HEADER LIGASE/DNA 23-AUG-04 1X9N
TITLE CRYSTAL STRUCTURE OF HUMAN DNA LIGASE I BOUND TO 5'-ADENYLATED, NICKED
TITLE 2 DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIDEOXY TERMINATED DNA;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-PHOSPHORYLATED DNA;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: TEMPLATE DNA;
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: DNA LIGASE I;
COMPND 15 CHAIN: A;
COMPND 16 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP];
COMPND 17 EC: 6.5.1.1;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 MOL_ID: 4;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: LIG1;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RP;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS DNA LIGASE, 5'-ADENYLATED NICKED DNA, PROTEIN-DNA COMPLEX, LIGASE-DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.PASCAL,P.J.O'BRIEN,A.E.TOMKINSON,T.ELLENBERGER
REVDAT 3 13-JUL-11 1X9N 1 VERSN
REVDAT 2 24-FEB-09 1X9N 1 VERSN
REVDAT 1 30-NOV-04 1X9N 0
JRNL AUTH J.M.PASCAL,P.J.O'BRIEN,A.E.TOMKINSON,T.ELLENBERGER
JRNL TITL HUMAN DNA LIGASE I COMPLETELY ENCIRCLES AND PARTIALLY
JRNL TITL 2 UNWINDS NICKED DNA.
JRNL REF NATURE V. 432 473 2004
JRNL REFN ISSN 0028-0836
JRNL PMID 15565146
JRNL DOI 10.1038/NATURE03082
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.80
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 50.0
REMARK 3 NUMBER OF REFLECTIONS : 24943
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1301
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1811
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.4130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4894
REMARK 3 NUCLEIC ACID ATOMS : 813
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.65000
REMARK 3 B22 (A**2) : -3.65000
REMARK 3 B33 (A**2) : 5.47000
REMARK 3 B12 (A**2) : -1.82000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.209
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.394
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.311
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.766
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5929 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8207 ; 1.524 ; 2.158
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 630 ; 6.603 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 890 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4186 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2408 ; 0.254 ; 0.200
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): 26 ; 0.316 ; 0.200
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): 3155 ; 0.458 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5078 ; 0.938 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2773 ; 1.587 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3126 ; 2.597 ; 4.500
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 : 4
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 262 A 535
REMARK 3 ORIGIN FOR THE GROUP (A): 53.8081 32.5779 64.4371
REMARK 3 T TENSOR
REMARK 3 T11: 0.3602 T22: 0.2820
REMARK 3 T33: 0.5749 T12: 0.0338
REMARK 3 T13: -0.1933 T23: 0.3443
REMARK 3 L TENSOR
REMARK 3 L11: 3.9895 L22: 2.0743
REMARK 3 L33: 2.2156 L12: 1.4420
REMARK 3 L13: 0.0323 L23: 1.0091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0941 S12: -0.1954 S13: -0.1516
REMARK 3 S21: 0.0904 S22: 0.1135 S23: 0.4208
REMARK 3 S31: 0.1322 S32: -0.0302 S33: -0.2076
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 536 A 747
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2927 40.7568 30.3652
REMARK 3 T TENSOR
REMARK 3 T11: 0.6517 T22: 0.7693
REMARK 3 T33: 0.4864 T12: 0.0041
REMARK 3 T13: -0.2627 T23: 0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 2.5908 L22: 2.2446
REMARK 3 L33: 0.9556 L12: 0.1867
REMARK 3 L13: 0.0622 L23: -0.6667
REMARK 3 S TENSOR
REMARK 3 S11: 0.1689 S12: 0.6150 S13: -0.0202
REMARK 3 S21: -0.3274 S22: 0.0148 S23: 0.3758
REMARK 3 S31: -0.1052 S32: -0.2482 S33: -0.1837
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 748 A 901
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3422 43.8775 40.3222
REMARK 3 T TENSOR
REMARK 3 T11: 0.4315 T22: 0.4872
REMARK 3 T33: 0.8080 T12: 0.0622
REMARK 3 T13: -0.3477 T23: 0.2832
REMARK 3 L TENSOR
REMARK 3 L11: 5.6181 L22: 3.7920
REMARK 3 L33: 4.3194 L12: 0.1438
REMARK 3 L13: 0.4227 L23: 0.4706
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: 0.2943 S13: -0.0817
REMARK 3 S21: -0.2877 S22: 0.0655 S23: 0.3420
REMARK 3 S31: -0.3951 S32: -0.3272 S33: -0.0833
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 13
REMARK 3 RESIDUE RANGE : C 1 C 9
REMARK 3 RESIDUE RANGE : D 7 D 26
REMARK 3 RESIDUE RANGE : C 100 C 100
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7841 35.3336 45.9060
REMARK 3 T TENSOR
REMARK 3 T11: 0.4026 T22: 0.2969
REMARK 3 T33: 0.7884 T12: -0.0538
REMARK 3 T13: -0.3157 T23: 0.1994
REMARK 3 L TENSOR
REMARK 3 L11: 2.5830 L22: 0.8286
REMARK 3 L33: 3.5126 L12: -0.5190
REMARK 3 L13: -0.7111 L23: -0.1536
REMARK 3 S TENSOR
REMARK 3 S11: -0.0363 S12: 0.2699 S13: -0.2147
REMARK 3 S21: -0.3180 S22: 0.1497 S23: 0.1582
REMARK 3 S31: -0.0001 S32: -0.1064 S33: -0.1135
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB030113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-03; NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL; NULL
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS; NSLS
REMARK 200 BEAMLINE : X25; X25; X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97880; 0.9787, 0.9791, 0.9635,
REMARK 200 1.1; 1.006, 1.011, 0.969, 1.1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 SI(111) OR (220); NULL; NULL
REMARK 200 OPTICS : NULL; NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ACE
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26365
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 10.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, PH 4.8,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.22750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.22750
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.22750
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: B, C, D, A
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 DG B 1
REMARK 465 DT B 2
REMARK 465 DA C 10
REMARK 465 DT C 11
REMARK 465 DT C 12
REMARK 465 DC C 13
REMARK 465 DG C 14
REMARK 465 DG C 15
REMARK 465 DC D 1
REMARK 465 DC D 2
REMARK 465 DG D 3
REMARK 465 DA D 4
REMARK 465 DA D 5
REMARK 465 DT D 6
REMARK 465 DA D 27
REMARK 465 DC D 28
REMARK 465 MET A 232
REMARK 465 THR A 233
REMARK 465 PRO A 234
REMARK 465 ARG A 235
REMARK 465 LYS A 236
REMARK 465 PRO A 237
REMARK 465 ALA A 238
REMARK 465 VAL A 239
REMARK 465 LYS A 240
REMARK 465 LYS A 241
REMARK 465 GLU A 242
REMARK 465 VAL A 243
REMARK 465 LYS A 244
REMARK 465 GLU A 245
REMARK 465 GLU A 246
REMARK 465 GLU A 247
REMARK 465 PRO A 248
REMARK 465 GLY A 249
REMARK 465 ALA A 250
REMARK 465 PRO A 251
REMARK 465 GLY A 252
REMARK 465 LYS A 253
REMARK 465 GLU A 254
REMARK 465 GLY A 255
REMARK 465 ALA A 256
REMARK 465 ALA A 257
REMARK 465 GLU A 258
REMARK 465 GLY A 259
REMARK 465 PRO A 260
REMARK 465 LEU A 261
REMARK 465 ASN A 385
REMARK 465 SER A 386
REMARK 465 ARG A 387
REMARK 465 SER A 388
REMARK 465 THR A 389
REMARK 465 GLN A 390
REMARK 465 ARG A 391
REMARK 465 LEU A 392
REMARK 465 GLN A 902
REMARK 465 ILE A 903
REMARK 465 GLN A 904
REMARK 465 ASN A 905
REMARK 465 GLN A 906
REMARK 465 GLN A 907
REMARK 465 GLY A 908
REMARK 465 GLU A 909
REMARK 465 ASP A 910
REMARK 465 SER A 911
REMARK 465 GLY A 912
REMARK 465 SER A 913
REMARK 465 ASP A 914
REMARK 465 PRO A 915
REMARK 465 GLU A 916
REMARK 465 ASP A 917
REMARK 465 THR A 918
REMARK 465 TYR A 919
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 DG B 3 P OP1 OP2
REMARK 470 DC D 7 P OP1 OP2
REMARK 470 ARG A 627 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 628 CG CD OE1 OE2
REMARK 470 ARG A 643 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 644 CG CD CE NZ
REMARK 470 GLU A 645 CG CD OE1 OE2
REMARK 470 VAL A 646 CG1 CG2
REMARK 470 GLU A 709 CG CD OE1 OE2
REMARK 470 GLU A 712 CG CD OE1 OE2
REMARK 470 GLU A 807 CG CD OE1 OE2
REMARK 470 ARG A 859 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 899 CG CD CE NZ
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 DG B 11 O3' DG B 11 C3' -0.037
REMARK 500 DG C 1 O3' DG C 1 C3' -0.075
REMARK 500 DT C 2 O3' DT C 2 C3' -0.042
REMARK 500 DC C 3 O3' DC C 3 C3' -0.056
REMARK 500 DG C 4 O3' DG C 4 C3' -0.052
REMARK 500 DC C 7 O3' DC C 7 C3' -0.037
REMARK 500 DG D 16 O3' DG D 16 C3' -0.049
REMARK 500 DA D 17 O3' DA D 17 C3' -0.036
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 DG B 6 O4' - C1' - N9 ANGL. DEV. = -4.9 DEGREES
REMARK 500 DT B 8 C5' - C4' - O4' ANGL. DEV. = 10.2 DEGREES
REMARK 500 DT B 8 O4' - C1' - N1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 DC B 10 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DC B 10 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DG B 9 C3' - O3' - P ANGL. DEV. = 8.0 DEGREES
REMARK 500 DT B 12 O4' - C4' - C3' ANGL. DEV. = -3.1 DEGREES
REMARK 500 DT B 12 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DT C 2 O4' - C1' - C2' ANGL. DEV. = 3.2 DEGREES
REMARK 500 DT C 2 C4 - C5 - C7 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT C 2 C6 - C5 - C7 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DA C 6 O5' - C5' - C4' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DT C 8 O4' - C4' - C3' ANGL. DEV. = -2.5 DEGREES
REMARK 500 DG C 9 O4' - C4' - C3' ANGL. DEV. = -2.4 DEGREES
REMARK 500 DC D 7 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT D 10 C4' - C3' - C2' ANGL. DEV. = -4.3 DEGREES
REMARK 500 DC D 11 O4' - C1' - N1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 DC D 12 N1 - C2 - O2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DC D 11 C3' - O3' - P ANGL. DEV. = 8.4 DEGREES
REMARK 500 DG D 13 C3' - C2' - C1' ANGL. DEV. = -5.4 DEGREES
REMARK 500 DG D 13 O4' - C1' - N9 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DA D 14 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC D 15 O4' - C4' - C3' ANGL. DEV. = -3.8 DEGREES
REMARK 500 DC D 15 N1 - C2 - O2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG D 16 O4' - C4' - C3' ANGL. DEV. = -4.0 DEGREES
REMARK 500 DA D 17 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC D 18 P - O5' - C5' ANGL. DEV. = -12.4 DEGREES
REMARK 500 DC D 18 O4' - C4' - C3' ANGL. DEV. = 4.3 DEGREES
REMARK 500 DA D 21 O4' - C1' - N9 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DT D 22 C3' - C2' - C1' ANGL. DEV. = -6.3 DEGREES
REMARK 500 DT D 22 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DC D 23 C3' - C2' - C1' ANGL. DEV. = -6.8 DEGREES
REMARK 500 DA D 24 O4' - C1' - N9 ANGL. DEV. = -5.2 DEGREES
REMARK 500 DC D 26 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 278 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 326 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 748 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 784 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 802 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 881 CB - CG - OD2 ANGL. DEV. = 5.7 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 PRO A 268 8.85 -68.59
REMARK 500 SER A 323 55.71 -159.04
REMARK 500 LEU A 366 -39.12 -39.69
REMARK 500 PRO A 396 173.35 -54.31
REMARK 500 LEU A 414 92.59 -65.03
REMARK 500 HIS A 436 -109.84 -129.90
REMARK 500 SER A 447 -6.96 -55.72
REMARK 500 ALA A 455 -149.83 -126.09
REMARK 500 ALA A 461 -58.55 -26.85
REMARK 500 ASP A 512 99.16 -160.86
REMARK 500 PHE A 558 32.86 -97.69
REMARK 500 SER A 615 146.48 -171.85
REMARK 500 GLU A 628 -72.06 -81.52
REMARK 500 LYS A 630 72.84 63.31
REMARK 500 LYS A 644 -81.62 -68.21
REMARK 500 VAL A 646 55.21 -102.08
REMARK 500 PHE A 660 -4.79 -156.39
REMARK 500 GLU A 692 -73.79 -110.36
REMARK 500 SER A 718 74.69 57.01
REMARK 500 ARG A 738 100.98 -168.30
REMARK 500 LYS A 747 -57.67 -25.96
REMARK 500 ASP A 748 -86.89 -8.00
REMARK 500 ASP A 751 -71.36 -60.92
REMARK 500 VAL A 753 107.82 -176.37
REMARK 500 ARG A 774 -159.73 -124.38
REMARK 500 SER A 839 -41.28 -158.38
REMARK 500 ASP A 848 -168.96 -163.36
REMARK 500 ALA A 857 125.90 -38.42
REMARK 500 ILE A 876 -55.05 -125.71
REMARK 500 GLN A 886 33.17 -94.57
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 AMP C 100
DBREF 1X9N A 233 919 UNP P18858 DNL1_HUMAN 233 919
DBREF 1X9N B 1 13 PDB 1X9N 1X9N 1 13
DBREF 1X9N C 1 15 PDB 1X9N 1X9N 1 15
DBREF 1X9N D 1 28 PDB 1X9N 1X9N 1 28
SEQADV 1X9N MET A 232 UNP P18858 INITIATING METHIONINE
SEQADV 1X9N MSE A 308 UNP P18858 MET 308 MODIFIED RESIDUE
SEQADV 1X9N MSE A 393 UNP P18858 MET 393 MODIFIED RESIDUE
SEQADV 1X9N MSE A 480 UNP P18858 MET 480 MODIFIED RESIDUE
SEQADV 1X9N MSE A 501 UNP P18858 MET 501 MODIFIED RESIDUE
SEQADV 1X9N MSE A 543 UNP P18858 MET 543 MODIFIED RESIDUE
SEQADV 1X9N MSE A 723 UNP P18858 MET 723 MODIFIED RESIDUE
SEQRES 1 B 13 DG DT DG DC DT DG DA DT DG DC DG DT DOC
SEQRES 1 C 15 DG DT DC DG DG DA DC DT DG DA DT DT DC
SEQRES 2 C 15 DG DG
SEQRES 1 D 28 DC DC DG DA DA DT DC DA DG DT DC DC DG
SEQRES 2 D 28 DA DC DG DA DC DG DC DA DT DC DA DG DC
SEQRES 3 D 28 DA DC
SEQRES 1 A 688 MET THR PRO ARG LYS PRO ALA VAL LYS LYS GLU VAL LYS
SEQRES 2 A 688 GLU GLU GLU PRO GLY ALA PRO GLY LYS GLU GLY ALA ALA
SEQRES 3 A 688 GLU GLY PRO LEU ASP PRO SER GLY TYR ASN PRO ALA LYS
SEQRES 4 A 688 ASN ASN TYR HIS PRO VAL GLU ASP ALA CYS TRP LYS PRO
SEQRES 5 A 688 GLY GLN LYS VAL PRO TYR LEU ALA VAL ALA ARG THR PHE
SEQRES 6 A 688 GLU LYS ILE GLU GLU VAL SER ALA ARG LEU ARG MSE VAL
SEQRES 7 A 688 GLU THR LEU SER ASN LEU LEU ARG SER VAL VAL ALA LEU
SEQRES 8 A 688 SER PRO PRO ASP LEU LEU PRO VAL LEU TYR LEU SER LEU
SEQRES 9 A 688 ASN HIS LEU GLY PRO PRO GLN GLN GLY LEU GLU LEU GLY
SEQRES 10 A 688 VAL GLY ASP GLY VAL LEU LEU LYS ALA VAL ALA GLN ALA
SEQRES 11 A 688 THR GLY ARG GLN LEU GLU SER VAL ARG ALA GLU ALA ALA
SEQRES 12 A 688 GLU LYS GLY ASP VAL GLY LEU VAL ALA GLU ASN SER ARG
SEQRES 13 A 688 SER THR GLN ARG LEU MSE LEU PRO PRO PRO PRO LEU THR
SEQRES 14 A 688 ALA SER GLY VAL PHE SER LYS PHE ARG ASP ILE ALA ARG
SEQRES 15 A 688 LEU THR GLY SER ALA SER THR ALA LYS LYS ILE ASP ILE
SEQRES 16 A 688 ILE LYS GLY LEU PHE VAL ALA CYS ARG HIS SER GLU ALA
SEQRES 17 A 688 ARG PHE ILE ALA ARG SER LEU SER GLY ARG LEU ARG LEU
SEQRES 18 A 688 GLY LEU ALA GLU GLN SER VAL LEU ALA ALA LEU SER GLN
SEQRES 19 A 688 ALA VAL SER LEU THR PRO PRO GLY GLN GLU PHE PRO PRO
SEQRES 20 A 688 ALA MSE VAL ASP ALA GLY LYS GLY LYS THR ALA GLU ALA
SEQRES 21 A 688 ARG LYS THR TRP LEU GLU GLU GLN GLY MSE ILE LEU LYS
SEQRES 22 A 688 GLN THR PHE CYS GLU VAL PRO ASP LEU ASP ARG ILE ILE
SEQRES 23 A 688 PRO VAL LEU LEU GLU HIS GLY LEU GLU ARG LEU PRO GLU
SEQRES 24 A 688 HIS CYS LYS LEU SER PRO GLY ILE PRO LEU LYS PRO MSE
SEQRES 25 A 688 LEU ALA HIS PRO THR ARG GLY ILE SER GLU VAL LEU LYS
SEQRES 26 A 688 ARG PHE GLU GLU ALA ALA PHE THR CYS GLU TYR LYS TYR
SEQRES 27 A 688 ASP GLY GLN ARG ALA GLN ILE HIS ALA LEU GLU GLY GLY
SEQRES 28 A 688 GLU VAL LYS ILE PHE SER ARG ASN GLN GLU ASP ASN THR
SEQRES 29 A 688 GLY LYS TYR PRO ASP ILE ILE SER ARG ILE PRO LYS ILE
SEQRES 30 A 688 LYS LEU PRO SER VAL THR SER PHE ILE LEU ASP THR GLU
SEQRES 31 A 688 ALA VAL ALA TRP ASP ARG GLU LYS LYS GLN ILE GLN PRO
SEQRES 32 A 688 PHE GLN VAL LEU THR THR ARG LYS ARG LYS GLU VAL ASP
SEQRES 33 A 688 ALA SER GLU ILE GLN VAL GLN VAL CYS LEU TYR ALA PHE
SEQRES 34 A 688 ASP LEU ILE TYR LEU ASN GLY GLU SER LEU VAL ARG GLU
SEQRES 35 A 688 PRO LEU SER ARG ARG ARG GLN LEU LEU ARG GLU ASN PHE
SEQRES 36 A 688 VAL GLU THR GLU GLY GLU PHE VAL PHE ALA THR SER LEU
SEQRES 37 A 688 ASP THR LYS ASP ILE GLU GLN ILE ALA GLU PHE LEU GLU
SEQRES 38 A 688 GLN SER VAL LYS ASP SER CYS GLU GLY LEU MSE VAL LYS
SEQRES 39 A 688 THR LEU ASP VAL ASP ALA THR TYR GLU ILE ALA LYS ARG
SEQRES 40 A 688 SER HIS ASN TRP LEU LYS LEU LYS LYS ASP TYR LEU ASP
SEQRES 41 A 688 GLY VAL GLY ASP THR LEU ASP LEU VAL VAL ILE GLY ALA
SEQRES 42 A 688 TYR LEU GLY ARG GLY LYS ARG ALA GLY ARG TYR GLY GLY
SEQRES 43 A 688 PHE LEU LEU ALA SER TYR ASP GLU ASP SER GLU GLU LEU
SEQRES 44 A 688 GLN ALA ILE CYS LYS LEU GLY THR GLY PHE SER ASP GLU
SEQRES 45 A 688 GLU LEU GLU GLU HIS HIS GLN SER LEU LYS ALA LEU VAL
SEQRES 46 A 688 LEU PRO SER PRO ARG PRO TYR VAL ARG ILE ASP GLY ALA
SEQRES 47 A 688 VAL ILE PRO ASP HIS TRP LEU ASP PRO SER ALA VAL TRP
SEQRES 48 A 688 GLU VAL LYS CYS ALA ASP LEU SER LEU SER PRO ILE TYR
SEQRES 49 A 688 PRO ALA ALA ARG GLY LEU VAL ASP SER ASP LYS GLY ILE
SEQRES 50 A 688 SER LEU ARG PHE PRO ARG PHE ILE ARG VAL ARG GLU ASP
SEQRES 51 A 688 LYS GLN PRO GLU GLN ALA THR THR SER ALA GLN VAL ALA
SEQRES 52 A 688 CYS LEU TYR ARG LYS GLN SER GLN ILE GLN ASN GLN GLN
SEQRES 53 A 688 GLY GLU ASP SER GLY SER ASP PRO GLU ASP THR TYR
MODRES 1X9N DOC B 13 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
MODRES 1X9N MSE A 308 MET SELENOMETHIONINE
MODRES 1X9N MSE A 393 MET SELENOMETHIONINE
MODRES 1X9N MSE A 480 MET SELENOMETHIONINE
MODRES 1X9N MSE A 501 MET SELENOMETHIONINE
MODRES 1X9N MSE A 543 MET SELENOMETHIONINE
MODRES 1X9N MSE A 723 MET SELENOMETHIONINE
HET DOC B 13 18
HET MSE A 308 8
HET MSE A 393 8
HET MSE A 480 8
HET MSE A 501 8
HET MSE A 543 8
HET MSE A 723 8
HET AMP C 100 23
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM MSE SELENOMETHIONINE
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 1 DOC C9 H14 N3 O6 P
FORMUL 4 MSE 6(C5 H11 N O2 SE)
FORMUL 5 AMP C10 H14 N5 O7 P
HELIX 1 1 ASP A 262 TYR A 266 5 5
HELIX 2 2 HIS A 274 ALA A 279 1 6
HELIX 3 3 PRO A 288 GLU A 301 1 14
HELIX 4 4 ALA A 304 SER A 323 1 20
HELIX 5 5 ASP A 326 ASN A 336 1 11
HELIX 6 6 PRO A 340 GLY A 344 5 5
HELIX 7 7 GLY A 350 GLY A 363 1 14
HELIX 8 8 GLN A 365 GLY A 377 1 13
HELIX 9 9 ASP A 378 ALA A 383 1 6
HELIX 10 10 THR A 400 LEU A 414 1 15
HELIX 11 11 ALA A 418 CYS A 434 1 17
HELIX 12 12 SER A 437 SER A 447 1 11
HELIX 13 13 ALA A 455 THR A 470 1 16
HELIX 14 14 THR A 488 VAL A 510 1 23
HELIX 15 15 ASP A 512 LEU A 528 1 17
HELIX 16 16 PRO A 529 CYS A 532 5 4
HELIX 17 17 GLY A 550 PHE A 558 1 9
HELIX 18 18 TYR A 598 ARG A 604 1 7
HELIX 19 19 ILE A 605 LYS A 609 5 5
HELIX 20 20 PRO A 634 THR A 639 1 6
HELIX 21 21 ASP A 647 ILE A 651 5 5
HELIX 22 22 PRO A 674 PHE A 686 1 13
HELIX 23 23 ASP A 703 ASP A 717 1 15
HELIX 24 24 LYS A 747 GLY A 752 1 6
HELIX 25 25 SER A 801 LEU A 815 1 15
HELIX 26 26 GLN A 883 ALA A 887 5 5
HELIX 27 27 THR A 889 SER A 901 1 13
SHEET 1 A 5 LEU A 544 THR A 548 0
SHEET 2 A 5 HIS A 740 LYS A 746 1 O TRP A 742 N HIS A 546
SHEET 3 A 5 CYS A 719 THR A 726 -1 N LEU A 722 O LEU A 745
SHEET 4 A 5 PHE A 563 TYR A 569 -1 N LYS A 568 O GLY A 721
SHEET 5 A 5 SER A 698 LEU A 699 -1 O LEU A 699 N CYS A 565
SHEET 1 B 5 VAL A 584 PHE A 587 0
SHEET 2 B 5 GLN A 572 ALA A 578 -1 N GLN A 575 O PHE A 587
SHEET 3 B 5 PHE A 616 TRP A 625 -1 O THR A 620 N ALA A 574
SHEET 4 B 5 GLN A 654 LEU A 665 -1 O CYS A 656 N VAL A 623
SHEET 5 B 5 GLU A 668 SER A 669 -1 O GLU A 668 N LEU A 665
SHEET 1 C 5 VAL A 584 PHE A 587 0
SHEET 2 C 5 GLN A 572 ALA A 578 -1 N GLN A 575 O PHE A 587
SHEET 3 C 5 PHE A 616 TRP A 625 -1 O THR A 620 N ALA A 574
SHEET 4 C 5 GLN A 654 LEU A 665 -1 O CYS A 656 N VAL A 623
SHEET 5 C 5 PHE A 693 PHE A 695 1 O VAL A 694 N LEU A 657
SHEET 1 D 6 VAL A 816 LEU A 817 0
SHEET 2 D 6 HIS A 834 LEU A 836 -1 O TRP A 835 N LEU A 817
SHEET 3 D 6 ASP A 755 LEU A 766 -1 N ILE A 762 O LEU A 836
SHEET 4 D 6 TYR A 775 ASP A 784 -1 O LEU A 779 N ILE A 762
SHEET 5 D 6 GLU A 789 LEU A 796 -1 O ILE A 793 N LEU A 780
SHEET 6 D 6 VAL A 824 ARG A 825 1 O ARG A 825 N ALA A 792
SHEET 1 E 5 VAL A 816 LEU A 817 0
SHEET 2 E 5 HIS A 834 LEU A 836 -1 O TRP A 835 N LEU A 817
SHEET 3 E 5 ASP A 755 LEU A 766 -1 N ILE A 762 O LEU A 836
SHEET 4 E 5 VAL A 841 CYS A 846 -1 O VAL A 844 N LEU A 757
SHEET 5 E 5 ARG A 874 VAL A 878 -1 O ARG A 877 N GLU A 843
SHEET 1 F 2 ASP A 848 SER A 852 0
SHEET 2 F 2 GLY A 867 ARG A 871 -1 O SER A 869 N SER A 850
LINK P DG C 1 O3P AMP C 100 1555 1555 1.59
LINK C ARG A 307 N MSE A 308 1555 1555 1.33
LINK C MSE A 308 N VAL A 309 1555 1555 1.33
LINK C MSE A 393 N LEU A 394 1555 1555 1.34
LINK C ALA A 479 N MSE A 480 1555 1555 1.33
LINK C MSE A 480 N VAL A 481 1555 1555 1.32
LINK C GLY A 500 N MSE A 501 1555 1555 1.33
LINK C MSE A 501 N ILE A 502 1555 1555 1.32
LINK C PRO A 542 N MSE A 543 1555 1555 1.33
LINK C MSE A 543 N LEU A 544 1555 1555 1.32
LINK C LEU A 722 N MSE A 723 1555 1555 1.33
LINK C MSE A 723 N VAL A 724 1555 1555 1.33
LINK O3' DT B 12 P DOC B 13 1555 1555 1.59
CISPEP 1 PHE A 476 PRO A 477 0 -2.09
SITE 1 AC1 13 GLU A 566 TYR A 567 LYS A 568 TYR A 569
SITE 2 AC1 13 ARG A 573 ARG A 589 GLU A 621 PHE A 660
SITE 3 AC1 13 MSE A 723 LYS A 725 TRP A 742 LYS A 744
SITE 4 AC1 13 DG C 1
CRYST1 161.889 161.889 88.455 90.00 90.00 120.00 P 63 6
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 0.006177 0.003566 0.000000 0.00000
SCALE2 0.000000 0.007133 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011305 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
