HEADER HYDROLASE 04-OCT-09 3K3S
TITLE CRYSTAL STRUCTURE OF ALTRONATE HYDROLASE (FRAGMENT 1-84) FROM SHIGELLA
TITLE 2 FLEXNERI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALTRONATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: RESIDUES 1-84;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI 2A STR. 2457T;
SOURCE 3 ORGANISM_TAXID: 198215;
SOURCE 4 GENE: S3338, SF3131, UXAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS ALTRONATE HYDROLASE, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HOU,M.CHRUSZCZ,X.XU,B.LE,M.D.ZIMMERMAN,A.SAVCHENKO,A.M.EDWARDS,
AUTHOR 2 A.JOACHIMIAK,W.MINOR,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 4 13-APR-22 3K3S 1 AUTHOR JRNL REMARK LINK
REVDAT 3 29-APR-15 3K3S 1 HETSYN
REVDAT 2 13-JUL-11 3K3S 1 VERSN
REVDAT 1 27-OCT-09 3K3S 0
JRNL AUTH J.HOU,M.CHRUSZCZ,X.XU,B.LE,M.D.ZIMMERMAN,A.SAVCHENKO,
JRNL AUTH 2 A.M.EDWARDS,A.JOACHIMIAK,W.MINOR
JRNL TITL CRYSTAL STRUCTURE OF ALTRONATE HYDROLASE (FRAGMENT 1-84)
JRNL TITL 2 FROM SHIGELLA FLEXNERI.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 58766
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2965
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4081
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 210
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5077
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 613
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 32.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.70000
REMARK 3 B22 (A**2) : 1.44000
REMARK 3 B33 (A**2) : -1.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.96000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.159
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.799
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5202 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3197 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7068 ; 1.514 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7866 ; 0.870 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 675 ; 6.986 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 229 ;34.157 ;24.672
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 821 ;13.712 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;19.880 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 849 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5934 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 983 ; 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): 3375 ; 0.695 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1401 ; 0.203 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5354 ; 1.252 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1827 ; 2.170 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1714 ; 3.370 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 84 4
REMARK 3 1 B 1 B 84 4
REMARK 3 1 C 1 C 84 4
REMARK 3 1 D 1 D 84 4
REMARK 3 1 E 1 E 84 4
REMARK 3 1 F 1 F 84 4
REMARK 3 1 G 1 G 84 4
REMARK 3 1 H 1 H 84 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 959 ; 0.64 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 959 ; 0.61 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 959 ; 0.75 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 959 ; 0.65 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 E (A): 959 ; 0.58 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 F (A): 959 ; 0.96 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 G (A): 959 ; 0.81 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 H (A): 959 ; 1.10 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 959 ; 0.99 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 959 ; 0.97 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 959 ; 0.76 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 959 ; 0.82 ; 2.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 959 ; 0.75 ; 2.00
REMARK 3 MEDIUM THERMAL 1 F (A**2): 959 ; 0.73 ; 2.00
REMARK 3 MEDIUM THERMAL 1 G (A**2): 959 ; 0.80 ; 2.00
REMARK 3 MEDIUM THERMAL 1 H (A**2): 959 ; 0.81 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 35
REMARK 3 ORIGIN FOR THE GROUP (A): -26.9830 -2.2510 62.2860
REMARK 3 T TENSOR
REMARK 3 T11: 0.0626 T22: 0.1689
REMARK 3 T33: 0.0382 T12: 0.0591
REMARK 3 T13: 0.0389 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 2.3719 L22: 1.9806
REMARK 3 L33: 2.4812 L12: -0.4621
REMARK 3 L13: -0.1164 L23: 0.5439
REMARK 3 S TENSOR
REMARK 3 S11: -0.2038 S12: -0.3846 S13: -0.1420
REMARK 3 S21: 0.1163 S22: 0.1652 S23: 0.1574
REMARK 3 S31: 0.2420 S32: 0.3041 S33: 0.0386
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 36 A 84
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9890 3.0090 51.2600
REMARK 3 T TENSOR
REMARK 3 T11: 0.0489 T22: 0.0609
REMARK 3 T33: 0.0211 T12: -0.0059
REMARK 3 T13: 0.0147 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 3.1459 L22: 0.9664
REMARK 3 L33: 2.3975 L12: 0.0304
REMARK 3 L13: -1.6135 L23: 0.7023
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: -0.0860 S13: 0.1471
REMARK 3 S21: -0.1172 S22: 0.0690 S23: 0.0367
REMARK 3 S31: -0.1337 S32: 0.1551 S33: -0.0494
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 : B 0 B 35
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6620 -15.0850 32.2620
REMARK 3 T TENSOR
REMARK 3 T11: 0.3615 T22: 0.0513
REMARK 3 T33: 0.1226 T12: -0.0069
REMARK 3 T13: 0.1182 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.5878 L22: 0.9479
REMARK 3 L33: 8.5505 L12: 0.6860
REMARK 3 L13: -0.7540 L23: 1.2953
REMARK 3 S TENSOR
REMARK 3 S11: -0.2339 S12: -0.0617 S13: -0.5178
REMARK 3 S21: 0.0412 S22: -0.0943 S23: -0.1342
REMARK 3 S31: 1.3706 S32: -0.0992 S33: 0.3282
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 : B 36 B 84
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4070 -5.7810 32.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1163 T22: 0.0668
REMARK 3 T33: 0.0285 T12: -0.0505
REMARK 3 T13: 0.0410 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 2.0951 L22: 1.3039
REMARK 3 L33: 3.2017 L12: -0.5007
REMARK 3 L13: -1.2051 L23: 0.1251
REMARK 3 S TENSOR
REMARK 3 S11: -0.1455 S12: 0.1123 S13: -0.0257
REMARK 3 S21: -0.1381 S22: -0.0181 S23: 0.0309
REMARK 3 S31: 0.2530 S32: -0.1907 S33: 0.1636
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 : C 0 C 35
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6450 -4.6770 46.4130
REMARK 3 T TENSOR
REMARK 3 T11: 0.0628 T22: 0.1700
REMARK 3 T33: 0.1866 T12: 0.0139
REMARK 3 T13: 0.0262 T23: 0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 3.8912 L22: 1.1425
REMARK 3 L33: 2.7895 L12: 0.2016
REMARK 3 L13: 0.4482 L23: -0.0819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: 0.6852 S13: 0.1234
REMARK 3 S21: -0.2343 S22: -0.0474 S23: -0.1332
REMARK 3 S31: 0.0180 S32: 0.1612 S33: 0.0660
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 : C 36 C 84
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9080 -3.3730 55.3460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0384 T22: 0.0467
REMARK 3 T33: 0.2358 T12: 0.0219
REMARK 3 T13: 0.0281 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 4.6813 L22: 1.9012
REMARK 3 L33: 3.3545 L12: 2.4809
REMARK 3 L13: -0.8064 L23: -0.8452
REMARK 3 S TENSOR
REMARK 3 S11: 0.0258 S12: 0.2075 S13: 0.5872
REMARK 3 S21: 0.0195 S22: 0.1230 S23: 0.1636
REMARK 3 S31: -0.2574 S32: -0.2210 S33: -0.1488
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 : D 0 D 35
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7210 -9.5520 45.9790
REMARK 3 T TENSOR
REMARK 3 T11: 0.1326 T22: 0.1330
REMARK 3 T33: 0.4464 T12: -0.0803
REMARK 3 T13: 0.0347 T23: -0.1677
REMARK 3 L TENSOR
REMARK 3 L11: 7.0298 L22: 2.2126
REMARK 3 L33: 6.5570 L12: -2.1439
REMARK 3 L13: -2.7490 L23: 2.7028
REMARK 3 S TENSOR
REMARK 3 S11: -0.2442 S12: 0.7496 S13: -1.4331
REMARK 3 S21: 0.0481 S22: -0.3436 S23: 0.6915
REMARK 3 S31: 0.6499 S32: -0.6738 S33: 0.5878
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 : D 36 D 84
REMARK 3 ORIGIN FOR THE GROUP (A): -44.4330 2.8620 46.2880
REMARK 3 T TENSOR
REMARK 3 T11: 0.0407 T22: 0.1248
REMARK 3 T33: 0.1046 T12: -0.0048
REMARK 3 T13: -0.0045 T23: -0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 4.1084 L22: 2.2825
REMARK 3 L33: 0.6172 L12: -1.9375
REMARK 3 L13: -0.5480 L23: 0.2982
REMARK 3 S TENSOR
REMARK 3 S11: 0.1128 S12: 0.5278 S13: -0.0477
REMARK 3 S21: -0.2394 S22: -0.1854 S23: 0.1041
REMARK 3 S31: -0.0744 S32: -0.1052 S33: 0.0726
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 : E 0 E 35
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1430 3.2990 41.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1105 T22: 0.2471
REMARK 3 T33: 0.0619 T12: -0.0075
REMARK 3 T13: 0.0209 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 4.0702 L22: 4.8253
REMARK 3 L33: 5.1195 L12: -0.8878
REMARK 3 L13: -2.9594 L23: 3.2748
REMARK 3 S TENSOR
REMARK 3 S11: 0.0504 S12: -0.6200 S13: 0.1184
REMARK 3 S21: 0.2383 S22: 0.1909 S23: -0.4479
REMARK 3 S31: 0.1945 S32: 0.8084 S33: -0.2412
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 : E 36 E 84
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8610 7.3070 30.4030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1793 T22: 0.1128
REMARK 3 T33: 0.0943 T12: -0.0151
REMARK 3 T13: 0.0723 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 1.4116 L22: 1.1638
REMARK 3 L33: 5.4359 L12: -0.1710
REMARK 3 L13: -1.9430 L23: 0.4713
REMARK 3 S TENSOR
REMARK 3 S11: 0.1546 S12: 0.0879 S13: 0.2334
REMARK 3 S21: -0.2305 S22: 0.0138 S23: 0.0387
REMARK 3 S31: -0.4418 S32: 0.0382 S33: -0.1684
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 : F 0 F 35
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7490 -1.7390 0.8110
REMARK 3 T TENSOR
REMARK 3 T11: 0.1873 T22: 0.2748
REMARK 3 T33: 0.1040 T12: 0.0323
REMARK 3 T13: 0.0354 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 4.1584 L22: 2.3659
REMARK 3 L33: 3.5538 L12: -0.8803
REMARK 3 L13: -0.0728 L23: -0.4631
REMARK 3 S TENSOR
REMARK 3 S11: 0.1270 S12: 0.6418 S13: 0.0148
REMARK 3 S21: -0.1988 S22: -0.1117 S23: 0.3761
REMARK 3 S31: -0.0900 S32: -0.5544 S33: -0.0153
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 : F 36 F 84
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9980 0.1780 12.8120
REMARK 3 T TENSOR
REMARK 3 T11: 0.2151 T22: 0.1701
REMARK 3 T33: 0.0924 T12: -0.0071
REMARK 3 T13: 0.0731 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 3.7956 L22: 1.6069
REMARK 3 L33: 6.6335 L12: -0.6274
REMARK 3 L13: -0.9699 L23: -1.2375
REMARK 3 S TENSOR
REMARK 3 S11: 0.1892 S12: 0.0497 S13: 0.3666
REMARK 3 S21: 0.1920 S22: -0.1348 S23: 0.1580
REMARK 3 S31: -0.4397 S32: -0.4138 S33: -0.0544
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 : G 0 G 35
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7380 0.4710 6.9350
REMARK 3 T TENSOR
REMARK 3 T11: 0.1666 T22: 0.1840
REMARK 3 T33: 0.0618 T12: 0.0149
REMARK 3 T13: 0.0797 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.9146 L22: 2.2625
REMARK 3 L33: 4.4264 L12: 0.3919
REMARK 3 L13: 2.1066 L23: -0.5956
REMARK 3 S TENSOR
REMARK 3 S11: 0.0654 S12: 0.3130 S13: -0.1500
REMARK 3 S21: -0.1912 S22: 0.0030 S23: -0.2454
REMARK 3 S31: 0.1857 S32: 0.6359 S33: -0.0683
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 : G 36 G 84
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7380 10.7440 9.7120
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.1305
REMARK 3 T33: 0.0534 T12: 0.0009
REMARK 3 T13: 0.0689 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.5642 L22: 3.0585
REMARK 3 L33: 2.7131 L12: 0.4477
REMARK 3 L13: 0.2717 L23: -0.3880
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: -0.0462 S13: 0.1113
REMARK 3 S21: 0.1508 S22: -0.0565 S23: 0.1802
REMARK 3 S31: -0.1894 S32: -0.0933 S33: 0.0449
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 : H 0 H 35
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2470 -2.5620 69.3020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0636 T22: 0.1461
REMARK 3 T33: 0.2238 T12: -0.0090
REMARK 3 T13: -0.0200 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 1.1254 L22: 2.2955
REMARK 3 L33: 3.1747 L12: 0.7385
REMARK 3 L13: -0.0028 L23: -0.4098
REMARK 3 S TENSOR
REMARK 3 S11: 0.1033 S12: -0.3060 S13: -0.1266
REMARK 3 S21: 0.2418 S22: -0.1373 S23: -0.3578
REMARK 3 S31: 0.1383 S32: 0.2980 S33: 0.0340
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 : H 36 H 84
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6690 7.9730 66.5360
REMARK 3 T TENSOR
REMARK 3 T11: 0.0391 T22: 0.0809
REMARK 3 T33: 0.2306 T12: 0.0212
REMARK 3 T13: 0.0304 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.9446 L22: 3.3276
REMARK 3 L33: 1.4216 L12: 1.7820
REMARK 3 L13: 0.2311 L23: -0.1999
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: -0.0629 S13: 0.3005
REMARK 3 S21: 0.1288 S22: 0.0113 S23: 0.4080
REMARK 3 S31: -0.1709 S32: -0.2250 S33: -0.0655
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 4
REMARK 4 3K3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055509.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SI-111 CHANNEL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1840
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53500
REMARK 200 R SYM FOR SHELL (I) : 0.53500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, SHELXD, DM, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH=7.0, 5% TACSIMATE
REMARK 280 PH=7.0, 10% PEG 5K MME, VAPOR DIFFUSION, TEMPERATURE 293K, PH 7.0
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 20.10900
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, 3, 4
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: 1780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: 3
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: 1520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H
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: 4
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: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G
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 MSE A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 MSE B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 MSE C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 ARG C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 GLN C -1
REMARK 465 MSE D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 ARG D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 GLN D -1
REMARK 465 MSE E -20
REMARK 465 GLY E -19
REMARK 465 SER E -18
REMARK 465 SER E -17
REMARK 465 HIS E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 SER E -10
REMARK 465 SER E -9
REMARK 465 GLY E -8
REMARK 465 ARG E -7
REMARK 465 GLU E -6
REMARK 465 ASN E -5
REMARK 465 LEU E -4
REMARK 465 TYR E -3
REMARK 465 PHE E -2
REMARK 465 GLN E -1
REMARK 465 MSE F -20
REMARK 465 GLY F -19
REMARK 465 SER F -18
REMARK 465 SER F -17
REMARK 465 HIS F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 SER F -10
REMARK 465 SER F -9
REMARK 465 GLY F -8
REMARK 465 ARG F -7
REMARK 465 GLU F -6
REMARK 465 ASN F -5
REMARK 465 LEU F -4
REMARK 465 TYR F -3
REMARK 465 PHE F -2
REMARK 465 GLN F -1
REMARK 465 MSE G -20
REMARK 465 GLY G -19
REMARK 465 SER G -18
REMARK 465 SER G -17
REMARK 465 HIS G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 HIS G -13
REMARK 465 HIS G -12
REMARK 465 HIS G -11
REMARK 465 SER G -10
REMARK 465 SER G -9
REMARK 465 GLY G -8
REMARK 465 ARG G -7
REMARK 465 GLU G -6
REMARK 465 ASN G -5
REMARK 465 LEU G -4
REMARK 465 TYR G -3
REMARK 465 PHE G -2
REMARK 465 GLN G -1
REMARK 465 MSE H -20
REMARK 465 GLY H -19
REMARK 465 SER H -18
REMARK 465 SER H -17
REMARK 465 HIS H -16
REMARK 465 HIS H -15
REMARK 465 HIS H -14
REMARK 465 HIS H -13
REMARK 465 HIS H -12
REMARK 465 HIS H -11
REMARK 465 SER H -10
REMARK 465 SER H -9
REMARK 465 GLY H -8
REMARK 465 ARG H -7
REMARK 465 GLU H -6
REMARK 465 ASN H -5
REMARK 465 LEU H -4
REMARK 465 TYR H -3
REMARK 465 PHE H -2
REMARK 465 GLN H -1
REMARK 465 LEU H 84
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MSE B 1 CG SE CE
REMARK 470 ASN B 29 CG OD1 ND2
REMARK 470 ASN G 29 CG OD1 ND2
REMARK 470 ASN H 29 CG OD1 ND2
REMARK 470 GLN H 30 CG CD OE1 NE2
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 HIS A 76 -164.34 -163.15
REMARK 500 ASP B 28 -119.89 52.94
REMARK 500 HIS B 76 -156.42 -158.02
REMARK 500 ASP C 28 -118.65 51.66
REMARK 500 ASP E 28 -153.49 53.99
REMARK 500 ASN E 29 40.09 -87.46
REMARK 500 ASP F 28 -120.12 49.44
REMARK 500 THR F 82 -132.64 -114.15
REMARK 500 ASP G 28 -123.71 49.65
REMARK 500 HIS G 76 -156.75 -155.36
REMARK 500 ASP H 28 -110.28 40.98
REMARK 500 GLN H 30 -150.50 51.50
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 MLA A 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA D 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT G 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H 86
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC28040.2 RELATED DB: TARGETDB
DBREF 3K3S A 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
DBREF 3K3S B 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
DBREF 3K3S C 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
DBREF 3K3S D 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
DBREF 3K3S E 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
DBREF 3K3S F 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
DBREF 3K3S G 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
DBREF 3K3S H 1 84 UNP Q83JJ2 Q83JJ2_SHIFL 1 84
SEQADV 3K3S MSE A -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY A -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER A -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER A -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS A -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS A -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS A -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS A -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS A -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS A -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER A -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER A -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY A -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG A -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU A -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN A -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU A -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR A -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE A -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN A -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY A 0 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S MSE B -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY B -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER B -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER B -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS B -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS B -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS B -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS B -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS B -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS B -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER B -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER B -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY B -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG B -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU B -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN B -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU B -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR B -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE B -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN B -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY B 0 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S MSE C -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY C -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER C -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER C -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS C -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS C -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS C -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS C -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS C -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS C -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER C -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER C -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY C -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG C -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU C -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN C -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU C -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR C -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE C -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN C -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY C 0 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S MSE D -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY D -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER D -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER D -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS D -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS D -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS D -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS D -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS D -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS D -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER D -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER D -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY D -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG D -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU D -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN D -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU D -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR D -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE D -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN D -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY D 0 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S MSE E -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY E -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER E -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER E -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS E -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS E -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS E -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS E -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS E -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS E -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER E -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER E -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY E -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG E -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU E -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN E -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU E -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR E -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE E -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN E -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY E 0 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S MSE F -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY F -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER F -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER F -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS F -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS F -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS F -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS F -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS F -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS F -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER F -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER F -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY F -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG F -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU F -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN F -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU F -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR F -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE F -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN F -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY F 0 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S MSE G -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY G -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER G -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER G -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS G -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS G -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS G -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS G -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS G -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS G -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER G -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER G -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY G -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG G -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU G -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN G -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU G -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR G -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE G -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN G -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY G 0 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S MSE H -20 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY H -19 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER H -18 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER H -17 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS H -16 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS H -15 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS H -14 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS H -13 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS H -12 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S HIS H -11 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER H -10 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S SER H -9 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY H -8 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ARG H -7 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLU H -6 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S ASN H -5 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S LEU H -4 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S TYR H -3 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S PHE H -2 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLN H -1 UNP Q83JJ2 EXPRESSION TAG
SEQADV 3K3S GLY H 0 UNP Q83JJ2 EXPRESSION TAG
SEQRES 1 A 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 A 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 A 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 A 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 A 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 A 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 A 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 A 105 LEU
SEQRES 1 B 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 B 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 B 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 B 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 B 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 B 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 B 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 B 105 LEU
SEQRES 1 C 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 C 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 C 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 C 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 C 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 C 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 C 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 C 105 LEU
SEQRES 1 D 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 D 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 D 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 D 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 D 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 D 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 D 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 D 105 LEU
SEQRES 1 E 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 E 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 E 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 E 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 E 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 E 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 E 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 E 105 LEU
SEQRES 1 F 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 F 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 F 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 F 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 F 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 F 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 F 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 F 105 LEU
SEQRES 1 G 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 G 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 G 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 G 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 G 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 G 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 G 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 G 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 G 105 LEU
SEQRES 1 H 105 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 H 105 ARG GLU ASN LEU TYR PHE GLN GLY MSE GLN TYR ILE LYS
SEQRES 3 H 105 ILE HIS ALA LEU ASP ASN VAL ALA VAL ALA LEU ALA ASP
SEQRES 4 H 105 LEU ALA GLU GLY THR GLU VAL SER VAL ASP ASN GLN THR
SEQRES 5 H 105 VAL THR LEU ARG GLN ASP VAL ALA ARG GLY HIS LYS PHE
SEQRES 6 H 105 ALA LEU THR ASP ILE ALA LYS GLY ALA ASN VAL ILE LYS
SEQRES 7 H 105 TYR GLY LEU PRO ILE GLY TYR ALA LEU ALA ASP ILE ALA
SEQRES 8 H 105 ALA GLY GLU HIS VAL HIS ALA HIS ASN THR ARG THR ASN
SEQRES 9 H 105 LEU
MODRES 3K3S MSE A 1 MET SELENOMETHIONINE
MODRES 3K3S MSE B 1 MET SELENOMETHIONINE
MODRES 3K3S MSE C 1 MET SELENOMETHIONINE
MODRES 3K3S MSE D 1 MET SELENOMETHIONINE
MODRES 3K3S MSE E 1 MET SELENOMETHIONINE
MODRES 3K3S MSE F 1 MET SELENOMETHIONINE
MODRES 3K3S MSE G 1 MET SELENOMETHIONINE
MODRES 3K3S MSE H 1 MET SELENOMETHIONINE
HET MSE A 1 16
HET MSE B 1 5
HET MSE C 1 8
HET MSE D 1 8
HET MSE E 1 8
HET MSE F 1 8
HET MSE G 1 8
HET MSE H 1 8
HET MLA A 85 7
HET ACT B 85 4
HET CL B 86 1
HET ACT C 85 4
HET MLA D 85 7
HET ACT E 85 4
HET ACT F 85 4
HET CL G 85 1
HET ACT G 86 4
HET CL H 85 1
HET ACT H 86 4
HETNAM MSE SELENOMETHIONINE
HETNAM MLA MALONIC ACID
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METHANEDICARBOXYLIC ACID
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 9 MLA 2(C3 H4 O4)
FORMUL 10 ACT 6(C2 H3 O2 1-)
FORMUL 11 CL 3(CL 1-)
FORMUL 20 HOH *613(H2 O)
SHEET 1 A 4 TYR A 3 ILE A 4 0
SHEET 2 A 4 VAL A 12 ALA A 15 -1 O VAL A 14 N ILE A 4
SHEET 3 A 4 LYS A 43 ALA A 45 -1 O PHE A 44 N ALA A 13
SHEET 4 A 4 HIS A 74 VAL A 75 -1 O VAL A 75 N LYS A 43
SHEET 1 B 2 GLU A 24 VAL A 27 0
SHEET 2 B 2 GLN A 30 THR A 33 -1 O VAL A 32 N VAL A 25
SHEET 1 C 3 ASN A 54 LYS A 57 0
SHEET 2 C 3 LEU A 60 ALA A 65 -1 O ILE A 62 N VAL A 55
SHEET 3 C 3 THR A 80 THR A 82 -1 O ARG A 81 N TYR A 64
SHEET 1 D 4 TYR B 3 ILE B 4 0
SHEET 2 D 4 VAL B 12 ALA B 15 -1 O VAL B 14 N ILE B 4
SHEET 3 D 4 LYS B 43 ALA B 45 -1 O PHE B 44 N ALA B 13
SHEET 4 D 4 HIS B 74 VAL B 75 -1 O VAL B 75 N LYS B 43
SHEET 1 E 2 GLU B 24 VAL B 27 0
SHEET 2 E 2 GLN B 30 THR B 33 -1 O GLN B 30 N VAL B 27
SHEET 1 F 3 ASN B 54 LYS B 57 0
SHEET 2 F 3 LEU B 60 ALA B 65 -1 O ILE B 62 N VAL B 55
SHEET 3 F 3 THR B 80 THR B 82 -1 O ARG B 81 N TYR B 64
SHEET 1 G 4 TYR C 3 ILE C 4 0
SHEET 2 G 4 VAL C 12 ALA C 15 -1 O VAL C 14 N ILE C 4
SHEET 3 G 4 LYS C 43 ALA C 45 -1 O PHE C 44 N ALA C 13
SHEET 4 G 4 HIS C 74 VAL C 75 -1 O VAL C 75 N LYS C 43
SHEET 1 H 2 GLU C 24 VAL C 27 0
SHEET 2 H 2 GLN C 30 THR C 33 -1 O VAL C 32 N VAL C 25
SHEET 1 I 3 ASN C 54 LYS C 57 0
SHEET 2 I 3 LEU C 60 ALA C 65 -1 O LEU C 60 N LYS C 57
SHEET 3 I 3 THR C 80 THR C 82 -1 O ARG C 81 N TYR C 64
SHEET 1 J 4 TYR D 3 ILE D 4 0
SHEET 2 J 4 VAL D 12 ALA D 15 -1 O VAL D 14 N ILE D 4
SHEET 3 J 4 LYS D 43 ALA D 45 -1 O PHE D 44 N ALA D 13
SHEET 4 J 4 HIS D 74 VAL D 75 -1 O VAL D 75 N LYS D 43
SHEET 1 K 2 GLU D 24 VAL D 27 0
SHEET 2 K 2 GLN D 30 THR D 33 -1 O GLN D 30 N VAL D 27
SHEET 1 L 3 ASN D 54 LYS D 57 0
SHEET 2 L 3 LEU D 60 ALA D 65 -1 O LEU D 60 N LYS D 57
SHEET 3 L 3 THR D 80 THR D 82 -1 O ARG D 81 N TYR D 64
SHEET 1 M 4 TYR E 3 ILE E 4 0
SHEET 2 M 4 VAL E 12 ALA E 15 -1 O VAL E 14 N ILE E 4
SHEET 3 M 4 LYS E 43 ALA E 45 -1 O PHE E 44 N ALA E 13
SHEET 4 M 4 HIS E 74 VAL E 75 -1 O VAL E 75 N LYS E 43
SHEET 1 N 2 GLU E 24 VAL E 27 0
SHEET 2 N 2 GLN E 30 THR E 33 -1 O VAL E 32 N VAL E 25
SHEET 1 O 3 ASN E 54 LYS E 57 0
SHEET 2 O 3 LEU E 60 ALA E 65 -1 O GLY E 63 N VAL E 55
SHEET 3 O 3 THR E 80 THR E 82 -1 O ARG E 81 N TYR E 64
SHEET 1 P 4 TYR F 3 ILE F 4 0
SHEET 2 P 4 VAL F 12 ALA F 15 -1 O VAL F 14 N ILE F 4
SHEET 3 P 4 LYS F 43 ALA F 45 -1 O PHE F 44 N ALA F 13
SHEET 4 P 4 HIS F 74 VAL F 75 -1 O VAL F 75 N LYS F 43
SHEET 1 Q 2 GLU F 24 VAL F 27 0
SHEET 2 Q 2 GLN F 30 THR F 33 -1 O VAL F 32 N VAL F 25
SHEET 1 R 3 ASN F 54 LYS F 57 0
SHEET 2 R 3 LEU F 60 ALA F 65 -1 O GLY F 63 N VAL F 55
SHEET 3 R 3 THR F 80 ARG F 81 -1 O ARG F 81 N TYR F 64
SHEET 1 S 4 TYR G 3 ILE G 4 0
SHEET 2 S 4 VAL G 12 ALA G 15 -1 O VAL G 14 N ILE G 4
SHEET 3 S 4 LYS G 43 ALA G 45 -1 O PHE G 44 N ALA G 13
SHEET 4 S 4 HIS G 74 VAL G 75 -1 O VAL G 75 N LYS G 43
SHEET 1 T 2 GLU G 24 VAL G 27 0
SHEET 2 T 2 GLN G 30 THR G 33 -1 O VAL G 32 N VAL G 25
SHEET 1 U 3 ASN G 54 LYS G 57 0
SHEET 2 U 3 LEU G 60 ALA G 65 -1 O GLY G 63 N VAL G 55
SHEET 3 U 3 THR G 80 THR G 82 -1 O ARG G 81 N TYR G 64
SHEET 1 V 4 TYR H 3 ILE H 4 0
SHEET 2 V 4 VAL H 12 ALA H 15 -1 O VAL H 14 N ILE H 4
SHEET 3 V 4 LYS H 43 ALA H 45 -1 O PHE H 44 N ALA H 13
SHEET 4 V 4 HIS H 74 VAL H 75 -1 O VAL H 75 N LYS H 43
SHEET 1 W 2 GLU H 24 SER H 26 0
SHEET 2 W 2 THR H 31 THR H 33 -1 O VAL H 32 N VAL H 25
SHEET 1 X 3 ASN H 54 LYS H 57 0
SHEET 2 X 3 LEU H 60 ALA H 65 -1 O GLY H 63 N VAL H 55
SHEET 3 X 3 THR H 80 THR H 82 -1 O ARG H 81 N TYR H 64
LINK C GLY A 0 N AMSE A 1 1555 1555 1.32
LINK C GLY A 0 N BMSE A 1 1555 1555 1.33
LINK C AMSE A 1 N GLN A 2 1555 1555 1.33
LINK C BMSE A 1 N GLN A 2 1555 1555 1.33
LINK C GLY B 0 N MSE B 1 1555 1555 1.34
LINK C MSE B 1 N GLN B 2 1555 1555 1.33
LINK C GLY C 0 N MSE C 1 1555 1555 1.32
LINK C MSE C 1 N GLN C 2 1555 1555 1.32
LINK C GLY D 0 N MSE D 1 1555 1555 1.33
LINK C MSE D 1 N GLN D 2 1555 1555 1.33
LINK C GLY E 0 N MSE E 1 1555 1555 1.34
LINK C MSE E 1 N GLN E 2 1555 1555 1.32
LINK C GLY F 0 N MSE F 1 1555 1555 1.32
LINK C MSE F 1 N GLN F 2 1555 1555 1.31
LINK C GLY G 0 N MSE G 1 1555 1555 1.33
LINK C MSE G 1 N GLN G 2 1555 1555 1.32
LINK C GLY H 0 N MSE H 1 1555 1555 1.34
LINK C MSE H 1 N GLN H 2 1555 1555 1.33
SITE 1 AC1 9 LYS A 43 LYS A 57 TYR A 58 ILE A 62
SITE 2 AC1 9 THR A 82 HOH A 445 HOH A 527 MLA D 85
SITE 3 AC1 9 HOH D 526
SITE 1 AC2 5 LYS B 43 LYS B 57 TYR B 58 ILE B 62
SITE 2 AC2 5 HOH B 597
SITE 1 AC3 2 ALA B 67 ASP B 68
SITE 1 AC4 6 LYS C 43 LYS C 57 TYR C 58 ILE C 62
SITE 2 AC4 6 THR C 82 HOH C 285
SITE 1 AC5 8 MLA A 85 HOH A 527 LYS D 43 LYS D 57
SITE 2 AC5 8 TYR D 58 THR D 82 HOH D 326 HOH D 526
SITE 1 AC6 5 LYS E 43 LYS E 57 TYR E 58 ILE E 62
SITE 2 AC6 5 LEU E 84
SITE 1 AC7 6 LYS F 43 LYS F 57 TYR F 58 ILE F 62
SITE 2 AC7 6 THR F 82 LEU F 84
SITE 1 AC8 1 ASP G 18
SITE 1 AC9 4 LYS G 43 LYS G 57 TYR G 58 ILE G 62
SITE 1 BC1 1 ARG H 40
SITE 1 BC2 3 LYS H 43 LYS H 57 TYR H 58
CRYST1 113.968 40.218 121.001 90.00 104.33 90.00 P 1 21 1 16
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 0.008770 0.000000 0.002240 0.00000
SCALE2 0.000000 0.024860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008530 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
