HEADER TRANSFERASE 22-SEP-16 5TET
TITLE TEV CLEAVED HUMAN ATP CITRATE LYASE BOUND TO 4S HYDROXYCITRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-CITRATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-425;
COMPND 5 SYNONYM: ATP-CITRATE (PRO-S-)-LYASE,ACL,CITRATE CLEAVAGE ENZYME;
COMPND 6 EC: 2.3.3.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ATP-CITRATE SYNTHASE;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 488-810;
COMPND 12 SYNONYM: ATP-CITRATE (PRO-S-)-LYASE,ACL,CITRATE CLEAVAGE ENZYME;
COMPND 13 EC: 2.3.3.8;
COMPND 14 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: ACLY;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ACLY;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TEV CLEAVED, ATP-GRASP FOLD, 4S HYDROXYCITRATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HU,M.E.FRASER
REVDAT 3 06-MAR-24 5TET 1 REMARK
REVDAT 2 16-AUG-17 5TET 1 JRNL
REVDAT 1 09-AUG-17 5TET 0
JRNL AUTH J.HU,A.KOMAKULA,M.E.FRASER
JRNL TITL BINDING OF HYDROXYCITRATE TO HUMAN ATP-CITRATE LYASE.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 73 660 2017
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 28777081
JRNL DOI 10.1107/S2059798317009871
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2152: ???)
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 45586
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2289
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 53.0963 - 5.5418 0.95 2811 141 0.1982 0.2233
REMARK 3 2 5.5418 - 4.3993 0.97 2748 134 0.1459 0.1691
REMARK 3 3 4.3993 - 3.8434 0.97 2729 133 0.1281 0.1682
REMARK 3 4 3.8434 - 3.4921 0.98 2705 135 0.1344 0.1761
REMARK 3 5 3.4921 - 3.2418 0.98 2695 131 0.1438 0.2244
REMARK 3 6 3.2418 - 3.0507 0.99 2705 150 0.1498 0.2323
REMARK 3 7 3.0507 - 2.8979 0.99 2709 143 0.1512 0.2210
REMARK 3 8 2.8979 - 2.7718 0.99 2663 163 0.1524 0.2430
REMARK 3 9 2.7718 - 2.6651 0.99 2744 126 0.1613 0.2213
REMARK 3 10 2.6651 - 2.5731 0.99 2676 152 0.1628 0.2552
REMARK 3 11 2.5731 - 2.4927 0.99 2704 144 0.1686 0.2667
REMARK 3 12 2.4927 - 2.4214 1.00 2667 151 0.1635 0.2431
REMARK 3 13 2.4214 - 2.3577 1.00 2732 146 0.1675 0.2285
REMARK 3 14 2.3577 - 2.3002 1.00 2644 168 0.1722 0.2308
REMARK 3 15 2.3002 - 2.2479 1.00 2712 132 0.1718 0.2748
REMARK 3 16 2.2479 - 2.2000 1.00 2653 140 0.1809 0.2511
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.040
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) : 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 : 0.012 5970
REMARK 3 ANGLE : 1.003 8081
REMARK 3 CHIRALITY : 0.056 897
REMARK 3 PLANARITY : 0.007 1034
REMARK 3 DIHEDRAL : 13.410 3581
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 5TET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000224071.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45650
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 53.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
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: NULL
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 (%): 54.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% OF P3350, 100 MM TRISHCL PH 7.5,
REMARK 280 125 MM AMMONIUM PHOSPHATE PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
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 27.60500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.50000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.75500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.50000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.60500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.75500
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: 5390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 GLU A 137
REMARK 465 GLY A 138
REMARK 465 GLY A 139
REMARK 465 VAL A 140
REMARK 465 ASP A 141
REMARK 465 VAL A 142
REMARK 465 GLY A 143
REMARK 465 ASP A 144
REMARK 465 VAL A 145
REMARK 465 ASP A 146
REMARK 465 ALA A 147
REMARK 465 LYS A 148
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 HH TYR B 588 O HOH B 1002 1.47
REMARK 500 HZ1 LYS B 732 O HOH B 1003 1.52
REMARK 500 HH TYR A 252 O HOH A 1005 1.59
REMARK 500 HE21 GLN B 777 OE2 GLU B 781 1.59
REMARK 500 O HOH B 1076 O HOH B 1156 2.02
REMARK 500 O HOH B 1168 O HOH B 1182 2.05
REMARK 500 O HOH A 1185 O HOH A 1199 2.13
REMARK 500 O HOH B 1045 O HOH B 1093 2.17
REMARK 500 O HOH B 1115 O HOH B 1182 2.17
REMARK 500 O HOH A 1153 O HOH A 1159 2.19
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 O HOH A 1181 O HOH B 1049 1455 2.18
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 GLN A 61 28.51 -144.60
REMARK 500 PHE A 347 -7.63 -148.94
REMARK 500 PHE A 430 -1.17 73.03
REMARK 500 LYS B 488 -141.66 -125.55
REMARK 500 HIS B 537 -163.98 -163.31
REMARK 500 CYS B 633 -59.28 -129.12
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 7A3 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TEQ RELATED DB: PDB
REMARK 900 RELATED ID: 5TES RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AMINO-TERMINAL PORTION OF HUMAN ACLY WAS REDESIGNED TO HAVE TEV
REMARK 999 PROTEASE CLEAVAGE SITES BORDERING THE LINKER REGION. BOTH CLEAVAGE
REMARK 999 SITES HAD THE SAME SEQUENCE, ENLYFQS, AND THESE RESIDUES WERE
REMARK 999 SUBSTITUTED FOR RESIDUES 426-432 AND 481-487 OF ACLY. A HIS10-TAG
REMARK 999 REPLACED RESIDUES 450-459 OF THE LINKER. THE PROTEIN WAS TERMINATED
REMARK 999 AT RESIDUE 810. WHEN CLEAVED, THE PROTEIN WOULD CONSIST OF RESIDUES
REMARK 999 2-425-ENLYFQ AND S-488-810 OF HACLY.
DBREF 5TET A 1 425 UNP P53396 ACLY_HUMAN 1 425
DBREF 5TET B 488 810 UNP P53396 ACLY_HUMAN 478 800
SEQADV 5TET GLU A 426 UNP P53396 SEE REMARK 999
SEQADV 5TET ASN A 427 UNP P53396 SEE REMARK 999
SEQADV 5TET LEU A 428 UNP P53396 SEE REMARK 999
SEQADV 5TET TYR A 429 UNP P53396 SEE REMARK 999
SEQADV 5TET PHE A 430 UNP P53396 SEE REMARK 999
SEQADV 5TET GLN A 431 UNP P53396 SEE REMARK 999
SEQADV 5TET SER B 487 UNP P53396 SEE REMARK 999
SEQRES 1 A 431 MET SER ALA LYS ALA ILE SER GLU GLN THR GLY LYS GLU
SEQRES 2 A 431 LEU LEU TYR LYS PHE ILE CYS THR THR SER ALA ILE GLN
SEQRES 3 A 431 ASN ARG PHE LYS TYR ALA ARG VAL THR PRO ASP THR ASP
SEQRES 4 A 431 TRP ALA ARG LEU LEU GLN ASP HIS PRO TRP LEU LEU SER
SEQRES 5 A 431 GLN ASN LEU VAL VAL LYS PRO ASP GLN LEU ILE LYS ARG
SEQRES 6 A 431 ARG GLY LYS LEU GLY LEU VAL GLY VAL ASN LEU THR LEU
SEQRES 7 A 431 ASP GLY VAL LYS SER TRP LEU LYS PRO ARG LEU GLY GLN
SEQRES 8 A 431 GLU ALA THR VAL GLY LYS ALA THR GLY PHE LEU LYS ASN
SEQRES 9 A 431 PHE LEU ILE GLU PRO PHE VAL PRO HIS SER GLN ALA GLU
SEQRES 10 A 431 GLU PHE TYR VAL CYS ILE TYR ALA THR ARG GLU GLY ASP
SEQRES 11 A 431 TYR VAL LEU PHE HIS HIS GLU GLY GLY VAL ASP VAL GLY
SEQRES 12 A 431 ASP VAL ASP ALA LYS ALA GLN LYS LEU LEU VAL GLY VAL
SEQRES 13 A 431 ASP GLU LYS LEU ASN PRO GLU ASP ILE LYS LYS HIS LEU
SEQRES 14 A 431 LEU VAL HIS ALA PRO GLU ASP LYS LYS GLU ILE LEU ALA
SEQRES 15 A 431 SER PHE ILE SER GLY LEU PHE ASN PHE TYR GLU ASP LEU
SEQRES 16 A 431 TYR PHE THR TYR LEU GLU ILE ASN PRO LEU VAL VAL THR
SEQRES 17 A 431 LYS ASP GLY VAL TYR VAL LEU ASP LEU ALA ALA LYS VAL
SEQRES 18 A 431 ASP ALA THR ALA ASP TYR ILE CYS LYS VAL LYS TRP GLY
SEQRES 19 A 431 ASP ILE GLU PHE PRO PRO PRO PHE GLY ARG GLU ALA TYR
SEQRES 20 A 431 PRO GLU GLU ALA TYR ILE ALA ASP LEU ASP ALA LYS SER
SEQRES 21 A 431 GLY ALA SER LEU LYS LEU THR LEU LEU ASN PRO LYS GLY
SEQRES 22 A 431 ARG ILE TRP THR MET VAL ALA GLY GLY GLY ALA SER VAL
SEQRES 23 A 431 VAL TYR SER ASP THR ILE CYS ASP LEU GLY GLY VAL ASN
SEQRES 24 A 431 GLU LEU ALA ASN TYR GLY GLU TYR SER GLY ALA PRO SER
SEQRES 25 A 431 GLU GLN GLN THR TYR ASP TYR ALA LYS THR ILE LEU SER
SEQRES 26 A 431 LEU MET THR ARG GLU LYS HIS PRO ASP GLY LYS ILE LEU
SEQRES 27 A 431 ILE ILE GLY GLY SER ILE ALA ASN PHE THR ASN VAL ALA
SEQRES 28 A 431 ALA THR PHE LYS GLY ILE VAL ARG ALA ILE ARG ASP TYR
SEQRES 29 A 431 GLN GLY PRO LEU LYS GLU HIS GLU VAL THR ILE PHE VAL
SEQRES 30 A 431 ARG ARG GLY GLY PRO ASN TYR GLN GLU GLY LEU ARG VAL
SEQRES 31 A 431 MET GLY GLU VAL GLY LYS THR THR GLY ILE PRO ILE HIS
SEQRES 32 A 431 VAL PHE GLY THR GLU THR HIS MET THR ALA ILE VAL GLY
SEQRES 33 A 431 MET ALA LEU GLY HIS ARG PRO ILE PRO GLU ASN LEU TYR
SEQRES 34 A 431 PHE GLN
SEQRES 1 B 324 SER LYS SER THR THR LEU PHE SER ARG HIS THR LYS ALA
SEQRES 2 B 324 ILE VAL TRP GLY MET GLN THR ARG ALA VAL GLN GLY MET
SEQRES 3 B 324 LEU ASP PHE ASP TYR VAL CYS SER ARG ASP GLU PRO SER
SEQRES 4 B 324 VAL ALA ALA MET VAL TYR PRO PHE THR GLY ASP HIS LYS
SEQRES 5 B 324 GLN LYS PHE TYR TRP GLY HIS LYS GLU ILE LEU ILE PRO
SEQRES 6 B 324 VAL PHE LYS ASN MET ALA ASP ALA MET ARG LYS HIS PRO
SEQRES 7 B 324 GLU VAL ASP VAL LEU ILE ASN PHE ALA SER LEU ARG SER
SEQRES 8 B 324 ALA TYR ASP SER THR MET GLU THR MET ASN TYR ALA GLN
SEQRES 9 B 324 ILE ARG THR ILE ALA ILE ILE ALA GLU GLY ILE PRO GLU
SEQRES 10 B 324 ALA LEU THR ARG LYS LEU ILE LYS LYS ALA ASP GLN LYS
SEQRES 11 B 324 GLY VAL THR ILE ILE GLY PRO ALA THR VAL GLY GLY ILE
SEQRES 12 B 324 LYS PRO GLY CYS PHE LYS ILE GLY ASN THR GLY GLY MET
SEQRES 13 B 324 LEU ASP ASN ILE LEU ALA SER LYS LEU TYR ARG PRO GLY
SEQRES 14 B 324 SER VAL ALA TYR VAL SER ARG SER GLY GLY MET SER ASN
SEQRES 15 B 324 GLU LEU ASN ASN ILE ILE SER ARG THR THR ASP GLY VAL
SEQRES 16 B 324 TYR GLU GLY VAL ALA ILE GLY GLY ASP ARG TYR PRO GLY
SEQRES 17 B 324 SER THR PHE MET ASP HIS VAL LEU ARG TYR GLN ASP THR
SEQRES 18 B 324 PRO GLY VAL LYS MET ILE VAL VAL LEU GLY GLU ILE GLY
SEQRES 19 B 324 GLY THR GLU GLU TYR LYS ILE CYS ARG GLY ILE LYS GLU
SEQRES 20 B 324 GLY ARG LEU THR LYS PRO ILE VAL CYS TRP CYS ILE GLY
SEQRES 21 B 324 THR CYS ALA THR MET PHE SER SER GLU VAL GLN PHE GLY
SEQRES 22 B 324 HIS ALA GLY ALA CYS ALA ASN GLN ALA SER GLU THR ALA
SEQRES 23 B 324 VAL ALA LYS ASN GLN ALA LEU LYS GLU ALA GLY VAL PHE
SEQRES 24 B 324 VAL PRO ARG SER PHE ASP GLU LEU GLY GLU ILE ILE GLN
SEQRES 25 B 324 SER VAL TYR GLU ASP LEU VAL ALA ASN GLY VAL ILE
HET 7A3 A 901 19
HET PO4 A 902 5
HET GOL A 903 14
HET GOL A 904 14
HET PO4 B 901 5
HETNAM 7A3 3-C-CARBOXY-2-DEOXY-D-ERYTHRO-PENTARIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 7A3 C6 H8 O8
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 8 HOH *414(H2 O)
HELIX 1 AA1 SER A 7 ILE A 19 1 13
HELIX 2 AA2 ASP A 39 HIS A 47 1 9
HELIX 3 AA3 PRO A 48 SER A 52 5 5
HELIX 4 AA4 THR A 77 LYS A 86 1 10
HELIX 5 AA5 SER A 114 ALA A 116 5 3
HELIX 6 AA6 ASN A 161 LEU A 169 1 9
HELIX 7 AA7 PRO A 174 ASP A 176 5 3
HELIX 8 AA8 LYS A 177 LEU A 195 1 19
HELIX 9 AA9 ALA A 225 GLY A 234 1 10
HELIX 10 AB1 TYR A 247 LYS A 259 1 13
HELIX 11 AB2 GLY A 281 LEU A 295 1 15
HELIX 12 AB3 SER A 312 MET A 327 1 16
HELIX 13 AB4 ASN A 349 TYR A 364 1 16
HELIX 14 AB5 TYR A 364 HIS A 371 1 8
HELIX 15 AB6 ASN A 383 GLY A 399 1 17
HELIX 16 AB7 THR A 412 LEU A 419 1 8
HELIX 17 AB8 PRO A 425 TYR A 429 5 5
HELIX 18 AB9 GLN B 505 CYS B 519 1 15
HELIX 19 AC1 ASN B 555 HIS B 563 1 9
HELIX 20 AC2 SER B 577 MET B 586 1 10
HELIX 21 AC3 PRO B 602 GLY B 617 1 16
HELIX 22 AC4 MET B 642 SER B 649 1 8
HELIX 23 AC5 SER B 663 THR B 678 1 16
HELIX 24 AC6 THR B 696 ASP B 706 1 11
HELIX 25 AC7 GLU B 724 GLU B 733 1 10
HELIX 26 AC8 GLY B 746 PHE B 752 5 7
HELIX 27 AC9 GLN B 767 GLU B 770 5 4
HELIX 28 AD1 THR B 771 GLY B 783 1 13
HELIX 29 AD2 SER B 789 ASP B 791 5 3
HELIX 30 AD3 GLU B 792 ASN B 807 1 16
SHEET 1 AA1 6 ALA A 3 ILE A 6 0
SHEET 2 AA1 6 ALA A 218 ASP A 222 -1 O VAL A 221 N LYS A 4
SHEET 3 AA1 6 PHE A 197 THR A 208 -1 N GLU A 201 O ALA A 218
SHEET 4 AA1 6 GLU A 118 THR A 126 -1 N VAL A 121 O ILE A 202
SHEET 5 AA1 6 GLY A 129 HIS A 135 -1 O LEU A 133 N CYS A 122
SHEET 6 AA1 6 GLN A 150 VAL A 154 -1 O GLN A 150 N PHE A 134
SHEET 1 AA2 4 ALA A 3 ILE A 6 0
SHEET 2 AA2 4 ALA A 218 ASP A 222 -1 O VAL A 221 N LYS A 4
SHEET 3 AA2 4 PHE A 197 THR A 208 -1 N GLU A 201 O ALA A 218
SHEET 4 AA2 4 GLY A 211 VAL A 214 -1 O TYR A 213 N VAL A 206
SHEET 1 AA3 4 ALA A 32 VAL A 34 0
SHEET 2 AA3 4 PHE A 105 PRO A 109 -1 O PHE A 105 N VAL A 34
SHEET 3 AA3 4 LEU A 55 PRO A 59 -1 N VAL A 56 O GLU A 108
SHEET 4 AA3 4 GLY A 73 LEU A 76 -1 O GLY A 73 N VAL A 57
SHEET 1 AA4 2 GLU A 92 VAL A 95 0
SHEET 2 AA4 2 ALA A 98 PHE A 101 -1 O ALA A 98 N VAL A 95
SHEET 1 AA5 2 SER A 263 LEU A 268 0
SHEET 2 AA5 2 ASN A 303 SER A 308 -1 O TYR A 304 N THR A 267
SHEET 1 AA6 4 ILE A 275 THR A 277 0
SHEET 2 AA6 4 LYS A 336 ILE A 340 1 O ILE A 337 N TRP A 276
SHEET 3 AA6 4 VAL A 373 ARG A 378 1 O PHE A 376 N ILE A 340
SHEET 4 AA6 4 ILE A 402 PHE A 405 1 O HIS A 403 N VAL A 377
SHEET 1 AA7 7 HIS B 537 TRP B 543 0
SHEET 2 AA7 7 LYS B 546 PHE B 553 -1 O LYS B 546 N TRP B 543
SHEET 3 AA7 7 VAL B 526 VAL B 530 1 N MET B 529 O PHE B 553
SHEET 4 AA7 7 ALA B 499 TRP B 502 1 N VAL B 501 O VAL B 530
SHEET 5 AA7 7 VAL B 568 ASN B 571 1 O ILE B 570 N TRP B 502
SHEET 6 AA7 7 THR B 593 ILE B 596 1 O ALA B 595 N ASN B 571
SHEET 7 AA7 7 THR B 619 ILE B 621 1 O ILE B 621 N ILE B 596
SHEET 1 AA8 6 PHE B 634 ILE B 636 0
SHEET 2 AA8 6 GLY B 628 LYS B 630 -1 N LYS B 630 O PHE B 634
SHEET 3 AA8 6 VAL B 681 ALA B 686 -1 O GLY B 684 N ILE B 629
SHEET 4 AA8 6 VAL B 657 SER B 661 1 N VAL B 657 O TYR B 682
SHEET 5 AA8 6 MET B 712 GLU B 718 1 O VAL B 714 N ALA B 658
SHEET 6 AA8 6 ILE B 740 ILE B 745 1 O VAL B 741 N ILE B 713
CISPEP 1 ASN A 203 PRO A 204 0 7.58
CISPEP 2 GLY B 622 PRO B 623 0 8.47
SITE 1 AC1 11 SER A 308 GLY A 309 SER A 343 ALA A 345
SITE 2 AC1 11 ASN A 346 PHE A 347 THR A 348 ARG A 379
SITE 3 AC1 11 HOH A1016 HOH A1079 PO4 B 901
SITE 1 AC2 8 LYS A 64 ARG A 65 ARG A 66 ASP A 216
SITE 2 AC2 8 HOH A1019 HOH A1054 HOH A1060 HOH A1082
SITE 1 AC3 7 LYS A 58 ARG A 66 ASN A 203 LEU A 215
SITE 2 AC3 7 ASP A 216 HOH A1003 HOH A1118
SITE 1 AC4 5 TYR A 124 LYS A 151 HOH A1010 TYR B 517
SITE 2 AC4 5 SER B 520
SITE 1 AC5 9 GLY A 281 GLY A 282 GLY A 283 7A3 A 901
SITE 2 AC5 9 SER B 663 GLY B 664 GLY B 665 HIS B 760
SITE 3 AC5 9 HOH B1038
CRYST1 55.210 83.510 193.000 90.00 90.00 90.00 P 21 21 21 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 0.018113 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011975 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005181 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
