HEADER IMMUNE SYSTEM/DNA 15-APR-15 4ZBN
TITLE NON-HELICAL DNA TRIPLEX FORMS A UNIQUE APTAMER SCAFFOLD FOR HIGH
TITLE 2 AFFINITY RECOGNITION OF NERVE GROWTH FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (28-MER);
COMPND 3 CHAIN: D, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BETA-NERVE GROWTH FACTOR;
COMPND 7 CHAIN: A, B;
COMPND 8 SYNONYM: BETA-NGF;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 GENE: NGF, NGFB;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, APTAMER, IMMUNE SYSTEM-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.DAVIES,T.E.EDWARDS
REVDAT 3 15-JUL-15 4ZBN 1 JRNL
REVDAT 2 17-JUN-15 4ZBN 1 JRNL
REVDAT 1 10-JUN-15 4ZBN 0
JRNL AUTH T.C.JARVIS,D.R.DAVIES,A.HISAMINATO,D.I.RESNICOW,S.GUPTA,
JRNL AUTH 2 S.M.WAUGH,A.NAGABUKURO,T.WADATSU,H.HISHIGAKI,B.GAWANDE,
JRNL AUTH 3 C.ZHANG,S.K.WOLK,W.S.MAYFIELD,Y.NAKAISHI,A.B.BURGIN,
JRNL AUTH 4 L.J.STEWART,T.E.EDWARDS,A.D.GELINAS,D.J.SCHNEIDER,N.JANJIC
JRNL TITL NON-HELICAL DNA TRIPLEX FORMS A UNIQUE APTAMER SCAFFOLD FOR
JRNL TITL 2 HIGH AFFINITY RECOGNITION OF NERVE GROWTH FACTOR.
JRNL REF STRUCTURE V. 23 1293 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26027732
JRNL DOI 10.1016/J.STR.2015.03.027
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 15532
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 824
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 970
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.15
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1506
REMARK 3 NUCLEIC ACID ATOMS : 1320
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.64000
REMARK 3 B22 (A**2) : 0.24000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.429
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.277
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.699
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3055 ; 0.013 ; 0.017
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4274 ; 2.112 ; 1.857
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 194 ; 8.219 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 66 ;27.225 ;22.424
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 243 ;16.097 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;20.219 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 434 ; 0.168 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1974 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 783 ; 2.558 ; 3.260
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 967 ; 3.971 ; 4.855
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2272 ; 3.125 ; 3.210
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4972 ; 7.427 ;29.402
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 : 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 11 A 32
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8233 -0.5409 12.3699
REMARK 3 T TENSOR
REMARK 3 T11: 0.1367 T22: 0.0917
REMARK 3 T33: 0.0681 T12: 0.0334
REMARK 3 T13: 0.0283 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 2.9313 L22: 2.9978
REMARK 3 L33: 3.2203 L12: 1.2231
REMARK 3 L13: 0.2150 L23: -0.0354
REMARK 3 S TENSOR
REMARK 3 S11: 0.1380 S12: 0.0431 S13: 0.3640
REMARK 3 S21: -0.0240 S22: -0.1919 S23: 0.3247
REMARK 3 S31: -0.3619 S32: -0.2808 S33: 0.0539
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 33 A 52
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6930 -12.2527 3.7944
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: 0.1411
REMARK 3 T33: 0.1277 T12: -0.0411
REMARK 3 T13: -0.0530 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 10.9351 L22: 3.1946
REMARK 3 L33: 6.4275 L12: 3.5472
REMARK 3 L13: -3.8525 L23: -1.1295
REMARK 3 S TENSOR
REMARK 3 S11: 0.0671 S12: 0.4655 S13: 0.0593
REMARK 3 S21: -0.2978 S22: 0.2450 S23: 0.3827
REMARK 3 S31: 0.2517 S32: -0.7259 S33: -0.3122
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 53 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0804 7.9916 18.7060
REMARK 3 T TENSOR
REMARK 3 T11: 0.2203 T22: 0.2325
REMARK 3 T33: 0.2097 T12: -0.1083
REMARK 3 T13: 0.0568 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 6.1493 L22: 2.3822
REMARK 3 L33: 1.9704 L12: 2.5259
REMARK 3 L13: 2.4359 L23: 1.8360
REMARK 3 S TENSOR
REMARK 3 S11: -0.3984 S12: 0.2935 S13: 0.8608
REMARK 3 S21: -0.2309 S22: 0.1685 S23: 0.3637
REMARK 3 S31: -0.4434 S32: 0.4316 S33: 0.2298
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 76 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9039 -2.3780 9.1516
REMARK 3 T TENSOR
REMARK 3 T11: 0.0812 T22: 0.1790
REMARK 3 T33: 0.0278 T12: 0.0284
REMARK 3 T13: 0.0000 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 3.7199 L22: 5.3970
REMARK 3 L33: 3.7735 L12: 3.2289
REMARK 3 L13: 1.7308 L23: 3.0550
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.3401 S13: 0.0146
REMARK 3 S21: -0.1550 S22: -0.0642 S23: 0.0532
REMARK 3 S31: -0.0386 S32: 0.0842 S33: 0.0755
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 103
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4178 -13.4620 0.4902
REMARK 3 T TENSOR
REMARK 3 T11: 0.3014 T22: 0.3217
REMARK 3 T33: 0.1275 T12: 0.0442
REMARK 3 T13: 0.0360 T23: -0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 6.0857 L22: 5.4272
REMARK 3 L33: 11.4370 L12: 2.0472
REMARK 3 L13: 7.4812 L23: 5.7236
REMARK 3 S TENSOR
REMARK 3 S11: -0.0846 S12: 0.5423 S13: -0.0497
REMARK 3 S21: -0.4446 S22: -0.1563 S23: 0.3562
REMARK 3 S31: -0.2735 S32: 0.3732 S33: 0.2409
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 104 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1103 4.0268 15.4967
REMARK 3 T TENSOR
REMARK 3 T11: 0.2240 T22: 0.2711
REMARK 3 T33: 0.1321 T12: -0.0133
REMARK 3 T13: -0.0322 T23: 0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 4.0970 L22: 8.7684
REMARK 3 L33: 2.4479 L12: 3.1607
REMARK 3 L13: 1.7719 L23: 4.4365
REMARK 3 S TENSOR
REMARK 3 S11: -0.1372 S12: 0.1409 S13: 0.3688
REMARK 3 S21: 0.0720 S22: 0.0821 S23: 0.1441
REMARK 3 S31: -0.0250 S32: 0.1615 S33: 0.0551
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 4 B 9
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3386 3.5079 8.6129
REMARK 3 T TENSOR
REMARK 3 T11: 0.2567 T22: 0.2899
REMARK 3 T33: 0.2302 T12: 0.0013
REMARK 3 T13: -0.0460 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 12.3439 L22: 9.0514
REMARK 3 L33: 1.1414 L12: -1.5108
REMARK 3 L13: -3.7466 L23: 0.5524
REMARK 3 S TENSOR
REMARK 3 S11: 0.5908 S12: 0.4326 S13: 0.6331
REMARK 3 S21: -0.8723 S22: -0.3764 S23: 0.1695
REMARK 3 S31: -0.1829 S32: -0.1266 S33: -0.2143
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 10 B 25
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3939 -8.3863 16.4666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.1635
REMARK 3 T33: 0.1097 T12: 0.1022
REMARK 3 T13: -0.0595 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 6.7215 L22: 6.1293
REMARK 3 L33: 2.2861 L12: 3.9769
REMARK 3 L13: -0.4577 L23: 1.0713
REMARK 3 S TENSOR
REMARK 3 S11: 0.2727 S12: -0.1199 S13: -0.6852
REMARK 3 S21: 0.4768 S22: -0.1595 S23: -0.7911
REMARK 3 S31: 0.2726 S32: 0.3790 S33: -0.1132
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 26 B 52
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5889 -21.6176 16.4329
REMARK 3 T TENSOR
REMARK 3 T11: 0.3553 T22: 0.0836
REMARK 3 T33: 0.2741 T12: -0.1199
REMARK 3 T13: -0.2192 T23: 0.1076
REMARK 3 L TENSOR
REMARK 3 L11: 5.5628 L22: 6.2909
REMARK 3 L33: 7.3578 L12: -1.9481
REMARK 3 L13: -3.4823 L23: -0.4194
REMARK 3 S TENSOR
REMARK 3 S11: 0.3317 S12: -0.2423 S13: -0.6999
REMARK 3 S21: -0.3612 S22: -0.0904 S23: -0.1811
REMARK 3 S31: 1.0667 S32: -0.2519 S33: -0.2413
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 53 B 78
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6577 -0.1495 25.5396
REMARK 3 T TENSOR
REMARK 3 T11: 0.2330 T22: 0.2680
REMARK 3 T33: 0.0224 T12: -0.0408
REMARK 3 T13: -0.0454 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 4.8108 L22: 8.5950
REMARK 3 L33: 3.3488 L12: 5.4408
REMARK 3 L13: 2.1644 L23: 2.9640
REMARK 3 S TENSOR
REMARK 3 S11: 0.6338 S12: -0.6638 S13: -0.0451
REMARK 3 S21: 1.2879 S22: -0.5558 S23: -0.2528
REMARK 3 S31: 0.4870 S32: 0.2938 S33: -0.0780
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 : B 79 B 99
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2156 -12.6606 19.6878
REMARK 3 T TENSOR
REMARK 3 T11: 0.1827 T22: 0.1203
REMARK 3 T33: 0.0919 T12: -0.0051
REMARK 3 T13: 0.0210 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 10.3559 L22: 6.7387
REMARK 3 L33: 3.8397 L12: 6.5363
REMARK 3 L13: 4.1278 L23: 3.1532
REMARK 3 S TENSOR
REMARK 3 S11: 0.4460 S12: 0.0526 S13: -0.4567
REMARK 3 S21: 0.6109 S22: -0.1705 S23: 0.0743
REMARK 3 S31: 0.4394 S32: 0.0046 S33: -0.2756
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 : B 100 B 114
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6160 -5.8952 22.9973
REMARK 3 T TENSOR
REMARK 3 T11: 0.3154 T22: 0.2128
REMARK 3 T33: 0.0257 T12: -0.0891
REMARK 3 T13: 0.0310 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 6.9807 L22: 10.0216
REMARK 3 L33: 2.5374 L12: 5.7580
REMARK 3 L13: 3.6869 L23: 4.5669
REMARK 3 S TENSOR
REMARK 3 S11: 0.4841 S12: -0.6782 S13: -0.2730
REMARK 3 S21: 0.7227 S22: -0.3765 S23: -0.0800
REMARK 3 S31: 0.1975 S32: -0.1986 S33: -0.1076
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 : D 1 D 8
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4237 4.1671 26.7682
REMARK 3 T TENSOR
REMARK 3 T11: 0.2344 T22: 0.3154
REMARK 3 T33: 0.3479 T12: 0.0862
REMARK 3 T13: 0.1028 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 5.6458 L22: 12.4488
REMARK 3 L33: 1.7314 L12: 6.5121
REMARK 3 L13: -0.3287 L23: -0.2624
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: -0.3255 S13: 0.9499
REMARK 3 S21: -0.7248 S22: -0.0101 S23: 1.0043
REMARK 3 S31: -0.3735 S32: -0.6475 S33: -0.0519
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 : D 9 D 14
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4736 12.7405 23.0958
REMARK 3 T TENSOR
REMARK 3 T11: 0.4502 T22: 0.4003
REMARK 3 T33: 0.5549 T12: 0.0606
REMARK 3 T13: 0.1684 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 6.9059 L22: 5.4368
REMARK 3 L33: 2.9897 L12: 4.6598
REMARK 3 L13: 3.7581 L23: 3.1203
REMARK 3 S TENSOR
REMARK 3 S11: -0.4136 S12: -0.3519 S13: 1.0890
REMARK 3 S21: -0.2393 S22: 0.0331 S23: 1.0739
REMARK 3 S31: -0.5750 S32: -0.5383 S33: 0.3805
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 : D 15 D 21
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6488 -8.6254 24.2833
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.2271
REMARK 3 T33: 0.1312 T12: -0.0939
REMARK 3 T13: 0.0463 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 2.7124 L22: 2.7432
REMARK 3 L33: 5.3487 L12: -1.2237
REMARK 3 L13: -0.9933 L23: -0.9531
REMARK 3 S TENSOR
REMARK 3 S11: -0.1118 S12: 0.0556 S13: 0.1640
REMARK 3 S21: 0.0938 S22: -0.1012 S23: 0.2743
REMARK 3 S31: 0.1667 S32: 0.0506 S33: 0.2130
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 22 D 28
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4789 7.5754 27.1038
REMARK 3 T TENSOR
REMARK 3 T11: 0.2532 T22: 0.2716
REMARK 3 T33: 0.1869 T12: -0.1039
REMARK 3 T13: 0.1684 T23: -0.1687
REMARK 3 L TENSOR
REMARK 3 L11: 0.3390 L22: 8.2110
REMARK 3 L33: 2.7699 L12: 1.1932
REMARK 3 L13: 0.4372 L23: -0.2427
REMARK 3 S TENSOR
REMARK 3 S11: 0.1993 S12: -0.1650 S13: 0.1155
REMARK 3 S21: 0.4493 S22: -0.1391 S23: 0.0343
REMARK 3 S31: 0.0551 S32: -0.1200 S33: -0.0602
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 : E 1 E 5
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6224 -19.2776 -1.2879
REMARK 3 T TENSOR
REMARK 3 T11: 0.3749 T22: 0.6143
REMARK 3 T33: 0.4594 T12: 0.1698
REMARK 3 T13: -0.0764 T23: -0.1513
REMARK 3 L TENSOR
REMARK 3 L11: 0.7476 L22: 9.1883
REMARK 3 L33: 10.8488 L12: 2.4336
REMARK 3 L13: 1.5621 L23: 7.3431
REMARK 3 S TENSOR
REMARK 3 S11: 0.0575 S12: 0.1399 S13: -0.4105
REMARK 3 S21: 0.3378 S22: 0.9831 S23: -1.1213
REMARK 3 S31: 1.0062 S32: 1.1078 S33: -1.0405
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 : E 6 E 9
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6228 -9.4456 15.5038
REMARK 3 T TENSOR
REMARK 3 T11: 0.3631 T22: 0.7942
REMARK 3 T33: 0.6751 T12: 0.1894
REMARK 3 T13: -0.1404 T23: 0.1656
REMARK 3 L TENSOR
REMARK 3 L11: 3.5329 L22: 11.6694
REMARK 3 L33: 11.4339 L12: 0.2941
REMARK 3 L13: -0.7592 L23: 11.3834
REMARK 3 S TENSOR
REMARK 3 S11: 0.0336 S12: -0.2792 S13: -0.1924
REMARK 3 S21: 0.9166 S22: 0.7289 S23: -0.9065
REMARK 3 S31: 0.9475 S32: 0.8733 S33: -0.7625
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 : E 12 E 19
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9599 -17.1041 3.9401
REMARK 3 T TENSOR
REMARK 3 T11: 0.3101 T22: 0.2437
REMARK 3 T33: 0.1636 T12: 0.1111
REMARK 3 T13: 0.0013 T23: -0.1324
REMARK 3 L TENSOR
REMARK 3 L11: 7.5268 L22: 4.2535
REMARK 3 L33: 2.0593 L12: 4.1471
REMARK 3 L13: 3.3751 L23: 1.8044
REMARK 3 S TENSOR
REMARK 3 S11: 0.2590 S12: 0.1907 S13: -0.5362
REMARK 3 S21: 0.1541 S22: 0.1072 S23: -0.1037
REMARK 3 S31: 0.3300 S32: 0.2065 S33: -0.3662
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 : E 20 E 28
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7473 -5.2407 10.5422
REMARK 3 T TENSOR
REMARK 3 T11: 0.2567 T22: 0.4286
REMARK 3 T33: 0.2951 T12: 0.0728
REMARK 3 T13: 0.0633 T23: -0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 2.3261 L22: 1.3352
REMARK 3 L33: 5.0482 L12: 0.8848
REMARK 3 L13: 3.0407 L23: 0.8799
REMARK 3 S TENSOR
REMARK 3 S11: -0.3187 S12: 0.2868 S13: -0.0882
REMARK 3 S21: -0.3072 S22: 0.1877 S23: -0.5073
REMARK 3 S31: -0.0733 S32: 0.6000 S33: 0.1310
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4ZBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15532
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.447
REMARK 200 RESOLUTION RANGE LOW (A) : 68.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % PEG 8000, 100 MM HEPES PH 6.0,
REMARK 280 100 MM MAGNESIUM ACETATE AND 20% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 54.60050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.35400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 54.60050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.35400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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 SER A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 HIS A 4
REMARK 465 PRO A 5
REMARK 465 ILE A 6
REMARK 465 PHE A 7
REMARK 465 HIS A 8
REMARK 465 ARG A 9
REMARK 465 GLY A 10
REMARK 465 ASN A 45
REMARK 465 ASN A 46
REMARK 465 PRO A 61
REMARK 465 ASN A 62
REMARK 465 PRO A 63
REMARK 465 VAL A 64
REMARK 465 ASP A 65
REMARK 465 LYS A 115
REMARK 465 ALA A 116
REMARK 465 VAL A 117
REMARK 465 ARG A 118
REMARK 465 ARG A 119
REMARK 465 ALA A 120
REMARK 465 SER B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 ILE B 44
REMARK 465 ASN B 45
REMARK 465 ASN B 46
REMARK 465 PRO B 61
REMARK 465 ASN B 62
REMARK 465 PRO B 63
REMARK 465 VAL B 64
REMARK 465 ASP B 65
REMARK 465 ASP B 93
REMARK 465 GLY B 94
REMARK 465 LYS B 95
REMARK 465 GLN B 96
REMARK 465 LYS B 115
REMARK 465 ALA B 116
REMARK 465 VAL B 117
REMARK 465 ARG B 118
REMARK 465 ARG B 119
REMARK 465 ALA B 120
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 CG CD CE NZ
REMARK 470 GLU A 35 CG CD OE1 OE2
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 GLN A 96 CG CD OE1 NE2
REMARK 470 ARG B 9 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 34 CG CD CE NZ
REMARK 470 MET B 37 CG SD CE
REMARK 470 GLU B 41 CG CD OE1 OE2
REMARK 470 LYS B 50 CG CD CE NZ
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
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 DUZ D 3 O3' DG D 4 P -0.098
REMARK 500 DC D 9 P DC D 9 O5' -0.064
REMARK 500 DUZ D 11 O3' DG D 12 P -0.117
REMARK 500 DUZ D 17 O3' DUZ D 18 P -0.098
REMARK 500 DUZ D 18 O3' DA D 19 P -0.094
REMARK 500 DUZ D 27 O3' DG D 28 P -0.088
REMARK 500 DUZ E 3 O3' DG E 4 P -0.074
REMARK 500 DUZ E 11 O3' DG E 12 P -0.117
REMARK 500 DUZ E 17 O3' DUZ E 18 P -0.090
REMARK 500 DUZ E 18 O3' DA E 19 P -0.086
REMARK 500 DUZ E 27 O3' DG E 28 P -0.112
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 DUZ D 3 O3' - P - OP1 ANGL. DEV. = 12.7 DEGREES
REMARK 500 DG D 4 O3' - P - O5' ANGL. DEV. = -15.5 DEGREES
REMARK 500 DG D 4 O3' - P - OP2 ANGL. DEV. = 14.6 DEGREES
REMARK 500 DUZ D 10 C3' - O3' - P ANGL. DEV. = 14.4 DEGREES
REMARK 500 DG D 12 O3' - P - O5' ANGL. DEV. = -15.2 DEGREES
REMARK 500 DUZ D 17 O3' - P - O5' ANGL. DEV. = -12.5 DEGREES
REMARK 500 DUZ D 17 O3' - P - OP1 ANGL. DEV. = 14.0 DEGREES
REMARK 500 DUZ D 17 C3' - O3' - P ANGL. DEV. = 9.1 DEGREES
REMARK 500 DA D 19 O3' - P - OP1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 DUZ D 24 O3' - P - OP1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 DUZ D 25 O3' - P - OP2 ANGL. DEV. = 12.9 DEGREES
REMARK 500 DUZ D 25 C3' - O3' - P ANGL. DEV. = 29.9 DEGREES
REMARK 500 DUZ D 27 C3' - O3' - P ANGL. DEV. = 24.0 DEGREES
REMARK 500 DUZ E 3 C3' - O3' - P ANGL. DEV. = 22.1 DEGREES
REMARK 500 DG E 4 O3' - P - OP2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 DUZ E 10 O3' - P - OP2 ANGL. DEV. = 36.0 DEGREES
REMARK 500 DUZ E 10 O3' - P - OP1 ANGL. DEV. = -21.9 DEGREES
REMARK 500 DUZ E 11 O3' - P - OP1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 DUZ E 11 C3' - O3' - P ANGL. DEV. = -11.4 DEGREES
REMARK 500 DG E 12 O3' - P - OP1 ANGL. DEV. = -14.6 DEGREES
REMARK 500 DUZ E 16 O3' - P - O5' ANGL. DEV. = 18.3 DEGREES
REMARK 500 DUZ E 17 O3' - P - OP1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 DUZ E 17 C3' - O3' - P ANGL. DEV. = 12.8 DEGREES
REMARK 500 DUZ E 18 C3' - O3' - P ANGL. DEV. = 19.1 DEGREES
REMARK 500 DA E 19 O3' - P - OP2 ANGL. DEV. = 22.3 DEGREES
REMARK 500 DA E 19 O5' - P - OP2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 DUZ E 24 C3' - O3' - P ANGL. DEV. = -8.5 DEGREES
REMARK 500 DUZ E 25 O3' - P - OP2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 DUZ E 25 C3' - O3' - P ANGL. DEV. = 19.6 DEGREES
REMARK 500 DUZ E 27 C3' - O3' - P ANGL. DEV. = 32.9 DEGREES
REMARK 500 DG E 28 O3' - P - OP2 ANGL. DEV. = -18.4 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 B 8 -9.15 -55.79
REMARK 500 ASP B 72 89.19 -64.49
REMARK 500 SER B 113 -152.37 -154.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG B 59 ASP B 60 -149.55
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 EPE D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ D 10 and DUZ D 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ D 16 and DUZ D 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ D 17 and DUZ D 18
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ D 24 and DUZ D 25
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ E 10 and DUZ E 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ E 16 and DUZ E 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ E 17 and DUZ E 18
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DUZ E 24 and DUZ E 25
DBREF 4ZBN D 1 28 PDB 4ZBN 4ZBN 1 28
DBREF 4ZBN E 1 28 PDB 4ZBN 4ZBN 1 28
DBREF 4ZBN A 1 120 UNP P01138 NGF_HUMAN 122 241
DBREF 4ZBN B 1 120 UNP P01138 NGF_HUMAN 122 241
SEQRES 1 D 28 DC DA DUZ DG DA DG DG DA DC DUZ DUZ DG DG
SEQRES 2 D 28 DG DG DUZ DUZ DUZ DA DG DC DC DG DUZ DUZ DG
SEQRES 3 D 28 DUZ DG
SEQRES 1 E 28 DC DA DUZ DG DA DG DG DA DC DUZ DUZ DG DG
SEQRES 2 E 28 DG DG DUZ DUZ DUZ DA DG DC DC DG DUZ DUZ DG
SEQRES 3 E 28 DUZ DG
SEQRES 1 A 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER
SEQRES 2 A 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR
SEQRES 3 A 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU
SEQRES 4 A 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR
SEQRES 5 A 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP
SEQRES 6 A 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER
SEQRES 7 A 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR
SEQRES 8 A 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE
SEQRES 9 A 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL
SEQRES 10 A 120 ARG ARG ALA
SEQRES 1 B 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER
SEQRES 2 B 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR
SEQRES 3 B 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU
SEQRES 4 B 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR
SEQRES 5 B 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP
SEQRES 6 B 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER
SEQRES 7 B 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR
SEQRES 8 B 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE
SEQRES 9 B 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL
SEQRES 10 B 120 ARG ARG ALA
HET DUZ D 3 29
HET DUZ D 10 29
HET DUZ D 11 29
HET DUZ D 16 29
HET DUZ D 17 29
HET DUZ D 18 29
HET DUZ D 24 29
HET DUZ D 25 29
HET DUZ D 27 29
HET DUZ E 3 29
HET DUZ E 10 29
HET DUZ E 11 29
HET DUZ E 16 29
HET DUZ E 17 29
HET DUZ E 18 29
HET DUZ E 24 29
HET DUZ E 25 29
HET DUZ E 27 29
HET EPE D 101 15
HETNAM DUZ 5-(BENZYLCARBAMOYL)-2'-DEOXYURIDINE 5'-(DIHYDROGEN
HETNAM 2 DUZ PHOSPHATE)
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 1 DUZ 18(C17 H20 N3 O9 P)
FORMUL 5 EPE C8 H18 N2 O4 S
FORMUL 6 HOH *21(H2 O)
HELIX 1 AA1 ILE B 6 GLY B 10 5 5
SHEET 1 AA1 5 PHE A 12 SER A 13 0
SHEET 2 AA1 5 ALA B 98 SER B 113 -1 O LEU B 112 N PHE A 12
SHEET 3 AA1 5 ASN B 77 MET B 92 -1 N THR B 91 O ALA B 98
SHEET 4 AA1 5 GLU B 35 VAL B 38 -1 N MET B 37 O MET B 92
SHEET 5 AA1 5 THR B 27 THR B 29 -1 N ALA B 28 O VAL B 36
SHEET 1 AA2 2 SER A 17 VAL A 22 0
SHEET 2 AA2 2 PHE A 53 CYS A 58 -1 O GLU A 55 N VAL A 20
SHEET 1 AA3 5 THR A 27 THR A 29 0
SHEET 2 AA3 5 GLU A 35 VAL A 38 -1 O VAL A 36 N ALA A 28
SHEET 3 AA3 5 ASN A 77 ASP A 93 -1 O MET A 92 N MET A 37
SHEET 4 AA3 5 GLN A 96 SER A 113 -1 O VAL A 111 N TYR A 79
SHEET 5 AA3 5 PHE B 12 SER B 13 -1 O PHE B 12 N LEU A 112
SHEET 1 AA4 2 GLU A 41 VAL A 42 0
SHEET 2 AA4 2 PHE A 49 LYS A 50 -1 O PHE A 49 N VAL A 42
SHEET 1 AA5 2 SER B 17 VAL B 22 0
SHEET 2 AA5 2 PHE B 53 CYS B 58 -1 O PHE B 53 N VAL B 22
SHEET 1 AA6 2 GLU B 41 VAL B 42 0
SHEET 2 AA6 2 PHE B 49 LYS B 50 -1 O PHE B 49 N VAL B 42
SSBOND 1 CYS A 15 CYS A 80 1555 1555 2.08
SSBOND 2 CYS A 58 CYS A 108 1555 1555 2.03
SSBOND 3 CYS A 68 CYS A 110 1555 1555 2.03
SSBOND 4 CYS B 15 CYS B 80 1555 1555 2.08
SSBOND 5 CYS B 58 CYS B 108 1555 1555 2.05
SSBOND 6 CYS B 68 CYS B 110 1555 1555 2.03
LINK O3' DA D 2 P DUZ D 3 1555 1555 1.61
LINK O3' DUZ D 3 P DG D 4 1555 1555 1.51
LINK O3' DC D 9 P DUZ D 10 1555 1555 1.58
LINK O3' DUZ D 10 P DUZ D 11 1555 1555 1.54
LINK O3' DUZ D 11 P DG D 12 1555 1555 1.49
LINK O3' DG D 15 P DUZ D 16 1555 1555 1.57
LINK O3' DUZ D 16 P DUZ D 17 1555 1555 1.61
LINK O3' DUZ D 17 P DUZ D 18 1555 1555 1.51
LINK O3' DUZ D 18 P DA D 19 1555 1555 1.51
LINK O3' DG D 23 P DUZ D 24 1555 1555 1.63
LINK O3' DUZ D 24 P DUZ D 25 1555 1555 1.64
LINK O3' DUZ D 25 P DG D 26 1555 1555 1.66
LINK O3' DG D 26 P DUZ D 27 1555 1555 1.60
LINK O3' DUZ D 27 P DG D 28 1555 1555 1.52
LINK O3' DA E 2 P DUZ E 3 1555 1555 1.63
LINK O3' DUZ E 3 P DG E 4 1555 1555 1.53
LINK O3' DC E 9 P DUZ E 10 1555 1555 1.58
LINK O3' DUZ E 10 P DUZ E 11 1555 1555 1.60
LINK O3' DUZ E 11 P DG E 12 1555 1555 1.49
LINK O3' DG E 15 P DUZ E 16 1555 1555 1.59
LINK O3' DUZ E 16 P DUZ E 17 1555 1555 1.66
LINK O3' DUZ E 17 P DUZ E 18 1555 1555 1.52
LINK O3' DUZ E 18 P DA E 19 1555 1555 1.52
LINK O3' DG E 23 P DUZ E 24 1555 1555 1.57
LINK O3' DUZ E 24 P DUZ E 25 1555 1555 1.58
LINK O3' DUZ E 25 P DG E 26 1555 1555 1.67
LINK O3' DG E 26 P DUZ E 27 1555 1555 1.59
LINK O3' DUZ E 27 P DG E 28 1555 1555 1.50
CISPEP 1 HIS B 4 PRO B 5 0 -13.09
CISPEP 2 HIS B 4 PRO B 5 0 -12.84
SITE 1 AC1 4 HIS A 75 DC D 1 DA D 19 DG D 20
SITE 1 AC2 9 ARG A 59 ARG A 69 DA D 8 DC D 9
SITE 2 AC2 9 DG D 12 DUZ D 25 DG D 26 DUZ D 27
SITE 3 AC2 9 DG D 28
SITE 1 AC3 13 TRP A 21 TYR A 52 ILE B 31 LYS B 32
SITE 2 AC3 13 PHE B 101 DUZ D 3 DG D 4 DG D 14
SITE 3 AC3 13 DG D 15 DUZ D 18 DA D 19 DC D 21
SITE 4 AC3 13 DC D 22
SITE 1 AC4 15 TRP A 21 TYR A 52 ILE B 31 LYS B 32
SITE 2 AC4 15 PHE B 101 DC D 1 DA D 2 DUZ D 3
SITE 3 AC4 15 DG D 14 DG D 15 DUZ D 16 DA D 19
SITE 4 AC4 15 DG D 20 DC D 21 DC D 22
SITE 1 AC5 12 SER A 17 VAL A 18 SER A 19 ARG A 59
SITE 2 AC5 12 HOH A 201 DG D 7 DA D 8 DUZ D 11
SITE 3 AC5 12 DG D 12 DG D 13 DG D 23 DG D 26
SITE 1 AC6 9 ARG B 59 ARG B 69 DA E 8 DC E 9
SITE 2 AC6 9 DG E 12 DUZ E 25 DG E 26 DUZ E 27
SITE 3 AC6 9 DG E 28
SITE 1 AC7 9 PHE A 101 TRP B 21 TYR B 52 DUZ E 3
SITE 2 AC7 9 DG E 4 DG E 15 DUZ E 18 DA E 19
SITE 3 AC7 9 DC E 21
SITE 1 AC8 12 LYS A 32 PHE A 101 HIS B 4 TRP B 21
SITE 2 AC8 12 TYR B 52 DC E 1 DA E 2 DUZ E 3
SITE 3 AC8 12 DG E 15 DUZ E 16 DA E 19 DC E 21
SITE 1 AC9 12 PHE B 7 SER B 17 VAL B 18 SER B 19
SITE 2 AC9 12 ARG B 59 DG E 7 DA E 8 DUZ E 11
SITE 3 AC9 12 DG E 12 DG E 13 DG E 23 DG E 26
CRYST1 109.201 60.708 68.589 90.00 95.57 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009157 0.000000 0.000892 0.00000
SCALE2 0.000000 0.016472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014649 0.00000
(ATOM LINES ARE NOT SHOWN.)
END