HEADER TRANSCRIPTION 07-FEB-13 3ZMD
TITLE CRYSTAL STRUCTURE OF ABSC, A MARR FAMILY TRANSCRIPTIONAL
TITLE 2 REGULATOR FROM STREPTOMYCES COELICOLOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE TRANSCRIPTIONAL REGULATOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ABSC;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: A TWENTY RESIDUE HIS-TAG WAS APPENDED AT THE
COMPND 7 N-TERMINUS OF THE WILD-TYPE SEQUENCE, BUT THIS WAS NOT VISIBLE IN
COMPND 8 THE ELECTRON DENSITY. RESIDUE NUMBERING IS RELATIVE TO THE
COMPND 9 FULL-LENGTH WILD-TYPE SEQUENCE.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;
SOURCE 3 ORGANISM_TAXID: 1902;
SOURCE 4 STRAIN: M145;
SOURCE 5 ATCC: BAA-471;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET15B;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B-ABSC
KEYWDS TRANSCRIPTION, MARR-FAMILY, WINGED HELIX MOTIF
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.M.STEVENSON,H.KOCK,S.MOOTIEN,S.C.DAVIES,M.J.BIBB,D.M.LAWSON
REVDAT 1 20-FEB-13 3ZMD 0
JRNL AUTH C.E.M.STEVENSON,H.KOCK,S.MOOTIEN,S.C.DAVIES,M.J.BIBB,
JRNL AUTH 2 D.M.LAWSON
JRNL TITL CRYSTAL STRUCTURE OF ABSC, A MARR FAMILY TRANSCRIPTIONAL
JRNL TITL 2 REGULATOR FROM STREPTOMYCES COELICOLOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.E.M.STEVENSON,H.KOCK,S.MOOTIEN,S.C.DAVIES,M.J.BIBB,
REMARK 1 AUTH 2 D.M.LAWSON
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF ABSC, A
REMARK 1 TITL 2 NOVEL REGULATOR OF ANTIBIOTIC PRODUCTION IN STREPTOMYCES
REMARK 1 TITL 3 COELICOLOR.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 233 2007
REMARK 1 REFN ISSN 1744-3091
REMARK 1 PMID 17329821
REMARK 1 DOI 10.1107/S1744309107007944
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.04
REMARK 3 NUMBER OF REFLECTIONS : 53215
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) : 0.21617
REMARK 3 R VALUE (WORKING SET) : 0.21477
REMARK 3 FREE R VALUE : 0.24282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2794
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) : 1.950
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.001
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3608
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.426
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.458
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4830
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 343
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.72
REMARK 3 B22 (A**2) : 0.32
REMARK 3 B33 (A**2) : -1.04
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.337
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4958 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3402 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6721 ; 1.445 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8264 ; 1.583 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 626 ; 4.801 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 254 ;31.078 ;23.425
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 904 ;14.828 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 53 ;17.695 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 768 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5527 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1026 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 6
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 7 154 B 7 154 4895 0.16 0.05
REMARK 3 2 A 7 153 C 7 153 4842 0.15 0.05
REMARK 3 3 A 7 154 D 7 154 5033 0.14 0.05
REMARK 3 4 B 7 153 C 7 153 4877 0.16 0.05
REMARK 3 5 B 7 154 D 7 154 5007 0.14 0.05
REMARK 3 6 C 7 153 D 7 153 4979 0.13 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 7 A 34
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4197 51.8583 57.4542
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.0704
REMARK 3 T33: 0.0312 T12: -0.0445
REMARK 3 T13: 0.0059 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 11.8123 L22: 13.1790
REMARK 3 L33: 7.2821 L12: -10.3962
REMARK 3 L13: 7.3531 L23: -5.5073
REMARK 3 S TENSOR
REMARK 3 S11: 0.1181 S12: 0.4789 S13: -0.1122
REMARK 3 S21: -0.4461 S22: -0.2891 S23: 0.0138
REMARK 3 S31: 0.0395 S32: 0.2712 S33: 0.1710
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 35 A 61
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6420 78.1515 48.5975
REMARK 3 T TENSOR
REMARK 3 T11: 0.2565 T22: 0.1448
REMARK 3 T33: 0.1107 T12: 0.0355
REMARK 3 T13: 0.0121 T23: 0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 9.0764 L22: 11.6245
REMARK 3 L33: 4.5589 L12: 7.5842
REMARK 3 L13: 2.6986 L23: -1.0485
REMARK 3 S TENSOR
REMARK 3 S11: 0.1215 S12: 0.0156 S13: -0.4579
REMARK 3 S21: -0.5068 S22: -0.0752 S23: -0.1153
REMARK 3 S31: 0.5900 S32: -0.1207 S33: -0.0463
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 62 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6701 77.1309 41.8726
REMARK 3 T TENSOR
REMARK 3 T11: 0.3374 T22: 0.1845
REMARK 3 T33: 0.1640 T12: 0.0442
REMARK 3 T13: 0.0880 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 12.3544 L22: 3.5171
REMARK 3 L33: 3.7636 L12: -2.7693
REMARK 3 L13: 3.0348 L23: -0.9449
REMARK 3 S TENSOR
REMARK 3 S11: -0.0215 S12: 0.3998 S13: -0.5473
REMARK 3 S21: -0.4669 S22: -0.0560 S23: -0.1351
REMARK 3 S31: 0.8064 S32: 0.2321 S33: 0.0775
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 91 A 138
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6522 77.4232 52.7418
REMARK 3 T TENSOR
REMARK 3 T11: 0.1846 T22: 0.1589
REMARK 3 T33: 0.0727 T12: -0.0246
REMARK 3 T13: 0.0027 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.9750 L22: 4.3670
REMARK 3 L33: 3.4901 L12: 1.6990
REMARK 3 L13: -1.7940 L23: -3.6284
REMARK 3 S TENSOR
REMARK 3 S11: 0.1287 S12: -0.0661 S13: 0.1550
REMARK 3 S21: -0.0824 S22: 0.0902 S23: 0.1239
REMARK 3 S31: -0.1606 S32: 0.0397 S33: -0.2188
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 139 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5953 64.3477 63.7928
REMARK 3 T TENSOR
REMARK 3 T11: 0.0882 T22: 0.1675
REMARK 3 T33: 0.1392 T12: 0.0029
REMARK 3 T13: -0.0241 T23: 0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 25.0413 L22: 6.9513
REMARK 3 L33: 31.5979 L12: 0.4655
REMARK 3 L13: -19.7504 L23: 2.9584
REMARK 3 S TENSOR
REMARK 3 S11: 0.2066 S12: -1.1355 S13: 0.6277
REMARK 3 S21: -0.1943 S22: -0.1488 S23: -0.3340
REMARK 3 S31: -1.3338 S32: 0.7276 S33: -0.0579
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 7 B 35
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0304 67.4229 58.2375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1293 T22: 0.0967
REMARK 3 T33: 0.0738 T12: -0.0133
REMARK 3 T13: 0.0151 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 11.0972 L22: 10.6431
REMARK 3 L33: 6.7504 L12: -9.3433
REMARK 3 L13: -7.5930 L23: 7.2301
REMARK 3 S TENSOR
REMARK 3 S11: 0.3388 S12: 0.5407 S13: 0.2318
REMARK 3 S21: -0.4431 S22: -0.3518 S23: -0.1350
REMARK 3 S31: -0.3238 S32: -0.3230 S33: 0.0131
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 36 B 81
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9481 45.0543 44.4214
REMARK 3 T TENSOR
REMARK 3 T11: 0.1677 T22: 0.0833
REMARK 3 T33: 0.1423 T12: 0.0540
REMARK 3 T13: -0.0125 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 4.0827 L22: 2.8605
REMARK 3 L33: 3.6983 L12: 0.9696
REMARK 3 L13: 0.0974 L23: 0.5469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0721 S12: -0.0657 S13: 0.5863
REMARK 3 S21: 0.0406 S22: -0.0358 S23: 0.3133
REMARK 3 S31: -0.3572 S32: -0.3650 S33: -0.0363
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 82 B 94
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2441 40.3757 35.9135
REMARK 3 T TENSOR
REMARK 3 T11: 0.2796 T22: 0.1174
REMARK 3 T33: 0.0769 T12: 0.0268
REMARK 3 T13: -0.0090 T23: 0.0511
REMARK 3 L TENSOR
REMARK 3 L11: 19.3654 L22: 2.7330
REMARK 3 L33: 5.1338 L12: 5.3155
REMARK 3 L13: -1.9008 L23: -3.0309
REMARK 3 S TENSOR
REMARK 3 S11: -0.3197 S12: 0.6050 S13: 0.1747
REMARK 3 S21: -0.3311 S22: 0.4221 S23: 0.0991
REMARK 3 S31: 0.4731 S32: -0.5543 S33: -0.1024
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 95 B 139
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3770 43.8681 52.3656
REMARK 3 T TENSOR
REMARK 3 T11: 0.0637 T22: 0.1703
REMARK 3 T33: 0.0566 T12: 0.0077
REMARK 3 T13: 0.0083 T23: 0.0740
REMARK 3 L TENSOR
REMARK 3 L11: 0.5157 L22: 3.3463
REMARK 3 L33: 4.6717 L12: 0.9325
REMARK 3 L13: 1.5423 L23: 2.6819
REMARK 3 S TENSOR
REMARK 3 S11: 0.0704 S12: -0.1098 S13: -0.0145
REMARK 3 S21: 0.0157 S22: -0.0854 S23: -0.1123
REMARK 3 S31: 0.2171 S32: -0.2512 S33: 0.0150
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 140 B 154
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3259 54.6569 61.5340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.0680
REMARK 3 T33: 0.1357 T12: -0.0006
REMARK 3 T13: -0.0578 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 15.1420 L22: 7.2062
REMARK 3 L33: 26.4495 L12: 0.7167
REMARK 3 L13: 7.3187 L23: -0.5866
REMARK 3 S TENSOR
REMARK 3 S11: 0.1322 S12: -0.2821 S13: -0.6489
REMARK 3 S21: -0.2732 S22: -0.0800 S23: 0.2218
REMARK 3 S31: 0.9458 S32: -0.0687 S33: -0.0522
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 : C 6 C 38
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2016 115.2660 58.5427
REMARK 3 T TENSOR
REMARK 3 T11: 0.0982 T22: 0.1099
REMARK 3 T33: 0.0454 T12: -0.0120
REMARK 3 T13: -0.0022 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 8.0331 L22: 9.2842
REMARK 3 L33: 4.2914 L12: -7.3652
REMARK 3 L13: 5.1584 L23: -4.6842
REMARK 3 S TENSOR
REMARK 3 S11: 0.2585 S12: 0.4252 S13: -0.1368
REMARK 3 S21: -0.4930 S22: -0.1844 S23: 0.2107
REMARK 3 S31: 0.2712 S32: 0.2239 S33: -0.0740
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 : C 39 C 89
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6193 137.1280 45.2968
REMARK 3 T TENSOR
REMARK 3 T11: 0.1976 T22: 0.0821
REMARK 3 T33: 0.1424 T12: -0.0075
REMARK 3 T13: 0.0478 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 4.6424 L22: 4.5199
REMARK 3 L33: 4.1329 L12: 0.7937
REMARK 3 L13: 0.7212 L23: -0.0526
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: 0.0816 S13: -0.6529
REMARK 3 S21: -0.0604 S22: -0.0291 S23: -0.3448
REMARK 3 S31: 0.4877 S32: 0.0472 S33: 0.0116
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 : C 90 C 101
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4574 146.7201 39.9761
REMARK 3 T TENSOR
REMARK 3 T11: 0.3218 T22: 0.1760
REMARK 3 T33: 0.1207 T12: 0.0402
REMARK 3 T13: 0.0669 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 21.8019 L22: 16.3902
REMARK 3 L33: 9.8593 L12: 12.3065
REMARK 3 L13: 5.5063 L23: 0.0748
REMARK 3 S TENSOR
REMARK 3 S11: -0.5857 S12: -0.2849 S13: 0.1761
REMARK 3 S21: 0.0687 S22: 0.1664 S23: -0.7359
REMARK 3 S31: -0.3476 S32: 0.4716 S33: 0.4193
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 : C 102 C 139
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8423 135.2382 57.3365
REMARK 3 T TENSOR
REMARK 3 T11: 0.1367 T22: 0.1073
REMARK 3 T33: 0.0256 T12: 0.0126
REMARK 3 T13: -0.0146 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.0790 L22: 5.7477
REMARK 3 L33: 5.8693 L12: 1.5762
REMARK 3 L13: -2.2436 L23: -5.2877
REMARK 3 S TENSOR
REMARK 3 S11: 0.0675 S12: -0.0537 S13: 0.1292
REMARK 3 S21: 0.3931 S22: 0.2232 S23: 0.2425
REMARK 3 S31: -0.3773 S32: -0.0639 S33: -0.2907
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 : C 140 C 154
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6450 126.6683 63.5676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1243 T22: 0.0894
REMARK 3 T33: 0.1114 T12: -0.0175
REMARK 3 T13: -0.0150 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 14.8132 L22: 7.0340
REMARK 3 L33: 17.5394 L12: 1.7778
REMARK 3 L13: -4.6168 L23: -2.3882
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: -0.5979 S13: 0.7299
REMARK 3 S21: -0.0451 S22: 0.1528 S23: -0.1631
REMARK 3 S31: -0.9451 S32: 0.6844 S33: -0.1758
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 : D 7 D 35
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7246 129.0750 59.5267
REMARK 3 T TENSOR
REMARK 3 T11: 0.1137 T22: 0.0496
REMARK 3 T33: 0.0294 T12: -0.0196
REMARK 3 T13: -0.0120 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 13.1147 L22: 11.7404
REMARK 3 L33: 7.2100 L12: -10.7542
REMARK 3 L13: -8.2262 L23: 6.9273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0838 S12: 0.2753 S13: 0.2243
REMARK 3 S21: -0.2646 S22: -0.0603 S23: -0.0823
REMARK 3 S31: -0.1440 S32: -0.1966 S33: -0.0236
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 : D 36 D 89
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6888 105.2360 46.0419
REMARK 3 T TENSOR
REMARK 3 T11: 0.1533 T22: 0.1097
REMARK 3 T33: 0.1363 T12: 0.0376
REMARK 3 T13: -0.0197 T23: -0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 4.0004 L22: 3.9070
REMARK 3 L33: 4.1489 L12: 0.2955
REMARK 3 L13: -1.0688 L23: -0.0593
REMARK 3 S TENSOR
REMARK 3 S11: 0.1532 S12: -0.1329 S13: 0.3131
REMARK 3 S21: 0.1015 S22: -0.1750 S23: 0.4816
REMARK 3 S31: -0.3233 S32: -0.3088 S33: 0.0218
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 : D 90 D 113
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8824 95.6896 43.5729
REMARK 3 T TENSOR
REMARK 3 T11: 0.1325 T22: 0.0884
REMARK 3 T33: 0.1476 T12: 0.0181
REMARK 3 T13: 0.0128 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 31.3255 L22: 3.5155
REMARK 3 L33: 4.0472 L12: 8.1024
REMARK 3 L13: 5.6783 L23: 2.1885
REMARK 3 S TENSOR
REMARK 3 S11: -0.0550 S12: -0.2741 S13: -0.7270
REMARK 3 S21: 0.0308 S22: -0.0274 S23: 0.2428
REMARK 3 S31: 0.1153 S32: -0.4762 S33: 0.0824
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 : D 114 D 138
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7662 111.7570 61.7917
REMARK 3 T TENSOR
REMARK 3 T11: 0.0107 T22: 0.1007
REMARK 3 T33: 0.0342 T12: 0.0070
REMARK 3 T13: -0.0036 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 2.5779 L22: 4.1578
REMARK 3 L33: 6.8540 L12: -0.5948
REMARK 3 L13: 0.2231 L23: 3.0242
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: 0.0556 S13: -0.1844
REMARK 3 S21: 0.0381 S22: 0.2288 S23: -0.2185
REMARK 3 S31: 0.2420 S32: 0.1471 S33: -0.2424
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 : D 139 D 154
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5697 116.6339 65.5651
REMARK 3 T TENSOR
REMARK 3 T11: 0.0630 T22: 0.1343
REMARK 3 T33: 0.1615 T12: 0.0151
REMARK 3 T13: 0.0417 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 26.5719 L22: 5.3792
REMARK 3 L33: 29.2489 L12: 1.7329
REMARK 3 L13: 19.8123 L23: 0.1990
REMARK 3 S TENSOR
REMARK 3 S11: 0.2088 S12: -0.9665 S13: -0.5429
REMARK 3 S21: -0.0776 S22: -0.0958 S23: 0.4686
REMARK 3 S31: 0.9648 S32: -0.3220 S33: -0.1130
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 3ZMD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-FEB-13.
REMARK 100 THE PDBE ID CODE IS EBI-55749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-06
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 : SRS
REMARK 200 BEAMLINE : PX10.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.490
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MX-225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56091
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.95
REMARK 200 RESOLUTION RANGE LOW (A) : 48.11
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.9
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.9
REMARK 200 R MERGE FOR SHELL (I) : 0.52
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE REFERENCE 1.
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 21.82400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.14500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.24150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.14500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.82400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.24150
REMARK 290 SMTRY3 4 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: 7210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.7 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 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: 6080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 ARG A 155
REMARK 465 GLY A 156
REMARK 465 ARG A 157
REMARK 465 PRO A 158
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 GLU B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 ARG B 155
REMARK 465 GLY B 156
REMARK 465 ARG B 157
REMARK 465 PRO B 158
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 THR C 3
REMARK 465 GLU C 4
REMARK 465 THR C 5
REMARK 465 ARG C 155
REMARK 465 GLY C 156
REMARK 465 ARG C 157
REMARK 465 PRO C 158
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 THR D 3
REMARK 465 GLU D 4
REMARK 465 THR D 5
REMARK 465 ALA D 6
REMARK 465 ARG D 155
REMARK 465 GLY D 156
REMARK 465 ARG D 157
REMARK 465 PRO D 158
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 LYS A 34 CD CE NZ
REMARK 470 GLN A 37 CG CD OE1 NE2
REMARK 470 ARG A 75 NE CZ NH1 NH2
REMARK 470 ARG A 98 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 99 NE CZ NH1 NH2
REMARK 470 ARG B 26 CD NE CZ NH1 NH2
REMARK 470 LYS B 34 CD CE NZ
REMARK 470 ARG B 75 NE CZ NH1 NH2
REMARK 470 ARG B 114 NE CZ NH1 NH2
REMARK 470 LYS B 142 CD CE NZ
REMARK 470 LYS B 145 CE NZ
REMARK 470 ARG C 26 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 73 CE NZ
REMARK 470 ARG C 75 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 97 CG OD1 OD2
REMARK 470 ARG C 99 CD NE CZ NH1 NH2
REMARK 470 LEU C 140 CG CD1 CD2
REMARK 470 LYS C 142 CD CE NZ
REMARK 470 LYS C 145 CE NZ
REMARK 470 ARG D 26 CD NE CZ NH1 NH2
REMARK 470 LYS D 34 CE NZ
REMARK 470 ARG D 75 CD NE CZ NH1 NH2
REMARK 470 ARG D 98 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 99 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 140 CG CD1 CD2
REMARK 470 LYS D 145 CE NZ
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 A 91 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 126 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU B 137 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG C 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 126 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG D 126 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG D 126 NE - CZ - NH2 ANGL. DEV. = -3.0 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 PHE A 128 -71.39 -152.61
REMARK 500 MET B 70 56.90 39.90
REMARK 500 PHE B 128 -70.53 -153.02
REMARK 500 ARG C 99 -149.18 56.21
REMARK 500 PHE C 128 -70.04 -152.28
REMARK 500 PHE D 128 -72.81 -152.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 2-HYDROXYBENZOIC ACID (SAL): SALICYLATE WAS NOT
REMARK 600 DELIBERATELY ADDED TO THE PROTEIN AT ANY STAGE, BUT THIS
REMARK 600 LIGAND WAS CONSISTENT WITH THE OBSERVED ELECTRON DENSITY.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 58 OD1
REMARK 620 2 SER A 53 O 79.4
REMARK 620 3 HOH A2034 O 155.6 108.6
REMARK 620 4 GLU D 56 OE2 86.4 99.1 114.0
REMARK 620 5 SER A 55 O 83.7 98.3 72.5 158.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 55 O
REMARK 620 2 CL B 303 CL 82.1
REMARK 620 3 ASP B 58 OD1 80.4 102.7
REMARK 620 4 GLU C 56 OE2 173.9 96.5 94.2
REMARK 620 5 SER B 53 O 101.9 176.0 78.2 79.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 53 O
REMARK 620 2 ASP C 58 OD1 78.7
REMARK 620 3 SER C 55 O 96.4 82.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 55 O
REMARK 620 2 GLU A 56 OE2 161.3
REMARK 620 3 ASP D 58 OD1 85.4 89.3
REMARK 620 4 SER D 53 O 97.8 98.9 80.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 303
DBREF 3ZMD A 1 158 UNP Q9L2B5 Q9L2B5_STRCO 1 158
DBREF 3ZMD B 1 158 UNP Q9L2B5 Q9L2B5_STRCO 1 158
DBREF 3ZMD C 1 158 UNP Q9L2B5 Q9L2B5_STRCO 1 158
DBREF 3ZMD D 1 158 UNP Q9L2B5 Q9L2B5_STRCO 1 158
SEQADV 3ZMD MET A -19 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY A -18 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER A -17 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER A -16 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS A -15 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS A -14 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS A -13 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS A -12 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS A -11 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS A -10 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER A -9 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER A -8 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY A -7 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD LEU A -6 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD VAL A -5 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD PRO A -4 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD ARG A -3 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY A -2 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER A -1 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS A 0 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD MET B -19 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY B -18 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER B -17 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER B -16 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS B -15 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS B -14 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS B -13 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS B -12 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS B -11 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS B -10 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER B -9 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER B -8 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY B -7 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD LEU B -6 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD VAL B -5 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD PRO B -4 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD ARG B -3 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY B -2 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER B -1 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS B 0 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD MET C -19 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY C -18 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER C -17 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER C -16 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS C -15 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS C -14 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS C -13 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS C -12 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS C -11 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS C -10 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER C -9 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER C -8 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY C -7 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD LEU C -6 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD VAL C -5 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD PRO C -4 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD ARG C -3 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY C -2 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER C -1 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS C 0 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD MET D -19 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY D -18 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER D -17 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER D -16 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS D -15 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS D -14 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS D -13 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS D -12 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS D -11 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS D -10 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER D -9 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER D -8 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY D -7 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD LEU D -6 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD VAL D -5 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD PRO D -4 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD ARG D -3 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD GLY D -2 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD SER D -1 UNP Q9L2B5 EXPRESSION TAG
SEQADV 3ZMD HIS D 0 UNP Q9L2B5 EXPRESSION TAG
SEQRES 1 A 178 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 178 LEU VAL PRO ARG GLY SER HIS MET GLU THR GLU THR ALA
SEQRES 3 A 178 THR ARG TRP LEU THR ASP THR GLU GLN CYS ALA TRP ARG
SEQRES 4 A 178 THR HIS LEU GLU VAL ASN ARG LEU LEU THR HIS GLN LEU
SEQRES 5 A 178 GLU LYS ASP LEU GLN PRO PHE GLY LEU THR MET ASN ASP
SEQRES 6 A 178 TYR GLU ILE LEU VAL ASN LEU SER GLU SER GLU GLY ASP
SEQRES 7 A 178 ARG MET ARG MET SER ASP LEU ALA THR ALA THR MET GLN
SEQRES 8 A 178 SER LYS SER ARG LEU SER HIS GLN ILE THR ARG MET GLU
SEQRES 9 A 178 ASN ALA ASN LEU VAL ARG ARG GLU ASN CYS GLU SER ASP
SEQRES 10 A 178 ARG ARG GLY LEU PHE ALA VAL LEU THR GLU HIS GLY LEU
SEQRES 11 A 178 GLU THR MET ARG LYS VAL ALA PRO HIS HIS VAL ALA SER
SEQRES 12 A 178 VAL ARG ARG HIS PHE ILE ASP LEU LEU ALA PRO GLU ASP
SEQRES 13 A 178 LEU THR GLU LEU ASP LYS ALA LEU LYS PRO ILE ALA GLU
SEQRES 14 A 178 HIS LEU ARG GLY GLN ARG GLY ARG PRO
SEQRES 1 B 178 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 178 LEU VAL PRO ARG GLY SER HIS MET GLU THR GLU THR ALA
SEQRES 3 B 178 THR ARG TRP LEU THR ASP THR GLU GLN CYS ALA TRP ARG
SEQRES 4 B 178 THR HIS LEU GLU VAL ASN ARG LEU LEU THR HIS GLN LEU
SEQRES 5 B 178 GLU LYS ASP LEU GLN PRO PHE GLY LEU THR MET ASN ASP
SEQRES 6 B 178 TYR GLU ILE LEU VAL ASN LEU SER GLU SER GLU GLY ASP
SEQRES 7 B 178 ARG MET ARG MET SER ASP LEU ALA THR ALA THR MET GLN
SEQRES 8 B 178 SER LYS SER ARG LEU SER HIS GLN ILE THR ARG MET GLU
SEQRES 9 B 178 ASN ALA ASN LEU VAL ARG ARG GLU ASN CYS GLU SER ASP
SEQRES 10 B 178 ARG ARG GLY LEU PHE ALA VAL LEU THR GLU HIS GLY LEU
SEQRES 11 B 178 GLU THR MET ARG LYS VAL ALA PRO HIS HIS VAL ALA SER
SEQRES 12 B 178 VAL ARG ARG HIS PHE ILE ASP LEU LEU ALA PRO GLU ASP
SEQRES 13 B 178 LEU THR GLU LEU ASP LYS ALA LEU LYS PRO ILE ALA GLU
SEQRES 14 B 178 HIS LEU ARG GLY GLN ARG GLY ARG PRO
SEQRES 1 C 178 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 178 LEU VAL PRO ARG GLY SER HIS MET GLU THR GLU THR ALA
SEQRES 3 C 178 THR ARG TRP LEU THR ASP THR GLU GLN CYS ALA TRP ARG
SEQRES 4 C 178 THR HIS LEU GLU VAL ASN ARG LEU LEU THR HIS GLN LEU
SEQRES 5 C 178 GLU LYS ASP LEU GLN PRO PHE GLY LEU THR MET ASN ASP
SEQRES 6 C 178 TYR GLU ILE LEU VAL ASN LEU SER GLU SER GLU GLY ASP
SEQRES 7 C 178 ARG MET ARG MET SER ASP LEU ALA THR ALA THR MET GLN
SEQRES 8 C 178 SER LYS SER ARG LEU SER HIS GLN ILE THR ARG MET GLU
SEQRES 9 C 178 ASN ALA ASN LEU VAL ARG ARG GLU ASN CYS GLU SER ASP
SEQRES 10 C 178 ARG ARG GLY LEU PHE ALA VAL LEU THR GLU HIS GLY LEU
SEQRES 11 C 178 GLU THR MET ARG LYS VAL ALA PRO HIS HIS VAL ALA SER
SEQRES 12 C 178 VAL ARG ARG HIS PHE ILE ASP LEU LEU ALA PRO GLU ASP
SEQRES 13 C 178 LEU THR GLU LEU ASP LYS ALA LEU LYS PRO ILE ALA GLU
SEQRES 14 C 178 HIS LEU ARG GLY GLN ARG GLY ARG PRO
SEQRES 1 D 178 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 178 LEU VAL PRO ARG GLY SER HIS MET GLU THR GLU THR ALA
SEQRES 3 D 178 THR ARG TRP LEU THR ASP THR GLU GLN CYS ALA TRP ARG
SEQRES 4 D 178 THR HIS LEU GLU VAL ASN ARG LEU LEU THR HIS GLN LEU
SEQRES 5 D 178 GLU LYS ASP LEU GLN PRO PHE GLY LEU THR MET ASN ASP
SEQRES 6 D 178 TYR GLU ILE LEU VAL ASN LEU SER GLU SER GLU GLY ASP
SEQRES 7 D 178 ARG MET ARG MET SER ASP LEU ALA THR ALA THR MET GLN
SEQRES 8 D 178 SER LYS SER ARG LEU SER HIS GLN ILE THR ARG MET GLU
SEQRES 9 D 178 ASN ALA ASN LEU VAL ARG ARG GLU ASN CYS GLU SER ASP
SEQRES 10 D 178 ARG ARG GLY LEU PHE ALA VAL LEU THR GLU HIS GLY LEU
SEQRES 11 D 178 GLU THR MET ARG LYS VAL ALA PRO HIS HIS VAL ALA SER
SEQRES 12 D 178 VAL ARG ARG HIS PHE ILE ASP LEU LEU ALA PRO GLU ASP
SEQRES 13 D 178 LEU THR GLU LEU ASP LYS ALA LEU LYS PRO ILE ALA GLU
SEQRES 14 D 178 HIS LEU ARG GLY GLN ARG GLY ARG PRO
HET SAL A 201 10
HET NA A 301 1
HET CL A 303 1
HET EDO A 401 4
HET EDO A 403 4
HET NA B 301 1
HET CL B 303 1
HET EDO B 401 4
HET EDO B 403 4
HET NA C 301 1
HET EDO C 401 4
HET EDO D 201 4
HET NA D 301 1
HET CL D 303 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM SAL 2-HYDROXYBENZOIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN SAL SALICYLIC ACID
FORMUL 5 EDO 6(C2 H6 O2)
FORMUL 6 CL 3(CL 1-)
FORMUL 7 NA 4(NA 1+)
FORMUL 8 SAL C7 H6 O3
FORMUL 9 HOH *343(H2 O)
HELIX 1 1 THR A 11 GLN A 37 1 27
HELIX 2 2 PRO A 38 GLY A 40 5 3
HELIX 3 3 THR A 42 GLU A 54 1 13
HELIX 4 4 SER A 55 GLY A 57 5 3
HELIX 5 5 MET A 62 THR A 69 1 8
HELIX 6 6 SER A 72 ALA A 86 1 15
HELIX 7 7 THR A 106 PHE A 128 1 23
HELIX 8 8 ILE A 129 LEU A 132 5 4
HELIX 9 9 ALA A 133 GLN A 154 1 22
HELIX 10 10 THR B 11 GLN B 37 1 27
HELIX 11 11 PRO B 38 GLY B 40 5 3
HELIX 12 12 THR B 42 GLU B 54 1 13
HELIX 13 13 SER B 55 GLY B 57 5 3
HELIX 14 14 MET B 62 THR B 69 1 8
HELIX 15 15 SER B 72 ALA B 86 1 15
HELIX 16 16 THR B 106 PHE B 128 1 23
HELIX 17 17 ILE B 129 LEU B 132 5 4
HELIX 18 18 ALA B 133 GLN B 154 1 22
HELIX 19 19 THR C 11 GLN C 37 1 27
HELIX 20 20 PRO C 38 GLY C 40 5 3
HELIX 21 21 THR C 42 GLU C 54 1 13
HELIX 22 22 SER C 55 GLY C 57 5 3
HELIX 23 23 MET C 62 THR C 69 1 8
HELIX 24 24 SER C 72 ALA C 86 1 15
HELIX 25 25 THR C 106 PHE C 128 1 23
HELIX 26 26 ILE C 129 LEU C 132 5 4
HELIX 27 27 ALA C 133 GLN C 154 1 22
HELIX 28 28 THR D 11 GLN D 37 1 27
HELIX 29 29 PRO D 38 GLY D 40 5 3
HELIX 30 30 THR D 42 GLU D 54 1 13
HELIX 31 31 SER D 55 GLY D 57 5 3
HELIX 32 32 MET D 62 THR D 69 1 8
HELIX 33 33 SER D 72 ALA D 86 1 15
HELIX 34 34 THR D 106 PHE D 128 1 23
HELIX 35 35 ILE D 129 LEU D 132 5 4
HELIX 36 36 ALA D 133 GLN D 154 1 22
SHEET 1 AA 3 ARG A 59 ARG A 61 0
SHEET 2 AA 3 PHE A 102 LEU A 105 -1 O ALA A 103 N MET A 60
SHEET 3 AA 3 VAL A 89 GLU A 92 -1 O ARG A 90 N VAL A 104
SHEET 1 BA 3 ARG B 59 ARG B 61 0
SHEET 2 BA 3 PHE B 102 LEU B 105 -1 O ALA B 103 N MET B 60
SHEET 3 BA 3 VAL B 89 GLU B 92 -1 O ARG B 90 N VAL B 104
SHEET 1 CA 3 ARG C 59 ARG C 61 0
SHEET 2 CA 3 LEU C 101 LEU C 105 -1 O ALA C 103 N MET C 60
SHEET 3 CA 3 VAL C 89 ASN C 93 -1 O ARG C 90 N VAL C 104
SHEET 1 DA 3 ARG D 59 ARG D 61 0
SHEET 2 DA 3 LEU D 101 LEU D 105 -1 O ALA D 103 N MET D 60
SHEET 3 DA 3 VAL D 89 ASN D 93 -1 O ARG D 90 N VAL D 104
LINK NA NA A 301 OD1 ASP A 58 1555 1555 2.65
LINK NA NA A 301 O SER A 53 1555 1555 2.80
LINK NA NA A 301 O HOH A2034 1555 1555 2.74
LINK NA NA A 301 OE2 GLU D 56 1555 1555 2.81
LINK NA NA A 301 O SER A 55 1555 1555 2.71
LINK NA NA B 301 O SER B 55 1555 1555 2.71
LINK NA NA B 301 CL CL B 303 1555 1555 3.04
LINK NA NA B 301 OD1 ASP B 58 1555 1555 2.80
LINK NA NA B 301 OE2 GLU C 56 1555 1545 2.97
LINK NA NA B 301 O SER B 53 1555 1555 2.67
LINK NA NA C 301 OD1 ASP C 58 1555 1555 2.67
LINK NA NA C 301 O SER C 55 1555 1555 2.77
LINK NA NA C 301 O SER C 53 1555 1555 2.84
LINK NA NA D 301 OE2 GLU A 56 1555 1555 2.61
LINK NA NA D 301 OD1 ASP D 58 1555 1555 2.59
LINK NA NA D 301 O SER D 53 1555 1555 2.87
LINK NA NA D 301 O SER D 55 1555 1555 2.70
SITE 1 AC1 8 TRP A 18 ARG A 19 LEU A 22 ARG A 26
SITE 2 AC1 8 EDO A 403 MET B 43 GLU B 47 HIS B 120
SITE 1 AC2 6 SER A 53 SER A 55 ASP A 58 CL A 303
SITE 2 AC2 6 HOH A2034 GLU D 56
SITE 1 AC3 4 GLY A 57 NA A 301 GLY D 57 NA D 301
SITE 1 AC4 4 ARG A 19 EDO A 403 TYR B 46 GLU B 54
SITE 1 AC5 7 GLN A 15 TRP A 18 ARG A 19 SAL A 201
SITE 2 AC5 7 EDO A 401 TYR B 46 HIS B 120
SITE 1 AC6 5 SER B 53 SER B 55 ASP B 58 CL B 303
SITE 2 AC6 5 GLU C 56
SITE 1 AC7 5 GLY B 57 NA B 301 GLY C 57 ASP C 58
SITE 2 AC7 5 NA C 301
SITE 1 AC8 5 MET A 43 HIS A 120 HOH A2031 TRP B 18
SITE 2 AC8 5 LEU B 22
SITE 1 AC9 3 GLN B 37 GLY B 40 ARG B 82
SITE 1 BC1 5 GLU B 56 CL B 303 SER C 53 SER C 55
SITE 2 BC1 5 ASP C 58
SITE 1 BC2 5 TRP C 18 LEU C 22 HOH C2089 GLU D 47
SITE 2 BC2 5 HIS D 120
SITE 1 BC3 7 MET C 43 TYR C 46 GLU C 47 HIS C 120
SITE 2 BC3 7 TRP D 18 LEU D 22 HOH D2072
SITE 1 BC4 5 GLU A 56 CL A 303 SER D 53 SER D 55
SITE 2 BC4 5 ASP D 58
SITE 1 BC5 3 ARG D 61 SER D 63 LEU D 101
CRYST1 43.648 120.483 144.290 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.022911 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006930 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
