HEADER OXIDOREDUCTASE 02-NOV-10 3PGJ
TITLE 2.49 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF SHIKIMATE 5-
TITLE 2 DEHYDROGENASE (AROE) FROM VIBRIO CHOLERAE O1 BIOVAR ELTOR STR. N16961
TITLE 3 IN COMPLEX WITH SHIKIMATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHIKIMATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.1.1.25;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR ELTOR;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: N16961;
SOURCE 5 GENE: AROE, VC_0056;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS SHIKIMATE 5-DEHYDROGENASE, SHIKIMATE, STRUCTURAL GENOMICS, CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, ALPHA/BETA
KEYWDS 3 DOMAIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,S.H.LIGHT,L.SHUVALOVA,L.PAPAZISI,W.F.ANDERSON,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 3 06-SEP-23 3PGJ 1 REMARK SEQADV
REVDAT 2 08-NOV-17 3PGJ 1 REMARK
REVDAT 1 24-NOV-10 3PGJ 0
JRNL AUTH A.S.HALAVATY,S.H.LIGHT,L.SHUVALOVA,L.PAPAZISI,W.F.ANDERSON,
JRNL AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 3 (CSGID)
JRNL TITL 2.49 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF SHIKIMATE
JRNL TITL 2 5-DEHYDROGENASE (AROE) FROM VIBRIO CHOLERAE O1 BIOVAR ELTOR
JRNL TITL 3 STR. N16961 IN COMPLEX WITH SHIKIMATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.49 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) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 32555
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1723
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) : 2.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1991
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 115
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.50000
REMARK 3 B22 (A**2) : 0.42000
REMARK 3 B33 (A**2) : 1.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.58000
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): 0.320
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.232
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.894
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8475 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5727 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11459 ; 1.416 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13948 ; 0.825 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1073 ; 0.938 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 390 ;18.359 ;24.308
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1429 ; 5.850 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ; 4.198 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1282 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9570 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1735 ; 0.000 ; 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): 5316 ; 0.578 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2215 ; 0.107 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8468 ; 1.132 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3159 ; 1.848 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2991 ; 3.103 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 5 A 80
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2868 -9.8243 37.2569
REMARK 3 T TENSOR
REMARK 3 T11: 0.0698 T22: 0.2519
REMARK 3 T33: 0.2723 T12: 0.0891
REMARK 3 T13: 0.0483 T23: 0.1158
REMARK 3 L TENSOR
REMARK 3 L11: 3.8318 L22: 4.9884
REMARK 3 L33: 4.0446 L12: -1.2131
REMARK 3 L13: -1.8642 L23: 1.1769
REMARK 3 S TENSOR
REMARK 3 S11: -0.1852 S12: -0.3586 S13: -0.3366
REMARK 3 S21: 0.5061 S22: 0.2797 S23: 0.1212
REMARK 3 S31: 0.2156 S32: 0.1880 S33: -0.0945
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 81 A 152
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3342 -2.9400 20.2124
REMARK 3 T TENSOR
REMARK 3 T11: 0.0396 T22: 0.2239
REMARK 3 T33: 0.2370 T12: 0.0180
REMARK 3 T13: -0.0129 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 1.7884 L22: 3.5074
REMARK 3 L33: 1.9215 L12: 0.8541
REMARK 3 L13: -0.9335 L23: -1.4950
REMARK 3 S TENSOR
REMARK 3 S11: -0.1316 S12: 0.0710 S13: -0.2936
REMARK 3 S21: -0.3166 S22: 0.0993 S23: 0.3911
REMARK 3 S31: 0.2281 S32: -0.0586 S33: 0.0323
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 153 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3239 6.3563 24.8302
REMARK 3 T TENSOR
REMARK 3 T11: 0.0132 T22: 0.2337
REMARK 3 T33: 0.1794 T12: 0.0316
REMARK 3 T13: -0.0059 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 2.5876 L22: 3.0117
REMARK 3 L33: 1.7738 L12: 0.9630
REMARK 3 L13: -0.9138 L23: -0.7569
REMARK 3 S TENSOR
REMARK 3 S11: 0.0637 S12: -0.2057 S13: 0.0034
REMARK 3 S21: -0.0016 S22: -0.0256 S23: -0.0994
REMARK 3 S31: -0.0627 S32: 0.2242 S33: -0.0381
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 5 B 121
REMARK 3 ORIGIN FOR THE GROUP (A): -35.0727 15.2590 3.8884
REMARK 3 T TENSOR
REMARK 3 T11: 0.0736 T22: 0.1513
REMARK 3 T33: 0.3373 T12: -0.0224
REMARK 3 T13: 0.0920 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 3.1956 L22: 2.8471
REMARK 3 L33: 5.4515 L12: -0.4590
REMARK 3 L13: 0.6329 L23: -0.7801
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: -0.0358 S13: 0.3288
REMARK 3 S21: -0.1772 S22: 0.1367 S23: 0.1340
REMARK 3 S31: -0.2994 S32: -0.4289 S33: -0.1671
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 : B 122 B 196
REMARK 3 ORIGIN FOR THE GROUP (A): -19.5839 12.7375 23.5415
REMARK 3 T TENSOR
REMARK 3 T11: 0.0504 T22: 0.4588
REMARK 3 T33: 0.2821 T12: 0.0768
REMARK 3 T13: -0.0123 T23: -0.1419
REMARK 3 L TENSOR
REMARK 3 L11: 8.1807 L22: 3.8830
REMARK 3 L33: 5.3885 L12: -1.6609
REMARK 3 L13: 1.3286 L23: 1.6349
REMARK 3 S TENSOR
REMARK 3 S11: -0.3292 S12: -1.2953 S13: 0.7406
REMARK 3 S21: 0.2478 S22: -0.0507 S23: -0.1111
REMARK 3 S31: -0.2563 S32: -0.7643 S33: 0.3799
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 197 B 275
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1750 4.9892 7.9340
REMARK 3 T TENSOR
REMARK 3 T11: 0.1228 T22: 0.1356
REMARK 3 T33: 0.2599 T12: 0.0533
REMARK 3 T13: 0.1116 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 6.8171 L22: 1.0875
REMARK 3 L33: 4.3783 L12: -0.2767
REMARK 3 L13: 4.0785 L23: -0.9144
REMARK 3 S TENSOR
REMARK 3 S11: 0.1211 S12: 0.1182 S13: -0.0337
REMARK 3 S21: -0.1900 S22: -0.0772 S23: -0.1578
REMARK 3 S31: 0.4291 S32: 0.3726 S33: -0.0438
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 : C 5 C 71
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5779 12.8602 -16.0135
REMARK 3 T TENSOR
REMARK 3 T11: 0.0587 T22: 0.1099
REMARK 3 T33: 0.1166 T12: -0.0312
REMARK 3 T13: 0.0393 T23: 0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 5.2238 L22: 7.5897
REMARK 3 L33: 4.9374 L12: 2.3002
REMARK 3 L13: 0.0188 L23: -1.7700
REMARK 3 S TENSOR
REMARK 3 S11: -0.0892 S12: -0.0720 S13: -0.0406
REMARK 3 S21: 0.1198 S22: -0.0223 S23: 0.0270
REMARK 3 S31: 0.1635 S32: -0.1088 S33: 0.1115
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 : C 72 C 202
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0422 23.1337 -36.5380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.3368
REMARK 3 T33: 0.3177 T12: -0.1094
REMARK 3 T13: -0.0010 T23: 0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 4.9417 L22: 1.2256
REMARK 3 L33: 4.7825 L12: -0.2888
REMARK 3 L13: 1.1682 L23: -1.4159
REMARK 3 S TENSOR
REMARK 3 S11: -0.1414 S12: 0.5871 S13: 0.3234
REMARK 3 S21: -0.2068 S22: 0.1719 S23: 0.1005
REMARK 3 S31: -0.1854 S32: -0.1333 S33: -0.0305
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 : C 203 C 275
REMARK 3 ORIGIN FOR THE GROUP (A): -44.3987 18.8229 -30.4222
REMARK 3 T TENSOR
REMARK 3 T11: 0.1009 T22: 0.5950
REMARK 3 T33: 0.5376 T12: -0.1082
REMARK 3 T13: -0.0162 T23: 0.1036
REMARK 3 L TENSOR
REMARK 3 L11: 4.3287 L22: 8.5025
REMARK 3 L33: 6.7806 L12: -2.7705
REMARK 3 L13: 1.6903 L23: -5.3200
REMARK 3 S TENSOR
REMARK 3 S11: 0.1156 S12: 0.1305 S13: 0.2441
REMARK 3 S21: -0.3289 S22: 0.6533 S23: 1.2284
REMARK 3 S31: 0.1527 S32: -1.5012 S33: -0.7689
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 : D 5 D 75
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4608 -1.3361 53.5346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1153 T22: 0.2140
REMARK 3 T33: 0.3512 T12: -0.0086
REMARK 3 T13: 0.1528 T23: 0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 6.8350 L22: 5.7176
REMARK 3 L33: 3.4902 L12: -1.7628
REMARK 3 L13: -0.0886 L23: -0.9458
REMARK 3 S TENSOR
REMARK 3 S11: 0.4024 S12: 0.3651 S13: 0.5600
REMARK 3 S21: -0.1795 S22: -0.5123 S23: -0.9646
REMARK 3 S31: -0.2114 S32: 0.4654 S33: 0.1098
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 : D 76 D 169
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3229 -4.9620 73.6907
REMARK 3 T TENSOR
REMARK 3 T11: 0.2818 T22: 0.2917
REMARK 3 T33: 0.3091 T12: -0.0312
REMARK 3 T13: -0.0830 T23: -0.1536
REMARK 3 L TENSOR
REMARK 3 L11: 2.7088 L22: 3.9547
REMARK 3 L33: 3.6364 L12: 0.8225
REMARK 3 L13: -2.0564 L23: -1.9437
REMARK 3 S TENSOR
REMARK 3 S11: 0.1449 S12: -0.3406 S13: 0.4465
REMARK 3 S21: 0.8300 S22: -0.0678 S23: -0.5076
REMARK 3 S31: -0.6576 S32: 0.4192 S33: -0.0770
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 : D 170 D 275
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7782 -13.9304 69.1096
REMARK 3 T TENSOR
REMARK 3 T11: 0.0588 T22: 0.2373
REMARK 3 T33: 0.2142 T12: 0.0528
REMARK 3 T13: 0.0478 T23: -0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 1.2802 L22: 6.5690
REMARK 3 L33: 2.9488 L12: 0.3609
REMARK 3 L13: -0.5752 L23: -1.4950
REMARK 3 S TENSOR
REMARK 3 S11: 0.0102 S12: 0.0145 S13: 0.0616
REMARK 3 S21: 0.4831 S22: 0.2060 S23: 0.0853
REMARK 3 S31: -0.0984 S32: -0.1571 S33: -0.2162
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 3PGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND[111]
REMARK 200 OPTICS : BE-LENSES/DIAMOND LAUE MONO
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34293
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.7700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.410
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: 3O8Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 7.5 MG/ML IN 10 MM TRIS/HCL
REMARK 280 PH 8.3, 0.5 M NACL, 5 MM BME. CRYSTALLIZATION CONDITION: THE
REMARK 280 CLASSIC SUITE H3 (#87) CONDITION (0.2 M AMMONIUM ACETATE, 0.1 M
REMARK 280 TRI-SODIUM CITRATE PH 5.6, 30 % (W/V) PEG4000). CRYSTAL WAS
REMARK 280 SOAKED IN 25 MM SHIKIMATE. , VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.82850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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: 2510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 ALA A 277
REMARK 465 LEU A 278
REMARK 465 MET B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 PRO B 14
REMARK 465 ILE B 15
REMARK 465 ASN B 16
REMARK 465 GLY B 276
REMARK 465 ALA B 277
REMARK 465 LEU B 278
REMARK 465 MET C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 SER C -16
REMARK 465 SER C -15
REMARK 465 GLY C -14
REMARK 465 VAL C -13
REMARK 465 ASP C -12
REMARK 465 LEU C -11
REMARK 465 GLY C -10
REMARK 465 THR C -9
REMARK 465 GLU C -8
REMARK 465 ASN C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 PHE C -4
REMARK 465 GLN C -3
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 3
REMARK 465 GLN C 4
REMARK 465 ALA C 194
REMARK 465 SER C 195
REMARK 465 LEU C 196
REMARK 465 ASP C 197
REMARK 465 GLY C 198
REMARK 465 GLU C 199
REMARK 465 LEU C 200
REMARK 465 GLY C 276
REMARK 465 ALA C 277
REMARK 465 LEU C 278
REMARK 465 MET D -23
REMARK 465 HIS D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 SER D -16
REMARK 465 SER D -15
REMARK 465 GLY D -14
REMARK 465 VAL D -13
REMARK 465 ASP D -12
REMARK 465 LEU D -11
REMARK 465 GLY D -10
REMARK 465 THR D -9
REMARK 465 GLU D -8
REMARK 465 ASN D -7
REMARK 465 LEU D -6
REMARK 465 TYR D -5
REMARK 465 PHE D -4
REMARK 465 GLN D -3
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 SER D 3
REMARK 465 GLN D 4
REMARK 465 GLY D 276
REMARK 465 ALA D 277
REMARK 465 LEU D 278
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 ASN A 13 64.40 -159.17
REMARK 500 HIS A 17 74.99 55.44
REMARK 500 PRO A 67 44.64 -99.67
REMARK 500 ALA A 131 42.34 -144.24
REMARK 500 ALA A 158 -55.09 -27.23
REMARK 500 TYR A 170 15.02 -68.17
REMARK 500 LEU A 181 98.43 -65.51
REMARK 500 PRO A 205 3.18 -62.75
REMARK 500 GLU A 275 27.64 -71.02
REMARK 500 ASP B 45 33.28 -90.19
REMARK 500 PRO B 67 47.50 -100.82
REMARK 500 ALA B 131 39.57 -140.23
REMARK 500 TYR B 170 51.90 -100.40
REMARK 500 LYS B 182 35.15 -148.86
REMARK 500 ALA B 202 80.40 -68.94
REMARK 500 PRO B 205 0.72 -60.36
REMARK 500 ASN C 13 107.86 -163.93
REMARK 500 PRO C 67 42.01 -107.67
REMARK 500 GLN C 146 53.91 77.34
REMARK 500 GLU C 172 102.10 -57.82
REMARK 500 GLU C 179 62.84 -68.23
REMARK 500 GLN C 180 -24.26 -162.48
REMARK 500 PRO C 205 -8.61 -52.41
REMARK 500 SER C 209 -157.23 -82.54
REMARK 500 GLN C 232 -55.87 -28.61
REMARK 500 HIS C 233 38.33 -88.50
REMARK 500 ASN D 13 109.68 -167.47
REMARK 500 THR D 65 -169.70 -108.13
REMARK 500 GLU D 172 91.75 -66.66
REMARK 500 PRO D 205 0.88 -67.14
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 SKM A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKM B 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKM C 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKM D 279
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O8Q RELATED DB: PDB
REMARK 900 1.45 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF SHIKIMATE 5-
REMARK 900 DEHYDROGENASE (AROE) FROM VIBRIO CHOLERAE
REMARK 900 RELATED ID: IDP90792 RELATED DB: TARGETDB
DBREF 3PGJ A 1 278 UNP Q9KVT3 AROE_VIBCH 1 278
DBREF 3PGJ B 1 278 UNP Q9KVT3 AROE_VIBCH 1 278
DBREF 3PGJ C 1 278 UNP Q9KVT3 AROE_VIBCH 1 278
DBREF 3PGJ D 1 278 UNP Q9KVT3 AROE_VIBCH 1 278
SEQADV 3PGJ MET A -23 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS A -22 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS A -21 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS A -20 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS A -19 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS A -18 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS A -17 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER A -16 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER A -15 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY A -14 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ VAL A -13 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASP A -12 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU A -11 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY A -10 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ THR A -9 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLU A -8 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN A -7 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU A -6 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ TYR A -5 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ PHE A -4 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLN A -3 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER A -2 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN A -1 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ALA A 0 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ MET B -23 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS B -22 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS B -21 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS B -20 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS B -19 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS B -18 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS B -17 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER B -16 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER B -15 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY B -14 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ VAL B -13 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASP B -12 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU B -11 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY B -10 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ THR B -9 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLU B -8 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN B -7 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU B -6 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ TYR B -5 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ PHE B -4 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLN B -3 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER B -2 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN B -1 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ALA B 0 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ MET C -23 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS C -22 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS C -21 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS C -20 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS C -19 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS C -18 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS C -17 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER C -16 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER C -15 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY C -14 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ VAL C -13 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASP C -12 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU C -11 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY C -10 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ THR C -9 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLU C -8 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN C -7 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU C -6 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ TYR C -5 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ PHE C -4 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLN C -3 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER C -2 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN C -1 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ALA C 0 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ MET D -23 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS D -22 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS D -21 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS D -20 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS D -19 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS D -18 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ HIS D -17 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER D -16 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER D -15 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY D -14 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ VAL D -13 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASP D -12 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU D -11 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLY D -10 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ THR D -9 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLU D -8 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN D -7 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ LEU D -6 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ TYR D -5 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ PHE D -4 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ GLN D -3 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ SER D -2 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ASN D -1 UNP Q9KVT3 EXPRESSION TAG
SEQADV 3PGJ ALA D 0 UNP Q9KVT3 EXPRESSION TAG
SEQRES 1 A 302 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 302 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ALA
SEQRES 3 A 302 SER GLN ILE ASP GLN TYR ALA VAL PHE GLY ASN PRO ILE
SEQRES 4 A 302 ASN HIS SER LYS SER PRO PHE ILE HIS THR LEU PHE ALA
SEQRES 5 A 302 ARG GLN THR GLN GLN SER MET ILE TYR THR ALA GLN CYS
SEQRES 6 A 302 VAL PRO VAL ASP GLY PHE THR GLU ALA ALA LYS HIS PHE
SEQRES 7 A 302 PHE ALA GLN GLY GLY ARG GLY CYS ASN VAL THR VAL PRO
SEQRES 8 A 302 PHE LYS GLU GLU ALA TYR ARG PHE ALA ASP ARG LEU THR
SEQRES 9 A 302 GLU ARG ALA ARG LEU ALA GLY ALA VAL ASN THR LEU LYS
SEQRES 10 A 302 LYS LEU ASP ASP GLY GLU ILE LEU GLY ASP ASN THR ASP
SEQRES 11 A 302 GLY GLU GLY LEU VAL GLN ASP LEU LEU ALA GLN GLN VAL
SEQRES 12 A 302 LEU LEU LYS GLY ALA THR ILE LEU LEU ILE GLY ALA GLY
SEQRES 13 A 302 GLY ALA ALA ARG GLY VAL LEU LYS PRO LEU LEU ASP GLN
SEQRES 14 A 302 GLN PRO ALA SER ILE THR VAL THR ASN ARG THR PHE ALA
SEQRES 15 A 302 LYS ALA GLU GLN LEU ALA GLU LEU VAL ALA ALA TYR GLY
SEQRES 16 A 302 GLU VAL LYS ALA GLN ALA PHE GLU GLN LEU LYS GLN SER
SEQRES 17 A 302 TYR ASP VAL ILE ILE ASN SER THR SER ALA SER LEU ASP
SEQRES 18 A 302 GLY GLU LEU PRO ALA ILE ASP PRO VAL ILE PHE SER SER
SEQRES 19 A 302 ARG SER VAL CYS TYR ASP MET MET TYR GLY LYS GLY TYR
SEQRES 20 A 302 THR VAL PHE ASN GLN TRP ALA ARG GLN HIS GLY CYS ALA
SEQRES 21 A 302 GLN ALA ILE ASP GLY LEU GLY MET LEU VAL GLY GLN ALA
SEQRES 22 A 302 ALA GLU SER PHE MET LEU TRP ARG GLY LEU ARG PRO GLY
SEQRES 23 A 302 THR LYS GLN ILE LEU ARG GLU LEU ARG LYS ASN LEU GLU
SEQRES 24 A 302 GLY ALA LEU
SEQRES 1 B 302 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 302 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ALA
SEQRES 3 B 302 SER GLN ILE ASP GLN TYR ALA VAL PHE GLY ASN PRO ILE
SEQRES 4 B 302 ASN HIS SER LYS SER PRO PHE ILE HIS THR LEU PHE ALA
SEQRES 5 B 302 ARG GLN THR GLN GLN SER MET ILE TYR THR ALA GLN CYS
SEQRES 6 B 302 VAL PRO VAL ASP GLY PHE THR GLU ALA ALA LYS HIS PHE
SEQRES 7 B 302 PHE ALA GLN GLY GLY ARG GLY CYS ASN VAL THR VAL PRO
SEQRES 8 B 302 PHE LYS GLU GLU ALA TYR ARG PHE ALA ASP ARG LEU THR
SEQRES 9 B 302 GLU ARG ALA ARG LEU ALA GLY ALA VAL ASN THR LEU LYS
SEQRES 10 B 302 LYS LEU ASP ASP GLY GLU ILE LEU GLY ASP ASN THR ASP
SEQRES 11 B 302 GLY GLU GLY LEU VAL GLN ASP LEU LEU ALA GLN GLN VAL
SEQRES 12 B 302 LEU LEU LYS GLY ALA THR ILE LEU LEU ILE GLY ALA GLY
SEQRES 13 B 302 GLY ALA ALA ARG GLY VAL LEU LYS PRO LEU LEU ASP GLN
SEQRES 14 B 302 GLN PRO ALA SER ILE THR VAL THR ASN ARG THR PHE ALA
SEQRES 15 B 302 LYS ALA GLU GLN LEU ALA GLU LEU VAL ALA ALA TYR GLY
SEQRES 16 B 302 GLU VAL LYS ALA GLN ALA PHE GLU GLN LEU LYS GLN SER
SEQRES 17 B 302 TYR ASP VAL ILE ILE ASN SER THR SER ALA SER LEU ASP
SEQRES 18 B 302 GLY GLU LEU PRO ALA ILE ASP PRO VAL ILE PHE SER SER
SEQRES 19 B 302 ARG SER VAL CYS TYR ASP MET MET TYR GLY LYS GLY TYR
SEQRES 20 B 302 THR VAL PHE ASN GLN TRP ALA ARG GLN HIS GLY CYS ALA
SEQRES 21 B 302 GLN ALA ILE ASP GLY LEU GLY MET LEU VAL GLY GLN ALA
SEQRES 22 B 302 ALA GLU SER PHE MET LEU TRP ARG GLY LEU ARG PRO GLY
SEQRES 23 B 302 THR LYS GLN ILE LEU ARG GLU LEU ARG LYS ASN LEU GLU
SEQRES 24 B 302 GLY ALA LEU
SEQRES 1 C 302 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 302 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ALA
SEQRES 3 C 302 SER GLN ILE ASP GLN TYR ALA VAL PHE GLY ASN PRO ILE
SEQRES 4 C 302 ASN HIS SER LYS SER PRO PHE ILE HIS THR LEU PHE ALA
SEQRES 5 C 302 ARG GLN THR GLN GLN SER MET ILE TYR THR ALA GLN CYS
SEQRES 6 C 302 VAL PRO VAL ASP GLY PHE THR GLU ALA ALA LYS HIS PHE
SEQRES 7 C 302 PHE ALA GLN GLY GLY ARG GLY CYS ASN VAL THR VAL PRO
SEQRES 8 C 302 PHE LYS GLU GLU ALA TYR ARG PHE ALA ASP ARG LEU THR
SEQRES 9 C 302 GLU ARG ALA ARG LEU ALA GLY ALA VAL ASN THR LEU LYS
SEQRES 10 C 302 LYS LEU ASP ASP GLY GLU ILE LEU GLY ASP ASN THR ASP
SEQRES 11 C 302 GLY GLU GLY LEU VAL GLN ASP LEU LEU ALA GLN GLN VAL
SEQRES 12 C 302 LEU LEU LYS GLY ALA THR ILE LEU LEU ILE GLY ALA GLY
SEQRES 13 C 302 GLY ALA ALA ARG GLY VAL LEU LYS PRO LEU LEU ASP GLN
SEQRES 14 C 302 GLN PRO ALA SER ILE THR VAL THR ASN ARG THR PHE ALA
SEQRES 15 C 302 LYS ALA GLU GLN LEU ALA GLU LEU VAL ALA ALA TYR GLY
SEQRES 16 C 302 GLU VAL LYS ALA GLN ALA PHE GLU GLN LEU LYS GLN SER
SEQRES 17 C 302 TYR ASP VAL ILE ILE ASN SER THR SER ALA SER LEU ASP
SEQRES 18 C 302 GLY GLU LEU PRO ALA ILE ASP PRO VAL ILE PHE SER SER
SEQRES 19 C 302 ARG SER VAL CYS TYR ASP MET MET TYR GLY LYS GLY TYR
SEQRES 20 C 302 THR VAL PHE ASN GLN TRP ALA ARG GLN HIS GLY CYS ALA
SEQRES 21 C 302 GLN ALA ILE ASP GLY LEU GLY MET LEU VAL GLY GLN ALA
SEQRES 22 C 302 ALA GLU SER PHE MET LEU TRP ARG GLY LEU ARG PRO GLY
SEQRES 23 C 302 THR LYS GLN ILE LEU ARG GLU LEU ARG LYS ASN LEU GLU
SEQRES 24 C 302 GLY ALA LEU
SEQRES 1 D 302 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 302 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET ALA
SEQRES 3 D 302 SER GLN ILE ASP GLN TYR ALA VAL PHE GLY ASN PRO ILE
SEQRES 4 D 302 ASN HIS SER LYS SER PRO PHE ILE HIS THR LEU PHE ALA
SEQRES 5 D 302 ARG GLN THR GLN GLN SER MET ILE TYR THR ALA GLN CYS
SEQRES 6 D 302 VAL PRO VAL ASP GLY PHE THR GLU ALA ALA LYS HIS PHE
SEQRES 7 D 302 PHE ALA GLN GLY GLY ARG GLY CYS ASN VAL THR VAL PRO
SEQRES 8 D 302 PHE LYS GLU GLU ALA TYR ARG PHE ALA ASP ARG LEU THR
SEQRES 9 D 302 GLU ARG ALA ARG LEU ALA GLY ALA VAL ASN THR LEU LYS
SEQRES 10 D 302 LYS LEU ASP ASP GLY GLU ILE LEU GLY ASP ASN THR ASP
SEQRES 11 D 302 GLY GLU GLY LEU VAL GLN ASP LEU LEU ALA GLN GLN VAL
SEQRES 12 D 302 LEU LEU LYS GLY ALA THR ILE LEU LEU ILE GLY ALA GLY
SEQRES 13 D 302 GLY ALA ALA ARG GLY VAL LEU LYS PRO LEU LEU ASP GLN
SEQRES 14 D 302 GLN PRO ALA SER ILE THR VAL THR ASN ARG THR PHE ALA
SEQRES 15 D 302 LYS ALA GLU GLN LEU ALA GLU LEU VAL ALA ALA TYR GLY
SEQRES 16 D 302 GLU VAL LYS ALA GLN ALA PHE GLU GLN LEU LYS GLN SER
SEQRES 17 D 302 TYR ASP VAL ILE ILE ASN SER THR SER ALA SER LEU ASP
SEQRES 18 D 302 GLY GLU LEU PRO ALA ILE ASP PRO VAL ILE PHE SER SER
SEQRES 19 D 302 ARG SER VAL CYS TYR ASP MET MET TYR GLY LYS GLY TYR
SEQRES 20 D 302 THR VAL PHE ASN GLN TRP ALA ARG GLN HIS GLY CYS ALA
SEQRES 21 D 302 GLN ALA ILE ASP GLY LEU GLY MET LEU VAL GLY GLN ALA
SEQRES 22 D 302 ALA GLU SER PHE MET LEU TRP ARG GLY LEU ARG PRO GLY
SEQRES 23 D 302 THR LYS GLN ILE LEU ARG GLU LEU ARG LYS ASN LEU GLU
SEQRES 24 D 302 GLY ALA LEU
HET SKM A 279 12
HET SKM B 279 12
HET SKM C 279 12
HET SKM D 279 12
HETNAM SKM (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC
HETNAM 2 SKM ACID
HETSYN SKM SHIKIMATE
FORMUL 5 SKM 4(C7 H10 O5)
FORMUL 9 HOH *115(H2 O)
HELIX 1 1 LYS A 19 GLN A 32 1 14
HELIX 2 2 GLY A 46 GLN A 57 1 12
HELIX 3 3 PHE A 68 ALA A 76 1 9
HELIX 4 4 THR A 80 GLY A 87 1 8
HELIX 5 5 THR A 105 GLN A 117 1 13
HELIX 6 6 GLY A 132 GLN A 145 1 14
HELIX 7 7 THR A 156 ALA A 168 1 13
HELIX 8 8 ALA A 169 GLY A 171 5 3
HELIX 9 9 GLU A 179 LEU A 181 5 3
HELIX 10 10 SER A 193 GLY A 198 1 6
HELIX 11 11 ASP A 204 PHE A 208 5 5
HELIX 12 12 THR A 224 HIS A 233 1 10
HELIX 13 13 GLY A 241 GLY A 258 1 18
HELIX 14 14 THR A 263 GLU A 275 1 13
HELIX 15 15 LYS B 19 THR B 31 1 13
HELIX 16 16 ASP B 45 GLN B 57 1 13
HELIX 17 17 PHE B 68 ALA B 76 1 9
HELIX 18 18 THR B 80 GLY B 87 1 8
HELIX 19 19 THR B 105 GLN B 117 1 13
HELIX 20 20 GLY B 132 GLY B 137 1 6
HELIX 21 21 VAL B 138 GLN B 145 1 8
HELIX 22 22 THR B 156 ALA B 169 1 14
HELIX 23 23 GLU B 179 LEU B 181 5 3
HELIX 24 24 ASP B 204 PHE B 208 5 5
HELIX 25 25 THR B 224 HIS B 233 1 10
HELIX 26 26 GLY B 241 GLY B 258 1 18
HELIX 27 27 THR B 263 GLU B 275 1 13
HELIX 28 28 LYS C 19 THR C 31 1 13
HELIX 29 29 GLY C 46 GLN C 57 1 12
HELIX 30 30 PHE C 68 ALA C 76 1 9
HELIX 31 31 THR C 80 GLY C 87 1 8
HELIX 32 32 THR C 105 GLN C 117 1 13
HELIX 33 33 GLY C 132 GLY C 137 1 6
HELIX 34 34 VAL C 138 GLN C 145 1 8
HELIX 35 35 THR C 156 ALA C 168 1 13
HELIX 36 36 ASP C 204 VAL C 206 5 3
HELIX 37 37 THR C 224 HIS C 233 1 10
HELIX 38 38 GLY C 241 GLY C 258 1 18
HELIX 39 39 THR C 263 GLU C 275 1 13
HELIX 40 40 LYS D 19 THR D 31 1 13
HELIX 41 41 GLY D 46 GLN D 57 1 12
HELIX 42 42 PHE D 68 ALA D 76 1 9
HELIX 43 43 THR D 80 GLY D 87 1 8
HELIX 44 44 THR D 105 GLN D 117 1 13
HELIX 45 45 GLY D 132 ASP D 144 1 13
HELIX 46 46 THR D 156 VAL D 167 1 12
HELIX 47 47 ALA D 168 GLY D 171 5 4
HELIX 48 48 GLU D 179 LEU D 181 5 3
HELIX 49 49 SER D 193 GLY D 198 5 6
HELIX 50 50 ASP D 204 PHE D 208 5 5
HELIX 51 51 THR D 224 HIS D 233 1 10
HELIX 52 52 GLY D 241 GLY D 258 1 18
HELIX 53 53 THR D 263 GLU D 275 1 13
SHEET 1 A 6 MET A 35 CYS A 41 0
SHEET 2 A 6 ASP A 6 GLY A 12 1 N ASP A 6 O ILE A 36
SHEET 3 A 6 GLY A 59 VAL A 64 1 O ASN A 63 N ALA A 9
SHEET 4 A 6 THR A 91 LYS A 94 -1 O LYS A 94 N ARG A 60
SHEET 5 A 6 ILE A 100 ASP A 103 -1 O LEU A 101 N LYS A 93
SHEET 6 A 6 ARG A 78 LEU A 79 1 N ARG A 78 O GLY A 102
SHEET 1 B 6 VAL A 173 ALA A 177 0
SHEET 2 B 6 SER A 149 ASN A 154 1 N VAL A 152 O LYS A 174
SHEET 3 B 6 THR A 125 ILE A 129 1 N ILE A 126 O THR A 151
SHEET 4 B 6 VAL A 187 ASN A 190 1 O ILE A 189 N LEU A 127
SHEET 5 B 6 VAL A 213 ASP A 216 1 O TYR A 215 N ILE A 188
SHEET 6 B 6 GLN A 237 ILE A 239 1 O GLN A 237 N CYS A 214
SHEET 1 C 6 MET B 35 CYS B 41 0
SHEET 2 C 6 ASP B 6 GLY B 12 1 N VAL B 10 O GLN B 40
SHEET 3 C 6 GLY B 61 VAL B 64 1 O ASN B 63 N ALA B 9
SHEET 4 C 6 THR B 91 LYS B 94 -1 O LEU B 92 N CYS B 62
SHEET 5 C 6 ILE B 100 ASP B 103 -1 O LEU B 101 N LYS B 93
SHEET 6 C 6 ARG B 78 LEU B 79 1 N ARG B 78 O GLY B 102
SHEET 1 D 6 VAL B 173 ALA B 177 0
SHEET 2 D 6 SER B 149 ASN B 154 1 N VAL B 152 O GLN B 176
SHEET 3 D 6 THR B 125 ILE B 129 1 N ILE B 126 O THR B 151
SHEET 4 D 6 VAL B 187 ASN B 190 1 O ILE B 189 N ILE B 129
SHEET 5 D 6 VAL B 213 ASP B 216 1 O TYR B 215 N ILE B 188
SHEET 6 D 6 GLN B 237 ILE B 239 1 O ILE B 239 N CYS B 214
SHEET 1 E 6 MET C 35 CYS C 41 0
SHEET 2 E 6 ASP C 6 GLY C 12 1 N VAL C 10 O GLN C 40
SHEET 3 E 6 GLY C 61 VAL C 64 1 O ASN C 63 N PHE C 11
SHEET 4 E 6 THR C 91 LYS C 94 -1 O LEU C 92 N CYS C 62
SHEET 5 E 6 ILE C 100 ASP C 103 -1 O LEU C 101 N LYS C 93
SHEET 6 E 6 ARG C 78 LEU C 79 1 N ARG C 78 O GLY C 102
SHEET 1 F 6 VAL C 173 ALA C 177 0
SHEET 2 F 6 SER C 149 ASN C 154 1 N VAL C 152 O LYS C 174
SHEET 3 F 6 THR C 125 ILE C 129 1 N LEU C 128 O THR C 151
SHEET 4 F 6 TYR C 185 ASN C 190 1 O ILE C 189 N ILE C 129
SHEET 5 F 6 PHE C 208 ASP C 216 1 O VAL C 213 N ASP C 186
SHEET 6 F 6 GLN C 237 ILE C 239 1 O ILE C 239 N CYS C 214
SHEET 1 G 6 MET D 35 CYS D 41 0
SHEET 2 G 6 ASP D 6 GLY D 12 1 N VAL D 10 O GLN D 40
SHEET 3 G 6 GLY D 59 VAL D 64 1 O ASN D 63 N PHE D 11
SHEET 4 G 6 THR D 91 LYS D 94 -1 O LYS D 94 N ARG D 60
SHEET 5 G 6 ILE D 100 ASP D 103 -1 O LEU D 101 N LYS D 93
SHEET 6 G 6 ARG D 78 LEU D 79 1 N ARG D 78 O GLY D 102
SHEET 1 H 6 VAL D 173 ALA D 177 0
SHEET 2 H 6 SER D 149 ASN D 154 1 N VAL D 152 O GLN D 176
SHEET 3 H 6 THR D 125 ILE D 129 1 N ILE D 126 O THR D 151
SHEET 4 H 6 VAL D 187 ASN D 190 1 O ILE D 189 N LEU D 127
SHEET 5 H 6 VAL D 213 ASP D 216 1 O TYR D 215 N ILE D 188
SHEET 6 H 6 GLN D 237 ILE D 239 1 O GLN D 237 N CYS D 214
SSBOND 1 CYS A 41 CYS D 41 1555 1555 2.05
SSBOND 2 CYS B 41 CYS C 41 1555 1555 2.05
CISPEP 1 ASN A 13 PRO A 14 0 -1.28
CISPEP 2 PRO A 14 ILE A 15 0 0.72
CISPEP 3 VAL A 66 PRO A 67 0 0.55
CISPEP 4 VAL B 66 PRO B 67 0 -0.09
CISPEP 5 ASN C 13 PRO C 14 0 0.06
CISPEP 6 VAL C 66 PRO C 67 0 0.18
CISPEP 7 ASN D 13 PRO D 14 0 0.09
CISPEP 8 VAL D 66 PRO D 67 0 0.45
SITE 1 AC1 9 SER A 18 SER A 20 ASN A 63 THR A 65
SITE 2 AC1 9 LYS A 69 ASN A 90 ASP A 106 GLN A 248
SITE 3 AC1 9 HOH A 287
SITE 1 AC2 10 VAL B 10 SER B 18 SER B 20 ASN B 63
SITE 2 AC2 10 THR B 65 LYS B 69 ASN B 90 ASP B 106
SITE 3 AC2 10 GLN B 248 HOH B 297
SITE 1 AC3 9 VAL C 10 SER C 18 SER C 20 ASN C 63
SITE 2 AC3 9 THR C 65 LYS C 69 ASN C 90 ASP C 106
SITE 3 AC3 9 GLN C 248
SITE 1 AC4 8 VAL D 10 SER D 18 SER D 20 THR D 65
SITE 2 AC4 8 LYS D 69 ASN D 90 ASP D 106 GLN D 248
CRYST1 75.527 83.657 79.585 90.00 93.51 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013240 0.000000 0.000813 0.00000
SCALE2 0.000000 0.011954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012589 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
