HEADER DNA-BINDING PROTEIN 10-JUN-11 3ZQM
TITLE CRYSTAL STRUCTURE OF THE SMALL TERMINASE OLIGOMERIZATION
TITLE 2 CORE DOMAIN FROM A SPP1-LIKE BACTERIOPHAGE (CRYSTAL FORM 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TERMINASE SMALL SUBUNIT;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 FRAGMENT: OLIGOMERIZATION CORE DOMAIN, RESIDUES 53-120;
COMPND 5 SYNONYM: SF6 SMALL TERMINASE G1P, G1P;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS PHAGE SF6;
SOURCE 3 ORGANISM_TAXID: 10773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS DNA-BINDING PROTEIN, MOLECULAR MOTOR, DNA PACKAGING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.BUTTNER,M.CHECHIK,M.ORTIZ-LOMBARDIA,C.SMITS,V.CHECHIK,G.JESCHKE,
AUTHOR 2 E.DYKEMAN,S.BENINI,J.C.ALONSO,A.A.ANTSON
REVDAT 3 15-FEB-12 3ZQM 1 JRNL
REVDAT 2 18-JAN-12 3ZQM 1 JRNL
REVDAT 1 28-DEC-11 3ZQM 0
JRNL AUTH C.R.BUTTNER,M.CHECHIK,M.ORTIZ-LOMBARDIA,C.SMITS,I.O.EBONG,
JRNL AUTH 2 V.CHECHIK,G.JESCHKE,E.DYKEMAN,S.BENINI,C.V.ROBINSON,
JRNL AUTH 3 J.C.ALONSO,A.A.ANTSON
JRNL TITL STRUCTURAL BASIS FOR DNA RECOGNITION AND LOADING INTO A
JRNL TITL 2 VIRAL PACKAGING MOTOR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 811 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22207627
JRNL DOI 10.1073/PNAS.1110270109
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0116
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.92
REMARK 3 NUMBER OF REFLECTIONS : 49111
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) : 0.17389
REMARK 3 R VALUE (WORKING SET) : 0.17175
REMARK 3 FREE R VALUE : 0.21351
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2644
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) : 1.850
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.898
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3026
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.211
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.247
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4382
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 423
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.483
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18
REMARK 3 B22 (A**2) : -0.70
REMARK 3 B33 (A**2) : 0.90
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.09
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.286
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4395 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3075 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5862 ; 1.581 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7658 ; 0.919 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 564 ; 5.458 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 170 ;35.452 ;26.471
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 984 ;14.178 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;10.550 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 713 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4707 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 681 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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 : 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 62 A 79
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2320 60.5110 73.6140
REMARK 3 T TENSOR
REMARK 3 T11: 0.1993 T22: 0.3298
REMARK 3 T33: 0.3503 T12: -0.0241
REMARK 3 T13: -0.0892 T23: 0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 5.9572 L22: 0.8377
REMARK 3 L33: 5.4271 L12: -0.9806
REMARK 3 L13: -4.3725 L23: 1.9424
REMARK 3 S TENSOR
REMARK 3 S11: -0.0022 S12: 0.0278 S13: 0.0072
REMARK 3 S21: -0.0422 S22: 0.1725 S23: -0.0902
REMARK 3 S31: -0.1080 S32: 0.2851 S33: -0.1704
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 80 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2130 74.8040 66.8360
REMARK 3 T TENSOR
REMARK 3 T11: 0.3099 T22: 0.2177
REMARK 3 T33: 0.3179 T12: -0.0099
REMARK 3 T13: -0.0495 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.6719 L22: 1.2966
REMARK 3 L33: 1.2650 L12: -0.5726
REMARK 3 L13: 0.5931 L23: -0.7485
REMARK 3 S TENSOR
REMARK 3 S11: -0.1588 S12: -0.0752 S13: 0.1003
REMARK 3 S21: 0.0012 S22: 0.0447 S23: -0.2857
REMARK 3 S31: -0.1790 S32: -0.0663 S33: 0.1141
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 108 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4470 58.2580 77.7590
REMARK 3 T TENSOR
REMARK 3 T11: 0.2762 T22: 0.2796
REMARK 3 T33: 0.3001 T12: -0.0039
REMARK 3 T13: -0.0298 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 2.3085 L22: 3.7806
REMARK 3 L33: 3.0473 L12: -2.7168
REMARK 3 L13: 1.8898 L23: -1.3185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: -0.0159 S13: 0.0279
REMARK 3 S21: -0.0725 S22: -0.1242 S23: -0.0681
REMARK 3 S31: 0.1650 S32: -0.1894 S33: 0.0654
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 65 B 80
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2850 61.8380 87.2790
REMARK 3 T TENSOR
REMARK 3 T11: 0.3233 T22: 0.2723
REMARK 3 T33: 0.2715 T12: 0.0263
REMARK 3 T13: -0.1328 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 4.4688 L22: 0.7546
REMARK 3 L33: 3.0451 L12: -1.8148
REMARK 3 L13: -2.0629 L23: 0.6480
REMARK 3 S TENSOR
REMARK 3 S11: -0.3231 S12: -0.5483 S13: 0.2272
REMARK 3 S21: 0.1823 S22: 0.2257 S23: -0.1180
REMARK 3 S31: -0.3834 S32: 0.0987 S33: 0.0975
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 81 B 107
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4500 75.4820 73.1600
REMARK 3 T TENSOR
REMARK 3 T11: 0.3249 T22: 0.2205
REMARK 3 T33: 0.3062 T12: 0.0139
REMARK 3 T13: -0.1028 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4607 L22: 1.4256
REMARK 3 L33: 1.8387 L12: -0.4192
REMARK 3 L13: -0.2132 L23: -1.1300
REMARK 3 S TENSOR
REMARK 3 S11: -0.1121 S12: -0.0732 S13: 0.1732
REMARK 3 S21: 0.1328 S22: 0.1596 S23: -0.1019
REMARK 3 S31: -0.0774 S32: -0.0521 S33: -0.0474
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 108 B 120
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2460 56.9580 81.6510
REMARK 3 T TENSOR
REMARK 3 T11: 0.2983 T22: 0.3027
REMARK 3 T33: 0.2546 T12: 0.0028
REMARK 3 T13: -0.0192 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 3.6496 L22: 5.3403
REMARK 3 L33: 4.5493 L12: -3.1793
REMARK 3 L13: 4.0282 L23: -3.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.1064 S12: -0.1258 S13: 0.0968
REMARK 3 S21: -0.1008 S22: -0.1715 S23: -0.2436
REMARK 3 S31: 0.1566 S32: -0.2066 S33: 0.0650
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 64 C 80
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0510 59.1020 91.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.3393 T22: 0.3902
REMARK 3 T33: 0.1593 T12: 0.0049
REMARK 3 T13: 0.0090 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 10.7129 L22: 0.4531
REMARK 3 L33: 0.5040 L12: 1.2083
REMARK 3 L13: 2.2961 L23: 0.2322
REMARK 3 S TENSOR
REMARK 3 S11: 0.1472 S12: -0.8876 S13: 0.0974
REMARK 3 S21: 0.1585 S22: -0.1417 S23: 0.0943
REMARK 3 S31: -0.0154 S32: -0.2193 S33: -0.0055
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 81 C 108
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7720 71.6360 73.8390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2915 T22: 0.2795
REMARK 3 T33: 0.2977 T12: 0.0322
REMARK 3 T13: -0.0464 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 0.4862 L22: 2.2522
REMARK 3 L33: 1.3725 L12: 0.1756
REMARK 3 L13: 0.1867 L23: -1.6070
REMARK 3 S TENSOR
REMARK 3 S11: -0.2506 S12: -0.0990 S13: 0.1144
REMARK 3 S21: 0.0042 S22: 0.1187 S23: -0.0256
REMARK 3 S31: -0.1322 S32: -0.2081 S33: 0.1319
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 109 C 120
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4210 52.2500 80.0460
REMARK 3 T TENSOR
REMARK 3 T11: 0.3598 T22: 0.3323
REMARK 3 T33: 0.2250 T12: -0.0563
REMARK 3 T13: -0.0125 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.8494 L22: 4.7479
REMARK 3 L33: 8.7713 L12: -0.2437
REMARK 3 L13: 1.7933 L23: -5.9447
REMARK 3 S TENSOR
REMARK 3 S11: -0.1428 S12: -0.1197 S13: -0.0572
REMARK 3 S21: -0.2182 S22: -0.0743 S23: -0.2971
REMARK 3 S31: 0.3235 S32: -0.1923 S33: 0.2171
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 65 D 80
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6710 51.4000 85.0650
REMARK 3 T TENSOR
REMARK 3 T11: 0.2944 T22: 0.4187
REMARK 3 T33: 0.1548 T12: -0.0898
REMARK 3 T13: 0.1003 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 4.1627 L22: 0.6298
REMARK 3 L33: 10.1515 L12: 1.6000
REMARK 3 L13: 5.4788 L23: 2.1736
REMARK 3 S TENSOR
REMARK 3 S11: 0.0448 S12: -0.4913 S13: -0.0359
REMARK 3 S21: 0.0223 S22: -0.1273 S23: -0.0121
REMARK 3 S31: 0.0603 S32: -0.7922 S33: 0.0824
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 81 D 107
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5280 66.8900 68.4540
REMARK 3 T TENSOR
REMARK 3 T11: 0.2827 T22: 0.3189
REMARK 3 T33: 0.2721 T12: 0.0026
REMARK 3 T13: -0.0289 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.1717 L22: 3.1204
REMARK 3 L33: 1.5899 L12: -0.2745
REMARK 3 L13: 0.4608 L23: -1.3467
REMARK 3 S TENSOR
REMARK 3 S11: -0.1166 S12: -0.0765 S13: 0.0684
REMARK 3 S21: 0.1185 S22: 0.0228 S23: 0.0502
REMARK 3 S31: -0.0737 S32: -0.3129 S33: 0.0938
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 108 D 120
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0900 47.3800 71.4710
REMARK 3 T TENSOR
REMARK 3 T11: 0.3381 T22: 0.3200
REMARK 3 T33: 0.2180 T12: -0.0718
REMARK 3 T13: 0.0487 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.2023 L22: 4.1148
REMARK 3 L33: 6.2192 L12: -0.4717
REMARK 3 L13: -0.1800 L23: -2.9851
REMARK 3 S TENSOR
REMARK 3 S11: -0.1015 S12: 0.1925 S13: 0.0728
REMARK 3 S21: 0.1999 S22: -0.1129 S23: -0.2759
REMARK 3 S31: 0.3612 S32: -0.1719 S33: 0.2144
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 : E 64 E 80
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6930 43.4040 72.5500
REMARK 3 T TENSOR
REMARK 3 T11: 0.3443 T22: 0.2915
REMARK 3 T33: 0.2056 T12: -0.2055
REMARK 3 T13: 0.1875 T23: -0.0824
REMARK 3 L TENSOR
REMARK 3 L11: 1.8203 L22: 0.6445
REMARK 3 L33: 8.0013 L12: -0.3054
REMARK 3 L13: -1.5656 L23: 2.2455
REMARK 3 S TENSOR
REMARK 3 S11: -0.1052 S12: -0.0824 S13: -0.0453
REMARK 3 S21: 0.0880 S22: -0.1593 S23: 0.0879
REMARK 3 S31: 0.2685 S32: -0.3651 S33: 0.2646
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 : E 81 E 108
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8520 60.7980 58.5200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2413 T22: 0.3088
REMARK 3 T33: 0.2853 T12: 0.0018
REMARK 3 T13: -0.0355 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 0.0564 L22: 3.9318
REMARK 3 L33: 1.0122 L12: -0.1518
REMARK 3 L13: -0.2230 L23: 0.0772
REMARK 3 S TENSOR
REMARK 3 S11: -0.0168 S12: 0.0467 S13: -0.0247
REMARK 3 S21: -0.1076 S22: -0.1511 S23: 0.1778
REMARK 3 S31: 0.0044 S32: -0.1493 S33: 0.1679
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 : E 109 E 120
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8140 41.8400 62.0430
REMARK 3 T TENSOR
REMARK 3 T11: 0.3242 T22: 0.3005
REMARK 3 T33: 0.2611 T12: -0.0423
REMARK 3 T13: 0.0244 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.3958 L22: 6.8450
REMARK 3 L33: 3.0446 L12: 1.2808
REMARK 3 L13: -0.9659 L23: -1.9163
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.0043 S13: 0.0257
REMARK 3 S21: 0.2786 S22: -0.0494 S23: -0.0777
REMARK 3 S31: 0.2616 S32: -0.0521 S33: 0.0609
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 : F 65 F 84
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3340 37.6600 54.7850
REMARK 3 T TENSOR
REMARK 3 T11: 0.3346 T22: 0.3009
REMARK 3 T33: 0.2615 T12: -0.0883
REMARK 3 T13: 0.0300 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 0.0388 L22: 2.2011
REMARK 3 L33: 2.9045 L12: 0.1458
REMARK 3 L13: -0.0156 L23: 2.1150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0126 S12: -0.0492 S13: -0.0275
REMARK 3 S21: 0.1316 S22: -0.4121 S23: 0.2091
REMARK 3 S31: 0.2096 S32: -0.1877 S33: 0.4247
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 : F 85 F 107
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3190 60.2070 48.7470
REMARK 3 T TENSOR
REMARK 3 T11: 0.3124 T22: 0.2857
REMARK 3 T33: 0.2614 T12: 0.0544
REMARK 3 T13: -0.0256 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0366 L22: 1.4550
REMARK 3 L33: 0.7178 L12: 0.0554
REMARK 3 L13: -0.0593 L23: 0.6179
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: -0.0493 S13: -0.0551
REMARK 3 S21: -0.2838 S22: -0.0935 S23: 0.1458
REMARK 3 S31: -0.1357 S32: -0.0557 S33: 0.1005
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 : F 108 F 120
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0960 40.7500 53.1620
REMARK 3 T TENSOR
REMARK 3 T11: 0.2902 T22: 0.2757
REMARK 3 T33: 0.2785 T12: -0.0001
REMARK 3 T13: 0.0102 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 1.3728 L22: 7.9284
REMARK 3 L33: 1.3009 L12: 2.4431
REMARK 3 L13: -0.8273 L23: -2.9005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0420 S12: -0.1118 S13: -0.0968
REMARK 3 S21: 0.0242 S22: -0.1280 S23: -0.2091
REMARK 3 S31: 0.0151 S32: 0.0889 S33: 0.0860
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 : G 63 G 84
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5850 35.6280 44.0970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2874 T22: 0.2687
REMARK 3 T33: 0.3201 T12: 0.0321
REMARK 3 T13: 0.0014 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 1.0443 L22: 1.1270
REMARK 3 L33: 1.2407 L12: 0.7067
REMARK 3 L13: -0.4406 L23: 0.5209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0809 S12: 0.1689 S13: -0.1663
REMARK 3 S21: 0.1682 S22: -0.0070 S23: -0.2241
REMARK 3 S31: 0.1561 S32: -0.1647 S33: -0.0739
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 : G 85 G 107
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4850 59.4810 42.1090
REMARK 3 T TENSOR
REMARK 3 T11: 0.3731 T22: 0.2796
REMARK 3 T33: 0.2124 T12: 0.0283
REMARK 3 T13: 0.0254 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 1.0863 L22: 1.5707
REMARK 3 L33: 0.1207 L12: -0.3763
REMARK 3 L13: 0.1749 L23: 0.2840
REMARK 3 S TENSOR
REMARK 3 S11: -0.0684 S12: -0.1309 S13: -0.1475
REMARK 3 S21: -0.4034 S22: 0.1218 S23: 0.0146
REMARK 3 S31: -0.1464 S32: 0.0208 S33: -0.0534
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 : G 108 G 120
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1450 41.9750 49.4690
REMARK 3 T TENSOR
REMARK 3 T11: 0.1761 T22: 0.3221
REMARK 3 T33: 0.3918 T12: 0.0653
REMARK 3 T13: 0.0577 T23: -0.0476
REMARK 3 L TENSOR
REMARK 3 L11: 3.9113 L22: 10.4737
REMARK 3 L33: 0.2988 L12: 0.5995
REMARK 3 L13: -0.9909 L23: -0.1926
REMARK 3 S TENSOR
REMARK 3 S11: -0.1684 S12: -0.3746 S13: -0.0797
REMARK 3 S21: 0.1067 S22: 0.3100 S23: 0.0956
REMARK 3 S31: 0.0201 S32: 0.1527 S33: -0.1416
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 : H 66 H 80
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7480 38.6460 41.7400
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.3143
REMARK 3 T33: 0.3568 T12: 0.1064
REMARK 3 T13: -0.0260 T23: -0.0696
REMARK 3 L TENSOR
REMARK 3 L11: 9.2186 L22: 8.6839
REMARK 3 L33: 2.4504 L12: 6.5227
REMARK 3 L13: 0.0245 L23: 3.1729
REMARK 3 S TENSOR
REMARK 3 S11: -0.3455 S12: 0.2977 S13: -0.1193
REMARK 3 S21: -0.3573 S22: 0.6180 S23: -0.4219
REMARK 3 S31: -0.0712 S32: 0.2999 S33: -0.2725
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 : H 81 H 107
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9050 60.4470 40.9200
REMARK 3 T TENSOR
REMARK 3 T11: 0.3152 T22: 0.3039
REMARK 3 T33: 0.2419 T12: -0.0472
REMARK 3 T13: 0.0999 T23: 0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 0.7841 L22: 3.0570
REMARK 3 L33: 0.1652 L12: -0.7155
REMARK 3 L13: 0.1111 L23: 0.4931
REMARK 3 S TENSOR
REMARK 3 S11: -0.1935 S12: 0.0745 S13: -0.0682
REMARK 3 S21: -0.4747 S22: 0.2793 S23: -0.1806
REMARK 3 S31: -0.1965 S32: 0.0990 S33: -0.0858
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 : H 108 H 120
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9190 46.1280 52.0940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1335 T22: 0.3049
REMARK 3 T33: 0.3848 T12: 0.0532
REMARK 3 T13: 0.0326 T23: -0.0846
REMARK 3 L TENSOR
REMARK 3 L11: 1.9710 L22: 7.6035
REMARK 3 L33: 1.3951 L12: 1.5031
REMARK 3 L13: 0.5078 L23: 1.0744
REMARK 3 S TENSOR
REMARK 3 S11: 0.1784 S12: 0.1126 S13: -0.1469
REMARK 3 S21: 0.1163 S22: 0.3898 S23: 0.0295
REMARK 3 S31: 0.0426 S32: 0.3473 S33: -0.5683
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 : I 63 I 80
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0240 45.3140 45.5070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0413 T22: 0.4660
REMARK 3 T33: 0.3966 T12: 0.0949
REMARK 3 T13: -0.0119 T23: -0.2465
REMARK 3 L TENSOR
REMARK 3 L11: 2.0145 L22: 4.5580
REMARK 3 L33: 7.5196 L12: 2.5571
REMARK 3 L13: 1.1700 L23: 4.4805
REMARK 3 S TENSOR
REMARK 3 S11: -0.1136 S12: 0.2636 S13: -0.1225
REMARK 3 S21: -0.0821 S22: 0.5575 S23: -0.3096
REMARK 3 S31: 0.0863 S32: 0.6671 S33: -0.4439
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 : I 81 I 107
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5650 65.7670 46.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.2355 T22: 0.3188
REMARK 3 T33: 0.3131 T12: -0.1332
REMARK 3 T13: 0.0914 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 1.5647 L22: 2.1475
REMARK 3 L33: 0.4917 L12: -0.9578
REMARK 3 L13: 0.6195 L23: 0.1979
REMARK 3 S TENSOR
REMARK 3 S11: -0.1343 S12: 0.1593 S13: 0.1176
REMARK 3 S21: -0.2777 S22: 0.2165 S23: -0.2160
REMARK 3 S31: -0.2163 S32: 0.2377 S33: -0.0822
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 : I 108 I 120
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5910 51.5200 59.6750
REMARK 3 T TENSOR
REMARK 3 T11: 0.1808 T22: 0.3417
REMARK 3 T33: 0.3745 T12: 0.0006
REMARK 3 T13: 0.0943 T23: -0.0816
REMARK 3 L TENSOR
REMARK 3 L11: 2.9481 L22: 10.5086
REMARK 3 L33: 0.3013 L12: -2.9581
REMARK 3 L13: 0.0835 L23: 1.3990
REMARK 3 S TENSOR
REMARK 3 S11: -0.3814 S12: 0.3730 S13: -0.4245
REMARK 3 S21: 0.3251 S22: 0.4757 S23: 0.2190
REMARK 3 S31: -0.0466 S32: 0.1761 S33: -0.0943
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 : J 65 J 80
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6700 53.6120 60.3250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0920 T22: 0.3932
REMARK 3 T33: 0.4250 T12: -0.0040
REMARK 3 T13: 0.0393 T23: -0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 2.9728 L22: 3.4206
REMARK 3 L33: 2.7734 L12: 1.3205
REMARK 3 L13: 1.8036 L23: 2.9814
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.3035 S13: -0.2069
REMARK 3 S21: -0.1790 S22: 0.3442 S23: -0.3364
REMARK 3 S31: -0.1641 S32: 0.3307 S33: -0.3045
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 : J 81 J 108
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1410 70.9840 56.7210
REMARK 3 T TENSOR
REMARK 3 T11: 0.2774 T22: 0.2693
REMARK 3 T33: 0.3292 T12: -0.0935
REMARK 3 T13: 0.0201 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.4694 L22: 0.6012
REMARK 3 L33: 1.7166 L12: -0.5699
REMARK 3 L13: 1.4279 L23: -0.2242
REMARK 3 S TENSOR
REMARK 3 S11: -0.1619 S12: 0.0047 S13: 0.1705
REMARK 3 S21: -0.0602 S22: 0.1289 S23: -0.2291
REMARK 3 S31: -0.1807 S32: 0.1680 S33: 0.0330
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 : J 109 J 120
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7050 55.7290 69.7870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1929 T22: 0.3012
REMARK 3 T33: 0.3493 T12: -0.0074
REMARK 3 T13: -0.0315 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 2.8857 L22: 3.2222
REMARK 3 L33: 3.2556 L12: -2.7504
REMARK 3 L13: 0.3215 L23: -1.6845
REMARK 3 S TENSOR
REMARK 3 S11: 0.0459 S12: -0.0826 S13: 0.0351
REMARK 3 S21: -0.1103 S22: 0.1362 S23: 0.0020
REMARK 3 S31: 0.1958 S32: -0.0402 S33: -0.1821
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
REMARK 3 RIDING POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 3ZQM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-11.
REMARK 100 THE PDBE ID CODE IS EBI-48581.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.971557
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52842
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.85
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.6
REMARK 200 R MERGE FOR SHELL (I) : 0.36
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MALONATE/IMIDAZOLE/BORIC
REMARK 280 ACID BUFFER SYSTEM PH 7.0, 25 % PEG 1500
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 30.00450
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, J, I, B, C, D, E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 49
REMARK 465 SER A 50
REMARK 465 HIS A 51
REMARK 465 MSE A 52
REMARK 465 ALA A 53
REMARK 465 ARG A 54
REMARK 465 ILE A 55
REMARK 465 ASP A 56
REMARK 465 ALA A 57
REMARK 465 ARG A 58
REMARK 465 LEU A 59
REMARK 465 LYS A 60
REMARK 465 GLU A 61
REMARK 465 GLY B 49
REMARK 465 SER B 50
REMARK 465 HIS B 51
REMARK 465 MSE B 52
REMARK 465 ALA B 53
REMARK 465 ARG B 54
REMARK 465 ILE B 55
REMARK 465 ASP B 56
REMARK 465 ALA B 57
REMARK 465 ARG B 58
REMARK 465 LEU B 59
REMARK 465 LYS B 60
REMARK 465 GLU B 61
REMARK 465 ILE B 62
REMARK 465 ASN B 63
REMARK 465 GLU B 64
REMARK 465 GLY C 49
REMARK 465 SER C 50
REMARK 465 HIS C 51
REMARK 465 MSE C 52
REMARK 465 ALA C 53
REMARK 465 ARG C 54
REMARK 465 ILE C 55
REMARK 465 ASP C 56
REMARK 465 ALA C 57
REMARK 465 ARG C 58
REMARK 465 LEU C 59
REMARK 465 LYS C 60
REMARK 465 GLU C 61
REMARK 465 ILE C 62
REMARK 465 ASN C 63
REMARK 465 GLU C 64
REMARK 465 GLY D 49
REMARK 465 SER D 50
REMARK 465 HIS D 51
REMARK 465 MSE D 52
REMARK 465 ALA D 53
REMARK 465 ARG D 54
REMARK 465 ILE D 55
REMARK 465 ASP D 56
REMARK 465 ALA D 57
REMARK 465 ARG D 58
REMARK 465 LEU D 59
REMARK 465 LYS D 60
REMARK 465 GLU D 61
REMARK 465 ILE D 62
REMARK 465 ASN D 63
REMARK 465 GLU D 64
REMARK 465 GLY E 49
REMARK 465 SER E 50
REMARK 465 HIS E 51
REMARK 465 MSE E 52
REMARK 465 ALA E 53
REMARK 465 ARG E 54
REMARK 465 ILE E 55
REMARK 465 ASP E 56
REMARK 465 ALA E 57
REMARK 465 ARG E 58
REMARK 465 LEU E 59
REMARK 465 LYS E 60
REMARK 465 GLU E 61
REMARK 465 ILE E 62
REMARK 465 ASN E 63
REMARK 465 GLY F 49
REMARK 465 SER F 50
REMARK 465 HIS F 51
REMARK 465 MSE F 52
REMARK 465 ALA F 53
REMARK 465 ARG F 54
REMARK 465 ILE F 55
REMARK 465 ASP F 56
REMARK 465 ALA F 57
REMARK 465 ARG F 58
REMARK 465 LEU F 59
REMARK 465 LYS F 60
REMARK 465 GLU F 61
REMARK 465 ILE F 62
REMARK 465 ASN F 63
REMARK 465 GLU F 64
REMARK 465 GLY G 49
REMARK 465 SER G 50
REMARK 465 HIS G 51
REMARK 465 MSE G 52
REMARK 465 ALA G 53
REMARK 465 ARG G 54
REMARK 465 ILE G 55
REMARK 465 ASP G 56
REMARK 465 ALA G 57
REMARK 465 ARG G 58
REMARK 465 LEU G 59
REMARK 465 LYS G 60
REMARK 465 GLU G 61
REMARK 465 GLY H 49
REMARK 465 SER H 50
REMARK 465 HIS H 51
REMARK 465 MSE H 52
REMARK 465 ALA H 53
REMARK 465 ARG H 54
REMARK 465 ILE H 55
REMARK 465 ASP H 56
REMARK 465 ALA H 57
REMARK 465 ARG H 58
REMARK 465 LEU H 59
REMARK 465 LYS H 60
REMARK 465 GLU H 61
REMARK 465 ILE H 62
REMARK 465 ASN H 63
REMARK 465 GLU H 64
REMARK 465 LYS H 65
REMARK 465 GLY I 49
REMARK 465 SER I 50
REMARK 465 HIS I 51
REMARK 465 MSE I 52
REMARK 465 ALA I 53
REMARK 465 ARG I 54
REMARK 465 ILE I 55
REMARK 465 ASP I 56
REMARK 465 ALA I 57
REMARK 465 ARG I 58
REMARK 465 LEU I 59
REMARK 465 LYS I 60
REMARK 465 GLU I 61
REMARK 465 ILE I 62
REMARK 465 GLY J 49
REMARK 465 SER J 50
REMARK 465 HIS J 51
REMARK 465 MSE J 52
REMARK 465 ALA J 53
REMARK 465 ARG J 54
REMARK 465 ILE J 55
REMARK 465 ASP J 56
REMARK 465 ALA J 57
REMARK 465 ARG J 58
REMARK 465 LEU J 59
REMARK 465 LYS J 60
REMARK 465 GLU J 61
REMARK 465 ILE J 62
REMARK 465 ASN J 63
REMARK 465 GLU J 64
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 J 110 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CMP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF G1P
REMARK 900 SMALL TERMINASE SUBUNIT FROM BACTERIOPHAGE SF6
REMARK 900 RELATED ID: 3ZQN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SMALL TERMINASE OLIGOMERIZATION
REMARK 900 CORE DOMAIN FROM A SPP1-LIKE BACTERIOPHAGE (CRYSTAL FORM 2)
REMARK 900 RELATED ID: 3ZQQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FULL-LENGTH SMALL TERMINASE
REMARK 900 FROM A SPP1-LIKE BACTERIOPHAGE
REMARK 900 RELATED ID: 3ZQP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SMALL TERMINASE OLIGOMERIZATION
REMARK 900 DOMAIN FROM A SPP1-LIKE BACTERIOPHAGE
REMARK 900 RELATED ID: 3ZQO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SMALL TERMINASE OLIGOMERIZATION
REMARK 900 CORE DOMAIN FROM A SPP1-LIKE BACTERIOPHAGE (CRYSTAL FORM 3)
DBREF 3ZQM A 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM B 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM C 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM D 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM E 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM F 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM G 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM H 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM I 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
DBREF 3ZQM J 53 120 UNP Q1EJR8 Q1EJR8_BPSF6 53 120
SEQADV 3ZQM GLY A 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER A 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS A 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE A 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY B 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER B 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS B 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE B 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY C 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER C 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS C 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE C 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY D 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER D 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS D 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE D 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY E 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER E 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS E 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE E 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY F 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER F 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS F 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE F 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY G 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER G 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS G 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE G 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY H 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER H 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS H 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE H 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY I 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER I 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS I 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE I 52 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM GLY J 49 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM SER J 50 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM HIS J 51 UNP Q1EJR8 EXPRESSION TAG
SEQADV 3ZQM MSE J 52 UNP Q1EJR8 EXPRESSION TAG
SEQRES 1 A 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 A 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 A 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 A 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 A 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 A 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 B 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 B 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 B 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 B 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 B 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 B 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 C 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 C 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 C 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 C 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 C 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 C 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 D 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 D 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 D 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 D 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 D 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 D 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 E 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 E 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 E 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 E 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 E 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 E 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 F 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 F 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 F 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 F 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 F 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 F 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 G 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 G 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 G 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 G 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 G 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 G 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 H 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 H 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 H 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 H 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 H 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 H 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 I 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 I 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 I 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 I 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 I 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 I 72 LEU GLU LEU LEU GLY LYS ALA
SEQRES 1 J 72 GLY SER HIS MSE ALA ARG ILE ASP ALA ARG LEU LYS GLU
SEQRES 2 J 72 ILE ASN GLU LYS LYS ILE LEU GLN ALA ASN GLU VAL LEU
SEQRES 3 J 72 GLU HIS LEU THR ARG ILE ALA LEU GLY GLN GLU LYS GLU
SEQRES 4 J 72 GLN VAL LEU MSE GLY ILE GLY LYS GLY ALA GLU THR LYS
SEQRES 5 J 72 THR HIS VAL GLU VAL SER ALA LYS ASP ARG ILE LYS ALA
SEQRES 6 J 72 LEU GLU LEU LEU GLY LYS ALA
MODRES 3ZQM MSE A 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE B 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE C 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE D 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE E 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE F 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE G 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE H 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE I 91 MET SELENOMETHIONINE
MODRES 3ZQM MSE J 91 MET SELENOMETHIONINE
HET MSE A 91 8
HET MSE B 91 8
HET MSE C 91 8
HET MSE D 91 8
HET MSE E 91 8
HET MSE F 91 8
HET MSE G 91 8
HET MSE H 91 8
HET MSE I 91 8
HET MSE J 91 8
HETNAM MSE SELENOMETHIONINE
FORMUL 11 MSE 10(C5 H11 N O2 SE)
FORMUL 12 HOH *423(H2 O)
HELIX 1 1 GLN A 69 LEU A 82 1 14
HELIX 2 2 SER A 106 ALA A 120 1 15
HELIX 3 3 GLN B 69 LEU B 82 1 14
HELIX 4 4 SER B 106 ALA B 120 1 15
HELIX 5 5 GLN C 69 LEU C 82 1 14
HELIX 6 6 SER C 106 ALA C 120 1 15
HELIX 7 7 GLN D 69 LEU D 82 1 14
HELIX 8 8 SER D 106 LYS D 119 1 14
HELIX 9 9 GLN E 69 LEU E 82 1 14
HELIX 10 10 SER E 106 ALA E 120 1 15
HELIX 11 11 GLN F 69 LEU F 82 1 14
HELIX 12 12 SER F 106 ALA F 120 1 15
HELIX 13 13 GLN G 69 LEU G 82 1 14
HELIX 14 14 SER G 106 ALA G 120 1 15
HELIX 15 15 GLN H 69 LEU H 82 1 14
HELIX 16 16 SER H 106 ALA H 120 1 15
HELIX 17 17 GLN I 69 LEU I 82 1 14
HELIX 18 18 SER I 106 ALA I 120 1 15
HELIX 19 19 GLN J 69 LEU J 82 1 14
HELIX 20 20 SER J 106 ALA J 120 1 15
SHEET 1 AA 2 LYS A 86 GLY A 94 0
SHEET 2 AA 2 ALA A 97 GLU A 104 -1 O ALA A 97 N ILE A 93
SHEET 1 BA 2 LYS B 86 GLY B 94 0
SHEET 2 BA 2 ALA B 97 GLU B 104 -1 O ALA B 97 N ILE B 93
SHEET 1 CA 2 LYS C 86 GLY C 94 0
SHEET 2 CA 2 ALA C 97 GLU C 104 -1 O ALA C 97 N ILE C 93
SHEET 1 DA 2 LYS D 86 GLY D 94 0
SHEET 2 DA 2 ALA D 97 GLU D 104 -1 O ALA D 97 N ILE D 93
SHEET 1 EA 2 LYS E 86 GLY E 94 0
SHEET 2 EA 2 ALA E 97 GLU E 104 -1 O ALA E 97 N ILE E 93
SHEET 1 FA 2 LYS F 86 GLY F 94 0
SHEET 2 FA 2 ALA F 97 GLU F 104 -1 O ALA F 97 N ILE F 93
SHEET 1 GA 2 LYS G 86 GLY G 94 0
SHEET 2 GA 2 ALA G 97 GLU G 104 -1 O ALA G 97 N ILE G 93
SHEET 1 HA 2 LYS H 86 GLY H 94 0
SHEET 2 HA 2 ALA H 97 GLU H 104 -1 O ALA H 97 N ILE H 93
SHEET 1 IA 2 LYS I 86 GLY I 94 0
SHEET 2 IA 2 ALA I 97 GLU I 104 -1 O ALA I 97 N ILE I 93
SHEET 1 JA 2 LYS J 86 GLY J 94 0
SHEET 2 JA 2 ALA J 97 GLU J 104 -1 O ALA J 97 N ILE J 93
LINK C LEU A 90 N MSE A 91 1555 1555 1.32
LINK C MSE A 91 N GLY A 92 1555 1555 1.33
LINK C LEU B 90 N MSE B 91 1555 1555 1.32
LINK C MSE B 91 N GLY B 92 1555 1555 1.33
LINK C LEU C 90 N MSE C 91 1555 1555 1.33
LINK C MSE C 91 N GLY C 92 1555 1555 1.31
LINK C LEU D 90 N MSE D 91 1555 1555 1.33
LINK C MSE D 91 N GLY D 92 1555 1555 1.32
LINK C LEU E 90 N MSE E 91 1555 1555 1.34
LINK C MSE E 91 N GLY E 92 1555 1555 1.32
LINK C LEU F 90 N MSE F 91 1555 1555 1.34
LINK C MSE F 91 N GLY F 92 1555 1555 1.32
LINK C LEU G 90 N MSE G 91 1555 1555 1.33
LINK C MSE G 91 N GLY G 92 1555 1555 1.33
LINK C LEU H 90 N MSE H 91 1555 1555 1.32
LINK C MSE H 91 N GLY H 92 1555 1555 1.33
LINK C LEU I 90 N MSE I 91 1555 1555 1.32
LINK C MSE I 91 N GLY I 92 1555 1555 1.33
LINK C LEU J 90 N MSE J 91 1555 1555 1.33
LINK C MSE J 91 N GLY J 92 1555 1555 1.33
CRYST1 64.954 60.009 81.442 90.00 100.43 90.00 P 1 21 1 20
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 0.015396 0.000000 0.002834 0.00000
SCALE2 0.000000 0.016664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012485 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
