HEADER TRANSFERASE/TRANSCRIPTION 28-MAR-14 4PZ8
TITLE PCE1 GUANYLYLTRANSFERASE BOUND TO SPT5 CTD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MRNA-CAPPING ENZYME SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GTP--RNA GUANYLYLTRANSFERASE, GTASE, MRNA
COMPND 5 GUANYLYLTRANSFERASE;
COMPND 6 EC: 2.7.7.50;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TRANSCRIPTION ELONGATION FACTOR SPT5;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: SPT5 C-TERMINAL DOMAIN PEPTIDE;
COMPND 12 SYNONYM: CHROMATIN ELONGATION FACTOR SPT5;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 284812;
SOURCE 5 STRAIN: 972 / ATCC 24843;
SOURCE 6 GENE: CEG1, CEG1/PCE1, PCE1, SPBC2F12.08C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CP-RIL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PSMT3 (SUMO);
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 15 ORGANISM_COMMON: FISSION YEAST;
SOURCE 16 ORGANISM_TAXID: 284812
KEYWDS NUCLEOTIDYL TRANSFERASE, RNA CAPPING ENZYME, RNA POLYMERASE II, SPT5,
KEYWDS 2 GUANYLATION, NUCLEAR, TRANSFERASE-TRANSCRIPTION COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.DOAMEKPOR,C.D.LIMA
REVDAT 4 20-SEP-23 4PZ8 1 REMARK SEQADV LINK
REVDAT 3 24-SEP-14 4PZ8 1 JRNL
REVDAT 2 02-JUL-14 4PZ8 1 AUTHOR
REVDAT 1 25-JUN-14 4PZ8 0
JRNL AUTH S.K.DOAMEKPOR,A.M.SANCHEZ,B.SCHWER,S.SHUMAN,C.D.LIMA
JRNL TITL HOW AN MRNA CAPPING ENZYME READS DISTINCT RNA POLYMERASE II
JRNL TITL 2 AND SPT5 CTD PHOSPHORYLATION CODES.
JRNL REF GENES DEV. V. 28 1323 2014
JRNL REFN ISSN 0890-9369
JRNL PMID 24939935
JRNL DOI 10.1101/GAD.242768.114
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.530
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 11036
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 529
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 38.4612 - 4.9185 0.97 2783 164 0.1840 0.2103
REMARK 3 2 4.9185 - 3.9052 0.96 2626 137 0.1532 0.2256
REMARK 3 3 3.9052 - 3.4119 0.93 2589 114 0.2130 0.2710
REMARK 3 4 3.4119 - 3.1000 0.91 2509 114 0.2920 0.3852
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) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.90
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 : 0.002 3210
REMARK 3 ANGLE : 0.610 4339
REMARK 3 CHIRALITY : 0.048 453
REMARK 3 PLANARITY : 0.003 543
REMARK 3 DIHEDRAL : 11.539 1212
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 4PZ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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-E
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 : SI(220) SIDE BOUNCE
REMARK 200 OPTICS : NULL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11169
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.15100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.33400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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 ENTRY 4PZ6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.35 M LITHIUM SULFATE, 0.5 M AMMONIUM
REMARK 280 SULFATE, 0.1 M SODIUM CITRATE, PH 6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.25600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 80.14050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.25600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.14050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.25600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 80.14050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.25600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 80.14050
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 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 SER A 0
REMARK 465 MET A 1
REMARK 465 LYS A 6
REMARK 465 ASP A 7
REMARK 465 ILE A 8
REMARK 465 GLU A 9
REMARK 465 SER A 374
REMARK 465 VAL A 375
REMARK 465 THR A 376
REMARK 465 LYS A 377
REMARK 465 ARG A 378
REMARK 465 LYS A 379
REMARK 465 LEU A 380
REMARK 465 ASP A 381
REMARK 465 GLU A 382
REMARK 465 THR A 383
REMARK 465 SER A 384
REMARK 465 ASN A 385
REMARK 465 ASP A 386
REMARK 465 ASP A 387
REMARK 465 ALA A 388
REMARK 465 PRO A 389
REMARK 465 ALA A 390
REMARK 465 ILE A 391
REMARK 465 LYS A 392
REMARK 465 LYS A 393
REMARK 465 VAL A 394
REMARK 465 ALA A 395
REMARK 465 LYS A 396
REMARK 465 GLU A 397
REMARK 465 SER A 398
REMARK 465 GLU A 399
REMARK 465 LYS A 400
REMARK 465 GLU A 401
REMARK 465 ILE A 402
REMARK 465 THR B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 ARG B 9
REMARK 465 THR B 10
REMARK 465 PRO B 11
REMARK 465 ALA B 12
REMARK 465 TRP B 13
REMARK 465 ASN B 14
REMARK 465 SER B 15
REMARK 465 GLY B 16
REMARK 465 SER B 17
REMARK 465 LYS B 18
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 SER A 4 -151.68 -153.54
REMARK 500 SER A 50 -169.19 -106.31
REMARK 500 ARG A 82 -77.10 -76.59
REMARK 500 ILE A 170 -57.48 -123.43
REMARK 500 GLU A 209 -54.33 -133.92
REMARK 500 GLU A 279 -74.26 -100.98
REMARK 500 LEU A 325 -61.93 -121.08
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 SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 511
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PZ6 RELATED DB: PDB
REMARK 900 RELATED ID: 4PZ7 RELATED DB: PDB
DBREF 4PZ8 A 1 402 UNP P40997 MCE1_SCHPO 1 402
DBREF 4PZ8 B 1 18 PDB 4PZ8 4PZ8 1 18
SEQADV 4PZ8 SER A 0 UNP P40997 EXPRESSION TAG
SEQRES 1 A 403 SER MET ALA PRO SER GLU LYS ASP ILE GLU GLU VAL SER
SEQRES 2 A 403 VAL PRO GLY VAL LEU ALA PRO ARG ASP ASP VAL ARG VAL
SEQRES 3 A 403 LEU LYS THR ARG ILE ALA LYS LEU LEU GLY THR SER PRO
SEQRES 4 A 403 ASP THR PHE PRO GLY SER GLN PRO VAL SER PHE SER LYS
SEQRES 5 A 403 LYS HIS LEU GLN ALA LEU LYS GLU LYS ASN TYR PHE VAL
SEQRES 6 A 403 CYS GLU GPL SER ASP GLY ILE ARG CYS LEU LEU TYR MET
SEQRES 7 A 403 THR GLU HIS PRO ARG TYR GLU ASN ARG PRO SER VAL TYR
SEQRES 8 A 403 LEU PHE ASP ARG LYS MET ASN PHE TYR HIS VAL GLU LYS
SEQRES 9 A 403 ILE PHE TYR PRO VAL GLU ASN ASP LYS SER GLY LYS LYS
SEQRES 10 A 403 TYR HIS VAL ASP THR LEU LEU ASP GLY GLU LEU VAL LEU
SEQRES 11 A 403 ASP ILE TYR PRO GLY GLY LYS LYS GLN LEU ARG TYR LEU
SEQRES 12 A 403 VAL PHE ASP CYS LEU ALA CYS ASP GLY ILE VAL TYR MET
SEQRES 13 A 403 SER ARG LEU LEU ASP LYS ARG LEU GLY ILE PHE ALA LYS
SEQRES 14 A 403 SER ILE GLN LYS PRO LEU ASP GLU TYR THR LYS THR HIS
SEQRES 15 A 403 MET ARG GLU THR ALA ILE PHE PRO PHE LEU THR SER LEU
SEQRES 16 A 403 LYS LYS MET GLU LEU GLY HIS GLY ILE LEU LYS LEU PHE
SEQRES 17 A 403 ASN GLU VAL ILE PRO ARG LEU ARG HIS GLY ASN ASP GLY
SEQRES 18 A 403 LEU ILE PHE THR CYS THR GLU THR PRO TYR VAL SER GLY
SEQRES 19 A 403 THR ASP GLN SER LEU LEU LYS TRP LYS PRO LYS GLU MET
SEQRES 20 A 403 ASN THR ILE ASP PHE MET LEU LYS LEU GLU PHE ALA GLN
SEQRES 21 A 403 PRO GLU GLU GLY ASP ILE ASP TYR SER ALA MET PRO GLU
SEQRES 22 A 403 PHE GLN LEU GLY VAL TRP GLU GLY ARG ASN MET TYR SER
SEQRES 23 A 403 PHE PHE ALA PHE MET TYR VAL ASP GLU LYS GLU TRP GLU
SEQRES 24 A 403 LYS LEU LYS SER PHE ASN VAL PRO LEU SER GLU ARG ILE
SEQRES 25 A 403 VAL GLU CYS TYR LEU ASP ASP GLU ASN ARG TRP ARG PHE
SEQRES 26 A 403 LEU ARG PHE ARG ASP ASP LYS ARG ASP ALA ASN HIS ILE
SEQRES 27 A 403 SER THR VAL LYS SER VAL LEU GLN SER ILE GLU ASP GLY
SEQRES 28 A 403 VAL SER LYS GLU ASP LEU LEU LYS GLU MET PRO ILE ILE
SEQRES 29 A 403 ARG GLU ALA TYR TYR ASN ARG LYS LYS PRO SER VAL THR
SEQRES 30 A 403 LYS ARG LYS LEU ASP GLU THR SER ASN ASP ASP ALA PRO
SEQRES 31 A 403 ALA ILE LYS LYS VAL ALA LYS GLU SER GLU LYS GLU ILE
SEQRES 1 B 18 THR PRO ALA TRP ASN SER GLY SER ARG THR PRO ALA TRP
SEQRES 2 B 18 ASN SER GLY SER LYS
MODRES 4PZ8 GPL A 67 LYS LYSINE GUANOSINE-5'-MONOPHOSPHATE
HET GPL A 67 32
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET SO4 A 508 5
HET SO4 A 509 5
HET SO4 A 510 5
HET SO4 A 511 5
HETNAM GPL LYSINE GUANOSINE-5'-MONOPHOSPHATE
HETNAM SO4 SULFATE ION
FORMUL 1 GPL C16 H26 N7 O9 P
FORMUL 3 SO4 11(O4 S 2-)
FORMUL 14 HOH *59(H2 O)
HELIX 1 1 PRO A 19 GLY A 35 1 17
HELIX 2 2 LYS A 51 LYS A 60 1 10
HELIX 3 3 MET A 155 ARG A 157 5 3
HELIX 4 4 LEU A 158 ILE A 170 1 13
HELIX 5 5 ILE A 170 HIS A 181 1 12
HELIX 6 6 HIS A 181 ALA A 186 1 6
HELIX 7 7 GLY A 202 GLU A 209 1 8
HELIX 8 8 VAL A 210 LEU A 214 5 5
HELIX 9 9 PRO A 243 MET A 246 5 4
HELIX 10 10 ASP A 293 LYS A 301 1 9
HELIX 11 11 HIS A 336 ASP A 349 1 14
HELIX 12 12 SER A 352 LYS A 358 1 7
HELIX 13 13 GLU A 359 ARG A 370 1 12
SHEET 1 A 7 VAL A 16 LEU A 17 0
SHEET 2 A 7 PHE A 98 VAL A 101 -1 O HIS A 100 N VAL A 16
SHEET 3 A 7 PRO A 87 PHE A 92 -1 N VAL A 89 O VAL A 101
SHEET 4 A 7 ILE A 71 GLU A 79 -1 N THR A 78 O SER A 88
SHEET 5 A 7 THR A 121 ILE A 131 -1 O LEU A 127 N ILE A 71
SHEET 6 A 7 LYS A 137 CYS A 149 -1 O ARG A 140 N VAL A 128
SHEET 7 A 7 ILE A 152 VAL A 153 -1 O ILE A 152 N CYS A 149
SHEET 1 B 7 VAL A 16 LEU A 17 0
SHEET 2 B 7 PHE A 98 VAL A 101 -1 O HIS A 100 N VAL A 16
SHEET 3 B 7 PRO A 87 PHE A 92 -1 N VAL A 89 O VAL A 101
SHEET 4 B 7 ILE A 71 GLU A 79 -1 N THR A 78 O SER A 88
SHEET 5 B 7 THR A 121 ILE A 131 -1 O LEU A 127 N ILE A 71
SHEET 6 B 7 LYS A 137 CYS A 149 -1 O ARG A 140 N VAL A 128
SHEET 7 B 7 LEU A 191 LEU A 194 1 O SER A 193 N TYR A 141
SHEET 1 C 5 SER A 44 SER A 48 0
SHEET 2 C 5 GLY A 233 TRP A 241 1 O ASP A 235 N GLN A 45
SHEET 3 C 5 ASN A 218 CYS A 225 -1 N PHE A 223 O LEU A 239
SHEET 4 C 5 TYR A 62 SER A 68 -1 N PHE A 63 O THR A 224
SHEET 5 C 5 GLU A 198 LEU A 199 -1 O GLU A 198 N VAL A 64
SHEET 1 D 5 TYR A 284 PHE A 289 0
SHEET 2 D 5 GLU A 272 TRP A 278 -1 N LEU A 275 O ALA A 288
SHEET 3 D 5 THR A 248 GLU A 256 -1 N GLU A 256 O GLU A 272
SHEET 4 D 5 ARG A 310 LEU A 316 -1 O CYS A 314 N ILE A 249
SHEET 5 D 5 TRP A 322 PHE A 327 -1 O ARG A 326 N GLU A 313
LINK C GLU A 66 N GPL A 67 1555 1555 1.33
LINK C GPL A 67 N SER A 68 1555 1555 1.33
SITE 1 AC1 5 LYS A 331 ALA A 334 ASN A 335 HIS A 336
SITE 2 AC1 5 THR A 339
SITE 1 AC2 4 ARG A 82 LYS A 331 ARG A 332 ASP A 333
SITE 1 AC3 2 ARG A 29 ARG A 281
SITE 1 AC4 4 PRO A 243 LYS A 244 SER A 352 LYS A 353
SITE 1 AC5 3 ASP A 250 ARG A 328 LYS A 331
SITE 1 AC6 2 ARG A 157 LYS A 161
SITE 1 AC7 4 HIS A 80 TYR A 83 HIS A 100 ARG A 332
SITE 1 AC8 3 ARG A 157 LEU A 158 LYS A 161
SITE 1 AC9 4 TYR A 291 LYS A 295 ARG A 321 PRO A 373
SITE 1 BC1 2 HIS A 201 TYR A 368
SITE 1 BC2 2 SER A 37 THR A 40
CRYST1 87.671 88.512 160.281 90.00 90.00 90.00 I 2 2 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 0.011406 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011298 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006239 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
