HEADER HYDROLASE 06-JUN-17 5W2J
TITLE CRYSTAL STRUCTURE OF DIMERIC FORM OF MOUSE GLUTAMINASE C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMINASE KIDNEY ISOFORM, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 141-551;
COMPND 5 SYNONYM: GLS;
COMPND 6 EC: 3.5.1.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UNIDENTIFIED PEPTIDE;
COMPND 11 CHAIN: F;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: GLS, GLS1, KIAA0838;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUTAMINE METABOLISM, GLUTAMINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.CERIONE,Y.LI
REVDAT 4 13-MAR-24 5W2J 1 REMARK
REVDAT 3 18-DEC-19 5W2J 1 REMARK
REVDAT 2 27-FEB-19 5W2J 1 REMARK
REVDAT 1 17-OCT-18 5W2J 0
JRNL AUTH Y.LI,J.W.ERICKSON,C.A.STALNECKER,W.P.KATT,Q.HUANG,
JRNL AUTH 2 R.A.CERIONE,S.RAMACHANDRAN
JRNL TITL MECHANISTIC BASIS OF GLUTAMINASE ACTIVATION: A KEY ENZYME
JRNL TITL 2 THAT PROMOTES GLUTAMINE METABOLISM IN CANCER CELLS.
JRNL REF J. BIOL. CHEM. V. 291 20900 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27542409
JRNL DOI 10.1074/JBC.M116.720268
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 51086
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6489
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 169
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5W2J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000227809.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51086
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 82.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 50.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% PEG8000, 10% GLYCEROL, 50 MM TRIS
REMARK 280 -HCL, PH 8.5, EVAPORATION, TEMPERATURE 293.15K
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 42.47000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.72500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.44000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.72500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.47000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.44000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F
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 LEU A 141
REMARK 465 PRO A 142
REMARK 465 GLY A 551
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 533 CG HIS A 533 CD2 0.067
REMARK 500 HIS B 235 CG HIS B 235 CD2 0.063
REMARK 500 HIS B 533 CG HIS B 533 CD2 0.056
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 156 99.69 64.02
REMARK 500 ASP A 253 17.24 -145.07
REMARK 500 GLN A 290 -135.44 55.83
REMARK 500 LYS A 325 -146.06 -137.51
REMARK 500 LYS A 404 36.67 70.22
REMARK 500 GLU A 408 135.49 -37.49
REMARK 500 TYR A 471 -134.70 52.44
REMARK 500 VAL A 500 -58.08 -124.05
REMARK 500 ALA A 542 -124.49 60.62
REMARK 500 VAL B 198 -50.10 -122.48
REMARK 500 ASP B 228 77.47 -110.93
REMARK 500 GLN B 290 -127.42 37.26
REMARK 500 ASN B 324 31.76 -69.46
REMARK 500 TYR B 471 -145.10 53.40
REMARK 500 ASN B 499 -0.09 71.21
REMARK 500 VAL B 500 -59.11 -124.62
REMARK 500 LYS B 512 -35.66 -39.17
REMARK 500 PHE B 541 32.67 -149.04
REMARK 500 ALA B 542 -131.12 62.75
REMARK 500 LYS B 543 46.46 -102.64
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 CL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 601
DBREF 5W2J A 141 551 UNP D3Z7P3 GLSK_MOUSE 141 551
DBREF 5W2J B 141 551 UNP D3Z7P3 GLSK_MOUSE 141 551
DBREF 5W2J F 3 16 PDB 5W2J 5W2J 3 16
SEQADV 5W2J LYS A 391 UNP D3Z7P3 ASP 391 ENGINEERED MUTATION
SEQADV 5W2J LYS B 391 UNP D3Z7P3 ASP 391 ENGINEERED MUTATION
SEQRES 1 A 411 LEU PRO SER LEU GLU ASP LEU LEU PHE TYR THR ILE ALA
SEQRES 2 A 411 GLU GLY GLN GLU LYS ILE PRO VAL HIS LYS PHE ILE THR
SEQRES 3 A 411 ALA LEU LYS SER THR GLY LEU ARG THR SER ASP PRO ARG
SEQRES 4 A 411 LEU LYS GLU CYS MET ASP MET LEU ARG LEU THR LEU GLN
SEQRES 5 A 411 THR THR SER ASP GLY VAL MET LEU ASP LYS ASP LEU PHE
SEQRES 6 A 411 LYS LYS CYS VAL GLN SER ASN ILE VAL LEU LEU THR GLN
SEQRES 7 A 411 ALA PHE ARG ARG LYS PHE VAL ILE PRO ASP PHE MET SER
SEQRES 8 A 411 PHE THR SER HIS ILE ASP GLU LEU TYR GLU SER ALA LYS
SEQRES 9 A 411 LYS GLN SER GLY GLY LYS VAL ALA ASP TYR ILE PRO GLN
SEQRES 10 A 411 LEU ALA LYS PHE SER PRO ASP LEU TRP GLY VAL SER VAL
SEQRES 11 A 411 CYS THR VAL ASP GLY GLN ARG HIS SER ILE GLY ASP THR
SEQRES 12 A 411 LYS VAL PRO PHE CYS LEU GLN SER CYS VAL LYS PRO LEU
SEQRES 13 A 411 LYS TYR ALA ILE ALA VAL ASN ASP LEU GLY THR GLU TYR
SEQRES 14 A 411 VAL HIS ARG TYR VAL GLY LYS GLU PRO SER GLY LEU ARG
SEQRES 15 A 411 PHE ASN LYS LEU PHE LEU ASN GLU ASP ASP LYS PRO HIS
SEQRES 16 A 411 ASN PRO MET VAL ASN ALA GLY ALA ILE VAL VAL THR SER
SEQRES 17 A 411 LEU ILE LYS GLN GLY VAL ASN ASN ALA GLU LYS PHE ASP
SEQRES 18 A 411 TYR VAL MET GLN PHE LEU ASN LYS MET ALA GLY ASN GLU
SEQRES 19 A 411 TYR VAL GLY PHE SER ASN ALA THR PHE GLN SER GLU ARG
SEQRES 20 A 411 GLU SER GLY LYS ARG ASN PHE ALA ILE GLY TYR TYR LEU
SEQRES 21 A 411 LYS GLU LYS LYS CYS PHE PRO GLU GLY THR ASP MET VAL
SEQRES 22 A 411 GLY ILE LEU ASP PHE TYR PHE GLN LEU CYS SER ILE GLU
SEQRES 23 A 411 VAL THR CYS GLU SER ALA SER VAL MET ALA ALA THR LEU
SEQRES 24 A 411 ALA ASN GLY GLY PHE CYS PRO ILE THR GLY GLU ARG VAL
SEQRES 25 A 411 LEU SER PRO GLU ALA VAL ARG ASN THR LEU SER LEU MET
SEQRES 26 A 411 HIS SER CYS GLY MET TYR ASP PHE SER GLY GLN PHE ALA
SEQRES 27 A 411 PHE HIS VAL GLY LEU PRO ALA LYS SER GLY VAL ALA GLY
SEQRES 28 A 411 GLY ILE LEU LEU VAL VAL PRO ASN VAL MET GLY MET MET
SEQRES 29 A 411 CYS TRP SER PRO PRO LEU ASP LYS MET GLY ASN SER VAL
SEQRES 30 A 411 LYS GLY ILE HIS PHE CYS HIS ASP LEU VAL SER LEU CYS
SEQRES 31 A 411 ASN PHE HIS ASN TYR ASP ASN LEU ARG HIS PHE ALA LYS
SEQRES 32 A 411 LYS LEU ASP PRO ARG ARG GLU GLY
SEQRES 1 B 411 LEU PRO SER LEU GLU ASP LEU LEU PHE TYR THR ILE ALA
SEQRES 2 B 411 GLU GLY GLN GLU LYS ILE PRO VAL HIS LYS PHE ILE THR
SEQRES 3 B 411 ALA LEU LYS SER THR GLY LEU ARG THR SER ASP PRO ARG
SEQRES 4 B 411 LEU LYS GLU CYS MET ASP MET LEU ARG LEU THR LEU GLN
SEQRES 5 B 411 THR THR SER ASP GLY VAL MET LEU ASP LYS ASP LEU PHE
SEQRES 6 B 411 LYS LYS CYS VAL GLN SER ASN ILE VAL LEU LEU THR GLN
SEQRES 7 B 411 ALA PHE ARG ARG LYS PHE VAL ILE PRO ASP PHE MET SER
SEQRES 8 B 411 PHE THR SER HIS ILE ASP GLU LEU TYR GLU SER ALA LYS
SEQRES 9 B 411 LYS GLN SER GLY GLY LYS VAL ALA ASP TYR ILE PRO GLN
SEQRES 10 B 411 LEU ALA LYS PHE SER PRO ASP LEU TRP GLY VAL SER VAL
SEQRES 11 B 411 CYS THR VAL ASP GLY GLN ARG HIS SER ILE GLY ASP THR
SEQRES 12 B 411 LYS VAL PRO PHE CYS LEU GLN SER CYS VAL LYS PRO LEU
SEQRES 13 B 411 LYS TYR ALA ILE ALA VAL ASN ASP LEU GLY THR GLU TYR
SEQRES 14 B 411 VAL HIS ARG TYR VAL GLY LYS GLU PRO SER GLY LEU ARG
SEQRES 15 B 411 PHE ASN LYS LEU PHE LEU ASN GLU ASP ASP LYS PRO HIS
SEQRES 16 B 411 ASN PRO MET VAL ASN ALA GLY ALA ILE VAL VAL THR SER
SEQRES 17 B 411 LEU ILE LYS GLN GLY VAL ASN ASN ALA GLU LYS PHE ASP
SEQRES 18 B 411 TYR VAL MET GLN PHE LEU ASN LYS MET ALA GLY ASN GLU
SEQRES 19 B 411 TYR VAL GLY PHE SER ASN ALA THR PHE GLN SER GLU ARG
SEQRES 20 B 411 GLU SER GLY LYS ARG ASN PHE ALA ILE GLY TYR TYR LEU
SEQRES 21 B 411 LYS GLU LYS LYS CYS PHE PRO GLU GLY THR ASP MET VAL
SEQRES 22 B 411 GLY ILE LEU ASP PHE TYR PHE GLN LEU CYS SER ILE GLU
SEQRES 23 B 411 VAL THR CYS GLU SER ALA SER VAL MET ALA ALA THR LEU
SEQRES 24 B 411 ALA ASN GLY GLY PHE CYS PRO ILE THR GLY GLU ARG VAL
SEQRES 25 B 411 LEU SER PRO GLU ALA VAL ARG ASN THR LEU SER LEU MET
SEQRES 26 B 411 HIS SER CYS GLY MET TYR ASP PHE SER GLY GLN PHE ALA
SEQRES 27 B 411 PHE HIS VAL GLY LEU PRO ALA LYS SER GLY VAL ALA GLY
SEQRES 28 B 411 GLY ILE LEU LEU VAL VAL PRO ASN VAL MET GLY MET MET
SEQRES 29 B 411 CYS TRP SER PRO PRO LEU ASP LYS MET GLY ASN SER VAL
SEQRES 30 B 411 LYS GLY ILE HIS PHE CYS HIS ASP LEU VAL SER LEU CYS
SEQRES 31 B 411 ASN PHE HIS ASN TYR ASP ASN LEU ARG HIS PHE ALA LYS
SEQRES 32 B 411 LYS LEU ASP PRO ARG ARG GLU GLY
SEQRES 1 F 14 ALA LYS GLY ALA LEU GLN GLU LEU GLY ALA GLY LEU THR
SEQRES 2 F 14 ALA
HET CL A 601 1
HET CL B 601 1
HETNAM CL CHLORIDE ION
FORMUL 4 CL 2(CL 1-)
FORMUL 6 HOH *169(H2 O)
HELIX 1 AA1 SER A 143 GLU A 154 1 12
HELIX 2 AA2 VAL A 161 SER A 170 1 10
HELIX 3 AA3 ASP A 177 ARG A 179 5 3
HELIX 4 AA4 LEU A 180 GLN A 192 1 13
HELIX 5 AA5 ASP A 201 GLN A 210 1 10
HELIX 6 AA6 ASN A 212 ARG A 221 1 10
HELIX 7 AA7 ASP A 228 LYS A 245 1 18
HELIX 8 AA8 ILE A 255 LYS A 260 1 6
HELIX 9 AA9 CYS A 292 GLY A 306 1 15
HELIX 10 AB1 GLY A 306 VAL A 314 1 9
HELIX 11 AB2 VAL A 339 SER A 348 1 10
HELIX 12 AB3 ASN A 355 ALA A 371 1 17
HELIX 13 AB4 SER A 379 SER A 389 1 11
HELIX 14 AB5 GLY A 390 LYS A 403 1 14
HELIX 15 AB6 ASP A 411 SER A 424 1 14
HELIX 16 AB7 THR A 428 ASN A 441 1 14
HELIX 17 AB8 SER A 454 GLY A 469 1 16
HELIX 18 AB9 MET A 470 ASP A 472 5 3
HELIX 19 AC1 PHE A 473 VAL A 481 1 9
HELIX 20 AC2 SER A 516 CYS A 530 1 15
HELIX 21 AC3 SER B 143 GLU B 154 1 12
HELIX 22 AC4 VAL B 161 THR B 171 1 11
HELIX 23 AC5 ASP B 177 ARG B 179 5 3
HELIX 24 AC6 LEU B 180 THR B 193 1 14
HELIX 25 AC7 LYS B 202 GLN B 210 1 9
HELIX 26 AC8 ASN B 212 ARG B 221 1 10
HELIX 27 AC9 ASP B 228 LYS B 244 1 17
HELIX 28 AD1 ILE B 255 LYS B 260 1 6
HELIX 29 AD2 GLN B 290 CYS B 292 5 3
HELIX 30 AD3 VAL B 293 GLY B 306 1 14
HELIX 31 AD4 GLY B 306 HIS B 311 1 6
HELIX 32 AD5 VAL B 339 SER B 348 1 10
HELIX 33 AD6 ASN B 355 ALA B 371 1 17
HELIX 34 AD7 SER B 379 SER B 389 1 11
HELIX 35 AD8 GLY B 390 LYS B 403 1 14
HELIX 36 AD9 ASP B 411 SER B 424 1 14
HELIX 37 AE1 THR B 428 ASN B 441 1 14
HELIX 38 AE2 SER B 454 GLY B 469 1 16
HELIX 39 AE3 MET B 470 ASP B 472 5 3
HELIX 40 AE4 PHE B 473 VAL B 481 1 9
HELIX 41 AE5 SER B 516 CYS B 530 1 15
HELIX 42 AE6 LYS F 4 ALA F 16 1 13
SHEET 1 AA1 2 ILE A 159 PRO A 160 0
SHEET 2 AA1 2 MET A 199 LEU A 200 -1 O LEU A 200 N ILE A 159
SHEET 1 AA2 2 LYS A 250 VAL A 251 0
SHEET 2 AA2 2 PRO A 509 LEU A 510 -1 O LEU A 510 N LYS A 250
SHEET 1 AA3 5 ARG A 277 GLY A 281 0
SHEET 2 AA3 5 GLY A 267 THR A 272 -1 N VAL A 270 O HIS A 278
SHEET 3 AA3 5 MET A 501 TRP A 506 -1 O GLY A 502 N CYS A 271
SHEET 4 AA3 5 GLY A 492 VAL A 497 -1 N VAL A 497 O MET A 501
SHEET 5 AA3 5 ALA A 485 SER A 487 -1 N LYS A 486 O LEU A 494
SHEET 1 AA4 3 PHE A 287 CYS A 288 0
SHEET 2 AA4 3 ILE A 425 VAL A 427 -1 O VAL A 427 N PHE A 287
SHEET 3 AA4 3 GLY A 377 PHE A 378 -1 N GLY A 377 O GLU A 426
SHEET 1 AA5 2 LYS B 158 PRO B 160 0
SHEET 2 AA5 2 MET B 199 ASP B 201 -1 O LEU B 200 N ILE B 159
SHEET 1 AA6 5 ARG B 277 GLY B 281 0
SHEET 2 AA6 5 GLY B 267 THR B 272 -1 N VAL B 270 O HIS B 278
SHEET 3 AA6 5 MET B 501 TRP B 506 -1 O GLY B 502 N CYS B 271
SHEET 4 AA6 5 GLY B 492 VAL B 497 -1 N VAL B 497 O MET B 501
SHEET 5 AA6 5 ALA B 485 SER B 487 -1 N LYS B 486 O LEU B 494
SHEET 1 AA7 3 PHE B 287 CYS B 288 0
SHEET 2 AA7 3 ILE B 425 VAL B 427 -1 O VAL B 427 N PHE B 287
SHEET 3 AA7 3 GLY B 377 PHE B 378 -1 N GLY B 377 O GLU B 426
CISPEP 1 GLY A 155 GLN A 156 0 -3.99
CISPEP 2 LYS A 325 LEU A 326 0 1.48
SITE 1 AC1 6 GLN A 290 SER A 291 TYR A 471 GLY A 488
SITE 2 AC1 6 VAL A 489 HOH A 753
SITE 1 AC2 5 GLN B 290 SER B 291 TYR B 471 GLY B 488
SITE 2 AC2 5 VAL B 489
CRYST1 84.940 100.880 145.450 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 0.011773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009913 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006875 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
