HEADER LIGASE/DNA 15-DEC-09 3L2P
TITLE HUMAN DNA LIGASE III RECOGNIZES DNA ENDS BY DYNAMIC SWITCHING BETWEEN
TITLE 2 TWO DNA BOUND STATES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA LIGASE 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 257-833;
COMPND 5 SYNONYM: DNA LIGASE III, POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP] 3;
COMPND 6 EC: 6.5.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 5'-D(P*CP*GP*GP*GP*AP*TP*GP*CP*GP*TP*C)-3';
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: 5'-D(*GP*TP*CP*GP*GP*AP*CP*TP*G)-3';
COMPND 14 CHAIN: C;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: 5'-D(*GP*CP*CP*AP*GP*TP*CP*CP*GP*AP*CP*GP*AP*CP*GP*CP*AP*TP
COMPND 18 *CP*CP*CP*G)-3';
COMPND 19 CHAIN: D;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LIG3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-28;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: SYNTHETIC CONSTRUCT;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 OTHER_DETAILS: SYNTHETIC CONSTRUCT;
SOURCE 16 MOL_ID: 4;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 OTHER_DETAILS: SYNTHETIC CONSTRUCT
KEYWDS DNA LIGASE, DNA REPAIR, ATP-BINDING, CELL CYCLE, CELL DIVISION, DNA
KEYWDS 2 DAMAGE, DNA RECOMBINATION, DNA REPLICATION, LIGASE, MAGNESIUM,
KEYWDS 3 METAL-BINDING, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, ZINC-
KEYWDS 4 FINGER, LIGASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.COTNER-GOHARA,I.K.KIM,M.HAMMEL,J.A.TAINER,A.TOMKINSON,
AUTHOR 2 T.ELLENBERGER
REVDAT 2 11-AUG-10 3L2P 1 JRNL
REVDAT 1 14-JUL-10 3L2P 0
JRNL AUTH E.COTNER-GOHARA,I.K.KIM,M.HAMMEL,J.A.TAINER,A.E.TOMKINSON,
JRNL AUTH 2 T.ELLENBERGER
JRNL TITL HUMAN DNA LIGASE III RECOGNIZES DNA ENDS BY DYNAMIC
JRNL TITL 2 SWITCHING BETWEEN TWO DNA-BOUND STATES.
JRNL REF BIOCHEMISTRY V. 49 6165 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20518483
JRNL DOI 10.1021/BI100503W
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 49.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 24119
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1287
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) : 1331
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4145
REMARK 3 NUCLEIC ACID ATOMS : 855
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 144.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
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): 0.806
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.383
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.303
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.042
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5200 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7206 ; 1.840 ; 2.182
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 530 ; 7.059 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;38.570 ;24.595
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 747 ;20.966 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;22.962 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 816 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3598 ; 0.006 ; 0.021
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): 2664 ; 0.516 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4268 ; 1.014 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2536 ; 1.673 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2938 ; 2.682 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : NULL
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
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 159 A 390
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9180 7.6830 54.4880
REMARK 3 T TENSOR
REMARK 3 T11: 0.2551 T22: 0.2582
REMARK 3 T33: 0.3132 T12: 0.0718
REMARK 3 T13: 0.0064 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 4.1114 L22: 2.4193
REMARK 3 L33: 2.2843 L12: -0.3772
REMARK 3 L13: -0.1493 L23: 0.0156
REMARK 3 S TENSOR
REMARK 3 S11: -0.1377 S12: 0.2796 S13: -0.5908
REMARK 3 S21: -0.3668 S22: -0.0013 S23: -0.2880
REMARK 3 S31: 0.5068 S32: 0.4252 S33: 0.1390
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 391 A 590
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3070 33.6310 60.5010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.1828
REMARK 3 T33: 0.3068 T12: 0.0938
REMARK 3 T13: -0.1133 T23: 0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 3.4009 L22: 2.1615
REMARK 3 L33: 3.2157 L12: -0.1284
REMARK 3 L13: -0.4678 L23: -0.1198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0287 S12: 0.1461 S13: 0.4297
REMARK 3 S21: -0.2559 S22: 0.0276 S23: 0.2916
REMARK 3 S31: -0.5717 S32: -0.4608 S33: 0.0010
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 591 A 745
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3560 33.5060 29.6090
REMARK 3 T TENSOR
REMARK 3 T11: 1.1147 T22: 0.8414
REMARK 3 T33: 0.3931 T12: 0.0283
REMARK 3 T13: -0.0676 T23: 0.2340
REMARK 3 L TENSOR
REMARK 3 L11: 2.4553 L22: 0.2373
REMARK 3 L33: 3.7540 L12: -0.1082
REMARK 3 L13: 0.9631 L23: -0.4616
REMARK 3 S TENSOR
REMARK 3 S11: -0.0700 S12: 0.8995 S13: 0.2828
REMARK 3 S21: -0.3937 S22: -0.0225 S23: 0.0494
REMARK 3 S31: -0.3553 S32: 0.2024 S33: 0.0926
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 11
REMARK 3 RESIDUE RANGE : C 12 C 20
REMARK 3 RESIDUE RANGE : D 23 D 42
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4670 23.8050 45.6750
REMARK 3 T TENSOR
REMARK 3 T11: 0.2686 T22: 0.3835
REMARK 3 T33: 0.3612 T12: -0.0536
REMARK 3 T13: -0.0836 T23: 0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 1.3831 L22: 1.7507
REMARK 3 L33: 1.6315 L12: -0.0835
REMARK 3 L13: -0.0862 L23: -0.1269
REMARK 3 S TENSOR
REMARK 3 S11: -0.0846 S12: 0.6376 S13: 0.2084
REMARK 3 S21: -0.6722 S22: -0.0058 S23: 0.1906
REMARK 3 S31: 0.0802 S32: 0.0956 S33: 0.0905
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3L2P COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB056757.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : CRYO-COOLED SI(111) DOUBLE
REMARK 200 CRYSTAL.
REMARK 200 OPTICS : CRYOGENICALLY-COOLED DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR.
REMARK 200 TRIPLE STRIPED VERTICAL AND
REMARK 200 HORIZANTAL FOCUSSING MIRRORS IN
REMARK 200 KIRKPATRICK-BAEZ GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25407
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 12.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
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) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.60200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 ACETATE PH 5.6, VAPOR DIFFUSION, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -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 -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 75.21550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 65.07450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 65.07450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.60775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 65.07450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 65.07450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 112.82325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 65.07450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.07450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.60775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 65.07450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.07450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 112.82325
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.21550
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C
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 207
REMARK 465 ALA A 208
REMARK 465 GLY A 209
REMARK 465 ASP A 210
REMARK 465 GLY A 211
REMARK 465 PHE A 212
REMARK 465 HIS A 213
REMARK 465 LYS A 376
REMARK 465 GLU A 377
REMARK 465 PRO A 378
REMARK 465 GLY A 379
REMARK 465 GLN A 380
REMARK 465 ARG A 381
REMARK 465 ARG A 382
REMARK 465 ALA A 383
REMARK 465 GLU A 596
REMARK 465 GLY A 597
REMARK 465 ALA A 598
REMARK 465 ASP A 666
REMARK 465 PRO A 667
REMARK 465 SER A 668
REMARK 465 LYS A 669
REMARK 465 ILE A 670
REMARK 465 PRO A 671
REMARK 465 SER A 672
REMARK 465 TRP A 673
REMARK 465 LEU A 674
REMARK 465 LYS A 675
REMARK 465 VAL A 676
REMARK 465 ASN A 677
REMARK 465 LYS A 678
REMARK 465 ILE A 679
REMARK 465 TYR A 680
REMARK 465 TYR A 681
REMARK 465 PRO A 682
REMARK 465 ASP A 683
REMARK 465 PHE A 684
REMARK 465 ILE A 685
REMARK 465 VAL A 686
REMARK 465 PRO A 687
REMARK 465 ASP A 688
REMARK 465 PRO A 689
REMARK 465 LYS A 690
REMARK 465 LYS A 691
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 HIS A 168 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 170 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 171 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 172 CG CD CE NZ
REMARK 470 THR A 230 OG1 CG2
REMARK 470 LYS A 237 CG CD CE NZ
REMARK 470 ASN A 248 CG OD1 ND2
REMARK 470 ARG A 268 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 275 CG CD CE NZ
REMARK 470 PHE A 277 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 282 CG CD CE NZ
REMARK 470 LYS A 480 CG CD CE NZ
REMARK 470 LYS A 483 CG CD CE NZ
REMARK 470 GLN A 499 CG CD OE1 NE2
REMARK 470 ASP A 500 CG OD1 OD2
REMARK 470 LYS A 635 CG CD CE NZ
REMARK 470 LYS A 662 CG CD CE NZ
REMARK 470 LYS A 665 CG CD CE NZ
REMARK 470 PHE A 702 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 704 CG CD CE NZ
REMARK 470 GLU A 706 CG CD OE1 OE2
REMARK 470 ASP A 711 CG OD1 OD2
REMARK 470 ARG A 722 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 727 CG CD CE NZ
REMARK 470 LYS A 730 CG CD CE NZ
REMARK 470 DC B 11 O3'
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 ASN A 502 CB ASN A 502 CG 0.172
REMARK 500 DC B 8 O3' DC B 8 C3' -0.039
REMARK 500 DG C 12 P DG C 12 O5' 0.123
REMARK 500 DG C 12 O5' DG C 12 C5' 0.179
REMARK 500 DG C 12 C5' DG C 12 C4' 0.070
REMARK 500 DC D 24 O3' DC D 24 C3' -0.040
REMARK 500 DC D 25 C1' DC D 25 N1 0.085
REMARK 500 DT D 28 O3' DT D 28 C3' -0.063
REMARK 500 DA D 35 O3' DA D 35 C3' -0.048
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 PRO A 538 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 DC B 1 O4' - C1' - N1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 DG B 2 C5' - C4' - O4' ANGL. DEV. = 7.1 DEGREES
REMARK 500 DG B 2 C3' - C2' - C1' ANGL. DEV. = -6.0 DEGREES
REMARK 500 DG B 2 O4' - C1' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DG B 2 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DG B 3 O4' - C1' - N9 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DT B 6 C4 - C5 - C7 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT B 6 C6 - C5 - C7 ANGL. DEV. = -4.0 DEGREES
REMARK 500 DG B 7 C4 - C5 - N7 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DG B 7 C5 - N7 - C8 ANGL. DEV. = -3.8 DEGREES
REMARK 500 DG B 7 N7 - C8 - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DT B 10 O4' - C4' - C3' ANGL. DEV. = -9.0 DEGREES
REMARK 500 DT B 10 N3 - C4 - O4 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DT B 10 C5 - C4 - O4 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DG C 12 O4' - C4' - C3' ANGL. DEV. = -5.8 DEGREES
REMARK 500 DG C 12 C5' - C4' - C3' ANGL. DEV. = 9.2 DEGREES
REMARK 500 DG C 12 C4' - C3' - C2' ANGL. DEV. = 7.4 DEGREES
REMARK 500 DG C 12 O4' - C1' - N9 ANGL. DEV. = 8.0 DEGREES
REMARK 500 DG C 12 C8 - N9 - C4 ANGL. DEV. = -3.3 DEGREES
REMARK 500 DT C 13 C5 - C4 - O4 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DC C 14 O5' - P - OP2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 DG C 15 O5' - C5' - C4' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DA C 17 O4' - C1' - C2' ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA C 17 O4' - C1' - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 DT C 19 O4' - C1' - N1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 DG C 20 N3 - C4 - C5 ANGL. DEV. = -3.5 DEGREES
REMARK 500 DG C 20 N3 - C4 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG D 23 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DG D 23 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DC D 24 O4' - C4' - C3' ANGL. DEV. = -3.7 DEGREES
REMARK 500 DC D 25 O4' - C4' - C3' ANGL. DEV. = -2.6 DEGREES
REMARK 500 DC D 25 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES
REMARK 500 DC D 25 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 DA D 32 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DC D 33 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DG D 34 O4' - C1' - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DA D 35 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC D 36 O5' - C5' - C4' ANGL. DEV. = -5.0 DEGREES
REMARK 500 DC D 38 O4' - C4' - C3' ANGL. DEV. = -2.4 DEGREES
REMARK 500 DC D 38 C1' - O4' - C4' ANGL. DEV. = -7.8 DEGREES
REMARK 500 DC D 38 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DC D 43 O4' - C4' - C3' ANGL. DEV. = -2.7 DEGREES
REMARK 500 DC D 43 C3' - C2' - C1' ANGL. DEV. = -7.0 DEGREES
REMARK 500 DC D 43 O4' - C1' - C2' ANGL. DEV. = -7.3 DEGREES
REMARK 500 DC D 42 C3' - O3' - P ANGL. DEV. = -7.8 DEGREES
REMARK 500 DG D 44 O4' - C1' - C2' ANGL. DEV. = -4.9 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 LYS A 205 -69.85 -101.40
REMARK 500 ASP A 236 -59.62 -27.41
REMARK 500 ASP A 262 103.40 -166.67
REMARK 500 PHE A 270 21.93 -77.44
REMARK 500 LYS A 275 22.32 -65.17
REMARK 500 SER A 276 -44.21 -136.05
REMARK 500 THR A 301 -27.47 -149.75
REMARK 500 SER A 315 22.44 -77.06
REMARK 500 ARG A 316 31.11 -140.24
REMARK 500 THR A 318 11.95 -69.10
REMARK 500 ALA A 319 -65.09 72.05
REMARK 500 LYS A 334 56.94 36.82
REMARK 500 ASP A 347 138.57 169.12
REMARK 500 PRO A 348 -32.01 -34.35
REMARK 500 VAL A 374 -85.85 -123.43
REMARK 500 MET A 391 -10.07 86.81
REMARK 500 CYS A 412 77.45 -115.83
REMARK 500 LEU A 443 18.29 58.84
REMARK 500 VAL A 451 -8.62 -162.78
REMARK 500 THR A 489 -8.35 -51.84
REMARK 500 ASN A 514 62.81 28.38
REMARK 500 PRO A 538 110.32 -25.24
REMARK 500 ARG A 540 -65.39 -132.32
REMARK 500 THR A 550 -20.72 -155.26
REMARK 500 GLU A 565 50.60 -100.13
REMARK 500 ALA A 643 -53.95 -128.21
REMARK 500 GLU A 657 10.14 -65.37
REMARK 500 MET A 660 71.54 -108.92
REMARK 500 ALA A 707 -34.03 -139.91
REMARK 500 THR A 709 -34.77 -37.20
REMARK 500 ALA A 710 93.61 -66.87
REMARK 500 ASP A 711 -32.72 43.08
REMARK 500 PHE A 717 61.17 39.32
REMARK 500 THR A 721 -75.93 -107.97
REMARK 500 LYS A 727 51.93 -105.41
REMARK 500 ASP A 728 85.65 -52.41
REMARK 500 TRP A 729 -173.57 67.89
REMARK 500 LYS A 730 -43.73 60.38
REMARK 500 ALA A 732 176.79 -59.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 AMP A 901
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 901
DBREF 3L2P A 170 746 UNP P49916 DNLI3_HUMAN 257 833
DBREF 3L2P B 1 11 PDB 3L2P 3L2P 1 11
DBREF 3L2P C 12 20 PDB 3L2P 3L2P 12 20
DBREF 3L2P D 23 44 PDB 3L2P 3L2P 23 44
SEQADV 3L2P HIS A 168 UNP P49916 EXPRESSION TAG
SEQADV 3L2P MET A 169 UNP P49916 EXPRESSION TAG
SEQRES 1 A 579 HIS MET ARG HIS LYS ASP CYS LEU LEU ARG GLU PHE ARG
SEQRES 2 A 579 LYS LEU CYS ALA MET VAL ALA ASP ASN PRO SER TYR ASN
SEQRES 3 A 579 THR LYS THR GLN ILE ILE GLN ASP PHE LEU ARG LYS GLY
SEQRES 4 A 579 SER ALA GLY ASP GLY PHE HIS GLY ASP VAL TYR LEU THR
SEQRES 5 A 579 VAL LYS LEU LEU LEU PRO GLY VAL ILE LYS THR VAL TYR
SEQRES 6 A 579 ASN LEU ASN ASP LYS GLN ILE VAL LYS LEU PHE SER ARG
SEQRES 7 A 579 ILE PHE ASN CYS ASN PRO ASP ASP MET ALA ARG ASP LEU
SEQRES 8 A 579 GLU GLN GLY ASP VAL SER GLU THR ILE ARG VAL PHE PHE
SEQRES 9 A 579 GLU GLN SER LYS SER PHE PRO PRO ALA ALA LYS SER LEU
SEQRES 10 A 579 LEU THR ILE GLN GLU VAL ASP GLU PHE LEU LEU ARG LEU
SEQRES 11 A 579 SER LYS LEU THR LYS GLU ASP GLU GLN GLN GLN ALA LEU
SEQRES 12 A 579 GLN ASP ILE ALA SER ARG CYS THR ALA ASN ASP LEU LYS
SEQRES 13 A 579 CYS ILE ILE ARG LEU ILE LYS HIS ASP LEU LYS MET ASN
SEQRES 14 A 579 SER GLY ALA LYS HIS VAL LEU ASP ALA LEU ASP PRO ASN
SEQRES 15 A 579 ALA TYR GLU ALA PHE LYS ALA SER ARG ASN LEU GLN ASP
SEQRES 16 A 579 VAL VAL GLU ARG VAL LEU HIS ASN ALA GLN GLU VAL GLU
SEQRES 17 A 579 LYS GLU PRO GLY GLN ARG ARG ALA LEU SER VAL GLN ALA
SEQRES 18 A 579 SER LEU MET THR PRO VAL GLN PRO MET LEU ALA GLU ALA
SEQRES 19 A 579 CYS LYS SER VAL GLU TYR ALA MET LYS LYS CYS PRO ASN
SEQRES 20 A 579 GLY MET PHE SER GLU ILE LYS TYR ASP GLY GLU ARG VAL
SEQRES 21 A 579 GLN VAL HIS LYS ASN GLY ASP HIS PHE SER TYR PHE SER
SEQRES 22 A 579 ARG SER LEU LYS PRO VAL LEU PRO HIS LYS VAL ALA HIS
SEQRES 23 A 579 PHE LYS ASP TYR ILE PRO GLN ALA PHE PRO GLY GLY HIS
SEQRES 24 A 579 SER MET ILE LEU ASP SER GLU VAL LEU LEU ILE ASP ASN
SEQRES 25 A 579 LYS THR GLY LYS PRO LEU PRO PHE GLY THR LEU GLY VAL
SEQRES 26 A 579 HIS LYS LYS ALA ALA PHE GLN ASP ALA ASN VAL CYS LEU
SEQRES 27 A 579 PHE VAL PHE ASP CYS ILE TYR PHE ASN ASP VAL SER LEU
SEQRES 28 A 579 MET ASP ARG PRO LEU CYS GLU ARG ARG LYS PHE LEU HIS
SEQRES 29 A 579 ASP ASN MET VAL GLU ILE PRO ASN ARG ILE MET PHE SER
SEQRES 30 A 579 GLU MET LYS ARG VAL THR LYS ALA LEU ASP LEU ALA ASP
SEQRES 31 A 579 MET ILE THR ARG VAL ILE GLN GLU GLY LEU GLU GLY LEU
SEQRES 32 A 579 VAL LEU LYS ASP VAL LYS GLY THR TYR GLU PRO GLY LYS
SEQRES 33 A 579 ARG HIS TRP LEU LYS VAL LYS LYS ASP TYR LEU ASN GLU
SEQRES 34 A 579 GLY ALA MET ALA ASP THR ALA ASP LEU VAL VAL LEU GLY
SEQRES 35 A 579 ALA PHE TYR GLY GLN GLY SER LYS GLY GLY MET MET SER
SEQRES 36 A 579 ILE PHE LEU MET GLY CYS TYR ASP PRO GLY SER GLN LYS
SEQRES 37 A 579 TRP CYS THR VAL THR LYS CYS ALA GLY GLY HIS ASP ASP
SEQRES 38 A 579 ALA THR LEU ALA ARG LEU GLN ASN GLU LEU ASP MET VAL
SEQRES 39 A 579 LYS ILE SER LYS ASP PRO SER LYS ILE PRO SER TRP LEU
SEQRES 40 A 579 LYS VAL ASN LYS ILE TYR TYR PRO ASP PHE ILE VAL PRO
SEQRES 41 A 579 ASP PRO LYS LYS ALA ALA VAL TRP GLU ILE THR GLY ALA
SEQRES 42 A 579 GLU PHE SER LYS SER GLU ALA HIS THR ALA ASP GLY ILE
SEQRES 43 A 579 SER ILE ARG PHE PRO ARG CYS THR ARG ILE ARG ASP ASP
SEQRES 44 A 579 LYS ASP TRP LYS SER ALA THR ASN LEU PRO GLN LEU LYS
SEQRES 45 A 579 GLU LEU TYR GLN LEU SER LYS
SEQRES 1 B 11 DC DG DG DG DA DT DG DC DG DT DC
SEQRES 1 C 9 DG DT DC DG DG DA DC DT DG
SEQRES 1 D 22 DG DC DC DA DG DT DC DC DG DA DC DG DA
SEQRES 2 D 22 DC DG DC DA DT DC DC DC DG
HET AMP A 901 22
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 5 AMP C10 H14 N5 O7 P
HELIX 1 1 HIS A 171 CYS A 174 5 4
HELIX 2 2 LEU A 175 ASP A 188 1 14
HELIX 3 3 SER A 191 LYS A 205 1 15
HELIX 4 4 ASP A 215 LEU A 224 1 10
HELIX 5 5 ASN A 235 ASN A 248 1 14
HELIX 6 6 ASN A 250 LEU A 258 1 9
HELIX 7 7 GLU A 259 GLY A 261 5 3
HELIX 8 8 ASP A 262 GLN A 273 1 12
HELIX 9 9 THR A 286 LYS A 299 1 14
HELIX 10 10 LYS A 302 SER A 315 1 14
HELIX 11 11 ALA A 319 LYS A 330 1 12
HELIX 12 12 GLY A 338 ALA A 345 1 8
HELIX 13 13 ASN A 349 SER A 357 1 9
HELIX 14 14 ASN A 359 GLU A 373 1 15
HELIX 15 15 SER A 404 CYS A 412 1 9
HELIX 16 16 LEU A 447 VAL A 451 5 5
HELIX 17 17 HIS A 453 ASP A 456 5 4
HELIX 18 18 TYR A 457 PHE A 462 1 6
HELIX 19 19 PRO A 486 LEU A 490 5 5
HELIX 20 20 GLY A 491 PHE A 498 1 8
HELIX 21 21 PRO A 522 MET A 534 1 13
HELIX 22 22 LYS A 551 GLU A 565 1 15
HELIX 23 23 ASP A 647 LEU A 654 1 8
HELIX 24 24 ASN A 734 LEU A 744 1 11
SHEET 1 A 5 LEU A 398 ALA A 401 0
SHEET 2 A 5 ARG A 584 VAL A 589 1 O TRP A 586 N GLU A 400
SHEET 3 A 5 LEU A 570 ASP A 574 -1 N LEU A 572 O LEU A 587
SHEET 4 A 5 MET A 416 ILE A 420 -1 N PHE A 417 O LYS A 573
SHEET 5 A 5 MET A 546 VAL A 549 -1 O VAL A 549 N MET A 416
SHEET 1 B 5 HIS A 435 PHE A 439 0
SHEET 2 B 5 GLU A 425 ASN A 432 -1 N ASN A 432 O HIS A 435
SHEET 3 B 5 SER A 467 LEU A 476 -1 O SER A 472 N VAL A 427
SHEET 4 B 5 VAL A 503 PHE A 513 -1 O CYS A 504 N LEU A 475
SHEET 5 B 5 VAL A 516 SER A 517 -1 O VAL A 516 N PHE A 513
SHEET 1 C 5 HIS A 435 PHE A 439 0
SHEET 2 C 5 GLU A 425 ASN A 432 -1 N ASN A 432 O HIS A 435
SHEET 3 C 5 SER A 467 LEU A 476 -1 O SER A 472 N VAL A 427
SHEET 4 C 5 VAL A 503 PHE A 513 -1 O CYS A 504 N LEU A 475
SHEET 5 C 5 ILE A 541 PHE A 543 1 O MET A 542 N VAL A 507
SHEET 1 D 5 TRP A 636 CYS A 642 0
SHEET 2 D 5 ILE A 623 TYR A 629 -1 N CYS A 628 O CYS A 637
SHEET 3 D 5 ASP A 601 PHE A 611 -1 N VAL A 606 O GLY A 627
SHEET 4 D 5 ALA A 693 GLY A 699 -1 O ILE A 697 N ALA A 603
SHEET 5 D 5 ARG A 719 CYS A 720 -1 O ARG A 719 N THR A 698
SHEET 1 E 2 PHE A 702 LYS A 704 0
SHEET 2 E 2 ILE A 713 ILE A 715 -1 O SER A 714 N SER A 703
LINK NZ LYS A 421 P AMP A 901 1555 1555 2.23
SITE 1 AC1 11 GLU A 419 ILE A 420 LYS A 421 TYR A 422
SITE 2 AC1 11 ARG A 426 PHE A 508 LYS A 573 TRP A 586
SITE 3 AC1 11 LYS A 588 LYS A 590 DG C 12
CRYST1 130.149 130.149 150.431 90.00 90.00 90.00 P 41 21 2 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 0.007684 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006648 0.00000
(ATOM LINES ARE NOT SHOWN.)
END