 ARG A 310 -1 O LEU A 308 N GLY A 298
SHEET 1 AA4 8 LYS A 358 ARG A 360 0
SHEET 2 AA4 8 ALA A 349 ASN A 352 -1 N VAL A 350 O GLU A 359
SHEET 3 AA4 8 THR A 397 CYS A 399 -1 O CYS A 399 N LEU A 351
SHEET 4 AA4 8 SER A 319 ASP A 328 -1 N ALA A 320 O LEU A 398
SHEET 5 AA4 8 GLY A 332 SER A 341 -1 O LEU A 334 N ALA A 326
SHEET 6 AA4 8 ILE A 383 ILE A 387 -1 O ALA A 384 N ALA A 337
SHEET 7 AA4 8 MET A 364 MET A 367 -1 N VAL A 365 O ALA A 385
SHEET 8 AA4 8 ARG A 372 ILE A 375 -1 O ALA A 373 N GLN A 366
SHEET 1 AA5 2 VAL A 343 SER A 345 0
SHEET 2 AA5 2 ASP A 377 CYS A 379 -1 O VAL A 378 N LEU A 344
SHEET 1 AA6 4 ARG A 447 THR A 450 0
SHEET 2 AA6 4 THR A 457 GLY A 461 -1 O ILE A 458 N ARG A 449
SHEET 3 AA6 4 ILE A 417 PRO A 423 -1 N VAL A 421 O THR A 457
SHEET 4 AA6 4 ALA A 482 ILE A 484 -1 O ASN A 483 N GLU A 422
SHEET 1 AA7 4 ARG A 447 THR A 450 0
SHEET 2 AA7 4 THR A 457 GLY A 461 -1 O ILE A 458 N ARG A 449
SHEET 3 AA7 4 ILE A 417 PRO A 423 -1 N VAL A 421 O THR A 457
SHEET 4 AA7 4 GLN A 488 VAL A 489 -1 O GLN A 488 N SER A 418
SHEET 1 AA8 4 ARG A 492 LYS A 494 0
SHEET 2 AA8 4 VAL A 609 THR A 621 -1 O LEU A 611 N ARG A 492
SHEET 3 AA8 4 GLY A 649 PRO A 657 -1 O ILE A 652 N VAL A 619
SHEET 4 AA8 4 ASP A 644 THR A 646 -1 N ASP A 644 O VAL A 651
SHEET 1 AA9 4 MET A 639 ILE A 640 0
SHEET 2 AA9 4 GLY A 649 PRO A 657 -1 O GLU A 655 N MET A 639
SHEET 3 AA9 4 VAL A 609 THR A 621 -1 N VAL A 619 O ILE A 652
SHEET 4 AA9 4 SER A 677 GLU A 687 -1 O ARG A 684 N VAL A 614
SHEET 1 AB1 4 CYS A 499 ARG A 507 0
SHEET 2 AB1 4 GLN A 514 ALA A 523 -1 O GLN A 514 N ARG A 507
SHEET 3 AB1 4 ASN A 571 GLY A 579 -1 O ALA A 575 N ARG A 521
SHEET 4 AB1 4 GLY A 531 ASN A 536 1 N GLU A 533 O LEU A 572
SHEET 1 AB2 7 ALA B 67 TRP B 72 0
SHEET 2 AB2 7 TYR B 83 ILE B 88 -1 O PHE B 85 N ALA B 70
SHEET 3 AB2 7 TYR B 10 ALA B 17 1 N ILE B 13 O ILE B 88
SHEET 4 AB2 7 GLY B 109 SER B 115 1 O VAL B 113 N VAL B 16
SHEET 5 AB2 7 ARG B 138 ASN B 143 1 O TYR B 141 N VAL B 112
SHEET 6 AB2 7 VAL B 263 LEU B 267 1 O ILE B 266 N ALA B 140
SHEET 7 AB2 7 PRO B 167 PRO B 169 1 N VAL B 168 O VAL B 263
SHEET 1 AB3 4 GLN B 171 ILE B 174 0
SHEET 2 AB3 4 GLY B 182 ASP B 185 -1 O GLY B 182 N ILE B 174
SHEET 3 AB3 4 ALA B 191 TRP B 194 -1 O ILE B 192 N GLN B 183
SHEET 4 AB3 4 TYR B 203 GLU B 206 -1 O ARG B 204 N TYR B 193
SHEET 1 AB4 2 ILE B 296 ASP B 300 0
SHEET 2 AB4 2 ASP B 303 ARG B 310 -1 O LEU B 308 N GLY B 298
SHEET 1 AB5 8 LYS B 358 ARG B 360 0
SHEET 2 AB5 8 ALA B 349 ASN B 352 -1 N VAL B 350 O GLU B 359
SHEET 3 AB5 8 THR B 397 CYS B 399 -1 O CYS B 399 N LEU B 351
SHEET 4 AB5 8 SER B 319 ALA B 326 -1 N ALA B 320 O LEU B 398
SHEET 5 AB5 8 LEU B 334 SER B 341 -1 O PHE B 336 N LYS B 324
SHEET 6 AB5 8 ILE B 383 ILE B 387 -1 O LEU B 386 N THR B 335
SHEET 7 AB5 8 MET B 364 MET B 367 -1 N VAL B 365 O ALA B 385
SHEET 8 AB5 8 ARG B 372 ILE B 375 -1 O ALA B 373 N GLN B 366
SHEET 1 AB6 2 VAL B 343 SER B 345 0
SHEET 2 AB6 2 ASP B 377 CYS B 379 -1 O VAL B 378 N LEU B 344
SHEET 1 AB7 4 ARG B 447 THR B 450 0
SHEET 2 AB7 4 THR B 457 GLY B 461 -1 O ILE B 458 N ARG B 449
SHEET 3 AB7 4 ILE B 417 PRO B 423 -1 N VAL B 421 O THR B 457
SHEET 4 AB7 4 ALA B 482 ILE B 484 -1 O ASN B 483 N GLU B 422
SHEET 1 AB8 4 ARG B 447 THR B 450 0
SHEET 2 AB8 4 THR B 457 GLY B 461 -1 O ILE B 458 N ARG B 449
SHEET 3 AB8 4 ILE B 417 PRO B 423 -1 N VAL B 421 O THR B 457
SHEET 4 AB8 4 GLN B 488 VAL B 489 -1 O GLN B 488 N SER B 418
SHEET 1 AB9 4 ARG B 492 LYS B 494 0
SHEET 2 AB9 4 VAL B 609 THR B 621 -1 O LEU B 611 N ARG B 492
SHEET 3 AB9 4 GLY B 649 PRO B 657 -1 O VAL B 656 N MET B 615
SHEET 4 AB9 4 ASP B 644 THR B 646 -1 N THR B 646 O GLY B 649
SHEET 1 AC1 4 MET B 639 ILE B 640 0
SHEET 2 AC1 4 GLY B 649 PRO B 657 -1 O GLU B 655 N MET B 639
SHEET 3 AC1 4 VAL B 609 THR B 621 -1 N MET B 615 O VAL B 656
SHEET 4 AC1 4 SER B 677 GLU B 687 -1 O ARG B 684 N VAL B 614
SHEET 1 AC2 4 CYS B 499 GLN B 508 0
SHEET 2 AC2 4 GLY B 513 ALA B 523 -1 O GLN B 514 N ARG B 507
SHEET 3 AC2 4 ASN B 571 GLY B 579 -1 O ALA B 575 N ARG B 521
SHEET 4 AC2 4 GLY B 531 ASN B 536 1 N GLU B 533 O LEU B 572
SITE 1 AC1 2 GLU A 229 GLU A 261
SITE 1 AC2 3 GLU B 229 ALA B 230 GLU B 261
SITE 1 AC3 2 GLU B 316 LYS B 403
CRYST1 49.434 79.968 183.516 90.00 94.21 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 0.020229 0.000000 0.001489 0.00000
SCALE2 0.000000 0.012505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005464 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
