HEADER HYDROLASE 10-OCT-18 6IJN
TITLE THE D295N MUTANT OF THE N6-METHYL-AMP DEAMINASE FROM ARABIDOPSIS
TITLE 2 THALIANA COMPLEXED WITH N6M-AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE/AMP DEAMINASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PUTATIVE ADENOSINE DEAMINASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT4G04880, T4B21.20, T4B21_20;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PURINE METABOLISM, DEAMINASE, N6-METHYLADENSOSINE, TIM-BARREL,
KEYWDS 2 INOSINE, EPIGENETICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XIE,Q.JIA
REVDAT 4 22-NOV-23 6IJN 1 REMARK
REVDAT 3 17-APR-19 6IJN 1 JRNL
REVDAT 2 20-FEB-19 6IJN 1 JRNL
REVDAT 1 06-FEB-19 6IJN 0
JRNL AUTH Q.JIA,W.XIE
JRNL TITL ALTERNATIVE CONFORMATION INDUCED BY SUBSTRATE BINDING FOR
JRNL TITL 2 ARABIDOPSIS THALIANAN6-METHYL-AMP DEAMINASE.
JRNL REF NUCLEIC ACIDS RES. V. 47 3233 2019
JRNL REFN ESSN 1362-4962
JRNL PMID 30721978
JRNL DOI 10.1093/NAR/GKZ070
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 42004
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2141
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.2824 - 4.0795 1.00 2859 153 0.1620 0.1740
REMARK 3 2 4.0795 - 3.2383 1.00 2753 129 0.1372 0.1713
REMARK 3 3 3.2383 - 2.8291 1.00 2697 148 0.1428 0.1486
REMARK 3 4 2.8291 - 2.5704 1.00 2678 139 0.1469 0.1890
REMARK 3 5 2.5704 - 2.3862 1.00 2686 122 0.1395 0.1551
REMARK 3 6 2.3862 - 2.2455 1.00 2669 136 0.1423 0.1747
REMARK 3 7 2.2455 - 2.1331 1.00 2672 137 0.1418 0.1723
REMARK 3 8 2.1331 - 2.0402 1.00 2658 142 0.1388 0.1452
REMARK 3 9 2.0402 - 1.9617 1.00 2600 161 0.1352 0.1677
REMARK 3 10 1.9617 - 1.8940 1.00 2646 155 0.1473 0.1995
REMARK 3 11 1.8940 - 1.8348 0.99 2605 149 0.1511 0.1949
REMARK 3 12 1.8348 - 1.7823 1.00 2579 148 0.1508 0.1883
REMARK 3 13 1.7823 - 1.7354 1.00 2629 148 0.1634 0.1900
REMARK 3 14 1.7354 - 1.6931 0.99 2632 136 0.1660 0.2054
REMARK 3 15 1.6931 - 1.6546 0.95 2500 138 0.1730 0.2187
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 2769
REMARK 3 ANGLE : 1.065 3754
REMARK 3 CHIRALITY : 0.069 444
REMARK 3 PLANARITY : 0.007 471
REMARK 3 DIHEDRAL : 17.759 1662
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6IJN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1300009254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NFPSS
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42279
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.051
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 13.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2ADA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 3350, 0.1 M NACL, 0.1 M TRIS
REMARK 280 -HCL (PH 9.0)., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.95600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.39600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.04300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.39600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.95600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.04300
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 LEU A -8
REMARK 465 GLU A -7
REMARK 465 VAL A -6
REMARK 465 LEU A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 GLY A -2
REMARK 465 PRO A -1
REMARK 465 ALA A 133
REMARK 465 SER A 134
REMARK 465 ASP A 135
REMARK 465 SER A 136
REMARK 465 GLN A 137
REMARK 465 LYS A 138
REMARK 465 LEU A 139
REMARK 465 HIS A 140
REMARK 465 ASN A 141
REMARK 465 ALA A 142
REMARK 465 GLY A 143
REMARK 465 ASP A 144
REMARK 465 GLY A 145
REMARK 465 ILE A 146
REMARK 465 GLY A 147
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 0 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 2 CG CD OE1 OE2
REMARK 470 GLU A 34 CG CD OE1 OE2
REMARK 470 LYS A 35 CG CD CE NZ
REMARK 470 VAL A 37 CG1 CG2
REMARK 470 GLN A 48 CG CD OE1 NE2
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 514 O HOH A 705 2.02
REMARK 500 O HOH A 720 O HOH A 789 2.02
REMARK 500 O HOH A 606 O HOH A 720 2.03
REMARK 500 O HOH A 590 O HOH A 685 2.08
REMARK 500 O HOH A 628 O HOH A 698 2.09
REMARK 500 O HOH A 643 O HOH A 724 2.10
REMARK 500 O HOH A 527 O HOH A 744 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 591 O HOH A 648 4445 2.15
REMARK 500 O HOH A 531 O HOH A 699 2554 2.19
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 ASN A 223 77.21 -167.34
REMARK 500 HIS A 240 -83.30 82.78
REMARK 500 ASN A 295 -71.72 67.93
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 6MZ A 401
DBREF 6IJN A 1 355 UNP Q8LPL7 Q8LPL7_ARATH 1 355
SEQADV 6IJN MET A -20 UNP Q8LPL7 INITIATING METHIONINE
SEQADV 6IJN GLY A -19 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN SER A -18 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN SER A -17 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -16 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -15 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -14 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -13 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -12 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -11 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -10 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A -9 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN LEU A -8 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN GLU A -7 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN VAL A -6 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN LEU A -5 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN PHE A -4 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN GLN A -3 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN GLY A -2 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN PRO A -1 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN HIS A 0 UNP Q8LPL7 EXPRESSION TAG
SEQADV 6IJN ASN A 295 UNP Q8LPL7 ASP 295 ENGINEERED MUTATION
SEQRES 1 A 376 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS HIS LEU
SEQRES 2 A 376 GLU VAL LEU PHE GLN GLY PRO HIS MET GLU TRP ILE GLN
SEQRES 3 A 376 SER LEU PRO LYS ILE GLU LEU HIS ALA HIS LEU ASN GLY
SEQRES 4 A 376 SER ILE ARG ASP SER THR LEU LEU GLU LEU ALA ARG VAL
SEQRES 5 A 376 LEU GLY GLU LYS GLY VAL ILE VAL PHE ALA ASP VAL GLU
SEQRES 6 A 376 HIS VAL ILE GLN LYS ASN ASP ARG SER LEU VAL GLU VAL
SEQRES 7 A 376 PHE LYS LEU PHE ASP LEU ILE HIS LYS LEU THR THR ASP
SEQRES 8 A 376 HIS LYS THR VAL THR ARG ILE THR ARG GLU VAL VAL GLU
SEQRES 9 A 376 ASP PHE ALA LEU GLU ASN VAL VAL TYR LEU GLU LEU ARG
SEQRES 10 A 376 THR THR PRO LYS ARG SER ASP SER ILE GLY MET SER LYS
SEQRES 11 A 376 ARG SER TYR MET GLU ALA VAL ILE GLN GLY LEU ARG SER
SEQRES 12 A 376 VAL SER GLU VAL ASP ILE ASP PHE VAL THR ALA SER ASP
SEQRES 13 A 376 SER GLN LYS LEU HIS ASN ALA GLY ASP GLY ILE GLY ARG
SEQRES 14 A 376 LYS LYS ILE TYR VAL ARG LEU LEU LEU SER ILE ASP ARG
SEQRES 15 A 376 ARG GLU THR THR GLU SER ALA MET GLU THR VAL LYS LEU
SEQRES 16 A 376 ALA LEU GLU MET ARG ASP VAL GLY VAL VAL GLY ILE ASP
SEQRES 17 A 376 LEU SER GLY ASN PRO LEU VAL GLY GLU TRP SER THR PHE
SEQRES 18 A 376 LEU PRO ALA LEU GLN TYR ALA LYS ASP ASN ASP LEU HIS
SEQRES 19 A 376 ILE THR LEU HIS CYS GLY GLU VAL PRO ASN PRO LYS GLU
SEQRES 20 A 376 ILE GLN ALA MET LEU ASP PHE LYS PRO HIS ARG ILE GLY
SEQRES 21 A 376 HIS ALA CYS PHE PHE LYS ASP GLU ASP TRP THR LYS LEU
SEQRES 22 A 376 LYS SER PHE ARG ILE PRO VAL GLU ILE CYS LEU THR SER
SEQRES 23 A 376 ASN ILE VAL THR LYS SER ILE SER SER ILE ASP ILE HIS
SEQRES 24 A 376 HIS PHE ALA ASP LEU TYR ASN ALA LYS HIS PRO LEU ILE
SEQRES 25 A 376 LEU CYS THR ASN ASP PHE GLY VAL PHE SER THR SER LEU
SEQRES 26 A 376 SER ASN GLU TYR ALA LEU ALA VAL ARG SER LEU GLY LEU
SEQRES 27 A 376 SER LYS SER GLU THR PHE ALA LEU ALA ARG ALA ALA ILE
SEQRES 28 A 376 ASP ALA THR PHE ALA GLU ASP GLU VAL LYS GLN GLN LEU
SEQRES 29 A 376 ARG PHE ILE PHE ASP SER ALA SER PRO GLU HIS VAL
HET 6MZ A 401 24
HETNAM 6MZ N6-METHYLADENOSINE-5'-MONOPHOSPHATE
FORMUL 2 6MZ C11 H16 N5 O7 P
FORMUL 3 HOH *305(H2 O)
HELIX 1 AA1 HIS A 0 LEU A 7 1 8
HELIX 2 AA2 ASN A 17 SER A 19 5 3
HELIX 3 AA3 ARG A 21 LYS A 35 1 15
HELIX 4 AA4 VAL A 39 ASN A 50 1 12
HELIX 5 AA5 SER A 53 THR A 69 1 17
HELIX 6 AA6 ASP A 70 GLU A 88 1 19
HELIX 7 AA7 SER A 102 GLY A 106 5 5
HELIX 8 AA8 SER A 108 SER A 122 1 15
HELIX 9 AA9 THR A 164 MET A 178 1 15
HELIX 10 AB1 ARG A 179 VAL A 181 5 3
HELIX 11 AB2 GLU A 196 ASN A 210 1 15
HELIX 12 AB3 ASN A 223 LYS A 234 1 12
HELIX 13 AB4 LYS A 245 ARG A 256 1 12
HELIX 14 AB5 CYS A 262 THR A 269 1 8
HELIX 15 AB6 SER A 274 ILE A 277 5 4
HELIX 16 AB7 HIS A 278 ALA A 286 1 9
HELIX 17 AB8 SER A 303 GLY A 316 1 14
HELIX 18 AB9 SER A 318 ALA A 329 1 12
HELIX 19 AC1 ILE A 330 THR A 333 5 4
HELIX 20 AC2 GLU A 336 SER A 351 1 16
HELIX 21 AC3 PRO A 352 HIS A 354 5 3
SHEET 1 AA1 4 LYS A 9 HIS A 15 0
SHEET 2 AA1 4 VAL A 90 THR A 97 1 O VAL A 91 N LYS A 9
SHEET 3 AA1 4 LYS A 150 ASP A 160 1 O TYR A 152 N LEU A 93
SHEET 4 AA1 4 ASP A 127 ASP A 129 1 N ASP A 129 O VAL A 153
SHEET 1 AA2 8 LYS A 9 HIS A 15 0
SHEET 2 AA2 8 VAL A 90 THR A 97 1 O VAL A 91 N LYS A 9
SHEET 3 AA2 8 LYS A 150 ASP A 160 1 O TYR A 152 N LEU A 93
SHEET 4 AA2 8 VAL A 183 SER A 189 1 O VAL A 184 N LEU A 155
SHEET 5 AA2 8 HIS A 213 CYS A 218 1 O THR A 215 N ILE A 186
SHEET 6 AA2 8 ARG A 237 HIS A 240 1 O GLY A 239 N LEU A 216
SHEET 7 AA2 8 VAL A 259 ILE A 261 1 O GLU A 260 N ILE A 238
SHEET 8 AA2 8 LEU A 290 LEU A 292 1 O ILE A 291 N ILE A 261
SITE 1 AC1 21 HIS A 15 LEU A 16 ASN A 17 PHE A 58
SITE 2 AC1 21 PHE A 61 HIS A 65 THR A 97 THR A 98
SITE 3 AC1 21 LYS A 100 ASP A 160 GLY A 190 HIS A 217
SITE 4 AC1 21 GLU A 220 HIS A 240 ASN A 295 ASP A 296
SITE 5 AC1 21 HOH A 508 HOH A 530 HOH A 550 HOH A 582
SITE 6 AC1 21 HOH A 640
CRYST1 49.912 80.086 86.792 90.00 90.00 90.00 P 21 21 21 4
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 0.020035 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012487 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011522 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
