HEADER LYASE 05-APR-12 4EIV
TITLE 1.37 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF APO-FORM OF A PUTATIVE
TITLE 2 DEOXYRIBOSE-PHOSPHATE ALDOLASE FROM TOXOPLASMA GONDII ME49
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYRIBOSE-PHOSPHATE ALDOLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 6-286;
COMPND 5 EC: 4.1.2.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;
SOURCE 3 ORGANISM_TAXID: 5811;
SOURCE 4 STRAIN: TOXOPLASMA GONDII ME49;
SOURCE 5 GENE: TGGT1_122370, TGME49_118750, TGVEG_010130;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCCK-N-HIS
KEYWDS CHEMOTHERAPY, BRAIN CYSTS, BRADYZOITE, STRUCTURAL GENOMICS, CENTER
KEYWDS 2 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, TIM-BARREL,
KEYWDS 3 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,J.RUAN,G.MINASOV,L.SHUVALOVA,A.UENO,M.IGARASHI,H.NGO,
AUTHOR 2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 6 13-SEP-23 4EIV 1 REMARK SEQADV LINK
REVDAT 5 15-NOV-17 4EIV 1 REMARK
REVDAT 4 04-MAR-15 4EIV 1 JRNL
REVDAT 3 12-NOV-14 4EIV 1 JRNL
REVDAT 2 01-OCT-14 4EIV 1 REMARK
REVDAT 1 23-MAY-12 4EIV 0
JRNL AUTH M.L.TONKIN,A.S.HALAVATY,R.RAMASWAMY,J.RUAN,M.IGARASHI,
JRNL AUTH 2 H.M.NGO,M.J.BOULANGER
JRNL TITL STRUCTURAL AND FUNCTIONAL DIVERGENCE OF THE ALDOLASE FOLD IN
JRNL TITL 2 TOXOPLASMA GONDII.
JRNL REF J.MOL.BIOL. V. 427 840 2015
JRNL REFN ISSN 0022-2836
JRNL PMID 25284756
JRNL DOI 10.1016/J.JMB.2014.09.019
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 101562
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5325
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7479
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 400
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3883
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 688
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.09000
REMARK 3 B22 (A**2) : -1.52000
REMARK 3 B33 (A**2) : -0.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.062
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.057
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.165
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4305 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2939 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5852 ; 1.428 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7180 ; 0.903 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 581 ; 4.002 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;31.010 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 762 ; 9.387 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;11.221 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 669 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4984 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 891 ; 0.002 ; 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): 2758 ; 1.181 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1139 ; 0.381 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4473 ; 1.847 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1547 ; 2.975 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1379 ; 4.393 ; 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): 7244 ; 1.136 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
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 50
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3251 -0.9644 16.0914
REMARK 3 T TENSOR
REMARK 3 T11: 0.0821 T22: 0.0803
REMARK 3 T33: 0.0490 T12: -0.0087
REMARK 3 T13: 0.0214 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.5973 L22: 3.3080
REMARK 3 L33: 0.6125 L12: 0.5086
REMARK 3 L13: -0.1112 L23: -0.3263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: -0.0546 S13: -0.0282
REMARK 3 S21: 0.4858 S22: -0.0803 S23: 0.1180
REMARK 3 S31: -0.1237 S32: -0.0102 S33: 0.0036
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 51 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4017 12.7779 10.8998
REMARK 3 T TENSOR
REMARK 3 T11: 0.0842 T22: 0.1101
REMARK 3 T33: 0.0862 T12: -0.0315
REMARK 3 T13: -0.0393 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.6858 L22: 2.2088
REMARK 3 L33: 1.3162 L12: 0.3152
REMARK 3 L13: -0.3117 L23: -0.7694
REMARK 3 S TENSOR
REMARK 3 S11: 0.0964 S12: -0.1705 S13: 0.0041
REMARK 3 S21: 0.4182 S22: -0.0861 S23: -0.1651
REMARK 3 S31: -0.1462 S32: 0.1181 S33: -0.0103
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 115 A 173
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4929 8.9763 -6.1908
REMARK 3 T TENSOR
REMARK 3 T11: 0.0107 T22: 0.1181
REMARK 3 T33: 0.1172 T12: 0.0033
REMARK 3 T13: -0.0006 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.1370 L22: 2.7203
REMARK 3 L33: 2.5234 L12: 0.2675
REMARK 3 L13: -0.3053 L23: -0.5325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: 0.1063 S13: 0.0105
REMARK 3 S21: -0.1597 S22: -0.0175 S23: -0.0895
REMARK 3 S31: -0.0115 S32: 0.0921 S33: 0.0164
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 174 A 200
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6779 -0.2188 -6.1729
REMARK 3 T TENSOR
REMARK 3 T11: 0.0321 T22: 0.0902
REMARK 3 T33: 0.0839 T12: 0.0062
REMARK 3 T13: -0.0064 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 2.2374 L22: 4.9129
REMARK 3 L33: 2.3787 L12: 0.7753
REMARK 3 L13: -0.5520 L23: 0.8978
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: 0.1952 S13: -0.0050
REMARK 3 S21: -0.2830 S22: -0.0138 S23: -0.2136
REMARK 3 S31: 0.0269 S32: -0.0185 S33: -0.0006
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 219 A 278
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8147 -6.5194 7.3599
REMARK 3 T TENSOR
REMARK 3 T11: 0.0294 T22: 0.1036
REMARK 3 T33: 0.1048 T12: 0.0004
REMARK 3 T13: 0.0004 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.7200 L22: 1.9261
REMARK 3 L33: 0.9921 L12: 0.3643
REMARK 3 L13: 0.0631 L23: -0.7487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: -0.0688 S13: -0.0021
REMARK 3 S21: 0.1262 S22: -0.0427 S23: 0.0135
REMARK 3 S31: 0.0260 S32: -0.0673 S33: 0.0217
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 : B 0 B 60
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2024 -34.2294 0.2347
REMARK 3 T TENSOR
REMARK 3 T11: 0.0293 T22: 0.0779
REMARK 3 T33: 0.0788 T12: -0.0014
REMARK 3 T13: -0.0127 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.2962 L22: 2.2627
REMARK 3 L33: 0.3513 L12: -0.4515
REMARK 3 L13: -0.2309 L23: 0.5927
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: 0.0173 S13: 0.0077
REMARK 3 S21: -0.1232 S22: -0.0472 S23: 0.1108
REMARK 3 S31: 0.0111 S32: -0.0704 S33: 0.0145
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 61 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8089 -42.3478 7.8572
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: 0.0651
REMARK 3 T33: 0.0950 T12: 0.0059
REMARK 3 T13: 0.0117 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.6372 L22: 0.9709
REMARK 3 L33: 3.7208 L12: -0.0522
REMARK 3 L13: 0.8345 L23: 0.0614
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: -0.0259 S13: -0.0509
REMARK 3 S21: 0.0021 S22: 0.0005 S23: -0.0941
REMARK 3 S31: 0.2793 S32: -0.0183 S33: 0.0006
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 120 B 172
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3370 -36.5870 19.6814
REMARK 3 T TENSOR
REMARK 3 T11: 0.0192 T22: 0.0878
REMARK 3 T33: 0.0890 T12: 0.0031
REMARK 3 T13: -0.0173 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 1.0790 L22: 1.8551
REMARK 3 L33: 2.4354 L12: -0.0899
REMARK 3 L13: -0.1790 L23: -0.0225
REMARK 3 S TENSOR
REMARK 3 S11: -0.0074 S12: -0.0980 S13: -0.0471
REMARK 3 S21: 0.1775 S22: -0.0141 S23: -0.1495
REMARK 3 S31: 0.0603 S32: 0.1427 S33: 0.0215
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 173 B 201
REMARK 3 ORIGIN FOR THE GROUP (A): -14.4155 -29.0027 22.1545
REMARK 3 T TENSOR
REMARK 3 T11: 0.0387 T22: 0.0517
REMARK 3 T33: 0.0427 T12: 0.0039
REMARK 3 T13: -0.0132 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 2.7528 L22: 2.6893
REMARK 3 L33: 2.0025 L12: 0.2115
REMARK 3 L13: 0.1456 L23: 0.5634
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: -0.1274 S13: 0.0132
REMARK 3 S21: 0.2489 S22: -0.0005 S23: -0.1149
REMARK 3 S31: -0.0183 S32: -0.0216 S33: 0.0096
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 202 B 276
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8958 -24.8875 9.6090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0028 T22: 0.0636
REMARK 3 T33: 0.0711 T12: 0.0002
REMARK 3 T13: 0.0001 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.8329 L22: 1.4258
REMARK 3 L33: 1.6190 L12: -0.1608
REMARK 3 L13: 0.2658 L23: -0.0815
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: 0.0240 S13: -0.0293
REMARK 3 S21: 0.0084 S22: 0.0072 S23: 0.0750
REMARK 3 S31: -0.0642 S32: -0.0791 S33: -0.0013
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 4EIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BE-LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107282
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.60200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3QYQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PACT SUITE B7(#19)-0.2 M NACL, 0.1
REMARK 280 M MES PH 6.0, 20% (W/V) PEG 6K. PROTEIN AT 12.7 MG/ML IN 10 MM
REMARK 280 TRIS-HCL PH 8.3, 500 MM NACL, 5 MM BME. , VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 35.99100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.18900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.64200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.18900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.99100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.64200
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 ARG A 201
REMARK 465 GLU A 202
REMARK 465 ASN A 203
REMARK 465 GLU A 204
REMARK 465 ARG A 205
REMARK 465 ILE A 206
REMARK 465 ARG A 207
REMARK 465 VAL A 208
REMARK 465 GLU A 209
REMARK 465 GLY A 210
REMARK 465 ILE A 211
REMARK 465 ASN A 212
REMARK 465 ARG A 213
REMARK 465 GLU A 214
REMARK 465 GLY A 215
REMARK 465 ALA A 216
REMARK 465 ALA A 217
REMARK 465 VAL A 218
REMARK 465 GLY A 279
REMARK 465 VAL A 280
REMARK 465 SER A 281
REMARK 465 PRO A 282
REMARK 465 ASP A 283
REMARK 465 THR A 284
REMARK 465 SER A 285
REMARK 465 PRO A 286
REMARK 465 MET B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 ASN B 203
REMARK 465 GLU B 204
REMARK 465 ARG B 205
REMARK 465 ILE B 206
REMARK 465 ARG B 207
REMARK 465 VAL B 208
REMARK 465 GLU B 209
REMARK 465 GLY B 210
REMARK 465 ILE B 211
REMARK 465 ASN B 212
REMARK 465 ARG B 213
REMARK 465 GLU B 214
REMARK 465 GLY B 215
REMARK 465 ALA B 216
REMARK 465 ALA B 217
REMARK 465 VAL B 218
REMARK 465 SER B 277
REMARK 465 VAL B 278
REMARK 465 GLY B 279
REMARK 465 VAL B 280
REMARK 465 SER B 281
REMARK 465 PRO B 282
REMARK 465 ASP B 283
REMARK 465 THR B 284
REMARK 465 SER B 285
REMARK 465 PRO B 286
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR B 0 C ILE B 6 N 0.172
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 ILE A 251 72.60 -103.30
REMARK 500 LYS A 255 11.79 -141.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR B 0 -12.46
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 CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QYQ RELATED DB: PDB
REMARK 900 1.8 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A PUTATIVE DEOXYRIBOSE-
REMARK 900 PHOSPHATE ALDOLASE FROM TOXOPLASMA GONDII ME49
REMARK 900 RELATED ID: IDP90300 RELATED DB: TARGETTRACK
DBREF 4EIV A 6 286 UNP B9PVB4 B9PVB4_TOXGO 6 286
DBREF 4EIV B 6 286 UNP B9PVB4 B9PVB4_TOXGO 6 286
SEQADV 4EIV MET A -15 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS A -14 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS A -13 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS A -12 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS A -11 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS A -10 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS A -9 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLU A -8 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV ASN A -7 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV LEU A -6 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV TYR A -5 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV PHE A -4 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLN A -3 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLY A -2 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLY A -1 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV THR A 0 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV MET B -15 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS B -14 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS B -13 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS B -12 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS B -11 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS B -10 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV HIS B -9 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLU B -8 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV ASN B -7 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV LEU B -6 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV TYR B -5 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV PHE B -4 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLN B -3 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLY B -2 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV GLY B -1 UNP B9PVB4 EXPRESSION TAG
SEQADV 4EIV THR B 0 UNP B9PVB4 EXPRESSION TAG
SEQRES 1 A 297 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 A 297 GLY GLY THR ILE TYR LYS GLN PHE THR SER ARG THR LEU
SEQRES 3 A 297 LEU ASN PHE PHE GLU VAL ALA ALA LEU THR ASP GLY GLU
SEQRES 4 A 297 THR ASN GLU SER VAL ALA ALA VAL CYS LYS ILE ALA ALA
SEQRES 5 A 297 LYS ASP PRO ALA ILE VAL GLY VAL SER VAL ARG PRO ALA
SEQRES 6 A 297 PHE VAL ARG PHE ILE ARG GLN GLU LEU VAL LYS SER ALA
SEQRES 7 A 297 PRO GLU VAL ALA GLY ILE LYS VAL CYS ALA ALA VAL ASN
SEQRES 8 A 297 PHE PRO GLU GLY THR GLY THR PRO ASP THR VAL SER LEU
SEQRES 9 A 297 GLU ALA VAL GLY ALA LEU LYS ASP GLY ALA ASP GLU ILE
SEQRES 10 A 297 GLU CYS LEU ILE ASP TRP ARG ARG MET ASN GLU ASN VAL
SEQRES 11 A 297 ALA ASP GLY GLU SER ARG ILE ARG LEU LEU VAL SER GLU
SEQRES 12 A 297 VAL LYS LYS VAL VAL GLY PRO LYS THR LEU LYS VAL VAL
SEQRES 13 A 297 LEU SER GLY GLY GLU LEU GLN GLY GLY ASP ILE ILE SER
SEQRES 14 A 297 ARG ALA ALA VAL ALA ALA LEU GLU GLY GLY ALA ASP PHE
SEQRES 15 A 297 LEU GLN THR SER SER GLY LEU GLY ALA THR HIS ALA THR
SEQRES 16 A 297 MET PHE THR VAL HIS LEU ILE SER ILE ALA LEU ARG GLU
SEQRES 17 A 297 TYR MET VAL ARG GLU ASN GLU ARG ILE ARG VAL GLU GLY
SEQRES 18 A 297 ILE ASN ARG GLU GLY ALA ALA VAL ARG CYS ILE GLY ILE
SEQRES 19 A 297 LYS ILE GLU VAL GLY ASP VAL HIS MET ALA GLU THR ALA
SEQRES 20 A 297 ASP PHE LEU MET GLN MET ILE PHE GLU ASN GLY PRO ARG
SEQRES 21 A 297 SER ILE VAL ARG ASP LYS PHE ARG VAL GLY GLY GLY PHE
SEQRES 22 A 297 ASN LEU LEU LYS GLU LEU ARG ASP CYS TYR GLU SER TRP
SEQRES 23 A 297 ASP SER VAL GLY VAL SER PRO ASP THR SER PRO
SEQRES 1 B 297 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 B 297 GLY GLY THR ILE TYR LYS GLN PHE THR SER ARG THR LEU
SEQRES 3 B 297 LEU ASN PHE PHE GLU VAL ALA ALA LEU THR ASP GLY GLU
SEQRES 4 B 297 THR ASN GLU SER VAL ALA ALA VAL CYS LYS ILE ALA ALA
SEQRES 5 B 297 LYS ASP PRO ALA ILE VAL GLY VAL SER VAL ARG PRO ALA
SEQRES 6 B 297 PHE VAL ARG PHE ILE ARG GLN GLU LEU VAL LYS SER ALA
SEQRES 7 B 297 PRO GLU VAL ALA GLY ILE LYS VAL CYS ALA ALA VAL ASN
SEQRES 8 B 297 PHE PRO GLU GLY THR GLY THR PRO ASP THR VAL SER LEU
SEQRES 9 B 297 GLU ALA VAL GLY ALA LEU LYS ASP GLY ALA ASP GLU ILE
SEQRES 10 B 297 GLU CYS LEU ILE ASP TRP ARG ARG MET ASN GLU ASN VAL
SEQRES 11 B 297 ALA ASP GLY GLU SER ARG ILE ARG LEU LEU VAL SER GLU
SEQRES 12 B 297 VAL LYS LYS VAL VAL GLY PRO LYS THR LEU LYS VAL VAL
SEQRES 13 B 297 LEU SER GLY GLY GLU LEU GLN GLY GLY ASP ILE ILE SER
SEQRES 14 B 297 ARG ALA ALA VAL ALA ALA LEU GLU GLY GLY ALA ASP PHE
SEQRES 15 B 297 LEU GLN THR SER SER GLY LEU GLY ALA THR HIS ALA THR
SEQRES 16 B 297 MET PHE THR VAL HIS LEU ILE SER ILE ALA LEU ARG GLU
SEQRES 17 B 297 TYR MET VAL ARG GLU ASN GLU ARG ILE ARG VAL GLU GLY
SEQRES 18 B 297 ILE ASN ARG GLU GLY ALA ALA VAL ARG CYS ILE GLY ILE
SEQRES 19 B 297 LYS ILE GLU VAL GLY ASP VAL HIS MET ALA GLU THR ALA
SEQRES 20 B 297 ASP PHE LEU MET GLN MET ILE PHE GLU ASN GLY PRO ARG
SEQRES 21 B 297 SER ILE VAL ARG ASP LYS PHE ARG VAL GLY GLY GLY PHE
SEQRES 22 B 297 ASN LEU LEU LYS GLU LEU ARG ASP CYS TYR GLU SER TRP
SEQRES 23 B 297 ASP SER VAL GLY VAL SER PRO ASP THR SER PRO
HET CL A 301 1
HET CL A 302 1
HET BME A 303 8
HET CL B 301 1
HET CL B 302 1
HET BME B 303 4
HETNAM CL CHLORIDE ION
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 3 CL 4(CL 1-)
FORMUL 5 BME 2(C2 H6 O S)
FORMUL 9 HOH *688(H2 O)
HELIX 1 1 THR A 0 ASN A 17 1 13
HELIX 2 2 THR A 29 LYS A 42 1 14
HELIX 3 3 PHE A 55 GLU A 62 1 8
HELIX 4 4 LEU A 63 SER A 66 5 4
HELIX 5 5 ALA A 67 ILE A 73 5 7
HELIX 6 6 THR A 87 ASP A 101 1 15
HELIX 7 7 TRP A 112 ASN A 118 1 7
HELIX 8 8 ASN A 118 GLY A 138 1 21
HELIX 9 9 GLY A 153 GLY A 168 1 16
HELIX 10 10 THR A 184 VAL A 200 1 17
HELIX 11 11 HIS A 231 GLY A 247 1 17
HELIX 12 12 PRO A 248 ILE A 251 5 4
HELIX 13 13 GLY A 261 SER A 274 1 14
HELIX 14 14 ILE B 6 PHE B 18 1 13
HELIX 15 15 THR B 29 LYS B 42 1 14
HELIX 16 16 ARG B 52 ALA B 54 5 3
HELIX 17 17 PHE B 55 GLU B 62 1 8
HELIX 18 18 GLU B 62 ALA B 67 1 6
HELIX 19 19 PRO B 68 ILE B 73 5 6
HELIX 20 20 THR B 87 ASP B 101 1 15
HELIX 21 21 ASP B 111 GLU B 117 5 7
HELIX 22 22 ASN B 118 GLY B 138 1 21
HELIX 23 23 GLY B 153 GLY B 167 1 15
HELIX 24 24 THR B 184 GLU B 202 1 19
HELIX 25 25 HIS B 231 GLY B 247 1 17
HELIX 26 26 PRO B 248 ILE B 251 5 4
HELIX 27 27 GLY B 261 SER B 274 1 14
SHEET 1 A 9 PHE A 19 ALA A 23 0
SHEET 2 A 9 GLY A 48 VAL A 51 1 O SER A 50 N VAL A 21
SHEET 3 A 9 LYS A 74 VAL A 79 1 O CYS A 76 N VAL A 49
SHEET 4 A 9 GLU A 105 LEU A 109 1 O GLU A 107 N ALA A 77
SHEET 5 A 9 THR A 141 VAL A 145 1 O LYS A 143 N ILE A 106
SHEET 6 A 9 PHE A 171 GLN A 173 1 O GLN A 173 N VAL A 144
SHEET 7 A 9 GLY A 222 GLU A 226 1 O LYS A 224 N LEU A 172
SHEET 8 A 9 PHE A 256 GLY A 260 1 O ARG A 257 N ILE A 225
SHEET 9 A 9 PHE A 19 ALA A 23 1 N GLU A 20 O VAL A 258
SHEET 1 B 9 PHE B 19 ALA B 22 0
SHEET 2 B 9 GLY B 48 VAL B 51 1 O SER B 50 N VAL B 21
SHEET 3 B 9 LYS B 74 VAL B 79 1 O CYS B 76 N VAL B 49
SHEET 4 B 9 GLU B 105 LEU B 109 1 O GLU B 107 N ALA B 77
SHEET 5 B 9 THR B 141 VAL B 145 1 O LYS B 143 N ILE B 106
SHEET 6 B 9 PHE B 171 GLN B 173 1 O GLN B 173 N VAL B 144
SHEET 7 B 9 GLY B 222 GLU B 226 1 O LYS B 224 N LEU B 172
SHEET 8 B 9 PHE B 256 GLY B 260 1 O GLY B 259 N ILE B 225
SHEET 9 B 9 PHE B 19 ALA B 22 1 N GLU B 20 O VAL B 258
LINK SG BCYS A 271 S2 BBME A 303 1555 1555 2.09
LINK SG CYS B 271 S2 BME B 303 1555 1555 2.12
CISPEP 1 ASP A 43 PRO A 44 0 -2.15
CISPEP 2 PHE A 81 PRO A 82 0 0.50
CISPEP 3 ASP B 43 PRO B 44 0 3.40
CISPEP 4 ASP B 43 PRO B 44 0 -5.88
CISPEP 5 PHE B 81 PRO B 82 0 -5.95
CISPEP 6 PHE B 81 PRO B 82 0 5.74
SITE 1 AC1 2 ASN A 17 ARG A 253
SITE 1 AC2 2 THR A 0 THR B 0
SITE 1 AC3 7 CYS A 271 SER A 274 HOH A 476 HOH A 499
SITE 2 AC3 7 HOH A 636 HOH A 649 HOH A 689
SITE 1 AC4 4 HOH A 613 ARG B 13 HOH B 435 HOH B 676
SITE 1 AC5 5 HOH A 571 GLY B 247 PRO B 248 ARG B 249
SITE 2 AC5 5 HOH B 652
SITE 1 AC6 1 CYS B 271
CRYST1 71.982 73.284 96.378 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013892 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010376 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
