HEADER OXIDOREDUCTASE 03-SEP-12 4GWG
TITLE CRYSTAL STRUCTURE ANALYSIS OF 6-PHOSPHOGLUCONATE DEHYDROGENASE APO-
TITLE 2 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.44;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PGD, PGDH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 6-PHOSPHOGLYCONATE DEHYDROGENASE, DEHYDROGENASE, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HE,L.ZHOU,L.ZHANG
REVDAT 4 13-SEP-23 4GWG 1 REMARK SEQADV
REVDAT 3 24-JAN-18 4GWG 1 AUTHOR
REVDAT 2 05-DEC-12 4GWG 1 REMARK
REVDAT 1 28-NOV-12 4GWG 0
JRNL AUTH T.HITOSUGI,L.ZHOU,S.ELF,J.FAN,H.B.KANG,J.H.SEO,C.SHAN,Q.DAI,
JRNL AUTH 2 L.ZHANG,J.XIE,T.L.GU,P.JIN,M.ALECKOVIC,G.LEROY,Y.KANG,
JRNL AUTH 3 J.A.SUDDERTH,R.J.DEBERARDINIS,C.H.LUAN,G.Z.CHEN,S.MULLER,
JRNL AUTH 4 D.M.SHIN,T.K.OWONIKOKO,S.LONIAL,M.L.ARELLANO,H.J.KHOURY,
JRNL AUTH 5 F.R.KHURI,B.H.LEE,K.YE,T.J.BOGGON,S.KANG,C.HE,J.CHEN
JRNL TITL PHOSPHOGLYCERATE MUTASE 1 COORDINATES GLYCOLYSIS AND
JRNL TITL 2 BIOSYNTHESIS TO PROMOTE TUMOR GROWTH.
JRNL REF CANCER CELL V. 22 585 2012
JRNL REFN ISSN 1535-6108
JRNL PMID 23153533
JRNL DOI 10.1016/J.CCR.2012.09.020
REMARK 2
REMARK 2 RESOLUTION. 1.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.230
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 188164
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 9421
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 29.0969 - 4.3167 1.00 6146 319 0.1635 0.1725
REMARK 3 2 4.3167 - 3.4280 0.74 4525 249 0.1469 0.1625
REMARK 3 3 3.4280 - 2.9952 1.00 6132 334 0.1566 0.1769
REMARK 3 4 2.9952 - 2.7216 1.00 6123 354 0.1662 0.1709
REMARK 3 5 2.7216 - 2.5266 1.00 6123 347 0.1667 0.1569
REMARK 3 6 2.5266 - 2.3777 1.00 6155 291 0.1650 0.1853
REMARK 3 7 2.3777 - 2.2587 0.80 4922 271 0.1630 0.1936
REMARK 3 8 2.2587 - 2.1604 0.77 4667 265 0.1731 0.1694
REMARK 3 9 2.1604 - 2.0773 1.00 6116 315 0.1557 0.1842
REMARK 3 10 2.0773 - 2.0056 1.00 6199 323 0.1553 0.1925
REMARK 3 11 2.0056 - 1.9429 1.00 6136 302 0.1586 0.1764
REMARK 3 12 1.9429 - 1.8874 0.81 5013 251 0.1906 0.2456
REMARK 3 13 1.8874 - 1.8377 1.00 6163 298 0.1529 0.1864
REMARK 3 14 1.8377 - 1.7929 1.00 6123 358 0.1602 0.1793
REMARK 3 15 1.7929 - 1.7521 1.00 6164 311 0.1609 0.1790
REMARK 3 16 1.7521 - 1.7148 1.00 6097 336 0.1616 0.1732
REMARK 3 17 1.7148 - 1.6805 1.00 6189 304 0.1577 0.2050
REMARK 3 18 1.6805 - 1.6488 1.00 6141 330 0.1572 0.1961
REMARK 3 19 1.6488 - 1.6194 1.00 6156 310 0.1634 0.1720
REMARK 3 20 1.6194 - 1.5919 1.00 6155 321 0.1620 0.1959
REMARK 3 21 1.5919 - 1.5663 1.00 6186 292 0.1674 0.1821
REMARK 3 22 1.5663 - 1.5422 1.00 6108 341 0.1768 0.2047
REMARK 3 23 1.5422 - 1.5195 1.00 6148 341 0.1784 0.1856
REMARK 3 24 1.5195 - 1.4981 1.00 6103 352 0.1777 0.1983
REMARK 3 25 1.4981 - 1.4778 1.00 6157 295 0.1852 0.2219
REMARK 3 26 1.4778 - 1.4586 1.00 6144 338 0.1910 0.2021
REMARK 3 27 1.4586 - 1.4404 1.00 6146 339 0.2027 0.2131
REMARK 3 28 1.4404 - 1.4231 1.00 6192 289 0.2030 0.2152
REMARK 3 29 1.4231 - 1.4065 1.00 6114 326 0.2155 0.2372
REMARK 3 30 1.4065 - 1.3907 0.98 6000 319 0.2210 0.2361
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 : 0.35
REMARK 3 B_SOL : 39.55
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.760
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) : -0.77440
REMARK 3 B22 (A**2) : -0.77440
REMARK 3 B33 (A**2) : 1.54870
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 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 : 0.005 3808
REMARK 3 ANGLE : 1.020 5152
REMARK 3 CHIRALITY : 0.071 557
REMARK 3 PLANARITY : 0.004 663
REMARK 3 DIHEDRAL : 12.584 1432
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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4GWG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 180
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) : 0.97857
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99063
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.391
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
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: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 3FWN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG3350, PH 6.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 65.44600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.64000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.64000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 98.16900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.64000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.64000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.72300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.64000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.64000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 98.16900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.64000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.64000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.72300
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 65.44600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1170 LIES ON A SPECIAL POSITION.
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 -1
REMARK 465 ASN A 0
REMARK 465 GLN A 307
REMARK 465 LYS A 308
REMARK 465 GLY A 470
REMARK 465 HIS A 471
REMARK 465 GLY A 472
REMARK 465 GLY A 473
REMARK 465 THR A 474
REMARK 465 VAL A 475
REMARK 465 SER A 476
REMARK 465 SER A 477
REMARK 465 SER A 478
REMARK 465 SER A 479
REMARK 465 TYR A 480
REMARK 465 ASN A 481
REMARK 465 ALA A 482
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 44 -94.69 -122.20
REMARK 500 CYS A 170 119.65 -170.96
REMARK 500 GLU A 176 -123.96 56.35
REMARK 500 THR A 225 -142.44 -115.92
REMARK 500 ASP A 228 111.86 -37.34
REMARK 500 ARG A 362 -152.59 -90.24
REMARK 500 THR A 453 156.42 77.52
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 MES A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JKV RELATED DB: PDB
REMARK 900 SAME PROTEIN WITHOUT COFACTOR
REMARK 900 RELATED ID: 4GWK RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH 3-PHOSPHOGLYCERATE SOAKING IN
DBREF 4GWG A 1 482 UNP P52209 6PGD_HUMAN 2 483
SEQADV 4GWG SER A -1 UNP P52209 EXPRESSION TAG
SEQADV 4GWG ASN A 0 UNP P52209 EXPRESSION TAG
SEQRES 1 A 484 SER ASN ALA GLN ALA ASP ILE ALA LEU ILE GLY LEU ALA
SEQRES 2 A 484 VAL MET GLY GLN ASN LEU ILE LEU ASN MET ASN ASP HIS
SEQRES 3 A 484 GLY PHE VAL VAL CYS ALA PHE ASN ARG THR VAL SER LYS
SEQRES 4 A 484 VAL ASP ASP PHE LEU ALA ASN GLU ALA LYS GLY THR LYS
SEQRES 5 A 484 VAL VAL GLY ALA GLN SER LEU LYS GLU MET VAL SER LYS
SEQRES 6 A 484 LEU LYS LYS PRO ARG ARG ILE ILE LEU LEU VAL LYS ALA
SEQRES 7 A 484 GLY GLN ALA VAL ASP ASP PHE ILE GLU LYS LEU VAL PRO
SEQRES 8 A 484 LEU LEU ASP THR GLY ASP ILE ILE ILE ASP GLY GLY ASN
SEQRES 9 A 484 SER GLU TYR ARG ASP THR THR ARG ARG CYS ARG ASP LEU
SEQRES 10 A 484 LYS ALA LYS GLY ILE LEU PHE VAL GLY SER GLY VAL SER
SEQRES 11 A 484 GLY GLY GLU GLU GLY ALA ARG TYR GLY PRO SER LEU MET
SEQRES 12 A 484 PRO GLY GLY ASN LYS GLU ALA TRP PRO HIS ILE LYS THR
SEQRES 13 A 484 ILE PHE GLN GLY ILE ALA ALA LYS VAL GLY THR GLY GLU
SEQRES 14 A 484 PRO CYS CYS ASP TRP VAL GLY ASP GLU GLY ALA GLY HIS
SEQRES 15 A 484 PHE VAL LYS MET VAL HIS ASN GLY ILE GLU TYR GLY ASP
SEQRES 16 A 484 MET GLN LEU ILE CYS GLU ALA TYR HIS LEU MET LYS ASP
SEQRES 17 A 484 VAL LEU GLY MET ALA GLN ASP GLU MET ALA GLN ALA PHE
SEQRES 18 A 484 GLU ASP TRP ASN LYS THR GLU LEU ASP SER PHE LEU ILE
SEQRES 19 A 484 GLU ILE THR ALA ASN ILE LEU LYS PHE GLN ASP THR ASP
SEQRES 20 A 484 GLY LYS HIS LEU LEU PRO LYS ILE ARG ASP SER ALA GLY
SEQRES 21 A 484 GLN LYS GLY THR GLY LYS TRP THR ALA ILE SER ALA LEU
SEQRES 22 A 484 GLU TYR GLY VAL PRO VAL THR LEU ILE GLY GLU ALA VAL
SEQRES 23 A 484 PHE ALA ARG CYS LEU SER SER LEU LYS ASP GLU ARG ILE
SEQRES 24 A 484 GLN ALA SER LYS LYS LEU LYS GLY PRO GLN LYS PHE GLN
SEQRES 25 A 484 PHE ASP GLY ASP LYS LYS SER PHE LEU GLU ASP ILE ARG
SEQRES 26 A 484 LYS ALA LEU TYR ALA SER LYS ILE ILE SER TYR ALA GLN
SEQRES 27 A 484 GLY PHE MET LEU LEU ARG GLN ALA ALA THR GLU PHE GLY
SEQRES 28 A 484 TRP THR LEU ASN TYR GLY GLY ILE ALA LEU MET TRP ARG
SEQRES 29 A 484 GLY GLY CYS ILE ILE ARG SER VAL PHE LEU GLY LYS ILE
SEQRES 30 A 484 LYS ASP ALA PHE ASP ARG ASN PRO GLU LEU GLN ASN LEU
SEQRES 31 A 484 LEU LEU ASP ASP PHE PHE LYS SER ALA VAL GLU ASN CYS
SEQRES 32 A 484 GLN ASP SER TRP ARG ARG ALA VAL SER THR GLY VAL GLN
SEQRES 33 A 484 ALA GLY ILE PRO MET PRO CYS PHE THR THR ALA LEU SER
SEQRES 34 A 484 PHE TYR ASP GLY TYR ARG HIS GLU MET LEU PRO ALA SER
SEQRES 35 A 484 LEU ILE GLN ALA GLN ARG ASP TYR PHE GLY ALA HIS THR
SEQRES 36 A 484 TYR GLU LEU LEU ALA LYS PRO GLY GLN PHE ILE HIS THR
SEQRES 37 A 484 ASN TRP THR GLY HIS GLY GLY THR VAL SER SER SER SER
SEQRES 38 A 484 TYR ASN ALA
HET MES A 501 12
HET MES A 502 12
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 2 MES 2(C6 H13 N O4 S)
FORMUL 4 HOH *580(H2 O)
HELIX 1 1 ALA A 11 HIS A 24 1 14
HELIX 2 2 VAL A 35 ASN A 44 1 10
HELIX 3 3 SER A 56 LYS A 63 1 8
HELIX 4 4 GLY A 77 VAL A 88 1 12
HELIX 5 5 PRO A 89 LEU A 91 5 3
HELIX 6 6 GLU A 104 LYS A 118 1 15
HELIX 7 7 GLY A 129 GLY A 137 1 9
HELIX 8 8 ALA A 148 ALA A 160 1 13
HELIX 9 9 GLY A 177 VAL A 207 1 31
HELIX 10 10 ALA A 211 ASN A 223 1 13
HELIX 11 11 SER A 229 PHE A 241 1 13
HELIX 12 12 LEU A 249 ILE A 253 5 5
HELIX 13 13 GLY A 263 GLY A 274 1 12
HELIX 14 14 VAL A 277 LEU A 292 1 16
HELIX 15 15 LEU A 292 LYS A 301 1 10
HELIX 16 16 ASP A 314 GLY A 349 1 36
HELIX 17 17 ASN A 353 TRP A 361 1 9
HELIX 18 18 SER A 369 ASN A 382 1 14
HELIX 19 19 ASN A 387 LEU A 390 5 4
HELIX 20 20 ASP A 391 GLY A 416 1 26
HELIX 21 21 MET A 419 ARG A 433 1 15
HELIX 22 22 PRO A 438 ALA A 451 1 14
SHEET 1 A 8 VAL A 52 GLY A 53 0
SHEET 2 A 8 VAL A 28 PHE A 31 1 N ALA A 30 O VAL A 52
SHEET 3 A 8 ILE A 5 ILE A 8 1 N ILE A 5 O CYS A 29
SHEET 4 A 8 ARG A 69 LEU A 72 1 O ILE A 71 N ALA A 6
SHEET 5 A 8 ILE A 96 ASP A 99 1 O ILE A 98 N LEU A 72
SHEET 6 A 8 LEU A 121 SER A 128 1 O VAL A 123 N ASP A 99
SHEET 7 A 8 SER A 139 GLY A 144 -1 O GLY A 143 N GLY A 124
SHEET 8 A 8 GLY A 174 ASP A 175 1 O GLY A 174 N GLY A 144
SHEET 1 B 2 TYR A 454 LEU A 456 0
SHEET 2 B 2 LYS A 459 ILE A 464 -1 O ILE A 464 N TYR A 454
CISPEP 1 LYS A 66 PRO A 67 0 -3.82
SITE 1 AC1 9 GLU A 104 TYR A 105 ARG A 106 MET A 184
SITE 2 AC1 9 TRP A 265 HOH A 617 HOH A 646 HOH A 813
SITE 3 AC1 9 HOH A1033
SITE 1 AC2 6 GLY A 130 GLU A 131 GLY A 166 GLY A 450
SITE 2 AC2 6 ALA A 451 HOH A1079
CRYST1 87.280 87.280 130.892 90.00 90.00 90.00 P 43 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 0.011457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END