HEADER LYASE/LYASE INHIBITOR 05-FEB-11 3QMR
TITLE CRYSTAL STRUCTURE OF THE MUTANT R160A,V182A OF OROTIDINE 5'-
TITLE 2 MONOPHOSPHATE DECARBOXYLASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
TITLE 3 COMPLEXED WITH THE INHIBITOR BMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OROTIDINE 5'-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OMP DECARBOXYLASE, OMPDCASE, OMPDECASE;
COMPND 5 EC: 4.1.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS STR.
SOURCE 3 DELTA H;
SOURCE 4 ORGANISM_TAXID: 187420;
SOURCE 5 GENE: PYRF, MTH_129;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TIM BARREL FOLD, 5'-MONOPHOSPHATE DECARBOXYLASE, INHIBITOR BMP,
KEYWDS 2 LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,B.DESAI,J.A.GERLT,S.C.ALMO
REVDAT 3 13-SEP-23 3QMR 1 REMARK SEQADV
REVDAT 2 19-JUN-13 3QMR 1 JRNL
REVDAT 1 08-FEB-12 3QMR 0
JRNL AUTH B.J.DESAI,B.M.WOOD,A.A.FEDOROV,E.V.FEDOROV,B.GORYANOVA,
JRNL AUTH 2 T.L.AMYES,J.P.RICHARD,S.C.ALMO,J.A.GERLT
JRNL TITL CONFORMATIONAL CHANGES IN OROTIDINE 5'-MONOPHOSPHATE
JRNL TITL 2 DECARBOXYLASE: A STRUCTURE-BASED EXPLANATION FOR HOW THE
JRNL TITL 3 5'-PHOSPHATE GROUP ACTIVATES THE ENZYME.
JRNL REF BIOCHEMISTRY V. 51 8665 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 23030629
JRNL DOI 10.1021/BI301188K
REMARK 2
REMARK 2 RESOLUTION. 1.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 95690
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4797
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 42.0368 - 4.1044 0.99 3203 160 0.2091 0.2107
REMARK 3 2 4.1044 - 3.2582 1.00 3124 182 0.2016 0.2031
REMARK 3 3 3.2582 - 2.8464 1.00 3143 160 0.2516 0.2624
REMARK 3 4 2.8464 - 2.5862 1.00 3131 159 0.2505 0.2331
REMARK 3 5 2.5862 - 2.4009 1.00 3097 173 0.2403 0.2760
REMARK 3 6 2.4009 - 2.2593 1.00 3146 180 0.2242 0.2453
REMARK 3 7 2.2593 - 2.1462 1.00 3088 169 0.2128 0.2324
REMARK 3 8 2.1462 - 2.0528 1.00 3111 156 0.2200 0.2412
REMARK 3 9 2.0528 - 1.9738 1.00 3137 146 0.2096 0.2242
REMARK 3 10 1.9738 - 1.9056 1.00 3082 178 0.2050 0.2329
REMARK 3 11 1.9056 - 1.8461 1.00 3106 182 0.1997 0.2424
REMARK 3 12 1.8461 - 1.7933 1.00 3113 155 0.2051 0.2284
REMARK 3 13 1.7933 - 1.7461 1.00 3087 160 0.2170 0.2538
REMARK 3 14 1.7461 - 1.7035 1.00 3106 164 0.2247 0.2696
REMARK 3 15 1.7035 - 1.6647 1.00 3094 151 0.2279 0.2551
REMARK 3 16 1.6647 - 1.6293 1.00 3112 176 0.2324 0.2567
REMARK 3 17 1.6293 - 1.5967 1.00 3110 154 0.2362 0.2737
REMARK 3 18 1.5967 - 1.5666 1.00 3080 180 0.2434 0.2853
REMARK 3 19 1.5666 - 1.5386 1.00 3098 172 0.2511 0.2822
REMARK 3 20 1.5386 - 1.5125 1.00 3106 148 0.2573 0.2751
REMARK 3 21 1.5125 - 1.4881 1.00 3100 158 0.2445 0.2794
REMARK 3 22 1.4881 - 1.4652 1.00 3091 154 0.2534 0.2801
REMARK 3 23 1.4652 - 1.4437 1.00 3136 148 0.2505 0.2668
REMARK 3 24 1.4437 - 1.4234 1.00 3055 172 0.2863 0.3223
REMARK 3 25 1.4234 - 1.4041 0.99 3062 179 0.3191 0.3364
REMARK 3 26 1.4041 - 1.3859 0.97 3027 143 0.3284 0.3377
REMARK 3 27 1.3859 - 1.3686 0.93 2855 154 0.3377 0.3469
REMARK 3 28 1.3686 - 1.3521 0.89 2785 147 0.3506 0.3880
REMARK 3 29 1.3521 - 1.3363 0.84 2615 129 0.3678 0.3747
REMARK 3 30 1.3363 - 1.3213 0.62 1893 108 0.3944 0.4147
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 39.87
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.770
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) : -1.02070
REMARK 3 B22 (A**2) : 2.43080
REMARK 3 B33 (A**2) : -1.41010
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.26370
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 3423
REMARK 3 ANGLE : 1.032 4634
REMARK 3 CHIRALITY : 0.072 529
REMARK 3 PLANARITY : 0.007 610
REMARK 3 DIHEDRAL : 11.755 1333
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 3QMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063840.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95690
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.321
REMARK 200 RESOLUTION RANGE LOW (A) : 42.016
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 3LTP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1M TRIS, 0.2M LITHIUM
REMARK 280 SULFATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.03500
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 SER A 3
REMARK 465 ARG A 4
REMARK 465 ARG A 5
REMARK 465 VAL A 6
REMARK 465 ASP A 7
REMARK 465 ASN A 227
REMARK 465 PRO A 228
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 SER B 3
REMARK 465 ARG B 4
REMARK 465 ARG B 5
REMARK 465 VAL B 6
REMARK 465 ASP B 7
REMARK 465 VAL B 8
REMARK 465 ASN B 227
REMARK 465 PRO B 228
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 72 54.14 37.75
REMARK 500 ALA A 74 43.67 -150.20
REMARK 500 PHE A 134 -41.27 -132.16
REMARK 500 ASN B 13 18.33 57.18
REMARK 500 LYS B 72 53.54 37.73
REMARK 500 ALA B 74 42.80 -150.52
REMARK 500 PHE B 134 -37.98 -130.37
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 BMP A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMP B 229
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LTP RELATED DB: PDB
REMARK 900 THE WILDTYPE PROTEIN COMPLEXED WITH THE SAME INHIBITOR
DBREF 3QMR A 1 228 UNP O26232 PYRF_METTH 1 228
DBREF 3QMR B 1 228 UNP O26232 PYRF_METTH 1 228
SEQADV 3QMR PRO A 101 UNP O26232 ARG 101 CONFLICT
SEQADV 3QMR ALA A 160 UNP O26232 ARG 160 ENGINEERED MUTATION
SEQADV 3QMR ALA A 182 UNP O26232 VAL 182 ENGINEERED MUTATION
SEQADV 3QMR PRO B 101 UNP O26232 ARG 101 CONFLICT
SEQADV 3QMR ALA B 160 UNP O26232 ARG 160 ENGINEERED MUTATION
SEQADV 3QMR ALA B 182 UNP O26232 VAL 182 ENGINEERED MUTATION
SEQRES 1 A 228 MET ARG SER ARG ARG VAL ASP VAL MET ASP VAL MET ASN
SEQRES 2 A 228 ARG LEU ILE LEU ALA MET ASP LEU MET ASN ARG ASP ASP
SEQRES 3 A 228 ALA LEU ARG VAL THR GLY GLU VAL ARG GLU TYR ILE ASP
SEQRES 4 A 228 THR VAL LYS ILE GLY TYR PRO LEU VAL LEU SER GLU GLY
SEQRES 5 A 228 MET ASP ILE ILE ALA GLU PHE ARG LYS ARG PHE GLY CYS
SEQRES 6 A 228 ARG ILE ILE ALA ASP PHE LYS VAL ALA ASP ILE PRO GLU
SEQRES 7 A 228 THR ASN GLU LYS ILE CYS ARG ALA THR PHE LYS ALA GLY
SEQRES 8 A 228 ALA ASP ALA ILE ILE VAL HIS GLY PHE PRO GLY ALA ASP
SEQRES 9 A 228 SER VAL ARG ALA CYS LEU ASN VAL ALA GLU GLU MET GLY
SEQRES 10 A 228 ARG GLU VAL PHE LEU LEU THR GLU MET SER HIS PRO GLY
SEQRES 11 A 228 ALA GLU MET PHE ILE GLN GLY ALA ALA ASP GLU ILE ALA
SEQRES 12 A 228 ARG MET GLY VAL ASP LEU GLY VAL LYS ASN TYR VAL GLY
SEQRES 13 A 228 PRO SER THR ALA PRO GLU ARG LEU SER ARG LEU ARG GLU
SEQRES 14 A 228 ILE ILE GLY GLN ASP SER PHE LEU ILE SER PRO GLY ALA
SEQRES 15 A 228 GLY ALA GLN GLY GLY ASP PRO GLY GLU THR LEU ARG PHE
SEQRES 16 A 228 ALA ASP ALA ILE ILE VAL GLY ARG SER ILE TYR LEU ALA
SEQRES 17 A 228 ASP ASN PRO ALA ALA ALA ALA ALA GLY ILE ILE GLU SER
SEQRES 18 A 228 ILE LYS ASP LEU LEU ASN PRO
SEQRES 1 B 228 MET ARG SER ARG ARG VAL ASP VAL MET ASP VAL MET ASN
SEQRES 2 B 228 ARG LEU ILE LEU ALA MET ASP LEU MET ASN ARG ASP ASP
SEQRES 3 B 228 ALA LEU ARG VAL THR GLY GLU VAL ARG GLU TYR ILE ASP
SEQRES 4 B 228 THR VAL LYS ILE GLY TYR PRO LEU VAL LEU SER GLU GLY
SEQRES 5 B 228 MET ASP ILE ILE ALA GLU PHE ARG LYS ARG PHE GLY CYS
SEQRES 6 B 228 ARG ILE ILE ALA ASP PHE LYS VAL ALA ASP ILE PRO GLU
SEQRES 7 B 228 THR ASN GLU LYS ILE CYS ARG ALA THR PHE LYS ALA GLY
SEQRES 8 B 228 ALA ASP ALA ILE ILE VAL HIS GLY PHE PRO GLY ALA ASP
SEQRES 9 B 228 SER VAL ARG ALA CYS LEU ASN VAL ALA GLU GLU MET GLY
SEQRES 10 B 228 ARG GLU VAL PHE LEU LEU THR GLU MET SER HIS PRO GLY
SEQRES 11 B 228 ALA GLU MET PHE ILE GLN GLY ALA ALA ASP GLU ILE ALA
SEQRES 12 B 228 ARG MET GLY VAL ASP LEU GLY VAL LYS ASN TYR VAL GLY
SEQRES 13 B 228 PRO SER THR ALA PRO GLU ARG LEU SER ARG LEU ARG GLU
SEQRES 14 B 228 ILE ILE GLY GLN ASP SER PHE LEU ILE SER PRO GLY ALA
SEQRES 15 B 228 GLY ALA GLN GLY GLY ASP PRO GLY GLU THR LEU ARG PHE
SEQRES 16 B 228 ALA ASP ALA ILE ILE VAL GLY ARG SER ILE TYR LEU ALA
SEQRES 17 B 228 ASP ASN PRO ALA ALA ALA ALA ALA GLY ILE ILE GLU SER
SEQRES 18 B 228 ILE LYS ASP LEU LEU ASN PRO
HET BMP A 229 22
HET BMP B 229 22
HETNAM BMP 6-HYDROXYURIDINE-5'-PHOSPHATE
FORMUL 3 BMP 2(C9 H13 N2 O10 P)
FORMUL 5 HOH *340(H2 O)
HELIX 1 1 VAL A 11 ASN A 13 5 3
HELIX 2 2 ASN A 23 VAL A 34 1 12
HELIX 3 3 TYR A 45 GLY A 52 1 8
HELIX 4 4 MET A 53 PHE A 63 1 11
HELIX 5 5 ILE A 76 ALA A 90 1 15
HELIX 6 6 GLY A 102 GLY A 117 1 16
HELIX 7 7 HIS A 128 MET A 133 5 6
HELIX 8 8 PHE A 134 GLY A 150 1 17
HELIX 9 9 ALA A 160 GLY A 172 1 13
HELIX 10 10 ASP A 188 LEU A 193 1 6
HELIX 11 11 GLY A 202 LEU A 207 1 6
HELIX 12 12 ASN A 210 ILE A 222 1 13
HELIX 13 13 LYS A 223 LEU A 226 5 4
HELIX 14 14 VAL B 11 ASN B 13 5 3
HELIX 15 15 ASN B 23 VAL B 34 1 12
HELIX 16 16 TYR B 45 GLY B 52 1 8
HELIX 17 17 MET B 53 GLY B 64 1 12
HELIX 18 18 ILE B 76 ALA B 90 1 15
HELIX 19 19 GLY B 102 GLY B 117 1 16
HELIX 20 20 HIS B 128 MET B 133 5 6
HELIX 21 21 PHE B 134 GLY B 150 1 17
HELIX 22 22 ALA B 160 GLY B 172 1 13
HELIX 23 23 ASP B 188 LEU B 193 1 6
HELIX 24 24 GLY B 202 LEU B 207 1 6
HELIX 25 25 ASN B 210 ILE B 222 1 13
HELIX 26 26 LYS B 223 LEU B 226 5 4
SHEET 1 A 9 LEU A 15 MET A 19 0
SHEET 2 A 9 THR A 40 GLY A 44 1 O LYS A 42 N LEU A 17
SHEET 3 A 9 ARG A 66 VAL A 73 1 O ASP A 70 N ILE A 43
SHEET 4 A 9 ALA A 94 HIS A 98 1 O ALA A 94 N ALA A 69
SHEET 5 A 9 GLU A 119 LEU A 123 1 O PHE A 121 N ILE A 95
SHEET 6 A 9 ASN A 153 VAL A 155 1 O ASN A 153 N LEU A 122
SHEET 7 A 9 PHE A 176 PRO A 180 1 O PHE A 176 N TYR A 154
SHEET 8 A 9 ALA A 198 VAL A 201 1 O ILE A 200 N SER A 179
SHEET 9 A 9 LEU A 15 MET A 19 1 N ILE A 16 O ILE A 199
SHEET 1 B 9 LEU B 15 MET B 19 0
SHEET 2 B 9 THR B 40 GLY B 44 1 O LYS B 42 N LEU B 17
SHEET 3 B 9 ARG B 66 VAL B 73 1 O ASP B 70 N ILE B 43
SHEET 4 B 9 ALA B 94 HIS B 98 1 O ALA B 94 N ALA B 69
SHEET 5 B 9 GLU B 119 LEU B 123 1 O LEU B 123 N VAL B 97
SHEET 6 B 9 ASN B 153 VAL B 155 1 O ASN B 153 N LEU B 122
SHEET 7 B 9 PHE B 176 SER B 179 1 O PHE B 176 N TYR B 154
SHEET 8 B 9 ALA B 198 VAL B 201 1 O ILE B 200 N SER B 179
SHEET 9 B 9 LEU B 15 MET B 19 1 N ILE B 16 O ILE B 199
SITE 1 AC1 20 ASP A 20 LYS A 42 ASP A 70 LYS A 72
SITE 2 AC1 20 MET A 126 SER A 127 PRO A 180 GLN A 185
SITE 3 AC1 20 GLY A 202 ARG A 203 HOH A 239 HOH A 241
SITE 4 AC1 20 HOH A 251 HOH A 259 HOH A 264 HOH A 267
SITE 5 AC1 20 HOH A 300 ASP B 75 ILE B 76 THR B 79
SITE 1 AC2 20 ASP A 75 ILE A 76 THR A 79 ASP B 20
SITE 2 AC2 20 LYS B 42 ASP B 70 LYS B 72 MET B 126
SITE 3 AC2 20 SER B 127 PRO B 180 GLN B 185 GLY B 202
SITE 4 AC2 20 ARG B 203 HOH B 230 HOH B 236 HOH B 242
SITE 5 AC2 20 HOH B 248 HOH B 256 HOH B 262 HOH B 276
CRYST1 59.772 64.070 61.639 90.00 115.46 90.00 P 1 21 1 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 0.016730 0.000000 0.007966 0.00000
SCALE2 0.000000 0.015608 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017968 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
