HEADER LIGASE 19-AUG-08 3E7X
TITLE CRYSTAL STRUCTURE OF DLTA: IMPLICATIONS FOR THE REACTION
TITLE 2 MECHANISM OF NON-RIBOSOMAL PEPTIDE SYNTHETASE (NRPS)
TITLE 3 ADENYLATION DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ALANINE--POLY(PHOSPHORIBITOL) LIGASE SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DLTA PROTEIN, D-ALANINE-ACTIVATING ENZYME, DAE, D-
COMPND 5 ALANINE-D-ALANYL CARRIER PROTEIN LIGASE, DCL;
COMPND 6 EC: 6.1.1.13;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: DLTA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS DLTA, NON-RIBOSOMAL PEPTIDE SYNTHETASE, NRPS, ADENYLATION
KEYWDS 2 DOMAIN, D-ALANYLATION, D-ALANINE-DALANYL, AMP, CYTOPLASM,
KEYWDS 3 LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.YONUS,P.NEUMANN,S.ZIMMERMANN,J.J.MAY,M.A.MARAHIEL,
AUTHOR 2 M.T.STUBBS
REVDAT 2 30-DEC-08 3E7X 1 JRNL VERSN
REVDAT 1 09-SEP-08 3E7X 0
JRNL AUTH H.YONUS,P.NEUMANN,S.ZIMMERMANN,J.J.MAY,
JRNL AUTH 2 M.A.MARAHIEL,M.T.STUBBS
JRNL TITL CRYSTAL STRUCTURE OF DLTA. IMPLICATIONS FOR THE
JRNL TITL 2 REACTION MECHANISM OF NON-RIBOSOMAL PEPTIDE
JRNL TITL 3 SYNTHETASE ADENYLATION DOMAINS
JRNL REF J.BIOL.CHEM. V. 283 32484 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18784082
JRNL DOI 10.1074/JBC.M800557200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2190991.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 15932
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 SET) : 0.179
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1037
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.64
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 755
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 53
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.045
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4035
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18000
REMARK 3 B22 (A**2) : -3.63000
REMARK 3 B33 (A**2) : 4.81000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.43
REMARK 3 LOW RESOLUTION CUTOFF (A) : 3.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.54
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 49.51
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : AMP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : AMP.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3E7X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048987.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91438
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15976
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.010
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.89
REMARK 200 R MERGE FOR SHELL (I) : 0.21800
REMARK 200 R SYM FOR SHELL (I) : 0.26900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
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: PDB CODE 3E7W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 1000, PH 6.5, VAPOR
REMARK 280 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 22.88250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.73550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.69450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.73550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.88250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.69450
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 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 HIS A 509
REMARK 465 HIS A 510
REMARK 465 HIS A 511
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 TYR A 14 71.86 -119.79
REMARK 500 GLN A 23 73.03 52.80
REMARK 500 HIS A 60 -94.43 -118.91
REMARK 500 ALA A 106 -7.18 -32.83
REMARK 500 LEU A 109 -160.56 -59.97
REMARK 500 SER A 110 -157.84 -137.93
REMARK 500 ASP A 112 61.60 67.42
REMARK 500 ALA A 113 -97.40 -104.04
REMARK 500 GLN A 117 75.01 -102.80
REMARK 500 LEU A 127 -0.91 -56.72
REMARK 500 GLU A 130 -116.59 -95.90
REMARK 500 SER A 133 113.46 -162.61
REMARK 500 GLN A 136 -35.92 -33.89
REMARK 500 TRP A 139 139.47 -36.91
REMARK 500 GLU A 142 -122.32 48.38
REMARK 500 PRO A 223 -37.09 -39.58
REMARK 500 LEU A 259 79.08 -118.89
REMARK 500 THR A 299 68.84 63.43
REMARK 500 VAL A 300 -76.68 73.15
REMARK 500 PRO A 325 -39.30 -28.06
REMARK 500 ILE A 331 77.64 -119.59
REMARK 500 ASP A 398 -158.87 -105.08
REMARK 500 ASN A 434 -71.61 -70.75
REMARK 500 HIS A 449 -141.51 -113.79
REMARK 500 PHE A 451 170.04 -57.72
REMARK 500 GLU A 452 -91.52 -98.08
REMARK 500 LYS A 453 -176.47 -67.17
REMARK 500 PHE A 455 2.49 -64.06
REMARK 500 ILE A 492 153.03 -43.01
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 A 512
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AMU RELATED DB: PDB
REMARK 900 RELATED ID: 1MD9 RELATED DB: PDB
REMARK 900 RELATED ID: 2DLS RELATED DB: PDB
REMARK 900 RELATED ID: 1BA3 RELATED DB: PDB
REMARK 900 RELATED ID: 1PG4 RELATED DB: PDB
REMARK 900 RELATED ID: 1HQB RELATED DB: PDB
REMARK 900 RELATED ID: 3E7W RELATED DB: PDB
DBREF 3E7X A 1 503 UNP P39581 DLTA_BACSU 1 503
SEQADV 3E7X ARG A 504 UNP P39581 EXPRESSION TAG
SEQADV 3E7X SER A 505 UNP P39581 EXPRESSION TAG
SEQADV 3E7X HIS A 506 UNP P39581 EXPRESSION TAG
SEQADV 3E7X HIS A 507 UNP P39581 EXPRESSION TAG
SEQADV 3E7X HIS A 508 UNP P39581 EXPRESSION TAG
SEQADV 3E7X HIS A 509 UNP P39581 EXPRESSION TAG
SEQADV 3E7X HIS A 510 UNP P39581 EXPRESSION TAG
SEQADV 3E7X HIS A 511 UNP P39581 EXPRESSION TAG
SEQRES 1 A 511 MET LYS LEU LEU HIS ALA ILE GLN THR HIS ALA GLU THR
SEQRES 2 A 511 TYR PRO GLN THR ASP ALA PHE ARG SER GLN GLY GLN SER
SEQRES 3 A 511 LEU THR TYR GLN GLU LEU TRP GLU GLN SER ASP ARG ALA
SEQRES 4 A 511 ALA ALA ALA ILE GLN LYS ARG ILE SER GLY GLU LYS LYS
SEQRES 5 A 511 SER PRO ILE LEU VAL TYR GLY HIS MET GLU PRO HIS MET
SEQRES 6 A 511 ILE VAL SER PHE LEU GLY SER VAL LYS ALA GLY HIS PRO
SEQRES 7 A 511 TYR ILE PRO VAL ASP LEU SER ILE PRO SER GLU ARG ILE
SEQRES 8 A 511 ALA LYS ILE ILE GLU SER SER GLY ALA GLU LEU LEU ILE
SEQRES 9 A 511 HIS ALA ALA GLY LEU SER ILE ASP ALA VAL GLY GLN GLN
SEQRES 10 A 511 ILE GLN THR VAL SER ALA GLU GLU LEU LEU GLU ASN GLU
SEQRES 11 A 511 GLY GLY SER VAL SER GLN ASP GLN TRP VAL LYS GLU HIS
SEQRES 12 A 511 GLU THR PHE TYR ILE ILE TYR THR SER GLY SER THR GLY
SEQRES 13 A 511 ASN PRO LYS GLY VAL GLN ILE SER ALA ALA ASN LEU GLN
SEQRES 14 A 511 SER PHE THR ASP TRP ILE CYS ALA ASP PHE PRO VAL SER
SEQRES 15 A 511 GLY GLY LYS ILE PHE LEU ASN GLN ALA PRO PHE SER PHE
SEQRES 16 A 511 ASP LEU SER VAL MET ASP LEU TYR PRO CYS LEU GLN SER
SEQRES 17 A 511 GLY GLY THR LEU HIS CYS VAL THR LYS ASP ALA VAL ASN
SEQRES 18 A 511 LYS PRO LYS VAL LEU PHE GLU GLU LEU LYS LYS SER GLY
SEQRES 19 A 511 LEU ASN VAL TRP THR SER THR PRO SER PHE VAL GLN MET
SEQRES 20 A 511 CYS LEU MET ASP PRO GLY PHE SER GLN ASP LEU LEU PRO
SEQRES 21 A 511 HIS ALA ASP THR PHE MET PHE CYS GLY GLU VAL LEU PRO
SEQRES 22 A 511 VAL SER VAL ALA LYS ALA LEU LEU GLU ARG PHE PRO LYS
SEQRES 23 A 511 ALA LYS ILE PHE ASN THR TYR GLY PRO THR GLU ALA THR
SEQRES 24 A 511 VAL ALA VAL THR SER VAL GLU ILE THR ASN ASP VAL ILE
SEQRES 25 A 511 SER ARG SER GLU SER LEU PRO VAL GLY PHE ALA LYS PRO
SEQRES 26 A 511 ASP MET ASN ILE PHE ILE MET ASP GLU GLU GLY GLN PRO
SEQRES 27 A 511 LEU PRO GLU GLY GLU LYS GLY GLU ILE VAL ILE ALA GLY
SEQRES 28 A 511 PRO SER VAL SER ARG GLY TYR LEU GLY GLU PRO GLU LEU
SEQRES 29 A 511 THR GLU LYS ALA PHE PHE SER HIS GLU GLY GLN TRP ALA
SEQRES 30 A 511 TYR ARG THR GLY ASP ALA GLY PHE ILE GLN ASP GLY GLN
SEQRES 31 A 511 ILE PHE CYS GLN GLY ARG LEU ASP PHE GLN ILE LYS LEU
SEQRES 32 A 511 HIS GLY TYR ARG MET GLU LEU GLU GLU ILE GLU PHE HIS
SEQRES 33 A 511 VAL ARG GLN SER GLN TYR VAL ARG SER ALA VAL VAL ILE
SEQRES 34 A 511 PRO TYR GLN PRO ASN GLY THR VAL GLU TYR LEU ILE ALA
SEQRES 35 A 511 ALA ILE VAL PRO GLU GLU HIS GLU PHE GLU LYS GLU PHE
SEQRES 36 A 511 GLN LEU THR SER ALA ILE LYS LYS GLU LEU ALA ALA SER
SEQRES 37 A 511 LEU PRO ALA TYR MET ILE PRO ARG LYS PHE ILE TYR GLN
SEQRES 38 A 511 ASP HIS ILE GLN MET THR ALA ASN GLY LYS ILE ASP ARG
SEQRES 39 A 511 LYS ARG ILE GLY GLU GLU VAL LEU VAL ARG SER HIS HIS
SEQRES 40 A 511 HIS HIS HIS HIS
HET AMP A 512 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 2 AMP C10 H14 N5 O7 P
FORMUL 3 HOH *211(H2 O)
HELIX 1 1 LYS A 2 TYR A 14 1 13
HELIX 2 2 TYR A 29 GLN A 44 1 16
HELIX 3 3 GLU A 62 ALA A 75 1 14
HELIX 4 4 PRO A 87 GLY A 99 1 13
HELIX 5 5 ALA A 123 LEU A 127 1 5
HELIX 6 6 ALA A 165 PHE A 179 1 15
HELIX 7 7 ASP A 196 SER A 208 1 13
HELIX 8 8 THR A 216 ASN A 221 1 6
HELIX 9 9 LYS A 222 GLY A 234 1 13
HELIX 10 10 THR A 241 LEU A 249 1 9
HELIX 11 11 PRO A 273 PHE A 284 1 12
HELIX 12 12 PRO A 295 THR A 299 5 5
HELIX 13 13 THR A 308 ARG A 314 1 7
HELIX 14 14 GLU A 361 ALA A 368 1 8
HELIX 15 15 LEU A 410 GLN A 419 1 10
HELIX 16 16 LYS A 453 LEU A 469 1 17
HELIX 17 17 PRO A 470 ILE A 474 5 5
HELIX 18 18 THR A 487 LYS A 491 5 5
HELIX 19 19 ASP A 493 SER A 505 1 13
SHEET 1 A 4 GLN A 25 THR A 28 0
SHEET 2 A 4 ASP A 18 SER A 22 -1 N ALA A 19 O LEU A 27
SHEET 3 A 4 THR A 211 CYS A 214 1 O LEU A 212 N ARG A 21
SHEET 4 A 4 ILE A 186 ASN A 189 1 N PHE A 187 O HIS A 213
SHEET 1 B 4 TYR A 79 ASP A 83 0
SHEET 2 B 4 ILE A 55 GLY A 59 1 N VAL A 57 O VAL A 82
SHEET 3 B 4 LEU A 102 HIS A 105 1 O ILE A 104 N TYR A 58
SHEET 4 B 4 THR A 120 SER A 122 1 O VAL A 121 N HIS A 105
SHEET 1 C 2 THR A 145 THR A 151 0
SHEET 2 C 2 LYS A 159 SER A 164 -1 O ILE A 163 N PHE A 146
SHEET 1 D 5 VAL A 237 SER A 240 0
SHEET 2 D 5 THR A 264 PHE A 267 1 O MET A 266 N TRP A 238
SHEET 3 D 5 LYS A 288 ASN A 291 1 O LYS A 288 N PHE A 265
SHEET 4 D 5 THR A 303 ILE A 307 -1 O VAL A 305 N ASN A 291
SHEET 5 D 5 PHE A 322 ALA A 323 -1 O PHE A 322 N SER A 304
SHEET 1 E 4 ASN A 328 MET A 332 0
SHEET 2 E 4 GLY A 345 ALA A 350 -1 O ALA A 350 N ASN A 328
SHEET 3 E 4 GLN A 375 GLN A 387 -1 O GLY A 384 N GLY A 345
SHEET 4 E 4 PHE A 369 HIS A 372 -1 N PHE A 370 O ALA A 377
SHEET 1 F 4 ASN A 328 MET A 332 0
SHEET 2 F 4 GLY A 345 ALA A 350 -1 O ALA A 350 N ASN A 328
SHEET 3 F 4 GLN A 375 GLN A 387 -1 O GLY A 384 N GLY A 345
SHEET 4 F 4 GLN A 390 ARG A 396 -1 O GLY A 395 N ALA A 383
SHEET 1 G 2 GLN A 400 LEU A 403 0
SHEET 2 G 2 TYR A 406 GLU A 409 -1 O MET A 408 N ILE A 401
SHEET 1 H 3 VAL A 423 TYR A 431 0
SHEET 2 H 3 TYR A 439 PRO A 446 -1 O ILE A 441 N ILE A 429
SHEET 3 H 3 LYS A 477 TYR A 480 1 O LYS A 477 N ALA A 442
SITE 1 AC1 16 GLY A 269 GLU A 270 ASN A 291 THR A 292
SITE 2 AC1 16 TYR A 293 GLY A 294 PRO A 295 THR A 296
SITE 3 AC1 16 ASP A 382 ARG A 396 LYS A 402 ARG A 407
SITE 4 AC1 16 HOH A 515 HOH A 529 HOH A 658 HOH A 718
CRYST1 45.765 91.389 121.471 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 0.021851 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008232 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
