HEADER TRANSFERASE 27-NOV-06 2O0L
TITLE HUMAN SPERMIDINE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPERMIDINE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PUTRESCINE AMINOPROPYLTRANSFERASE, SPDSY;
COMPND 5 EC: 2.5.1.16;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SRM, SPS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SPERMIDINE SYNTHASE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MIN,H.WU,H.ZENG,P.LOPPNAU,J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,A.BOCHKAREV,A.N.PLOTNIKOV,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (SGC)
REVDAT 5 27-DEC-23 2O0L 1 REMARK SEQADV
REVDAT 4 13-JUL-11 2O0L 1 VERSN
REVDAT 3 24-FEB-09 2O0L 1 VERSN
REVDAT 2 18-SEP-07 2O0L 1 JRNL
REVDAT 1 12-DEC-06 2O0L 0
JRNL AUTH H.WU,J.MIN,Y.IKEGUCHI,H.ZENG,A.DONG,P.LOPPNAU,A.E.PEGG,
JRNL AUTH 2 A.N.PLOTNIKOV
JRNL TITL STRUCTURE AND MECHANISM OF SPERMIDINE SYNTHASES.
JRNL REF BIOCHEMISTRY V. 46 8331 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17585781
JRNL DOI 10.1021/BI602498K
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 36969
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1945
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) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.04
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2445
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 124
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4443
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 265
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.25000
REMARK 3 B22 (A**2) : -0.38000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.216
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.195
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.898
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4596 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6225 ; 1.521 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 556 ; 6.787 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 217 ;36.311 ;24.608
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 787 ;14.717 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;19.166 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 681 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3483 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2172 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3050 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 324 ; 0.158 ; 0.200
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): 55 ; 0.182 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.211 ; 0.200
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): 2904 ; 0.718 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4511 ; 1.079 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1977 ; 2.041 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1714 ; 2.922 ; 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 : 30
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 16 A 36
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3168 21.7112 67.3151
REMARK 3 T TENSOR
REMARK 3 T11: 0.0078 T22: 0.1084
REMARK 3 T33: 0.0972 T12: 0.0130
REMARK 3 T13: 0.0153 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 0.8158 L22: 2.1675
REMARK 3 L33: 6.0630 L12: 0.7268
REMARK 3 L13: -0.7987 L23: -1.8995
REMARK 3 S TENSOR
REMARK 3 S11: 0.0316 S12: -0.0523 S13: 0.1380
REMARK 3 S21: 0.1496 S22: 0.1361 S23: 0.2750
REMARK 3 S31: -0.0170 S32: -0.4070 S33: -0.1677
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 37 A 54
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5420 28.4169 81.0850
REMARK 3 T TENSOR
REMARK 3 T11: 0.0936 T22: 0.0948
REMARK 3 T33: 0.0429 T12: -0.0266
REMARK 3 T13: 0.0696 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 3.0368 L22: 6.1781
REMARK 3 L33: 1.2351 L12: 0.2886
REMARK 3 L13: -1.7095 L23: -1.4576
REMARK 3 S TENSOR
REMARK 3 S11: 0.1772 S12: -0.1315 S13: 0.3747
REMARK 3 S21: 0.4630 S22: 0.0781 S23: 0.4471
REMARK 3 S31: -0.2571 S32: 0.0430 S33: -0.2553
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 55 A 72
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1096 21.4648 75.2062
REMARK 3 T TENSOR
REMARK 3 T11: 0.0759 T22: 0.0935
REMARK 3 T33: 0.0338 T12: -0.0050
REMARK 3 T13: 0.0331 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 2.1143 L22: 0.1187
REMARK 3 L33: 1.3448 L12: -0.5005
REMARK 3 L13: 0.4086 L23: -0.0790
REMARK 3 S TENSOR
REMARK 3 S11: -0.0150 S12: 0.0536 S13: 0.1127
REMARK 3 S21: 0.0100 S22: 0.0290 S23: 0.0340
REMARK 3 S31: 0.0542 S32: -0.1670 S33: -0.0140
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 73 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8991 24.7276 69.3560
REMARK 3 T TENSOR
REMARK 3 T11: 0.0752 T22: 0.0812
REMARK 3 T33: 0.0494 T12: 0.0091
REMARK 3 T13: -0.0025 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 3.6703 L22: 2.5365
REMARK 3 L33: 1.3012 L12: 1.8389
REMARK 3 L13: -1.4604 L23: -1.3155
REMARK 3 S TENSOR
REMARK 3 S11: 0.1228 S12: -0.0406 S13: 0.0422
REMARK 3 S21: 0.2289 S22: -0.0710 S23: -0.0187
REMARK 3 S31: -0.1087 S32: 0.0652 S33: -0.0518
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 94 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): 42.4313 31.6555 76.2371
REMARK 3 T TENSOR
REMARK 3 T11: 0.1108 T22: 0.0808
REMARK 3 T33: 0.0336 T12: -0.0168
REMARK 3 T13: -0.0241 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.8921 L22: 2.6670
REMARK 3 L33: 1.8813 L12: -0.3482
REMARK 3 L13: -0.8599 L23: -0.4551
REMARK 3 S TENSOR
REMARK 3 S11: 0.1645 S12: -0.1403 S13: 0.0162
REMARK 3 S21: 0.2720 S22: -0.1481 S23: -0.2196
REMARK 3 S31: -0.1222 S32: 0.1465 S33: -0.0164
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 122 A 146
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7771 30.2195 83.2871
REMARK 3 T TENSOR
REMARK 3 T11: 0.1527 T22: 0.0901
REMARK 3 T33: -0.0170 T12: -0.0590
REMARK 3 T13: 0.0220 T23: -0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 2.3225 L22: 2.2283
REMARK 3 L33: 0.8705 L12: 1.0103
REMARK 3 L13: -0.5059 L23: -1.3862
REMARK 3 S TENSOR
REMARK 3 S11: 0.2829 S12: -0.3169 S13: 0.0927
REMARK 3 S21: 0.3417 S22: -0.2218 S23: -0.0338
REMARK 3 S31: -0.1368 S32: -0.0206 S33: -0.0611
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 147 A 175
REMARK 3 ORIGIN FOR THE GROUP (A): 37.6358 41.6742 74.3586
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.0466
REMARK 3 T33: 0.0414 T12: -0.0179
REMARK 3 T13: 0.0383 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 2.1772 L22: 2.1458
REMARK 3 L33: 0.9434 L12: -0.2859
REMARK 3 L13: 0.4063 L23: 0.5922
REMARK 3 S TENSOR
REMARK 3 S11: 0.1302 S12: -0.0868 S13: 0.1071
REMARK 3 S21: 0.1537 S22: -0.0675 S23: 0.1036
REMARK 3 S31: -0.0970 S32: -0.0936 S33: -0.0627
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 : A 187 A 202
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6600 43.8041 64.4324
REMARK 3 T TENSOR
REMARK 3 T11: 0.0936 T22: 0.0437
REMARK 3 T33: 0.0646 T12: -0.0157
REMARK 3 T13: 0.0326 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 7.2186 L22: 5.3063
REMARK 3 L33: 4.2792 L12: -2.2361
REMARK 3 L13: -0.5932 L23: 0.5379
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: 0.1530 S13: 0.0547
REMARK 3 S21: -0.1017 S22: 0.0019 S23: 0.0906
REMARK 3 S31: -0.2131 S32: 0.0104 S33: -0.0376
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 : A 203 A 218
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6608 30.7312 56.4899
REMARK 3 T TENSOR
REMARK 3 T11: 0.0160 T22: 0.0663
REMARK 3 T33: 0.1124 T12: 0.0172
REMARK 3 T13: 0.0129 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 3.2276 L22: 0.5815
REMARK 3 L33: 1.4907 L12: 1.3592
REMARK 3 L13: 1.1631 L23: 0.5887
REMARK 3 S TENSOR
REMARK 3 S11: 0.0151 S12: -0.0064 S13: 0.2589
REMARK 3 S21: 0.1564 S22: -0.0364 S23: 0.0859
REMARK 3 S31: -0.0042 S32: -0.1016 S33: 0.0213
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 : A 219 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3130 39.4319 52.9017
REMARK 3 T TENSOR
REMARK 3 T11: 0.0679 T22: 0.0193
REMARK 3 T33: 0.0541 T12: 0.0592
REMARK 3 T13: 0.0113 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 31.7525 L22: 12.8610
REMARK 3 L33: 11.6579 L12: 12.2780
REMARK 3 L13: 4.9307 L23: 2.3617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: 0.4775 S13: -0.0364
REMARK 3 S21: -0.2221 S22: 0.1283 S23: 0.4164
REMARK 3 S31: 0.0411 S32: -0.0518 S33: -0.1646
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 : A 226 A 248
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1993 28.1866 60.0114
REMARK 3 T TENSOR
REMARK 3 T11: 0.0541 T22: 0.0772
REMARK 3 T33: 0.0440 T12: 0.0021
REMARK 3 T13: 0.0062 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.5142 L22: 2.9701
REMARK 3 L33: 0.1583 L12: 1.6864
REMARK 3 L13: -0.3902 L23: -0.6182
REMARK 3 S TENSOR
REMARK 3 S11: 0.0820 S12: -0.0317 S13: -0.0318
REMARK 3 S21: 0.1087 S22: -0.1008 S23: -0.0349
REMARK 3 S31: -0.0593 S32: 0.0412 S33: 0.0188
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 : A 249 A 263
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7722 32.8188 58.5246
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.0531
REMARK 3 T33: 0.0987 T12: 0.0121
REMARK 3 T13: 0.0165 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.0984 L22: 2.6087
REMARK 3 L33: 2.9606 L12: -1.0464
REMARK 3 L13: -0.0114 L23: 0.2350
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: 0.0419 S13: -0.1952
REMARK 3 S21: -0.2536 S22: 0.0673 S23: -0.1098
REMARK 3 S31: 0.1065 S32: 0.0445 S33: -0.1204
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 : A 264 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): 48.6500 17.8429 71.5007
REMARK 3 T TENSOR
REMARK 3 T11: 0.0577 T22: 0.1085
REMARK 3 T33: 0.0656 T12: 0.0016
REMARK 3 T13: -0.0660 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 5.5175 L22: 7.6161
REMARK 3 L33: 5.0428 L12: 3.8789
REMARK 3 L13: -5.0652 L23: -2.1753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0254 S12: -0.3252 S13: -0.1467
REMARK 3 S21: 0.4538 S22: -0.1925 S23: -0.4474
REMARK 3 S31: -0.1687 S32: 0.3586 S33: 0.2179
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 : A 277 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4489 20.6765 58.0684
REMARK 3 T TENSOR
REMARK 3 T11: 0.0534 T22: 0.0573
REMARK 3 T33: 0.1023 T12: -0.0043
REMARK 3 T13: 0.0113 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 2.0900 L22: 0.6372
REMARK 3 L33: 5.5300 L12: -0.5572
REMARK 3 L13: 2.5125 L23: -1.3458
REMARK 3 S TENSOR
REMARK 3 S11: -0.0534 S12: 0.0437 S13: -0.0160
REMARK 3 S21: 0.0031 S22: -0.0066 S23: -0.0455
REMARK 3 S31: 0.0729 S32: 0.0881 S33: 0.0600
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 : A 295 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7923 28.9566 44.6893
REMARK 3 T TENSOR
REMARK 3 T11: 0.0706 T22: -0.0039
REMARK 3 T33: 0.0627 T12: -0.0140
REMARK 3 T13: 0.0017 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 14.5993 L22: 10.0703
REMARK 3 L33: 15.0278 L12: 4.5749
REMARK 3 L13: -5.9887 L23: 0.8543
REMARK 3 S TENSOR
REMARK 3 S11: -0.1969 S12: 0.1563 S13: 0.5053
REMARK 3 S21: -0.9725 S22: 0.0952 S23: -0.0139
REMARK 3 S31: -0.8780 S32: 0.1321 S33: 0.1017
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 : B 15 B 20
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1973 16.8907 61.4257
REMARK 3 T TENSOR
REMARK 3 T11: 0.0456 T22: 0.1526
REMARK 3 T33: 0.0701 T12: -0.0595
REMARK 3 T13: -0.0058 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 15.7266 L22: 13.6645
REMARK 3 L33: 24.1305 L12: 8.7037
REMARK 3 L13: -10.1211 L23: 2.0339
REMARK 3 S TENSOR
REMARK 3 S11: -0.4654 S12: -0.5668 S13: -0.9743
REMARK 3 S21: 1.5743 S22: 0.2270 S23: -0.5310
REMARK 3 S31: 1.3853 S32: -1.6875 S33: 0.2384
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 21 B 38
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2875 12.6087 62.2916
REMARK 3 T TENSOR
REMARK 3 T11: 0.0326 T22: 0.0999
REMARK 3 T33: 0.0585 T12: -0.0028
REMARK 3 T13: 0.0447 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 3.4309 L22: 0.6050
REMARK 3 L33: 1.2157 L12: -0.7849
REMARK 3 L13: 1.8472 L23: -0.1159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: -0.0736 S13: -0.1788
REMARK 3 S21: 0.0882 S22: -0.0024 S23: 0.1054
REMARK 3 S31: 0.0383 S32: -0.0724 S33: 0.0085
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 39 B 45
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6002 8.0915 49.6763
REMARK 3 T TENSOR
REMARK 3 T11: -0.0691 T22: 0.1110
REMARK 3 T33: 0.1751 T12: 0.0244
REMARK 3 T13: 0.0303 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 1.8513 L22: 30.7770
REMARK 3 L33: 6.8663 L12: 4.7207
REMARK 3 L13: 2.1019 L23: -3.8031
REMARK 3 S TENSOR
REMARK 3 S11: 0.1886 S12: 0.0057 S13: -0.3308
REMARK 3 S21: -0.1364 S22: -0.2157 S23: 1.2043
REMARK 3 S31: 0.2602 S32: -0.0717 S33: 0.0271
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 46 B 77
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5414 10.7078 50.7637
REMARK 3 T TENSOR
REMARK 3 T11: 0.0271 T22: 0.0861
REMARK 3 T33: 0.0756 T12: 0.0005
REMARK 3 T13: 0.0070 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 2.4381 L22: 0.9507
REMARK 3 L33: 0.9896 L12: 0.8295
REMARK 3 L13: -0.0840 L23: -0.3687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0857 S12: 0.0443 S13: -0.1797
REMARK 3 S21: -0.0268 S22: 0.0053 S23: 0.0761
REMARK 3 S31: 0.0278 S32: -0.0804 S33: 0.0804
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 78 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3002 4.1721 40.0169
REMARK 3 T TENSOR
REMARK 3 T11: 0.0348 T22: 0.0648
REMARK 3 T33: 0.0813 T12: 0.0055
REMARK 3 T13: -0.0005 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.6321 L22: 1.0371
REMARK 3 L33: 1.4668 L12: 0.3996
REMARK 3 L13: -0.0531 L23: 0.0863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0022 S12: 0.0487 S13: -0.0974
REMARK 3 S21: -0.1104 S22: 0.0002 S23: 0.0269
REMARK 3 S31: -0.0357 S32: 0.0219 S33: 0.0020
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 125 B 144
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4041 5.5249 40.8162
REMARK 3 T TENSOR
REMARK 3 T11: 0.0163 T22: 0.0693
REMARK 3 T33: 0.0901 T12: 0.0122
REMARK 3 T13: -0.0465 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 2.1026 L22: 3.5173
REMARK 3 L33: 1.3863 L12: -1.5835
REMARK 3 L13: -0.7818 L23: -0.9153
REMARK 3 S TENSOR
REMARK 3 S11: 0.1371 S12: 0.1737 S13: -0.3075
REMARK 3 S21: -0.1737 S22: -0.1113 S23: 0.1929
REMARK 3 S31: -0.0594 S32: -0.1953 S33: -0.0257
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 145 B 177
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9628 -5.8984 42.5017
REMARK 3 T TENSOR
REMARK 3 T11: 0.0309 T22: 0.0560
REMARK 3 T33: 0.0948 T12: -0.0128
REMARK 3 T13: 0.0160 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.4714 L22: 3.4664
REMARK 3 L33: 1.8500 L12: 0.2517
REMARK 3 L13: -0.1690 L23: -0.3621
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: -0.0390 S13: -0.1333
REMARK 3 S21: 0.1922 S22: -0.0679 S23: 0.1826
REMARK 3 S31: 0.0326 S32: -0.1500 S33: 0.0159
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 178 B 186
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0062 -6.8362 56.1447
REMARK 3 T TENSOR
REMARK 3 T11: 0.0632 T22: 0.0621
REMARK 3 T33: 0.1549 T12: 0.0601
REMARK 3 T13: 0.0497 T23: 0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 0.3262 L22: 9.0167
REMARK 3 L33: 22.0930 L12: -1.6772
REMARK 3 L13: 1.4970 L23: -5.2500
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: -1.3270 S13: -0.0349
REMARK 3 S21: 1.0521 S22: -0.1238 S23: 0.1579
REMARK 3 S31: 0.6304 S32: 0.4646 S33: 0.1076
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 187 B 207
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4303 -7.0147 48.3880
REMARK 3 T TENSOR
REMARK 3 T11: 0.0487 T22: 0.0817
REMARK 3 T33: 0.1055 T12: 0.0054
REMARK 3 T13: -0.0003 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 2.7824 L22: 4.5166
REMARK 3 L33: 2.7434 L12: -0.1341
REMARK 3 L13: 0.6227 L23: -0.3301
REMARK 3 S TENSOR
REMARK 3 S11: -0.0440 S12: -0.1542 S13: -0.0407
REMARK 3 S21: 0.2650 S22: 0.1290 S23: 0.1197
REMARK 3 S31: 0.2132 S32: -0.0688 S33: -0.0850
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 208 B 220
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7800 3.6973 64.4593
REMARK 3 T TENSOR
REMARK 3 T11: 0.0635 T22: 0.0657
REMARK 3 T33: 0.0508 T12: -0.0226
REMARK 3 T13: 0.0290 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 5.7333 L22: 9.9549
REMARK 3 L33: 3.0352 L12: -5.7512
REMARK 3 L13: -0.9769 L23: 2.1947
REMARK 3 S TENSOR
REMARK 3 S11: -0.1057 S12: -0.0651 S13: -0.4907
REMARK 3 S21: 0.3556 S22: -0.1370 S23: 0.3043
REMARK 3 S31: 0.1745 S32: -0.0361 S33: 0.2427
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 221 B 228
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8270 -6.3105 57.7113
REMARK 3 T TENSOR
REMARK 3 T11: 0.0175 T22: 0.0676
REMARK 3 T33: 0.0653 T12: -0.0045
REMARK 3 T13: -0.0067 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 7.6388 L22: 12.0670
REMARK 3 L33: 16.2261 L12: -6.1247
REMARK 3 L13: -5.8586 L23: 4.7550
REMARK 3 S TENSOR
REMARK 3 S11: 0.1315 S12: -0.4327 S13: 0.0292
REMARK 3 S21: 0.0654 S22: 0.0679 S23: -0.1525
REMARK 3 S31: 0.0478 S32: 0.2585 S33: -0.1994
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 229 B 248
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2129 9.1792 56.0106
REMARK 3 T TENSOR
REMARK 3 T11: 0.0486 T22: 0.0863
REMARK 3 T33: 0.0427 T12: 0.0130
REMARK 3 T13: -0.0076 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 1.6582 L22: 2.4421
REMARK 3 L33: 0.0296 L12: -1.7557
REMARK 3 L13: -0.1295 L23: 0.2436
REMARK 3 S TENSOR
REMARK 3 S11: 0.1002 S12: -0.0482 S13: -0.0608
REMARK 3 S21: -0.1280 S22: -0.0908 S23: 0.0356
REMARK 3 S31: -0.0171 S32: 0.0210 S33: -0.0095
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 249 B 263
REMARK 3 ORIGIN FOR THE GROUP (A): 42.8022 1.9468 48.1231
REMARK 3 T TENSOR
REMARK 3 T11: 0.0329 T22: 0.0636
REMARK 3 T33: 0.1159 T12: 0.0040
REMARK 3 T13: 0.0024 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.1159 L22: 2.0379
REMARK 3 L33: 2.1613 L12: 0.1983
REMARK 3 L13: 0.4153 L23: -0.3583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0602 S12: 0.0108 S13: 0.0442
REMARK 3 S21: 0.1604 S22: 0.0107 S23: -0.2269
REMARK 3 S31: -0.2418 S32: 0.0375 S33: -0.0710
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 264 B 290
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7263 15.6729 43.5317
REMARK 3 T TENSOR
REMARK 3 T11: 0.0632 T22: 0.0754
REMARK 3 T33: 0.0912 T12: -0.0032
REMARK 3 T13: 0.0245 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.3745 L22: 1.7323
REMARK 3 L33: 3.4084 L12: 0.0449
REMARK 3 L13: 0.2979 L23: -0.7992
REMARK 3 S TENSOR
REMARK 3 S11: 0.0763 S12: 0.1080 S13: 0.0228
REMARK 3 S21: -0.2139 S22: -0.0282 S23: -0.0409
REMARK 3 S31: 0.0313 S32: 0.1310 S33: -0.0481
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 291 B 299
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4927 8.4122 66.1856
REMARK 3 T TENSOR
REMARK 3 T11: 0.0736 T22: 0.0328
REMARK 3 T33: 0.0718 T12: 0.0223
REMARK 3 T13: 0.0153 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 10.4521 L22: 10.0728
REMARK 3 L33: 8.6493 L12: 1.1702
REMARK 3 L13: 3.7420 L23: 5.4585
REMARK 3 S TENSOR
REMARK 3 S11: -0.0664 S12: -0.2620 S13: -0.5524
REMARK 3 S21: 0.2157 S22: 0.0046 S23: -0.2528
REMARK 3 S31: 0.6795 S32: 0.2429 S33: 0.0618
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2O0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : VARIMAX
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36969
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 81.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M MG(OAC)2, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
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 30.29650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 PRO A 3
REMARK 465 GLY A 4
REMARK 465 PRO A 5
REMARK 465 ASP A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 GLY A 12
REMARK 465 PRO A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ASP A 176
REMARK 465 PRO A 177
REMARK 465 MET A 178
REMARK 465 GLY A 179
REMARK 465 PRO A 180
REMARK 465 ALA A 181
REMARK 465 GLU A 182
REMARK 465 SER A 183
REMARK 465 LEU A 184
REMARK 465 PHE A 185
REMARK 465 LYS A 186
REMARK 465 VAL A 301
REMARK 465 SER A 302
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 PRO B 3
REMARK 465 GLY B 4
REMARK 465 PRO B 5
REMARK 465 ASP B 6
REMARK 465 GLY B 7
REMARK 465 PRO B 8
REMARK 465 ALA B 9
REMARK 465 ALA B 10
REMARK 465 SER B 11
REMARK 465 GLY B 12
REMARK 465 PRO B 13
REMARK 465 ALA B 14
REMARK 465 ASP B 300
REMARK 465 VAL B 301
REMARK 465 SER B 302
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 SER A 175 OG
REMARK 470 GLN A 269 CG CD OE1 NE2
REMARK 470 MET B 178 CG SD CE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 532 O HOH A 613 2.09
REMARK 500 OD1 ASP B 165 O HOH B 413 2.15
REMARK 500 NH2 ARG B 95 O HOH B 384 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 GLU B 76 CB GLU B 76 CG 0.127
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 55 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 55 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG B 95 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 95 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 PRO B 177 C - N - CA ANGL. DEV. = 13.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 43 87.05 -155.88
REMARK 500 ASN A 93 75.83 -154.77
REMARK 500 HIS A 213 56.68 -146.46
REMARK 500 ILE A 238 106.83 -161.41
REMARK 500 TYR A 278 -53.94 -127.20
REMARK 500 ASN B 93 63.80 -164.24
REMARK 500 SER B 175 -168.01 -67.23
REMARK 500 PRO B 177 -49.68 -23.96
REMARK 500 MET B 178 -167.32 -66.30
REMARK 500 HIS B 213 53.34 -140.05
REMARK 500 ILE B 238 103.32 -169.50
REMARK 500 TYR B 278 -58.35 -124.83
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 S4M A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S4M A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O05 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SPERMIDINE SYNTHASE IN COMPLEX WITH 5-
REMARK 900 METHYLTHIOADENOSINE
REMARK 900 RELATED ID: 2O06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SPERMIDINE SYNTHASE IN COMPLEX WITH 5-
REMARK 900 METHYLTHIOADENOSINE AND 1,4-DIAMINOBUTANE
REMARK 900 RELATED ID: 2O07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SPERMIDINE SYNTHASE IN COMPLEX WITH 5-
REMARK 900 METHYLTHIOADENOSINE AND SPERMIDINE
DBREF 2O0L A 1 302 UNP P19623 SPEE_HUMAN 1 302
DBREF 2O0L B 1 302 UNP P19623 SPEE_HUMAN 1 302
SEQADV 2O0L GLY A -1 UNP P19623 CLONING ARTIFACT
SEQADV 2O0L SER A 0 UNP P19623 CLONING ARTIFACT
SEQADV 2O0L GLY B -1 UNP P19623 CLONING ARTIFACT
SEQADV 2O0L SER B 0 UNP P19623 CLONING ARTIFACT
SEQRES 1 A 304 GLY SER MET GLU PRO GLY PRO ASP GLY PRO ALA ALA SER
SEQRES 2 A 304 GLY PRO ALA ALA ILE ARG GLU GLY TRP PHE ARG GLU THR
SEQRES 3 A 304 CYS SER LEU TRP PRO GLY GLN ALA LEU SER LEU GLN VAL
SEQRES 4 A 304 GLU GLN LEU LEU HIS HIS ARG ARG SER ARG TYR GLN ASP
SEQRES 5 A 304 ILE LEU VAL PHE ARG SER LYS THR TYR GLY ASN VAL LEU
SEQRES 6 A 304 VAL LEU ASP GLY VAL ILE GLN CYS THR GLU ARG ASP GLU
SEQRES 7 A 304 PHE SER TYR GLN GLU MET ILE ALA ASN LEU PRO LEU CYS
SEQRES 8 A 304 SER HIS PRO ASN PRO ARG LYS VAL LEU ILE ILE GLY GLY
SEQRES 9 A 304 GLY ASP GLY GLY VAL LEU ARG GLU VAL VAL LYS HIS PRO
SEQRES 10 A 304 SER VAL GLU SER VAL VAL GLN CYS GLU ILE ASP GLU ASP
SEQRES 11 A 304 VAL ILE GLN VAL SER LYS LYS PHE LEU PRO GLY MET ALA
SEQRES 12 A 304 ILE GLY TYR SER SER SER LYS LEU THR LEU HIS VAL GLY
SEQRES 13 A 304 ASP GLY PHE GLU PHE MET LYS GLN ASN GLN ASP ALA PHE
SEQRES 14 A 304 ASP VAL ILE ILE THR ASP SER SER ASP PRO MET GLY PRO
SEQRES 15 A 304 ALA GLU SER LEU PHE LYS GLU SER TYR TYR GLN LEU MET
SEQRES 16 A 304 LYS THR ALA LEU LYS GLU ASP GLY VAL LEU CYS CYS GLN
SEQRES 17 A 304 GLY GLU CYS GLN TRP LEU HIS LEU ASP LEU ILE LYS GLU
SEQRES 18 A 304 MET ARG GLN PHE CYS GLN SER LEU PHE PRO VAL VAL ALA
SEQRES 19 A 304 TYR ALA TYR CYS THR ILE PRO THR TYR PRO SER GLY GLN
SEQRES 20 A 304 ILE GLY PHE MET LEU CYS SER LYS ASN PRO SER THR ASN
SEQRES 21 A 304 PHE GLN GLU PRO VAL GLN PRO LEU THR GLN GLN GLN VAL
SEQRES 22 A 304 ALA GLN MET GLN LEU LYS TYR TYR ASN SER ASP VAL HIS
SEQRES 23 A 304 ARG ALA ALA PHE VAL LEU PRO GLU PHE ALA ARG LYS ALA
SEQRES 24 A 304 LEU ASN ASP VAL SER
SEQRES 1 B 304 GLY SER MET GLU PRO GLY PRO ASP GLY PRO ALA ALA SER
SEQRES 2 B 304 GLY PRO ALA ALA ILE ARG GLU GLY TRP PHE ARG GLU THR
SEQRES 3 B 304 CYS SER LEU TRP PRO GLY GLN ALA LEU SER LEU GLN VAL
SEQRES 4 B 304 GLU GLN LEU LEU HIS HIS ARG ARG SER ARG TYR GLN ASP
SEQRES 5 B 304 ILE LEU VAL PHE ARG SER LYS THR TYR GLY ASN VAL LEU
SEQRES 6 B 304 VAL LEU ASP GLY VAL ILE GLN CYS THR GLU ARG ASP GLU
SEQRES 7 B 304 PHE SER TYR GLN GLU MET ILE ALA ASN LEU PRO LEU CYS
SEQRES 8 B 304 SER HIS PRO ASN PRO ARG LYS VAL LEU ILE ILE GLY GLY
SEQRES 9 B 304 GLY ASP GLY GLY VAL LEU ARG GLU VAL VAL LYS HIS PRO
SEQRES 10 B 304 SER VAL GLU SER VAL VAL GLN CYS GLU ILE ASP GLU ASP
SEQRES 11 B 304 VAL ILE GLN VAL SER LYS LYS PHE LEU PRO GLY MET ALA
SEQRES 12 B 304 ILE GLY TYR SER SER SER LYS LEU THR LEU HIS VAL GLY
SEQRES 13 B 304 ASP GLY PHE GLU PHE MET LYS GLN ASN GLN ASP ALA PHE
SEQRES 14 B 304 ASP VAL ILE ILE THR ASP SER SER ASP PRO MET GLY PRO
SEQRES 15 B 304 ALA GLU SER LEU PHE LYS GLU SER TYR TYR GLN LEU MET
SEQRES 16 B 304 LYS THR ALA LEU LYS GLU ASP GLY VAL LEU CYS CYS GLN
SEQRES 17 B 304 GLY GLU CYS GLN TRP LEU HIS LEU ASP LEU ILE LYS GLU
SEQRES 18 B 304 MET ARG GLN PHE CYS GLN SER LEU PHE PRO VAL VAL ALA
SEQRES 19 B 304 TYR ALA TYR CYS THR ILE PRO THR TYR PRO SER GLY GLN
SEQRES 20 B 304 ILE GLY PHE MET LEU CYS SER LYS ASN PRO SER THR ASN
SEQRES 21 B 304 PHE GLN GLU PRO VAL GLN PRO LEU THR GLN GLN GLN VAL
SEQRES 22 B 304 ALA GLN MET GLN LEU LYS TYR TYR ASN SER ASP VAL HIS
SEQRES 23 B 304 ARG ALA ALA PHE VAL LEU PRO GLU PHE ALA ARG LYS ALA
SEQRES 24 B 304 LEU ASN ASP VAL SER
HET S4M A 501 24
HET S4M A 502 24
HETNAM S4M 5'-[(S)-(3-AMINOPROPYL)(METHYL)-LAMBDA~4~-SULFANYL]-5'-
HETNAM 2 S4M DEOXYADENOSINE
FORMUL 3 S4M 2(C14 H24 N6 O3 S)
FORMUL 5 HOH *265(H2 O)
HELIX 1 1 GLU A 76 CYS A 89 1 14
HELIX 2 2 GLY A 105 VAL A 112 1 8
HELIX 3 3 ASP A 126 LEU A 137 1 12
HELIX 4 4 LEU A 137 ILE A 142 1 6
HELIX 5 5 GLY A 143 SER A 146 5 4
HELIX 6 6 ASP A 155 GLN A 162 1 8
HELIX 7 7 GLU A 187 ALA A 196 1 10
HELIX 8 8 HIS A 213 PHE A 228 1 16
HELIX 9 9 TYR A 241 SER A 243 5 3
HELIX 10 10 THR A 267 MET A 274 1 8
HELIX 11 11 ASN A 280 ALA A 287 1 8
HELIX 12 12 PRO A 291 ASP A 300 1 10
HELIX 13 13 GLU B 76 CYS B 89 1 14
HELIX 14 14 GLY B 105 LYS B 113 1 9
HELIX 15 15 ASP B 126 LEU B 137 1 12
HELIX 16 16 LEU B 137 ILE B 142 1 6
HELIX 17 17 GLY B 143 SER B 146 5 4
HELIX 18 18 ASP B 155 LYS B 161 1 7
HELIX 19 19 MET B 178 LYS B 186 5 9
HELIX 20 20 GLU B 187 ALA B 196 1 10
HELIX 21 21 HIS B 213 PHE B 228 1 16
HELIX 22 22 TYR B 241 SER B 243 5 3
HELIX 23 23 THR B 267 MET B 274 1 8
HELIX 24 24 ASN B 280 ALA B 287 1 8
HELIX 25 25 PRO B 291 ASN B 299 1 9
SHEET 1 A 5 TRP A 20 GLU A 23 0
SHEET 2 A 5 GLN A 31 ARG A 45 -1 O LEU A 35 N PHE A 21
SHEET 3 A 5 GLN B 31 ARG B 45 -1 O ALA B 32 N SER A 34
SHEET 4 A 5 TRP B 20 GLU B 23 -1 N GLU B 23 O LEU B 33
SHEET 5 A 5 ILE B 16 ARG B 17 -1 N ARG B 17 O TRP B 20
SHEET 1 B 8 VAL A 68 THR A 72 0
SHEET 2 B 8 ASN A 61 LEU A 65 -1 N LEU A 63 O GLN A 70
SHEET 3 B 8 ASP A 50 SER A 56 -1 N PHE A 54 O VAL A 62
SHEET 4 B 8 GLN A 31 ARG A 45 -1 N HIS A 42 O VAL A 53
SHEET 5 B 8 GLN B 31 ARG B 45 -1 O ALA B 32 N SER A 34
SHEET 6 B 8 ASP B 50 SER B 56 -1 O VAL B 53 N HIS B 42
SHEET 7 B 8 ASN B 61 LEU B 65 -1 O VAL B 64 N LEU B 52
SHEET 8 B 8 VAL B 68 THR B 72 -1 O GLN B 70 N LEU B 63
SHEET 1 C 7 LEU A 149 VAL A 153 0
SHEET 2 C 7 SER A 119 GLU A 124 1 N GLN A 122 O HIS A 152
SHEET 3 C 7 LYS A 96 GLY A 101 1 N ILE A 99 O VAL A 121
SHEET 4 C 7 PHE A 167 ASP A 173 1 O ILE A 171 N ILE A 100
SHEET 5 C 7 LEU A 197 GLN A 206 1 O LYS A 198 N PHE A 167
SHEET 6 C 7 GLN A 245 SER A 252 -1 O MET A 249 N CYS A 205
SHEET 7 C 7 VAL A 230 THR A 237 -1 N ALA A 234 O PHE A 248
SHEET 1 D 7 LEU B 149 VAL B 153 0
SHEET 2 D 7 SER B 119 GLU B 124 1 N GLN B 122 O HIS B 152
SHEET 3 D 7 LYS B 96 GLY B 101 1 N ILE B 99 O VAL B 121
SHEET 4 D 7 PHE B 167 ASP B 173 1 O ILE B 171 N LEU B 98
SHEET 5 D 7 LEU B 197 GLN B 206 1 O LYS B 198 N PHE B 167
SHEET 6 D 7 GLN B 245 SER B 252 -1 O CYS B 251 N LEU B 203
SHEET 7 D 7 VAL B 230 THR B 237 -1 N ALA B 234 O PHE B 248
SITE 1 AC1 17 GLN A 49 GLN A 70 TYR A 79 GLN A 80
SITE 2 AC1 17 GLY A 101 GLY A 103 ASP A 104 CYS A 123
SITE 3 AC1 17 GLU A 124 ILE A 125 ASP A 126 VAL A 129
SITE 4 AC1 17 GLY A 154 ASP A 155 GLY A 156 ASP A 173
SITE 5 AC1 17 TYR A 241
SITE 1 AC2 22 GLN B 49 LEU B 65 GLN B 70 GLN B 80
SITE 2 AC2 22 GLY B 101 GLY B 103 ASP B 104 CYS B 123
SITE 3 AC2 22 GLU B 124 ILE B 125 ASP B 126 VAL B 129
SITE 4 AC2 22 GLY B 154 ASP B 155 GLY B 156 ASP B 173
SITE 5 AC2 22 SER B 175 PRO B 180 ALA B 181 SER B 183
SITE 6 AC2 22 LEU B 184 TYR B 241
CRYST1 58.323 60.593 86.667 90.00 108.96 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017146 0.000000 0.005890 0.00000
SCALE2 0.000000 0.016504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012200 0.00000
(ATOM LINES ARE NOT SHOWN.)
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