HEADER LYASE/LYASE INHIBITOR 24-FEB-16 5IDZ
TITLE STRUCTURE OF HUMAN ENOLASE 2 IN COMPLEX WITH (S)-(1-HYDROXY-2-
TITLE 2 OXOPIPERIDIN-3-YL)PHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA-ENOLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 2-PHOSPHO-D-GLYCERATE HYDRO-LYASE, ENOLASE 2, NEURAL
COMPND 5 ENOLASE, NEURON-SPECIFIC ENOLASE, NSE;
COMPND 6 EC: 4.2.1.11;
COMPND 7 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: ENO2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PJL-H6
KEYWDS ENOLASE GAMMA, GLYCOLYSIS, NEURON SPECIFIC ENOLASE, CARBOHYDRATE
KEYWDS 2 METABOLISM, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.G.LEONARD,F.L.MULLER
REVDAT 4 27-SEP-23 5IDZ 1 REMARK LINK
REVDAT 3 08-JAN-20 5IDZ 1 REMARK
REVDAT 2 24-APR-19 5IDZ 1 REMARK
REVDAT 1 22-FEB-17 5IDZ 0
JRNL AUTH Y.H.LIN,N.SATANI,N.HAMMOUDI,F.FELINI,P.G.LEONARD,D.MAXWELL,
JRNL AUTH 2 T.LINK,G.R.LEE,A.BOSAJOU,S.DUOLI,J.R.MARSZALEK,Y.T.SUN,
JRNL AUTH 3 J.MCMURRAY,P.J.MANDAL,M.E.DIFRANCESCO,B.CZAKO,A.WANG,
JRNL AUTH 4 W.BORNMANN,R.A.DEPINHO,F.L.MULLER
JRNL TITL POMHEX, A CELL-PERMEABLE ENOLASE INHIBITOR FOR COLLATERAL
JRNL TITL 2 LETHALITY TARGETING OF ENO1-DELETED GLIOBLASTOMA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9-1662
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 26345
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1383
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 54.3816 - 5.6643 1.00 2643 161 0.1423 0.1624
REMARK 3 2 5.6643 - 4.4966 1.00 2567 112 0.1367 0.1619
REMARK 3 3 4.4966 - 3.9284 1.00 2533 120 0.1375 0.1935
REMARK 3 4 3.9284 - 3.5693 1.00 2469 155 0.1522 0.2141
REMARK 3 5 3.5693 - 3.3135 1.00 2497 129 0.1809 0.2563
REMARK 3 6 3.3135 - 3.1182 1.00 2476 130 0.1939 0.2938
REMARK 3 7 3.1182 - 2.9620 1.00 2449 142 0.1848 0.2212
REMARK 3 8 2.9620 - 2.8331 1.00 2472 137 0.1843 0.2685
REMARK 3 9 2.8331 - 2.7240 1.00 2422 154 0.2018 0.2705
REMARK 3 10 2.7240 - 2.6300 0.99 2434 143 0.2120 0.3248
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.35
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.69
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 : 0.004 6865
REMARK 3 ANGLE : 0.692 9271
REMARK 3 CHIRALITY : 0.025 1035
REMARK 3 PLANARITY : 0.002 1218
REMARK 3 DIHEDRAL : 13.109 2549
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 5IDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218707.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.1.1
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26400
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
REMARK 200 RESOLUTION RANGE LOW (A) : 79.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.33900
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: PHASER 2.5.6
REMARK 200 STARTING MODEL: PDB ENTRY 4ZCW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM ACETATE, 100 MM BIS
REMARK 280 -TRIS, 18-22% W/V PEG3350, 6.5, OVERNIGHT CRYSTAL SOAK IN
REMARK 280 RESERVOIR SOLUTION SUPPLEMENTED WITH 4 MM COMPOUND, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING 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 34.05000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.23000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.37000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.23000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.05000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.37000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 HIS A 437
REMARK 465 HIS A 438
REMARK 465 HIS A 439
REMARK 465 HIS A 440
REMARK 465 HIS B 435
REMARK 465 HIS B 436
REMARK 465 HIS B 437
REMARK 465 HIS B 438
REMARK 465 HIS B 439
REMARK 465 HIS B 440
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 141 -28.46 -141.18
REMARK 500 ASN A 161 -162.94 -79.79
REMARK 500 ASP A 260 44.23 -150.28
REMARK 500 PRO A 288 47.69 -72.45
REMARK 500 ASP A 318 -79.40 -121.26
REMARK 500 VAL A 322 40.56 32.10
REMARK 500 ASN A 338 16.50 -140.42
REMARK 500 THR A 395 39.93 -141.70
REMARK 500 ARG A 400 127.31 67.81
REMARK 500 ASN B 161 -157.29 -75.77
REMARK 500 ASP B 260 44.72 -151.31
REMARK 500 PRO B 264 131.47 -35.00
REMARK 500 THR B 265 108.65 -50.13
REMARK 500 ASP B 318 -73.18 -125.37
REMARK 500 VAL B 322 38.95 31.67
REMARK 500 THR B 395 45.04 -144.11
REMARK 500 ARG B 400 123.16 66.39
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 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 245 OD2
REMARK 620 2 GLU A 293 OE2 77.5
REMARK 620 3 ASP A 318 OD2 164.7 91.2
REMARK 620 4 6BM A 501 O08 103.8 167.3 89.5
REMARK 620 5 6BM A 501 O07 92.4 90.1 97.8 77.2
REMARK 620 6 HOH A 623 O 88.3 97.5 83.0 95.2 172.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 245 OD2
REMARK 620 2 GLU B 293 OE2 79.6
REMARK 620 3 ASP B 318 OD1 158.4 80.3
REMARK 620 4 6BM B 501 O07 91.8 85.6 94.5
REMARK 620 5 6BM B 501 O08 109.3 162.2 92.2 78.8
REMARK 620 6 HOH B 633 O 92.7 96.2 81.7 175.4 98.7
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 MG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BM A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZCW RELATED DB: PDB
REMARK 900 HUMAN ENOLASE 2 IN COMPLEX WITH SF2312 INHIBITOR
REMARK 900 RELATED ID: 4ZA0 RELATED DB: PDB
REMARK 900 HUMAN ENOLASE 2 IN COMPLEX WITH PHOSPHONOACETOHYDROXAMATE INHIBITOR
DBREF 5IDZ A 1 434 UNP P09104 ENOG_HUMAN 1 434
DBREF 5IDZ B 1 434 UNP P09104 ENOG_HUMAN 1 434
SEQADV 5IDZ HIS A 435 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS A 436 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS A 437 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS A 438 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS A 439 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS A 440 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS B 435 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS B 436 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS B 437 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS B 438 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS B 439 UNP P09104 EXPRESSION TAG
SEQADV 5IDZ HIS B 440 UNP P09104 EXPRESSION TAG
SEQRES 1 A 440 MET SER ILE GLU LYS ILE TRP ALA ARG GLU ILE LEU ASP
SEQRES 2 A 440 SER ARG GLY ASN PRO THR VAL GLU VAL ASP LEU TYR THR
SEQRES 3 A 440 ALA LYS GLY LEU PHE ARG ALA ALA VAL PRO SER GLY ALA
SEQRES 4 A 440 SER THR GLY ILE TYR GLU ALA LEU GLU LEU ARG ASP GLY
SEQRES 5 A 440 ASP LYS GLN ARG TYR LEU GLY LYS GLY VAL LEU LYS ALA
SEQRES 6 A 440 VAL ASP HIS ILE ASN SER THR ILE ALA PRO ALA LEU ILE
SEQRES 7 A 440 SER SER GLY LEU SER VAL VAL GLU GLN GLU LYS LEU ASP
SEQRES 8 A 440 ASN LEU MET LEU GLU LEU ASP GLY THR GLU ASN LYS SER
SEQRES 9 A 440 LYS PHE GLY ALA ASN ALA ILE LEU GLY VAL SER LEU ALA
SEQRES 10 A 440 VAL CYS LYS ALA GLY ALA ALA GLU ARG GLU LEU PRO LEU
SEQRES 11 A 440 TYR ARG HIS ILE ALA GLN LEU ALA GLY ASN SER ASP LEU
SEQRES 12 A 440 ILE LEU PRO VAL PRO ALA PHE ASN VAL ILE ASN GLY GLY
SEQRES 13 A 440 SER HIS ALA GLY ASN LYS LEU ALA MET GLN GLU PHE MET
SEQRES 14 A 440 ILE LEU PRO VAL GLY ALA GLU SER PHE ARG ASP ALA MET
SEQRES 15 A 440 ARG LEU GLY ALA GLU VAL TYR HIS THR LEU LYS GLY VAL
SEQRES 16 A 440 ILE LYS ASP LYS TYR GLY LYS ASP ALA THR ASN VAL GLY
SEQRES 17 A 440 ASP GLU GLY GLY PHE ALA PRO ASN ILE LEU GLU ASN SER
SEQRES 18 A 440 GLU ALA LEU GLU LEU VAL LYS GLU ALA ILE ASP LYS ALA
SEQRES 19 A 440 GLY TYR THR GLU LYS ILE VAL ILE GLY MET ASP VAL ALA
SEQRES 20 A 440 ALA SER GLU PHE TYR ARG ASP GLY LYS TYR ASP LEU ASP
SEQRES 21 A 440 PHE LYS SER PRO THR ASP PRO SER ARG TYR ILE THR GLY
SEQRES 22 A 440 ASP GLN LEU GLY ALA LEU TYR GLN ASP PHE VAL ARG ASP
SEQRES 23 A 440 TYR PRO VAL VAL SER ILE GLU ASP PRO PHE ASP GLN ASP
SEQRES 24 A 440 ASP TRP ALA ALA TRP SER LYS PHE THR ALA ASN VAL GLY
SEQRES 25 A 440 ILE GLN ILE VAL GLY ASP ASP LEU THR VAL THR ASN PRO
SEQRES 26 A 440 LYS ARG ILE GLU ARG ALA VAL GLU GLU LYS ALA CYS ASN
SEQRES 27 A 440 CYS LEU LEU LEU LYS VAL ASN GLN ILE GLY SER VAL THR
SEQRES 28 A 440 GLU ALA ILE GLN ALA CYS LYS LEU ALA GLN GLU ASN GLY
SEQRES 29 A 440 TRP GLY VAL MET VAL SER HIS ARG SER GLY GLU THR GLU
SEQRES 30 A 440 ASP THR PHE ILE ALA ASP LEU VAL VAL GLY LEU CYS THR
SEQRES 31 A 440 GLY GLN ILE LYS THR GLY ALA PRO CYS ARG SER GLU ARG
SEQRES 32 A 440 LEU ALA LYS TYR ASN GLN LEU MET ARG ILE GLU GLU GLU
SEQRES 33 A 440 LEU GLY ASP GLU ALA ARG PHE ALA GLY HIS ASN PHE ARG
SEQRES 34 A 440 ASN PRO SER VAL LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 440 MET SER ILE GLU LYS ILE TRP ALA ARG GLU ILE LEU ASP
SEQRES 2 B 440 SER ARG GLY ASN PRO THR VAL GLU VAL ASP LEU TYR THR
SEQRES 3 B 440 ALA LYS GLY LEU PHE ARG ALA ALA VAL PRO SER GLY ALA
SEQRES 4 B 440 SER THR GLY ILE TYR GLU ALA LEU GLU LEU ARG ASP GLY
SEQRES 5 B 440 ASP LYS GLN ARG TYR LEU GLY LYS GLY VAL LEU LYS ALA
SEQRES 6 B 440 VAL ASP HIS ILE ASN SER THR ILE ALA PRO ALA LEU ILE
SEQRES 7 B 440 SER SER GLY LEU SER VAL VAL GLU GLN GLU LYS LEU ASP
SEQRES 8 B 440 ASN LEU MET LEU GLU LEU ASP GLY THR GLU ASN LYS SER
SEQRES 9 B 440 LYS PHE GLY ALA ASN ALA ILE LEU GLY VAL SER LEU ALA
SEQRES 10 B 440 VAL CYS LYS ALA GLY ALA ALA GLU ARG GLU LEU PRO LEU
SEQRES 11 B 440 TYR ARG HIS ILE ALA GLN LEU ALA GLY ASN SER ASP LEU
SEQRES 12 B 440 ILE LEU PRO VAL PRO ALA PHE ASN VAL ILE ASN GLY GLY
SEQRES 13 B 440 SER HIS ALA GLY ASN LYS LEU ALA MET GLN GLU PHE MET
SEQRES 14 B 440 ILE LEU PRO VAL GLY ALA GLU SER PHE ARG ASP ALA MET
SEQRES 15 B 440 ARG LEU GLY ALA GLU VAL TYR HIS THR LEU LYS GLY VAL
SEQRES 16 B 440 ILE LYS ASP LYS TYR GLY LYS ASP ALA THR ASN VAL GLY
SEQRES 17 B 440 ASP GLU GLY GLY PHE ALA PRO ASN ILE LEU GLU ASN SER
SEQRES 18 B 440 GLU ALA LEU GLU LEU VAL LYS GLU ALA ILE ASP LYS ALA
SEQRES 19 B 440 GLY TYR THR GLU LYS ILE VAL ILE GLY MET ASP VAL ALA
SEQRES 20 B 440 ALA SER GLU PHE TYR ARG ASP GLY LYS TYR ASP LEU ASP
SEQRES 21 B 440 PHE LYS SER PRO THR ASP PRO SER ARG TYR ILE THR GLY
SEQRES 22 B 440 ASP GLN LEU GLY ALA LEU TYR GLN ASP PHE VAL ARG ASP
SEQRES 23 B 440 TYR PRO VAL VAL SER ILE GLU ASP PRO PHE ASP GLN ASP
SEQRES 24 B 440 ASP TRP ALA ALA TRP SER LYS PHE THR ALA ASN VAL GLY
SEQRES 25 B 440 ILE GLN ILE VAL GLY ASP ASP LEU THR VAL THR ASN PRO
SEQRES 26 B 440 LYS ARG ILE GLU ARG ALA VAL GLU GLU LYS ALA CYS ASN
SEQRES 27 B 440 CYS LEU LEU LEU LYS VAL ASN GLN ILE GLY SER VAL THR
SEQRES 28 B 440 GLU ALA ILE GLN ALA CYS LYS LEU ALA GLN GLU ASN GLY
SEQRES 29 B 440 TRP GLY VAL MET VAL SER HIS ARG SER GLY GLU THR GLU
SEQRES 30 B 440 ASP THR PHE ILE ALA ASP LEU VAL VAL GLY LEU CYS THR
SEQRES 31 B 440 GLY GLN ILE LYS THR GLY ALA PRO CYS ARG SER GLU ARG
SEQRES 32 B 440 LEU ALA LYS TYR ASN GLN LEU MET ARG ILE GLU GLU GLU
SEQRES 33 B 440 LEU GLY ASP GLU ALA ARG PHE ALA GLY HIS ASN PHE ARG
SEQRES 34 B 440 ASN PRO SER VAL LEU HIS HIS HIS HIS HIS HIS
HET MG A 500 1
HET 6BM A 501 12
HET PGE A 502 10
HET MG B 500 1
HET 6BM B 501 12
HET PGE B 502 10
HETNAM MG MAGNESIUM ION
HETNAM 6BM [(3S)-1-HYDROXY-2-OXOPIPERIDIN-3-YL]PHOSPHONIC ACID
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 MG 2(MG 2+)
FORMUL 4 6BM 2(C5 H10 N O5 P)
FORMUL 5 PGE 2(C6 H14 O4)
FORMUL 9 HOH *154(H2 O)
HELIX 1 AA1 ARG A 56 LYS A 60 5 5
HELIX 2 AA2 VAL A 62 THR A 72 1 11
HELIX 3 AA3 THR A 72 GLY A 81 1 10
HELIX 4 AA4 GLU A 86 GLY A 99 1 14
HELIX 5 AA5 GLY A 107 ARG A 126 1 20
HELIX 6 AA6 PRO A 129 GLY A 139 1 11
HELIX 7 AA7 SER A 177 GLY A 201 1 25
HELIX 8 AA8 LYS A 202 THR A 205 5 4
HELIX 9 AA9 GLU A 219 GLY A 235 1 17
HELIX 10 AB1 ALA A 247 GLU A 250 5 4
HELIX 11 AB2 ASP A 266 TYR A 270 5 5
HELIX 12 AB3 THR A 272 TYR A 287 1 16
HELIX 13 AB4 ASP A 300 ALA A 309 1 10
HELIX 14 AB5 ASN A 324 LYS A 335 1 12
HELIX 15 AB6 LYS A 343 GLY A 348 1 6
HELIX 16 AB7 SER A 349 GLU A 362 1 14
HELIX 17 AB8 THR A 379 LEU A 388 1 10
HELIX 18 AB9 ARG A 400 GLY A 418 1 19
HELIX 19 AC1 ALA A 424 PHE A 428 5 5
HELIX 20 AC2 ASN A 430 HIS A 435 5 6
HELIX 21 AC3 ARG B 56 LYS B 60 5 5
HELIX 22 AC4 VAL B 62 THR B 72 1 11
HELIX 23 AC5 THR B 72 GLY B 81 1 10
HELIX 24 AC6 GLU B 86 GLY B 99 1 14
HELIX 25 AC7 GLY B 107 ARG B 126 1 20
HELIX 26 AC8 PRO B 129 GLY B 139 1 11
HELIX 27 AC9 SER B 177 GLY B 201 1 25
HELIX 28 AD1 LYS B 202 THR B 205 5 4
HELIX 29 AD2 GLU B 219 GLY B 235 1 17
HELIX 30 AD3 ALA B 247 GLU B 250 5 4
HELIX 31 AD4 THR B 272 TYR B 287 1 16
HELIX 32 AD5 ASP B 300 ALA B 309 1 10
HELIX 33 AD6 ASN B 324 GLU B 334 1 11
HELIX 34 AD7 LYS B 343 GLY B 348 1 6
HELIX 35 AD8 SER B 349 ASN B 363 1 15
HELIX 36 AD9 THR B 379 LEU B 388 1 10
HELIX 37 AE1 ARG B 400 GLY B 418 1 19
HELIX 38 AE2 ASP B 419 ALA B 421 5 3
HELIX 39 AE3 GLY B 425 PHE B 428 5 4
HELIX 40 AE4 ASN B 430 LEU B 434 5 5
SHEET 1 AA1 3 LYS A 5 LEU A 12 0
SHEET 2 AA1 3 PRO A 18 THR A 26 -1 O ASP A 23 N TRP A 7
SHEET 3 AA1 3 GLY A 29 ALA A 34 -1 O ALA A 33 N VAL A 22
SHEET 1 AA2 9 VAL A 147 PRO A 148 0
SHEET 2 AA2 9 GLN A 392 LYS A 394 1 O ILE A 393 N VAL A 147
SHEET 3 AA2 9 GLY A 366 SER A 370 1 N VAL A 369 O LYS A 394
SHEET 4 AA2 9 CYS A 339 LEU A 342 1 N LEU A 340 O MET A 368
SHEET 5 AA2 9 GLN A 314 GLY A 317 1 N GLY A 317 O CYS A 339
SHEET 6 AA2 9 VAL A 289 GLU A 293 1 N ILE A 292 O GLN A 314
SHEET 7 AA2 9 VAL A 241 ASP A 245 1 N MET A 244 O GLU A 293
SHEET 8 AA2 9 GLU A 167 LEU A 171 -1 N MET A 169 O GLY A 243
SHEET 9 AA2 9 PHE A 150 ASN A 154 -1 N VAL A 152 O PHE A 168
SHEET 1 AA3 2 TYR A 252 ARG A 253 0
SHEET 2 AA3 2 LYS A 256 TYR A 257 -1 O LYS A 256 N ARG A 253
SHEET 1 AA4 3 LYS B 5 LEU B 12 0
SHEET 2 AA4 3 PRO B 18 THR B 26 -1 O TYR B 25 N LYS B 5
SHEET 3 AA4 3 GLY B 29 ALA B 34 -1 O ALA B 33 N VAL B 22
SHEET 1 AA5 2 ILE B 144 LEU B 145 0
SHEET 2 AA5 2 ARG B 422 PHE B 423 1 O ARG B 422 N LEU B 145
SHEET 1 AA6 9 VAL B 147 PRO B 148 0
SHEET 2 AA6 9 GLN B 392 LYS B 394 1 O ILE B 393 N VAL B 147
SHEET 3 AA6 9 GLY B 366 SER B 370 1 N VAL B 369 O LYS B 394
SHEET 4 AA6 9 CYS B 339 LEU B 342 1 N LEU B 340 O GLY B 366
SHEET 5 AA6 9 GLN B 314 GLY B 317 1 N GLY B 317 O CYS B 339
SHEET 6 AA6 9 VAL B 289 GLU B 293 1 N ILE B 292 O VAL B 316
SHEET 7 AA6 9 VAL B 241 ASP B 245 1 N MET B 244 O GLU B 293
SHEET 8 AA6 9 GLU B 167 LEU B 171 -1 N GLU B 167 O ASP B 245
SHEET 9 AA6 9 PHE B 150 ASN B 154 -1 N VAL B 152 O PHE B 168
SHEET 1 AA7 3 TYR B 252 ARG B 253 0
SHEET 2 AA7 3 LYS B 256 ASP B 258 -1 O LYS B 256 N ARG B 253
SHEET 3 AA7 3 TYR B 270 ILE B 271 -1 O ILE B 271 N TYR B 257
LINK OD2 ASP A 245 MG MG A 500 1555 1555 2.15
LINK OE2 GLU A 293 MG MG A 500 1555 1555 2.07
LINK OD2 ASP A 318 MG MG A 500 1555 1555 2.12
LINK MG MG A 500 O08 6BM A 501 1555 1555 2.10
LINK MG MG A 500 O07 6BM A 501 1555 1555 2.21
LINK MG MG A 500 O HOH A 623 1555 1555 2.07
LINK OD2 ASP B 245 MG MG B 500 1555 1555 2.13
LINK OE2 GLU B 293 MG MG B 500 1555 1555 2.08
LINK OD1 ASP B 318 MG MG B 500 1555 1555 2.12
LINK MG MG B 500 O07 6BM B 501 1555 1555 2.21
LINK MG MG B 500 O08 6BM B 501 1555 1555 2.01
LINK MG MG B 500 O HOH B 633 1555 1555 2.07
CISPEP 1 MET B 1 SER B 2 0 -5.99
SITE 1 AC1 5 ASP A 245 GLU A 293 ASP A 318 6BM A 501
SITE 2 AC1 5 HOH A 623
SITE 1 AC2 14 ALA A 39 GLN A 166 GLU A 167 ASP A 245
SITE 2 AC2 14 GLU A 293 ASP A 318 LEU A 341 LYS A 343
SITE 3 AC2 14 HIS A 371 ARG A 372 SER A 373 LYS A 394
SITE 4 AC2 14 MG A 500 HOH A 623
SITE 1 AC3 2 LYS A 5 TYR A 25
SITE 1 AC4 5 ASP B 245 GLU B 293 ASP B 318 6BM B 501
SITE 2 AC4 5 HOH B 633
SITE 1 AC5 14 ALA B 39 GLN B 166 GLU B 167 ASP B 245
SITE 2 AC5 14 GLU B 293 ASP B 318 LEU B 341 LYS B 343
SITE 3 AC5 14 HIS B 371 ARG B 372 SER B 373 LYS B 394
SITE 4 AC5 14 MG B 500 HOH B 633
SITE 1 AC6 3 LYS B 5 TRP B 7 TYR B 25
CRYST1 68.100 108.740 116.460 90.00 90.00 90.00 P 21 21 21 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 0.014684 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009196 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008587 0.00000
(ATOM LINES ARE NOT SHOWN.)
END