HEADER HYDROLASE 04-JAN-16 5HCN
TITLE GPN-LOOP GTPASE NPA3 IN COMPLEX WITH GMPPCP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GPN-LOOP GTPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 1-264 DELTA 203-211;
COMPND 5 SYNONYM: ESSENTIAL PCL1-INTERACTING ATPASE 1,GPN-LOOP GTPASE NPA3,
COMPND 6 NUCLEOLAR PRERIBOSOMAL-ASSOCIATED PROTEIN 3;
COMPND 7 EC: 3.6.5.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: NPA3, EPA1, GPN1, YJR072C, J1821;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GPN-LOOP GTPASE, CHAPERONE, ASSEMBLY, RNA POLYMERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.NIESSER,F.R.WAGNER,D.KOSTREWA,W.MUEHLBACHER,P.CRAMER
REVDAT 5 06-SEP-17 5HCN 1 REMARK
REVDAT 4 24-FEB-16 5HCN 1 JRNL
REVDAT 3 27-JAN-16 5HCN 1 REMARK
REVDAT 2 20-JAN-16 5HCN 1
REVDAT 1 13-JAN-16 5HCN 0
JRNL AUTH J.NIESSER,F.R.WAGNER,D.KOSTREWA,W.MUHLBACHER,P.CRAMER
JRNL TITL STRUCTURE OF GPN-LOOP GTPASE NPA3 AND IMPLICATIONS FOR RNA
JRNL TITL 2 POLYMERASE II ASSEMBLY.
JRNL REF MOL.CELL.BIOL. V. 36 820 2015
JRNL REFN ESSN 1098-5549
JRNL PMID 26711263
JRNL DOI 10.1128/MCB.01009-15
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 20172
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 403
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 36.7634 - 3.1727 1.00 6820 139 0.1830 0.1833
REMARK 3 2 3.1727 - 2.5184 1.00 6544 133 0.2910 0.3387
REMARK 3 3 2.5184 - 2.2001 0.99 6405 131 0.3293 0.4125
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 41.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 121.3
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 : 0.007 2104
REMARK 3 ANGLE : 1.145 2836
REMARK 3 CHIRALITY : 0.042 315
REMARK 3 PLANARITY : 0.005 350
REMARK 3 DIHEDRAL : 16.107 775
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9295 18.3738 9.9674
REMARK 3 T TENSOR
REMARK 3 T11: 1.0421 T22: 1.0051
REMARK 3 T33: 1.0193 T12: -0.0097
REMARK 3 T13: 0.0312 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.9514 L22: 2.2900
REMARK 3 L33: 0.8155 L12: -0.5717
REMARK 3 L13: 0.1690 L23: -1.3507
REMARK 3 S TENSOR
REMARK 3 S11: -0.1710 S12: -0.0600 S13: -0.2462
REMARK 3 S21: 0.0813 S22: 0.2583 S23: 0.2106
REMARK 3 S31: -0.1018 S32: -0.0862 S33: -0.0001
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 5HCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216833.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99888
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20172
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 14.11
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.12
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 1.55000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.070
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM HEPES (PH 7.5), 200 MM SODIUM
REMARK 280 CHLORIDE, 5 MM MAGNESIUM CHLORIDE, 10 MM DTT, SMALL TUBES,
REMARK 280 TEMPERATURE 281.15K
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 28.38000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.12000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 14.19000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.12000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.12000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.57000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.12000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.12000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 14.19000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.12000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.12000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.57000
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 28.38000
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: 1940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 64
REMARK 465 GLU A 65
REMARK 465 ASN A 66
REMARK 465 TYR A 67
REMARK 465 GLN A 68
REMARK 465 LEU A 69
REMARK 465 HIS A 270
REMARK 465 HIS A 271
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 PRO A 47 O2 GOL A 304 2.03
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 OH TYR A 213 OH TYR A 213 7555 2.12
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 LEU A 44 -72.82 -78.14
REMARK 500 PRO A 47 -70.11 -26.99
REMARK 500 GLN A 110 95.02 -51.61
REMARK 500 ASP A 200 49.15 -77.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 17 OG1
REMARK 620 2 GCP A 302 O2G 164.5
REMARK 620 3 GCP A 302 O2B 101.6 92.6
REMARK 620 4 HOH A 401 O 92.7 71.8 153.5
REMARK 620 5 HOH A 402 O 89.3 87.9 77.1 80.9
REMARK 620 6 HOH A 404 O 91.9 87.5 115.2 86.2 167.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GCP A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305
DBREF 5HCN A 2 264 UNP P47122 GPN1_YEAST 2 264
SEQADV 5HCN A UNP P47122 LEU 203 DELETION
SEQADV 5HCN A UNP P47122 ASN 204 DELETION
SEQADV 5HCN A UNP P47122 GLY 205 DELETION
SEQADV 5HCN A UNP P47122 ASP 206 DELETION
SEQADV 5HCN A UNP P47122 ASN 207 DELETION
SEQADV 5HCN A UNP P47122 GLY 208 DELETION
SEQADV 5HCN A UNP P47122 LEU 209 DELETION
SEQADV 5HCN A UNP P47122 GLY 210 DELETION
SEQADV 5HCN A UNP P47122 SER 211 DELETION
SEQADV 5HCN LYS A 265 UNP P47122 EXPRESSION TAG
SEQADV 5HCN HIS A 266 UNP P47122 EXPRESSION TAG
SEQADV 5HCN HIS A 267 UNP P47122 EXPRESSION TAG
SEQADV 5HCN HIS A 268 UNP P47122 EXPRESSION TAG
SEQADV 5HCN HIS A 269 UNP P47122 EXPRESSION TAG
SEQADV 5HCN HIS A 270 UNP P47122 EXPRESSION TAG
SEQADV 5HCN HIS A 271 UNP P47122 EXPRESSION TAG
SEQRES 1 A 261 SER LEU SER THR ILE ILE CYS ILE GLY MET ALA GLY SER
SEQRES 2 A 261 GLY LYS THR THR PHE MET GLN ARG LEU ASN SER HIS LEU
SEQRES 3 A 261 ARG ALA GLU LYS THR PRO PRO TYR VAL ILE ASN LEU ASP
SEQRES 4 A 261 PRO ALA VAL LEU ARG VAL PRO TYR GLY ALA ASN ILE ASP
SEQRES 5 A 261 ILE ARG ASP SER ILE LYS TYR LYS LYS VAL MET GLU ASN
SEQRES 6 A 261 TYR GLN LEU GLY PRO ASN GLY ALA ILE VAL THR SER LEU
SEQRES 7 A 261 ASN LEU PHE SER THR LYS ILE ASP GLN VAL ILE ARG LEU
SEQRES 8 A 261 VAL GLU GLN LYS LYS ASP LYS PHE GLN ASN CYS ILE ILE
SEQRES 9 A 261 ASP THR PRO GLY GLN ILE GLU CYS PHE VAL TRP SER ALA
SEQRES 10 A 261 SER GLY ALA ILE ILE THR GLU SER PHE ALA SER SER PHE
SEQRES 11 A 261 PRO THR VAL ILE ALA TYR ILE VAL ASP THR PRO ARG ASN
SEQRES 12 A 261 SER SER PRO THR THR PHE MET SER ASN MET LEU TYR ALA
SEQRES 13 A 261 CYS SER ILE LEU TYR LYS THR LYS LEU PRO MET ILE VAL
SEQRES 14 A 261 VAL PHE ASN LYS THR ASP VAL CYS LYS ALA ASP PHE ALA
SEQRES 15 A 261 LYS GLU TRP MET THR ASP PHE GLU SER PHE GLN ALA ALA
SEQRES 16 A 261 ILE LYS GLU ASP GLN ASP GLY TYR MET SER SER LEU VAL
SEQRES 17 A 261 ASN SER MET SER LEU MET LEU GLU GLU PHE TYR SER GLN
SEQRES 18 A 261 LEU ASP VAL VAL GLY VAL SER SER PHE THR GLY ASP GLY
SEQRES 19 A 261 PHE ASP GLU PHE MET GLN CYS VAL ASP LYS LYS VAL ASP
SEQRES 20 A 261 GLU TYR ASP GLN TYR TYR LYS LYS HIS HIS HIS HIS HIS
SEQRES 21 A 261 HIS
HET DAO A 301 14
HET GCP A 302 32
HET MG A 303 1
HET GOL A 304 6
HET GOL A 305 6
HETNAM DAO LAURIC ACID
HETNAM GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 DAO C12 H24 O2
FORMUL 3 GCP C11 H18 N5 O13 P3
FORMUL 4 MG MG 2+
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *5(H2 O)
HELIX 1 AA1 GLY A 15 GLU A 30 1 16
HELIX 2 AA2 ASN A 72 LYS A 85 1 14
HELIX 3 AA3 LYS A 85 LYS A 96 1 12
HELIX 4 AA4 ILE A 111 TRP A 116 1 6
HELIX 5 AA5 SER A 117 SER A 129 1 13
HELIX 6 AA6 ASP A 140 ASN A 144 5 5
HELIX 7 AA7 SER A 146 LYS A 165 1 20
HELIX 8 AA8 LYS A 174 CYS A 178 5 5
HELIX 9 AA9 ASP A 181 LYS A 198 1 18
HELIX 10 AB1 SER A 215 GLN A 231 1 17
HELIX 11 AB2 GLY A 244 TYR A 263 1 20
HELIX 12 AB3 LYS A 264 HIS A 267 5 4
SHEET 1 AA1 7 ILE A 52 ASP A 53 0
SHEET 2 AA1 7 TYR A 35 ASN A 38 1 N VAL A 36 O ILE A 52
SHEET 3 AA1 7 ASN A 102 ASP A 106 1 O ILE A 104 N TYR A 35
SHEET 4 AA1 7 SER A 4 ILE A 9 1 N CYS A 8 O ILE A 105
SHEET 5 AA1 7 THR A 133 VAL A 139 1 O ALA A 136 N ILE A 7
SHEET 6 AA1 7 MET A 168 PHE A 172 1 O VAL A 171 N VAL A 139
SHEET 7 AA1 7 LEU A 232 GLY A 236 1 O ASP A 233 N VAL A 170
LINK OG1 THR A 17 MG MG A 303 1555 1555 2.10
LINK O2G GCP A 302 MG MG A 303 1555 1555 2.08
LINK O2B GCP A 302 MG MG A 303 1555 1555 2.06
LINK MG MG A 303 O HOH A 401 1555 1555 2.05
LINK MG MG A 303 O HOH A 402 1555 1555 2.11
LINK MG MG A 303 O HOH A 404 1555 1555 2.09
CISPEP 1 TYR A 60 LYS A 61 0 6.96
SITE 1 AC1 5 ASN A 144 MET A 154 CYS A 158 TRP A 186
SITE 2 AC1 5 LEU A 232
SITE 1 AC2 18 ALA A 12 GLY A 13 SER A 14 GLY A 15
SITE 2 AC2 18 LYS A 16 THR A 17 THR A 18 GLY A 109
SITE 3 AC2 18 ASN A 173 LYS A 174 ASP A 176 SER A 238
SITE 4 AC2 18 SER A 239 PHE A 240 MG A 303 HOH A 401
SITE 5 AC2 18 HOH A 402 HOH A 404
SITE 1 AC3 5 THR A 17 GCP A 302 HOH A 401 HOH A 402
SITE 2 AC3 5 HOH A 404
SITE 1 AC4 4 GLN A 21 ARG A 45 PRO A 47 VAL A 177
SITE 1 AC5 6 LYS A 179 PHE A 182 TRP A 186 ASP A 189
SITE 2 AC5 6 SER A 216 LEU A 217
CRYST1 116.240 116.240 56.760 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 0.008603 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008603 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017618 0.00000
(ATOM LINES ARE NOT SHOWN.)
END