HEADER OXIDOREDUCTASE 28-MAR-16 3JD4
TITLE GLUTAMATE DEHYDROGENASE IN COMPLEX WITH NADH AND GTP, CLOSED
TITLE 2 CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 58-558;
COMPND 5 SYNONYM: GDH 1;
COMPND 6 EC: 1.4.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS GLUTAMATE METABOLISM, MITOCHONDRIA, OXIDOREDUCTASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.J.BORGNIA,S.BANERJEE,A.MERK,D.MATTHIES,A.BARTESAGHI,P.RAO,
AUTHOR 2 J.PIERSON,L.A.EARL,V.FALCONIERI,S.SUBRAMANIAM,J.L.S.MILNE
REVDAT 4 21-FEB-24 3JD4 1 REMARK
REVDAT 3 18-JUL-18 3JD4 1 REMARK
REVDAT 2 11-MAY-16 3JD4 1 JRNL
REVDAT 1 27-APR-16 3JD4 0
JRNL AUTH M.J.BORGNIA,S.BANERJEE,A.MERK,D.MATTHIES,A.BARTESAGHI,P.RAO,
JRNL AUTH 2 J.PIERSON,L.A.EARL,V.FALCONIERI,S.SUBRAMANIAM,J.L.MILNE
JRNL TITL USING CRYO-EM TO MAP SMALL LIGANDS ON DYNAMIC METABOLIC
JRNL TITL 2 ENZYMES: STUDIES WITH GLUTAMATE DEHYDROGENASE.
JRNL REF MOL.PHARMACOL. V. 89 645 2016
JRNL REFN ISSN 0026-895X
JRNL PMID 27036132
JRNL DOI 10.1124/MOL.116.103382
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CTFFIND, COOT, PHENIX, ROSETTA, UCSF
REMARK 3 CHIMERA, EMAN, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 3MW9
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : REFINEMENT PROTOCOL--FLEXIBLE
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 0.638
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.400
REMARK 3 NUMBER OF PARTICLES : 20429
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: (SINGLE PARTICLE--APPLIED SYMMETRY: D3)
REMARK 4
REMARK 4 3JD4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000160550.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : TERNARY COMPLEX OF BOVINE
REMARK 245 GLUTAMATE DEHYDROGENASE WITH
REMARK 245 GTP AND NADH; L-GLUTAMATE:NAD(P)
REMARK 245 + OXIDOREDUCTASE (DEAMINATING)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00
REMARK 245 SAMPLE SUPPORT DETAILS : 200 MESH QUANTIFOIL R2/2 GRIDS
REMARK 245 (QUANTIFOIL MICRO TOOLS)
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FOR 3-6 SECONDS BEFORE
REMARK 245 PLUNGING INTO LIQUID ETHANE
REMARK 245 (FEI VITROBOT MARK IV).
REMARK 245 SAMPLE BUFFER : 100 MM POTASSIUM PHOSPHATE,
REMARK 245 0.1% N-OCTYL GLUCOPYRANOSIDE,
REMARK 245 20 MM NADH
REMARK 245 PH : 6.80
REMARK 245 SAMPLE DETAILS : ONE HOMOHEXAMER OF GDH BINDS 12
REMARK 245 MOLECULES OF NADH AND 6 MOLECULES OF GTP
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 27-JUL-14
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 5000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4500.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : 78426
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 ARG B 3
REMARK 465 GLU B 4
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 ARG C 3
REMARK 465 GLU C 4
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 ARG D 3
REMARK 465 GLU D 4
REMARK 465 ALA E 1
REMARK 465 ASP E 2
REMARK 465 ARG E 3
REMARK 465 GLU E 4
REMARK 465 ALA F 1
REMARK 465 ASP F 2
REMARK 465 ARG F 3
REMARK 465 GLU F 4
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 O HIS D 195 NZ LYS D 201 2.16
REMARK 500 O HIS C 195 NZ LYS C 201 2.16
REMARK 500 O HIS A 195 NZ LYS A 201 2.16
REMARK 500 O HIS B 195 NZ LYS B 201 2.16
REMARK 500 O HIS E 195 NZ LYS E 201 2.16
REMARK 500 O HIS F 195 NZ LYS F 201 2.16
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 LYS A 27 4.46 -69.76
REMARK 500 PRO A 121 59.77 -62.54
REMARK 500 PRO A 160 -3.07 -59.58
REMARK 500 VAL A 162 -63.45 -120.97
REMARK 500 ILE A 187 -61.07 -99.44
REMARK 500 PHE A 252 -0.65 -57.24
REMARK 500 GLU A 275 -168.35 -161.59
REMARK 500 ALA A 307 -167.62 -160.10
REMARK 500 CYS A 319 -165.50 -160.98
REMARK 500 THR A 427 99.71 -69.85
REMARK 500 SER A 441 0.18 -65.74
REMARK 500 LYS B 27 4.45 -69.75
REMARK 500 PRO B 121 59.90 -62.63
REMARK 500 PRO B 160 -3.13 -59.51
REMARK 500 VAL B 162 -63.47 -120.90
REMARK 500 ILE B 187 -61.05 -99.44
REMARK 500 PHE B 252 -0.61 -57.32
REMARK 500 GLU B 275 -168.35 -161.60
REMARK 500 ALA B 307 -167.59 -160.16
REMARK 500 CYS B 319 -165.49 -160.95
REMARK 500 THR B 427 99.04 -69.74
REMARK 500 SER B 441 0.19 -65.69
REMARK 500 LYS C 27 4.50 -69.77
REMARK 500 PRO C 121 59.80 -62.54
REMARK 500 PRO C 160 -3.01 -59.63
REMARK 500 VAL C 162 -63.44 -120.92
REMARK 500 ILE C 187 -60.99 -99.48
REMARK 500 PHE C 252 -0.66 -57.26
REMARK 500 GLU C 275 -168.36 -161.57
REMARK 500 ALA C 307 -167.60 -160.10
REMARK 500 CYS C 319 -165.50 -160.95
REMARK 500 THR C 427 99.20 -69.55
REMARK 500 SER C 441 0.18 -65.66
REMARK 500 LYS D 27 4.41 -69.72
REMARK 500 PRO D 121 59.90 -62.60
REMARK 500 PRO D 160 -3.05 -59.61
REMARK 500 VAL D 162 -63.41 -120.95
REMARK 500 ILE D 187 -61.00 -99.49
REMARK 500 PHE D 252 -0.60 -57.36
REMARK 500 GLU D 275 -168.32 -161.63
REMARK 500 ALA D 307 -167.67 -160.13
REMARK 500 CYS D 319 -165.48 -160.96
REMARK 500 THR D 427 99.83 -69.75
REMARK 500 SER D 441 0.15 -65.68
REMARK 500 LYS E 27 4.50 -69.79
REMARK 500 PRO E 121 59.82 -62.55
REMARK 500 PRO E 160 -3.10 -59.57
REMARK 500 VAL E 162 -63.47 -120.89
REMARK 500 ILE E 187 -61.07 -99.44
REMARK 500 PHE E 252 -0.55 -57.37
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 497 VAL A 498 -145.61
REMARK 500 GLY B 497 VAL B 498 -145.61
REMARK 500 GLY C 497 VAL C 498 -145.62
REMARK 500 GLY D 497 VAL D 498 -145.64
REMARK 500 GLY E 497 VAL E 498 -145.61
REMARK 500 GLY F 497 VAL F 498 -145.65
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 NAI A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI E 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP E 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI F 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP F 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-6633 RELATED DB: EMDB
REMARK 900 GLUTAMATE DEHYDROGENASE IN COMPLEX WITH GTP AND NADH, CLOSED
REMARK 900 CONFORMATION
REMARK 900 RELATED ID: EMD-6630 RELATED DB: EMDB
REMARK 900 GLUTAMATE DEHYDROGENASE, UNLIGANDED
REMARK 900 RELATED ID: EMD-6631 RELATED DB: EMDB
REMARK 900 GLUTAMATE DEHYDROGENASE IN COMPLEX WITH GTP
REMARK 900 RELATED ID: EMD-6634 RELATED DB: EMDB
REMARK 900 GLUTAMATE DEHYDROGENASE IN COMPLEX WITH NADH, CLOSED CONFORMATION
REMARK 900 RELATED ID: EMD-6635 RELATED DB: EMDB
REMARK 900 GLUTAMATE DEHYDROGENASE IN COMPLEX WITH NADH, OPEN CONFORMATION
REMARK 900 RELATED ID: EMD-6632 RELATED DB: EMDB
REMARK 900 GLUTAMATE DEHYDROGENASE IN COMPLEX WITH GTP AND NADH, OPEN
REMARK 900 CONFORMATION
REMARK 900 RELATED ID: 3JCZ RELATED DB: PDB
REMARK 900 RELATED ID: 3JD0 RELATED DB: PDB
REMARK 900 RELATED ID: 3JD1 RELATED DB: PDB
REMARK 900 RELATED ID: 3JD2 RELATED DB: PDB
REMARK 900 RELATED ID: 3JD3 RELATED DB: PDB
DBREF 3JD4 A 1 501 UNP P00366 DHE3_BOVIN 58 558
DBREF 3JD4 B 1 501 UNP P00366 DHE3_BOVIN 58 558
DBREF 3JD4 C 1 501 UNP P00366 DHE3_BOVIN 58 558
DBREF 3JD4 D 1 501 UNP P00366 DHE3_BOVIN 58 558
DBREF 3JD4 E 1 501 UNP P00366 DHE3_BOVIN 58 558
DBREF 3JD4 F 1 501 UNP P00366 DHE3_BOVIN 58 558
SEQRES 1 A 501 ALA ASP ARG GLU ASP ASP PRO ASN PHE PHE LYS MET VAL
SEQRES 2 A 501 GLU GLY PHE PHE ASP ARG GLY ALA SER ILE VAL GLU ASP
SEQRES 3 A 501 LYS LEU VAL GLU ASP LEU LYS THR ARG GLU THR GLU GLU
SEQRES 4 A 501 GLN LYS ARG ASN ARG VAL ARG SER ILE LEU ARG ILE ILE
SEQRES 5 A 501 LYS PRO CYS ASN HIS VAL LEU SER LEU SER PHE PRO ILE
SEQRES 6 A 501 ARG ARG ASP ASP GLY SER TRP GLU VAL ILE GLU GLY TYR
SEQRES 7 A 501 ARG ALA GLN HIS SER GLN HIS ARG THR PRO CYS LYS GLY
SEQRES 8 A 501 GLY ILE ARG TYR SER THR ASP VAL SER VAL ASP GLU VAL
SEQRES 9 A 501 LYS ALA LEU ALA SER LEU MET THR TYR LYS CYS ALA VAL
SEQRES 10 A 501 VAL ASP VAL PRO PHE GLY GLY ALA LYS ALA GLY VAL LYS
SEQRES 11 A 501 ILE ASN PRO LYS ASN TYR THR ASP ASN GLU LEU GLU LYS
SEQRES 12 A 501 ILE THR ARG ARG PHE THR MET GLU LEU ALA LYS LYS GLY
SEQRES 13 A 501 PHE ILE GLY PRO GLY VAL ASP VAL PRO ALA PRO ASP MET
SEQRES 14 A 501 SER THR GLY GLU ARG GLU MET SER TRP ILE ALA ASP THR
SEQRES 15 A 501 TYR ALA SER THR ILE GLY HIS TYR ASP ILE ASN ALA HIS
SEQRES 16 A 501 ALA CYS VAL THR GLY LYS PRO ILE SER GLN GLY GLY ILE
SEQRES 17 A 501 HIS GLY ARG ILE SER ALA THR GLY ARG GLY VAL PHE HIS
SEQRES 18 A 501 GLY ILE GLU ASN PHE ILE ASN GLU ALA SER TYR MET SER
SEQRES 19 A 501 ILE LEU GLY MET THR PRO GLY PHE GLY ASP LYS THR PHE
SEQRES 20 A 501 VAL VAL GLN GLY PHE GLY ASN VAL GLY LEU HIS SER MET
SEQRES 21 A 501 ARG TYR LEU HIS ARG PHE GLY ALA LYS CYS ILE THR VAL
SEQRES 22 A 501 GLY GLU SER ASP GLY SER ILE TRP ASN PRO ASP GLY ILE
SEQRES 23 A 501 ASP PRO LYS GLU LEU GLU ASP PHE LYS LEU GLN HIS GLY
SEQRES 24 A 501 THR ILE LEU GLY PHE PRO LYS ALA LYS ILE TYR GLU GLY
SEQRES 25 A 501 SER ILE LEU GLU VAL ASP CYS ASP ILE LEU ILE PRO ALA
SEQRES 26 A 501 ALA SER GLU LYS GLN LEU THR LYS SER ASN ALA PRO ARG
SEQRES 27 A 501 VAL LYS ALA LYS ILE ILE ALA GLU GLY ALA ASN GLY PRO
SEQRES 28 A 501 THR THR PRO GLU ALA ASP LYS ILE PHE LEU GLU ARG ASN
SEQRES 29 A 501 ILE MET VAL ILE PRO ASP LEU TYR LEU ASN ALA GLY GLY
SEQRES 30 A 501 VAL THR VAL SER TYR PHE GLU TRP LEU ASN ASN LEU ASN
SEQRES 31 A 501 HIS VAL SER TYR GLY ARG LEU THR PHE LYS TYR GLU ARG
SEQRES 32 A 501 ASP SER ASN TYR HIS LEU LEU MET SER VAL GLN GLU SER
SEQRES 33 A 501 LEU GLU ARG LYS PHE GLY LYS HIS GLY GLY THR ILE PRO
SEQRES 34 A 501 ILE VAL PRO THR ALA GLU PHE GLN ASP ARG ILE SER GLY
SEQRES 35 A 501 ALA SER GLU LYS ASP ILE VAL HIS SER GLY LEU ALA TYR
SEQRES 36 A 501 THR MET GLU ARG SER ALA ARG GLN ILE MET ARG THR ALA
SEQRES 37 A 501 MET LYS TYR ASN LEU GLY LEU ASP LEU ARG THR ALA ALA
SEQRES 38 A 501 TYR VAL ASN ALA ILE GLU LYS VAL PHE ARG VAL TYR ASN
SEQRES 39 A 501 GLU ALA GLY VAL THR PHE THR
SEQRES 1 B 501 ALA ASP ARG GLU ASP ASP PRO ASN PHE PHE LYS MET VAL
SEQRES 2 B 501 GLU GLY PHE PHE ASP ARG GLY ALA SER ILE VAL GLU ASP
SEQRES 3 B 501 LYS LEU VAL GLU ASP LEU LYS THR ARG GLU THR GLU GLU
SEQRES 4 B 501 GLN LYS ARG ASN ARG VAL ARG SER ILE LEU ARG ILE ILE
SEQRES 5 B 501 LYS PRO CYS ASN HIS VAL LEU SER LEU SER PHE PRO ILE
SEQRES 6 B 501 ARG ARG ASP ASP GLY SER TRP GLU VAL ILE GLU GLY TYR
SEQRES 7 B 501 ARG ALA GLN HIS SER GLN HIS ARG THR PRO CYS LYS GLY
SEQRES 8 B 501 GLY ILE ARG TYR SER THR ASP VAL SER VAL ASP GLU VAL
SEQRES 9 B 501 LYS ALA LEU ALA SER LEU MET THR TYR LYS CYS ALA VAL
SEQRES 10 B 501 VAL ASP VAL PRO PHE GLY GLY ALA LYS ALA GLY VAL LYS
SEQRES 11 B 501 ILE ASN PRO LYS ASN TYR THR ASP ASN GLU LEU GLU LYS
SEQRES 12 B 501 ILE THR ARG ARG PHE THR MET GLU LEU ALA LYS LYS GLY
SEQRES 13 B 501 PHE ILE GLY PRO GLY VAL ASP VAL PRO ALA PRO ASP MET
SEQRES 14 B 501 SER THR GLY GLU ARG GLU MET SER TRP ILE ALA ASP THR
SEQRES 15 B 501 TYR ALA SER THR ILE GLY HIS TYR ASP ILE ASN ALA HIS
SEQRES 16 B 501 ALA CYS VAL THR GLY LYS PRO ILE SER GLN GLY GLY ILE
SEQRES 17 B 501 HIS GLY ARG ILE SER ALA THR GLY ARG GLY VAL PHE HIS
SEQRES 18 B 501 GLY ILE GLU ASN PHE ILE ASN GLU ALA SER TYR MET SER
SEQRES 19 B 501 ILE LEU GLY MET THR PRO GLY PHE GLY ASP LYS THR PHE
SEQRES 20 B 501 VAL VAL GLN GLY PHE GLY ASN VAL GLY LEU HIS SER MET
SEQRES 21 B 501 ARG TYR LEU HIS ARG PHE GLY ALA LYS CYS ILE THR VAL
SEQRES 22 B 501 GLY GLU SER ASP GLY SER ILE TRP ASN PRO ASP GLY ILE
SEQRES 23 B 501 ASP PRO LYS GLU LEU GLU ASP PHE LYS LEU GLN HIS GLY
SEQRES 24 B 501 THR ILE LEU GLY PHE PRO LYS ALA LYS ILE TYR GLU GLY
SEQRES 25 B 501 SER ILE LEU GLU VAL ASP CYS ASP ILE LEU ILE PRO ALA
SEQRES 26 B 501 ALA SER GLU LYS GLN LEU THR LYS SER ASN ALA PRO ARG
SEQRES 27 B 501 VAL LYS ALA LYS ILE ILE ALA GLU GLY ALA ASN GLY PRO
SEQRES 28 B 501 THR THR PRO GLU ALA ASP LYS ILE PHE LEU GLU ARG ASN
SEQRES 29 B 501 ILE MET VAL ILE PRO ASP LEU TYR LEU ASN ALA GLY GLY
SEQRES 30 B 501 VAL THR VAL SER TYR PHE GLU TRP LEU ASN ASN LEU ASN
SEQRES 31 B 501 HIS VAL SER TYR GLY ARG LEU THR PHE LYS TYR GLU ARG
SEQRES 32 B 501 ASP SER ASN TYR HIS LEU LEU MET SER VAL GLN GLU SER
SEQRES 33 B 501 LEU GLU ARG LYS PHE GLY LYS HIS GLY GLY THR ILE PRO
SEQRES 34 B 501 ILE VAL PRO THR ALA GLU PHE GLN ASP ARG ILE SER GLY
SEQRES 35 B 501 ALA SER GLU LYS ASP ILE VAL HIS SER GLY LEU ALA TYR
SEQRES 36 B 501 THR MET GLU ARG SER ALA ARG GLN ILE MET ARG THR ALA
SEQRES 37 B 501 MET LYS TYR ASN LEU GLY LEU ASP LEU ARG THR ALA ALA
SEQRES 38 B 501 TYR VAL ASN ALA ILE GLU LYS VAL PHE ARG VAL TYR ASN
SEQRES 39 B 501 GLU ALA GLY VAL THR PHE THR
SEQRES 1 C 501 ALA ASP ARG GLU ASP ASP PRO ASN PHE PHE LYS MET VAL
SEQRES 2 C 501 GLU GLY PHE PHE ASP ARG GLY ALA SER ILE VAL GLU ASP
SEQRES 3 C 501 LYS LEU VAL GLU ASP LEU LYS THR ARG GLU THR GLU GLU
SEQRES 4 C 501 GLN LYS ARG ASN ARG VAL ARG SER ILE LEU ARG ILE ILE
SEQRES 5 C 501 LYS PRO CYS ASN HIS VAL LEU SER LEU SER PHE PRO ILE
SEQRES 6 C 501 ARG ARG ASP ASP GLY SER TRP GLU VAL ILE GLU GLY TYR
SEQRES 7 C 501 ARG ALA GLN HIS SER GLN HIS ARG THR PRO CYS LYS GLY
SEQRES 8 C 501 GLY ILE ARG TYR SER THR ASP VAL SER VAL ASP GLU VAL
SEQRES 9 C 501 LYS ALA LEU ALA SER LEU MET THR TYR LYS CYS ALA VAL
SEQRES 10 C 501 VAL ASP VAL PRO PHE GLY GLY ALA LYS ALA GLY VAL LYS
SEQRES 11 C 501 ILE ASN PRO LYS ASN TYR THR ASP ASN GLU LEU GLU LYS
SEQRES 12 C 501 ILE THR ARG ARG PHE THR MET GLU LEU ALA LYS LYS GLY
SEQRES 13 C 501 PHE ILE GLY PRO GLY VAL ASP VAL PRO ALA PRO ASP MET
SEQRES 14 C 501 SER THR GLY GLU ARG GLU MET SER TRP ILE ALA ASP THR
SEQRES 15 C 501 TYR ALA SER THR ILE GLY HIS TYR ASP ILE ASN ALA HIS
SEQRES 16 C 501 ALA CYS VAL THR GLY LYS PRO ILE SER GLN GLY GLY ILE
SEQRES 17 C 501 HIS GLY ARG ILE SER ALA THR GLY ARG GLY VAL PHE HIS
SEQRES 18 C 501 GLY ILE GLU ASN PHE ILE ASN GLU ALA SER TYR MET SER
SEQRES 19 C 501 ILE LEU GLY MET THR PRO GLY PHE GLY ASP LYS THR PHE
SEQRES 20 C 501 VAL VAL GLN GLY PHE GLY ASN VAL GLY LEU HIS SER MET
SEQRES 21 C 501 ARG TYR LEU HIS ARG PHE GLY ALA LYS CYS ILE THR VAL
SEQRES 22 C 501 GLY GLU SER ASP GLY SER ILE TRP ASN PRO ASP GLY ILE
SEQRES 23 C 501 ASP PRO LYS GLU LEU GLU ASP PHE LYS LEU GLN HIS GLY
SEQRES 24 C 501 THR ILE LEU GLY PHE PRO LYS ALA LYS ILE TYR GLU GLY
SEQRES 25 C 501 SER ILE LEU GLU VAL ASP CYS ASP ILE LEU ILE PRO ALA
SEQRES 26 C 501 ALA SER GLU LYS GLN LEU THR LYS SER ASN ALA PRO ARG
SEQRES 27 C 501 VAL LYS ALA LYS ILE ILE ALA GLU GLY ALA ASN GLY PRO
SEQRES 28 C 501 THR THR PRO GLU ALA ASP LYS ILE PHE LEU GLU ARG ASN
SEQRES 29 C 501 ILE MET VAL ILE PRO ASP LEU TYR LEU ASN ALA GLY GLY
SEQRES 30 C 501 VAL THR VAL SER TYR PHE GLU TRP LEU ASN ASN LEU ASN
SEQRES 31 C 501 HIS VAL SER TYR GLY ARG LEU THR PHE LYS TYR GLU ARG
SEQRES 32 C 501 ASP SER ASN TYR HIS LEU LEU MET SER VAL GLN GLU SER
SEQRES 33 C 501 LEU GLU ARG LYS PHE GLY LYS HIS GLY GLY THR ILE PRO
SEQRES 34 C 501 ILE VAL PRO THR ALA GLU PHE GLN ASP ARG ILE SER GLY
SEQRES 35 C 501 ALA SER GLU LYS ASP ILE VAL HIS SER GLY LEU ALA TYR
SEQRES 36 C 501 THR MET GLU ARG SER ALA ARG GLN ILE MET ARG THR ALA
SEQRES 37 C 501 MET LYS TYR ASN LEU GLY LEU ASP LEU ARG THR ALA ALA
SEQRES 38 C 501 TYR VAL ASN ALA ILE GLU LYS VAL PHE ARG VAL TYR ASN
SEQRES 39 C 501 GLU ALA GLY VAL THR PHE THR
SEQRES 1 D 501 ALA ASP ARG GLU ASP ASP PRO ASN PHE PHE LYS MET VAL
SEQRES 2 D 501 GLU GLY PHE PHE ASP ARG GLY ALA SER ILE VAL GLU ASP
SEQRES 3 D 501 LYS LEU VAL GLU ASP LEU LYS THR ARG GLU THR GLU GLU
SEQRES 4 D 501 GLN LYS ARG ASN ARG VAL ARG SER ILE LEU ARG ILE ILE
SEQRES 5 D 501 LYS PRO CYS ASN HIS VAL LEU SER LEU SER PHE PRO ILE
SEQRES 6 D 501 ARG ARG ASP ASP GLY SER TRP GLU VAL ILE GLU GLY TYR
SEQRES 7 D 501 ARG ALA GLN HIS SER GLN HIS ARG THR PRO CYS LYS GLY
SEQRES 8 D 501 GLY ILE ARG TYR SER THR ASP VAL SER VAL ASP GLU VAL
SEQRES 9 D 501 LYS ALA LEU ALA SER LEU MET THR TYR LYS CYS ALA VAL
SEQRES 10 D 501 VAL ASP VAL PRO PHE GLY GLY ALA LYS ALA GLY VAL LYS
SEQRES 11 D 501 ILE ASN PRO LYS ASN TYR THR ASP ASN GLU LEU GLU LYS
SEQRES 12 D 501 ILE THR ARG ARG PHE THR MET GLU LEU ALA LYS LYS GLY
SEQRES 13 D 501 PHE ILE GLY PRO GLY VAL ASP VAL PRO ALA PRO ASP MET
SEQRES 14 D 501 SER THR GLY GLU ARG GLU MET SER TRP ILE ALA ASP THR
SEQRES 15 D 501 TYR ALA SER THR ILE GLY HIS TYR ASP ILE ASN ALA HIS
SEQRES 16 D 501 ALA CYS VAL THR GLY LYS PRO ILE SER GLN GLY GLY ILE
SEQRES 17 D 501 HIS GLY ARG ILE SER ALA THR GLY ARG GLY VAL PHE HIS
SEQRES 18 D 501 GLY ILE GLU ASN PHE ILE ASN GLU ALA SER TYR MET SER
SEQRES 19 D 501 ILE LEU GLY MET THR PRO GLY PHE GLY ASP LYS THR PHE
SEQRES 20 D 501 VAL VAL GLN GLY PHE GLY ASN VAL GLY LEU HIS SER MET
SEQRES 21 D 501 ARG TYR LEU HIS ARG PHE GLY ALA LYS CYS ILE THR VAL
SEQRES 22 D 501 GLY GLU SER ASP GLY SER ILE TRP ASN PRO ASP GLY ILE
SEQRES 23 D 501 ASP PRO LYS GLU LEU GLU ASP PHE LYS LEU GLN HIS GLY
SEQRES 24 D 501 THR ILE LEU GLY PHE PRO LYS ALA LYS ILE TYR GLU GLY
SEQRES 25 D 501 SER ILE LEU GLU VAL ASP CYS ASP ILE LEU ILE PRO ALA
SEQRES 26 D 501 ALA SER GLU LYS GLN LEU THR LYS SER ASN ALA PRO ARG
SEQRES 27 D 501 VAL LYS ALA LYS ILE ILE ALA GLU GLY ALA ASN GLY PRO
SEQRES 28 D 501 THR THR PRO GLU ALA ASP LYS ILE PHE LEU GLU ARG ASN
SEQRES 29 D 501 ILE MET VAL ILE PRO ASP LEU TYR LEU ASN ALA GLY GLY
SEQRES 30 D 501 VAL THR VAL SER TYR PHE GLU TRP LEU ASN ASN LEU ASN
SEQRES 31 D 501 HIS VAL SER TYR GLY ARG LEU THR PHE LYS TYR GLU ARG
SEQRES 32 D 501 ASP SER ASN TYR HIS LEU LEU MET SER VAL GLN GLU SER
SEQRES 33 D 501 LEU GLU ARG LYS PHE GLY LYS HIS GLY GLY THR ILE PRO
SEQRES 34 D 501 ILE VAL PRO THR ALA GLU PHE GLN ASP ARG ILE SER GLY
SEQRES 35 D 501 ALA SER GLU LYS ASP ILE VAL HIS SER GLY LEU ALA TYR
SEQRES 36 D 501 THR MET GLU ARG SER ALA ARG GLN ILE MET ARG THR ALA
SEQRES 37 D 501 MET LYS TYR ASN LEU GLY LEU ASP LEU ARG THR ALA ALA
SEQRES 38 D 501 TYR VAL ASN ALA ILE GLU LYS VAL PHE ARG VAL TYR ASN
SEQRES 39 D 501 GLU ALA GLY VAL THR PHE THR
SEQRES 1 E 501 ALA ASP ARG GLU ASP ASP PRO ASN PHE PHE LYS MET VAL
SEQRES 2 E 501 GLU GLY PHE PHE ASP ARG GLY ALA SER ILE VAL GLU ASP
SEQRES 3 E 501 LYS LEU VAL GLU ASP LEU LYS THR ARG GLU THR GLU GLU
SEQRES 4 E 501 GLN LYS ARG ASN ARG VAL ARG SER ILE LEU ARG ILE ILE
SEQRES 5 E 501 LYS PRO CYS ASN HIS VAL LEU SER LEU SER PHE PRO ILE
SEQRES 6 E 501 ARG ARG ASP ASP GLY SER TRP GLU VAL ILE GLU GLY TYR
SEQRES 7 E 501 ARG ALA GLN HIS SER GLN HIS ARG THR PRO CYS LYS GLY
SEQRES 8 E 501 GLY ILE ARG TYR SER THR ASP VAL SER VAL ASP GLU VAL
SEQRES 9 E 501 LYS ALA LEU ALA SER LEU MET THR TYR LYS CYS ALA VAL
SEQRES 10 E 501 VAL ASP VAL PRO PHE GLY GLY ALA LYS ALA GLY VAL LYS
SEQRES 11 E 501 ILE ASN PRO LYS ASN TYR THR ASP ASN GLU LEU GLU LYS
SEQRES 12 E 501 ILE THR ARG ARG PHE THR MET GLU LEU ALA LYS LYS GLY
SEQRES 13 E 501 PHE ILE GLY PRO GLY VAL ASP VAL PRO ALA PRO ASP MET
SEQRES 14 E 501 SER THR GLY GLU ARG GLU MET SER TRP ILE ALA ASP THR
SEQRES 15 E 501 TYR ALA SER THR ILE GLY HIS TYR ASP ILE ASN ALA HIS
SEQRES 16 E 501 ALA CYS VAL THR GLY LYS PRO ILE SER GLN GLY GLY ILE
SEQRES 17 E 501 HIS GLY ARG ILE SER ALA THR GLY ARG GLY VAL PHE HIS
SEQRES 18 E 501 GLY ILE GLU ASN PHE ILE ASN GLU ALA SER TYR MET SER
SEQRES 19 E 501 ILE LEU GLY MET THR PRO GLY PHE GLY ASP LYS THR PHE
SEQRES 20 E 501 VAL VAL GLN GLY PHE GLY ASN VAL GLY LEU HIS SER MET
SEQRES 21 E 501 ARG TYR LEU HIS ARG PHE GLY ALA LYS CYS ILE THR VAL
SEQRES 22 E 501 GLY GLU SER ASP GLY SER ILE TRP ASN PRO ASP GLY ILE
SEQRES 23 E 501 ASP PRO LYS GLU LEU GLU ASP PHE LYS LEU GLN HIS GLY
SEQRES 24 E 501 THR ILE LEU GLY PHE PRO LYS ALA LYS ILE TYR GLU GLY
SEQRES 25 E 501 SER ILE LEU GLU VAL ASP CYS ASP ILE LEU ILE PRO ALA
SEQRES 26 E 501 ALA SER GLU LYS GLN LEU THR LYS SER ASN ALA PRO ARG
SEQRES 27 E 501 VAL LYS ALA LYS ILE ILE ALA GLU GLY ALA ASN GLY PRO
SEQRES 28 E 501 THR THR PRO GLU ALA ASP LYS ILE PHE LEU GLU ARG ASN
SEQRES 29 E 501 ILE MET VAL ILE PRO ASP LEU TYR LEU ASN ALA GLY GLY
SEQRES 30 E 501 VAL THR VAL SER TYR PHE GLU TRP LEU ASN ASN LEU ASN
SEQRES 31 E 501 HIS VAL SER TYR GLY ARG LEU THR PHE LYS TYR GLU ARG
SEQRES 32 E 501 ASP SER ASN TYR HIS LEU LEU MET SER VAL GLN GLU SER
SEQRES 33 E 501 LEU GLU ARG LYS PHE GLY LYS HIS GLY GLY THR ILE PRO
SEQRES 34 E 501 ILE VAL PRO THR ALA GLU PHE GLN ASP ARG ILE SER GLY
SEQRES 35 E 501 ALA SER GLU LYS ASP ILE VAL HIS SER GLY LEU ALA TYR
SEQRES 36 E 501 THR MET GLU ARG SER ALA ARG GLN ILE MET ARG THR ALA
SEQRES 37 E 501 MET LYS TYR ASN LEU GLY LEU ASP LEU ARG THR ALA ALA
SEQRES 38 E 501 TYR VAL ASN ALA ILE GLU LYS VAL PHE ARG VAL TYR ASN
SEQRES 39 E 501 GLU ALA GLY VAL THR PHE THR
SEQRES 1 F 501 ALA ASP ARG GLU ASP ASP PRO ASN PHE PHE LYS MET VAL
SEQRES 2 F 501 GLU GLY PHE PHE ASP ARG GLY ALA SER ILE VAL GLU ASP
SEQRES 3 F 501 LYS LEU VAL GLU ASP LEU LYS THR ARG GLU THR GLU GLU
SEQRES 4 F 501 GLN LYS ARG ASN ARG VAL ARG SER ILE LEU ARG ILE ILE
SEQRES 5 F 501 LYS PRO CYS ASN HIS VAL LEU SER LEU SER PHE PRO ILE
SEQRES 6 F 501 ARG ARG ASP ASP GLY SER TRP GLU VAL ILE GLU GLY TYR
SEQRES 7 F 501 ARG ALA GLN HIS SER GLN HIS ARG THR PRO CYS LYS GLY
SEQRES 8 F 501 GLY ILE ARG TYR SER THR ASP VAL SER VAL ASP GLU VAL
SEQRES 9 F 501 LYS ALA LEU ALA SER LEU MET THR TYR LYS CYS ALA VAL
SEQRES 10 F 501 VAL ASP VAL PRO PHE GLY GLY ALA LYS ALA GLY VAL LYS
SEQRES 11 F 501 ILE ASN PRO LYS ASN TYR THR ASP ASN GLU LEU GLU LYS
SEQRES 12 F 501 ILE THR ARG ARG PHE THR MET GLU LEU ALA LYS LYS GLY
SEQRES 13 F 501 PHE ILE GLY PRO GLY VAL ASP VAL PRO ALA PRO ASP MET
SEQRES 14 F 501 SER THR GLY GLU ARG GLU MET SER TRP ILE ALA ASP THR
SEQRES 15 F 501 TYR ALA SER THR ILE GLY HIS TYR ASP ILE ASN ALA HIS
SEQRES 16 F 501 ALA CYS VAL THR GLY LYS PRO ILE SER GLN GLY GLY ILE
SEQRES 17 F 501 HIS GLY ARG ILE SER ALA THR GLY ARG GLY VAL PHE HIS
SEQRES 18 F 501 GLY ILE GLU ASN PHE ILE ASN GLU ALA SER TYR MET SER
SEQRES 19 F 501 ILE LEU GLY MET THR PRO GLY PHE GLY ASP LYS THR PHE
SEQRES 20 F 501 VAL VAL GLN GLY PHE GLY ASN VAL GLY LEU HIS SER MET
SEQRES 21 F 501 ARG TYR LEU HIS ARG PHE GLY ALA LYS CYS ILE THR VAL
SEQRES 22 F 501 GLY GLU SER ASP GLY SER ILE TRP ASN PRO ASP GLY ILE
SEQRES 23 F 501 ASP PRO LYS GLU LEU GLU ASP PHE LYS LEU GLN HIS GLY
SEQRES 24 F 501 THR ILE LEU GLY PHE PRO LYS ALA LYS ILE TYR GLU GLY
SEQRES 25 F 501 SER ILE LEU GLU VAL ASP CYS ASP ILE LEU ILE PRO ALA
SEQRES 26 F 501 ALA SER GLU LYS GLN LEU THR LYS SER ASN ALA PRO ARG
SEQRES 27 F 501 VAL LYS ALA LYS ILE ILE ALA GLU GLY ALA ASN GLY PRO
SEQRES 28 F 501 THR THR PRO GLU ALA ASP LYS ILE PHE LEU GLU ARG ASN
SEQRES 29 F 501 ILE MET VAL ILE PRO ASP LEU TYR LEU ASN ALA GLY GLY
SEQRES 30 F 501 VAL THR VAL SER TYR PHE GLU TRP LEU ASN ASN LEU ASN
SEQRES 31 F 501 HIS VAL SER TYR GLY ARG LEU THR PHE LYS TYR GLU ARG
SEQRES 32 F 501 ASP SER ASN TYR HIS LEU LEU MET SER VAL GLN GLU SER
SEQRES 33 F 501 LEU GLU ARG LYS PHE GLY LYS HIS GLY GLY THR ILE PRO
SEQRES 34 F 501 ILE VAL PRO THR ALA GLU PHE GLN ASP ARG ILE SER GLY
SEQRES 35 F 501 ALA SER GLU LYS ASP ILE VAL HIS SER GLY LEU ALA TYR
SEQRES 36 F 501 THR MET GLU ARG SER ALA ARG GLN ILE MET ARG THR ALA
SEQRES 37 F 501 MET LYS TYR ASN LEU GLY LEU ASP LEU ARG THR ALA ALA
SEQRES 38 F 501 TYR VAL ASN ALA ILE GLU LYS VAL PHE ARG VAL TYR ASN
SEQRES 39 F 501 GLU ALA GLY VAL THR PHE THR
HET NAI A 601 44
HET GTP A 602 32
HET NAI A 603 44
HET NAI B 602 44
HET GTP B 603 32
HET NAI B 601 44
HET NAI C 601 44
HET NAI C 602 44
HET GTP C 603 32
HET NAI D 601 44
HET GTP D 602 32
HET NAI D 603 44
HET NAI E 602 44
HET GTP E 603 32
HET NAI E 601 44
HET NAI F 601 44
HET NAI F 602 44
HET GTP F 603 32
HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETSYN NAI NADH
FORMUL 7 NAI 12(C21 H29 N7 O14 P2)
FORMUL 8 GTP 6(C10 H16 N5 O14 P3)
HELIX 1 1 ASN A 8 GLU A 30 1 23
HELIX 2 2 THR A 37 LYS A 53 1 17
HELIX 3 3 SER A 100 VAL A 118 1 19
HELIX 4 4 ASN A 139 LYS A 155 1 17
HELIX 5 5 GLY A 172 ILE A 187 1 16
HELIX 6 6 ASN A 193 VAL A 198 5 6
HELIX 7 7 PRO A 202 GLY A 206 5 5
HELIX 8 8 SER A 213 ASN A 228 1 16
HELIX 9 9 GLU A 229 GLY A 237 1 9
HELIX 10 10 GLY A 253 ARG A 265 1 13
HELIX 11 11 ASP A 287 HIS A 298 1 12
HELIX 12 12 SER A 313 VAL A 317 5 5
HELIX 13 13 ASN A 335 VAL A 339 5 5
HELIX 14 14 THR A 353 ARG A 363 1 11
HELIX 15 15 PRO A 369 ASN A 374 1 6
HELIX 16 16 ASN A 374 ASN A 388 1 15
HELIX 17 17 GLY A 395 LEU A 397 5 3
HELIX 18 18 THR A 398 PHE A 421 1 24
HELIX 19 19 GLY A 422 GLY A 425 5 4
HELIX 20 20 THR A 433 ARG A 439 1 7
HELIX 21 21 SER A 444 TYR A 471 1 28
HELIX 22 22 ASP A 476 ALA A 496 1 21
HELIX 23 23 ASN B 8 GLU B 30 1 23
HELIX 24 24 THR B 37 LYS B 53 1 17
HELIX 25 25 SER B 100 VAL B 118 1 19
HELIX 26 26 ASN B 139 LYS B 155 1 17
HELIX 27 27 GLY B 172 ILE B 187 1 16
HELIX 28 28 ASN B 193 VAL B 198 5 6
HELIX 29 29 PRO B 202 GLY B 206 5 5
HELIX 30 30 SER B 213 ASN B 228 1 16
HELIX 31 31 GLU B 229 GLY B 237 1 9
HELIX 32 32 GLY B 253 ARG B 265 1 13
HELIX 33 33 ASP B 287 HIS B 298 1 12
HELIX 34 34 SER B 313 VAL B 317 5 5
HELIX 35 35 ASN B 335 VAL B 339 5 5
HELIX 36 36 THR B 353 ARG B 363 1 11
HELIX 37 37 PRO B 369 ASN B 374 1 6
HELIX 38 38 ASN B 374 ASN B 388 1 15
HELIX 39 39 GLY B 395 LEU B 397 5 3
HELIX 40 40 THR B 398 PHE B 421 1 24
HELIX 41 41 GLY B 422 GLY B 425 5 4
HELIX 42 42 THR B 433 ARG B 439 1 7
HELIX 43 43 SER B 444 TYR B 471 1 28
HELIX 44 44 ASP B 476 ALA B 496 1 21
HELIX 45 45 ASN C 8 GLU C 30 1 23
HELIX 46 46 THR C 37 LYS C 53 1 17
HELIX 47 47 SER C 100 VAL C 118 1 19
HELIX 48 48 ASN C 139 LYS C 155 1 17
HELIX 49 49 GLY C 172 ILE C 187 1 16
HELIX 50 50 ASN C 193 VAL C 198 5 6
HELIX 51 51 PRO C 202 GLY C 206 5 5
HELIX 52 52 SER C 213 ASN C 228 1 16
HELIX 53 53 GLU C 229 GLY C 237 1 9
HELIX 54 54 GLY C 253 ARG C 265 1 13
HELIX 55 55 ASP C 287 HIS C 298 1 12
HELIX 56 56 SER C 313 VAL C 317 5 5
HELIX 57 57 ASN C 335 VAL C 339 5 5
HELIX 58 58 THR C 353 ARG C 363 1 11
HELIX 59 59 PRO C 369 ASN C 374 1 6
HELIX 60 60 ASN C 374 ASN C 388 1 15
HELIX 61 61 GLY C 395 LEU C 397 5 3
HELIX 62 62 THR C 398 PHE C 421 1 24
HELIX 63 63 GLY C 422 GLY C 425 5 4
HELIX 64 64 THR C 433 ARG C 439 1 7
HELIX 65 65 SER C 444 TYR C 471 1 28
HELIX 66 66 ASP C 476 ALA C 496 1 21
HELIX 67 67 ASN D 8 GLU D 30 1 23
HELIX 68 68 THR D 37 LYS D 53 1 17
HELIX 69 69 SER D 100 VAL D 118 1 19
HELIX 70 70 ASN D 139 LYS D 155 1 17
HELIX 71 71 GLY D 172 ILE D 187 1 16
HELIX 72 72 ASN D 193 VAL D 198 5 6
HELIX 73 73 PRO D 202 GLY D 206 5 5
HELIX 74 74 SER D 213 ASN D 228 1 16
HELIX 75 75 GLU D 229 GLY D 237 1 9
HELIX 76 76 GLY D 253 ARG D 265 1 13
HELIX 77 77 ASP D 287 HIS D 298 1 12
HELIX 78 78 SER D 313 VAL D 317 5 5
HELIX 79 79 ASN D 335 VAL D 339 5 5
HELIX 80 80 THR D 353 ARG D 363 1 11
HELIX 81 81 PRO D 369 ASN D 374 1 6
HELIX 82 82 ASN D 374 ASN D 388 1 15
HELIX 83 83 GLY D 395 LEU D 397 5 3
HELIX 84 84 THR D 398 PHE D 421 1 24
HELIX 85 85 GLY D 422 GLY D 425 5 4
HELIX 86 86 THR D 433 ARG D 439 1 7
HELIX 87 87 SER D 444 TYR D 471 1 28
HELIX 88 88 ASP D 476 ALA D 496 1 21
HELIX 89 89 ASN E 8 GLU E 30 1 23
HELIX 90 90 THR E 37 LYS E 53 1 17
HELIX 91 91 SER E 100 VAL E 118 1 19
HELIX 92 92 ASN E 139 LYS E 155 1 17
HELIX 93 93 GLY E 172 ILE E 187 1 16
HELIX 94 94 ASN E 193 VAL E 198 5 6
HELIX 95 95 PRO E 202 GLY E 206 5 5
HELIX 96 96 SER E 213 ASN E 228 1 16
HELIX 97 97 GLU E 229 GLY E 237 1 9
HELIX 98 98 GLY E 253 ARG E 265 1 13
HELIX 99 99 ASP E 287 HIS E 298 1 12
HELIX 100 100 SER E 313 VAL E 317 5 5
HELIX 101 101 ASN E 335 VAL E 339 5 5
HELIX 102 102 THR E 353 ARG E 363 1 11
HELIX 103 103 PRO E 369 ASN E 374 1 6
HELIX 104 104 ASN E 374 ASN E 388 1 15
HELIX 105 105 GLY E 395 LEU E 397 5 3
HELIX 106 106 THR E 398 PHE E 421 1 24
HELIX 107 107 GLY E 422 GLY E 425 5 4
HELIX 108 108 THR E 433 ARG E 439 1 7
HELIX 109 109 SER E 444 TYR E 471 1 28
HELIX 110 110 ASP E 476 ALA E 496 1 21
HELIX 111 111 ASN F 8 GLU F 30 1 23
HELIX 112 112 THR F 37 LYS F 53 1 17
HELIX 113 113 SER F 100 VAL F 118 1 19
HELIX 114 114 ASN F 139 LYS F 155 1 17
HELIX 115 115 GLY F 172 ILE F 187 1 16
HELIX 116 116 ASN F 193 VAL F 198 5 6
HELIX 117 117 PRO F 202 GLY F 206 5 5
HELIX 118 118 SER F 213 ASN F 228 1 16
HELIX 119 119 GLU F 229 GLY F 237 1 9
HELIX 120 120 GLY F 253 ARG F 265 1 13
HELIX 121 121 ASP F 287 HIS F 298 1 12
HELIX 122 122 SER F 313 VAL F 317 5 5
HELIX 123 123 ASN F 335 VAL F 339 5 5
HELIX 124 124 THR F 353 ARG F 363 1 11
HELIX 125 125 PRO F 369 ASN F 374 1 6
HELIX 126 126 ASN F 374 ASN F 388 1 15
HELIX 127 127 GLY F 395 LEU F 397 5 3
HELIX 128 128 THR F 398 PHE F 421 1 24
HELIX 129 129 GLY F 422 GLY F 425 5 4
HELIX 130 130 THR F 433 ARG F 439 1 7
HELIX 131 131 SER F 444 TYR F 471 1 28
HELIX 132 132 ASP F 476 ALA F 496 1 21
SHEET 1 A 5 HIS A 57 SER A 60 0
SHEET 2 A 5 GLY A 77 GLN A 81 -1 O GLN A 81 N HIS A 57
SHEET 3 A 5 GLY A 123 VAL A 129 -1 O LYS A 126 N ALA A 80
SHEET 4 A 5 CYS A 89 TYR A 95 1 N ARG A 94 O ALA A 127
SHEET 5 A 5 ASP A 163 ALA A 166 1 O VAL A 164 N CYS A 89
SHEET 1 B 2 ILE A 65 ARG A 66 0
SHEET 2 B 2 TRP A 72 GLU A 73 -1 O GLU A 73 N ILE A 65
SHEET 1 C 4 THR A 246 GLN A 250 0
SHEET 2 C 4 LYS A 269 GLY A 274 1 O ILE A 271 N PHE A 247
SHEET 3 C 4 SER A 279 TRP A 281 -1 O ILE A 280 N VAL A 273
SHEET 4 C 4 LYS A 308 TYR A 310 -1 O LYS A 308 N TRP A 281
SHEET 1 D 3 ILE A 321 LEU A 322 0
SHEET 2 D 3 ILE A 343 ILE A 344 1 O ILE A 343 N LEU A 322
SHEET 3 D 3 MET A 366 VAL A 367 1 O MET A 366 N ILE A 344
SHEET 1 E 5 HIS B 57 SER B 60 0
SHEET 2 E 5 GLY B 77 GLN B 81 -1 O GLN B 81 N HIS B 57
SHEET 3 E 5 GLY B 123 VAL B 129 -1 O LYS B 126 N ALA B 80
SHEET 4 E 5 CYS B 89 TYR B 95 1 N ARG B 94 O ALA B 127
SHEET 5 E 5 ASP B 163 ALA B 166 1 O VAL B 164 N CYS B 89
SHEET 1 F 2 ILE B 65 ARG B 66 0
SHEET 2 F 2 TRP B 72 GLU B 73 -1 O GLU B 73 N ILE B 65
SHEET 1 G 4 THR B 246 GLN B 250 0
SHEET 2 G 4 LYS B 269 GLY B 274 1 O ILE B 271 N PHE B 247
SHEET 3 G 4 SER B 279 TRP B 281 -1 O ILE B 280 N VAL B 273
SHEET 4 G 4 LYS B 308 TYR B 310 -1 O LYS B 308 N TRP B 281
SHEET 1 H 3 ILE B 321 LEU B 322 0
SHEET 2 H 3 ILE B 343 ILE B 344 1 O ILE B 343 N LEU B 322
SHEET 3 H 3 MET B 366 VAL B 367 1 O MET B 366 N ILE B 344
SHEET 1 I 5 HIS C 57 SER C 60 0
SHEET 2 I 5 GLY C 77 GLN C 81 -1 O GLN C 81 N HIS C 57
SHEET 3 I 5 GLY C 123 VAL C 129 -1 O LYS C 126 N ALA C 80
SHEET 4 I 5 CYS C 89 TYR C 95 1 N ARG C 94 O ALA C 127
SHEET 5 I 5 ASP C 163 ALA C 166 1 O VAL C 164 N CYS C 89
SHEET 1 J 2 ILE C 65 ARG C 66 0
SHEET 2 J 2 TRP C 72 GLU C 73 -1 O GLU C 73 N ILE C 65
SHEET 1 K 4 THR C 246 GLN C 250 0
SHEET 2 K 4 LYS C 269 GLY C 274 1 O ILE C 271 N PHE C 247
SHEET 3 K 4 SER C 279 TRP C 281 -1 O ILE C 280 N VAL C 273
SHEET 4 K 4 LYS C 308 TYR C 310 -1 O LYS C 308 N TRP C 281
SHEET 1 L 3 ILE C 321 LEU C 322 0
SHEET 2 L 3 ILE C 343 ILE C 344 1 O ILE C 343 N LEU C 322
SHEET 3 L 3 MET C 366 VAL C 367 1 O MET C 366 N ILE C 344
SHEET 1 M 5 HIS D 57 SER D 60 0
SHEET 2 M 5 GLY D 77 GLN D 81 -1 O GLN D 81 N HIS D 57
SHEET 3 M 5 GLY D 123 VAL D 129 -1 O LYS D 126 N ALA D 80
SHEET 4 M 5 CYS D 89 TYR D 95 1 N ARG D 94 O ALA D 127
SHEET 5 M 5 ASP D 163 ALA D 166 1 O VAL D 164 N CYS D 89
SHEET 1 N 2 ILE D 65 ARG D 66 0
SHEET 2 N 2 TRP D 72 GLU D 73 -1 O GLU D 73 N ILE D 65
SHEET 1 O 4 THR D 246 GLN D 250 0
SHEET 2 O 4 LYS D 269 GLY D 274 1 O ILE D 271 N PHE D 247
SHEET 3 O 4 SER D 279 TRP D 281 -1 O ILE D 280 N VAL D 273
SHEET 4 O 4 LYS D 308 TYR D 310 -1 O LYS D 308 N TRP D 281
SHEET 1 P 3 ILE D 321 LEU D 322 0
SHEET 2 P 3 ILE D 343 ILE D 344 1 O ILE D 343 N LEU D 322
SHEET 3 P 3 MET D 366 VAL D 367 1 O MET D 366 N ILE D 344
SHEET 1 Q 5 HIS E 57 SER E 60 0
SHEET 2 Q 5 GLY E 77 GLN E 81 -1 O GLN E 81 N HIS E 57
SHEET 3 Q 5 GLY E 123 VAL E 129 -1 O LYS E 126 N ALA E 80
SHEET 4 Q 5 CYS E 89 TYR E 95 1 N ARG E 94 O ALA E 127
SHEET 5 Q 5 ASP E 163 ALA E 166 1 O VAL E 164 N CYS E 89
SHEET 1 R 2 ILE E 65 ARG E 66 0
SHEET 2 R 2 TRP E 72 GLU E 73 -1 O GLU E 73 N ILE E 65
SHEET 1 S 4 THR E 246 GLN E 250 0
SHEET 2 S 4 LYS E 269 GLY E 274 1 O ILE E 271 N PHE E 247
SHEET 3 S 4 SER E 279 TRP E 281 -1 O ILE E 280 N VAL E 273
SHEET 4 S 4 LYS E 308 TYR E 310 -1 O LYS E 308 N TRP E 281
SHEET 1 T 3 ILE E 321 LEU E 322 0
SHEET 2 T 3 ILE E 343 ILE E 344 1 O ILE E 343 N LEU E 322
SHEET 3 T 3 MET E 366 VAL E 367 1 O MET E 366 N ILE E 344
SHEET 1 U 5 HIS F 57 SER F 60 0
SHEET 2 U 5 GLY F 77 GLN F 81 -1 O GLN F 81 N HIS F 57
SHEET 3 U 5 GLY F 123 VAL F 129 -1 O LYS F 126 N ALA F 80
SHEET 4 U 5 CYS F 89 TYR F 95 1 N ARG F 94 O ALA F 127
SHEET 5 U 5 ASP F 163 ALA F 166 1 O VAL F 164 N CYS F 89
SHEET 1 V 2 ILE F 65 ARG F 66 0
SHEET 2 V 2 TRP F 72 GLU F 73 -1 O GLU F 73 N ILE F 65
SHEET 1 W 4 THR F 246 GLN F 250 0
SHEET 2 W 4 LYS F 269 GLY F 274 1 O ILE F 271 N PHE F 247
SHEET 3 W 4 SER F 279 TRP F 281 -1 O ILE F 280 N VAL F 273
SHEET 4 W 4 LYS F 308 TYR F 310 -1 O LYS F 308 N TRP F 281
SHEET 1 X 3 ILE F 321 LEU F 322 0
SHEET 2 X 3 ILE F 343 ILE F 344 1 O ILE F 343 N LEU F 322
SHEET 3 X 3 MET F 366 VAL F 367 1 O MET F 366 N ILE F 344
CISPEP 1 THR A 87 PRO A 88 0 0.57
CISPEP 2 THR B 87 PRO B 88 0 0.64
CISPEP 3 THR C 87 PRO C 88 0 0.71
CISPEP 4 THR D 87 PRO D 88 0 0.62
CISPEP 5 THR E 87 PRO E 88 0 0.64
CISPEP 6 THR F 87 PRO F 88 0 0.53
SITE 1 AC1 16 ARG A 94 ASP A 168 MET A 169 SER A 170
SITE 2 AC1 16 THR A 215 GLN A 250 GLY A 251 GLY A 253
SITE 3 AC1 16 ASN A 254 VAL A 255 GLU A 275 SER A 276
SITE 4 AC1 16 ALA A 325 ALA A 326 GLY A 347 ASN A 349
SITE 1 AC2 7 HIS A 209 SER A 213 ARG A 261 TYR A 262
SITE 2 AC2 7 ARG A 265 GLU A 292 HIS A 450
SITE 1 AC3 17 HIS A 195 GLN A 205 GLY A 206 ASN A 387
SITE 2 AC3 17 ASN A 388 HIS A 391 VAL A 392 SER A 393
SITE 3 AC3 17 GLU A 445 HIS C 85 ARG C 86 THR C 87
SITE 4 AC3 17 CYS C 115 ASP C 119 VAL C 120 PRO C 121
SITE 5 AC3 17 LYS C 488
SITE 1 AC4 17 HIS A 85 ARG A 86 THR A 87 CYS A 115
SITE 2 AC4 17 ASP A 119 VAL A 120 PRO A 121 LYS A 488
SITE 3 AC4 17 HIS B 195 GLN B 205 GLY B 206 ASN B 387
SITE 4 AC4 17 ASN B 388 HIS B 391 VAL B 392 SER B 393
SITE 5 AC4 17 GLU B 445
SITE 1 AC5 16 ARG B 94 ASP B 168 MET B 169 SER B 170
SITE 2 AC5 16 THR B 215 GLN B 250 GLY B 251 GLY B 253
SITE 3 AC5 16 ASN B 254 VAL B 255 GLU B 275 SER B 276
SITE 4 AC5 16 ALA B 325 ALA B 326 GLY B 347 ASN B 349
SITE 1 AC6 7 HIS B 209 SER B 213 ARG B 261 TYR B 262
SITE 2 AC6 7 ARG B 265 GLU B 292 HIS B 450
SITE 1 AC7 17 HIS B 85 ARG B 86 THR B 87 CYS B 115
SITE 2 AC7 17 ASP B 119 VAL B 120 PRO B 121 LYS B 488
SITE 3 AC7 17 HIS C 195 GLN C 205 GLY C 206 ASN C 387
SITE 4 AC7 17 ASN C 388 HIS C 391 VAL C 392 SER C 393
SITE 5 AC7 17 GLU C 445
SITE 1 AC8 17 ARG C 94 ASP C 168 MET C 169 SER C 170
SITE 2 AC8 17 THR C 215 GLN C 250 GLY C 251 GLY C 253
SITE 3 AC8 17 ASN C 254 VAL C 255 GLU C 275 SER C 276
SITE 4 AC8 17 ALA C 325 ALA C 326 GLY C 347 ASN C 349
SITE 5 AC8 17 ASN C 374
SITE 1 AC9 7 HIS C 209 SER C 213 ARG C 261 TYR C 262
SITE 2 AC9 7 ARG C 265 GLU C 292 HIS C 450
SITE 1 BC1 16 ARG D 94 ASP D 168 MET D 169 SER D 170
SITE 2 BC1 16 THR D 215 GLN D 250 GLY D 251 GLY D 253
SITE 3 BC1 16 ASN D 254 VAL D 255 GLU D 275 SER D 276
SITE 4 BC1 16 ALA D 325 ALA D 326 GLY D 347 ASN D 349
SITE 1 BC2 7 HIS D 209 SER D 213 ARG D 261 TYR D 262
SITE 2 BC2 7 ARG D 265 GLU D 292 HIS D 450
SITE 1 BC3 17 HIS D 195 GLN D 205 GLY D 206 ASN D 387
SITE 2 BC3 17 ASN D 388 HIS D 391 VAL D 392 SER D 393
SITE 3 BC3 17 GLU D 445 HIS F 85 ARG F 86 THR F 87
SITE 4 BC3 17 CYS F 115 ASP F 119 VAL F 120 PRO F 121
SITE 5 BC3 17 LYS F 488
SITE 1 BC4 17 HIS D 85 ARG D 86 THR D 87 CYS D 115
SITE 2 BC4 17 ASP D 119 VAL D 120 PRO D 121 LYS D 488
SITE 3 BC4 17 HIS E 195 GLN E 205 GLY E 206 ASN E 387
SITE 4 BC4 17 ASN E 388 HIS E 391 VAL E 392 SER E 393
SITE 5 BC4 17 GLU E 445
SITE 1 BC5 16 ARG E 94 ASP E 168 MET E 169 SER E 170
SITE 2 BC5 16 THR E 215 GLN E 250 GLY E 251 GLY E 253
SITE 3 BC5 16 ASN E 254 VAL E 255 GLU E 275 SER E 276
SITE 4 BC5 16 ALA E 325 ALA E 326 GLY E 347 ASN E 349
SITE 1 BC6 7 HIS E 209 SER E 213 ARG E 261 TYR E 262
SITE 2 BC6 7 ARG E 265 GLU E 292 HIS E 450
SITE 1 BC7 17 HIS E 85 ARG E 86 THR E 87 CYS E 115
SITE 2 BC7 17 ASP E 119 VAL E 120 PRO E 121 LYS E 488
SITE 3 BC7 17 HIS F 195 GLN F 205 GLY F 206 ASN F 387
SITE 4 BC7 17 ASN F 388 HIS F 391 VAL F 392 SER F 393
SITE 5 BC7 17 GLU F 445
SITE 1 BC8 17 ARG F 94 ASP F 168 MET F 169 SER F 170
SITE 2 BC8 17 THR F 215 GLN F 250 GLY F 251 GLY F 253
SITE 3 BC8 17 ASN F 254 VAL F 255 GLU F 275 SER F 276
SITE 4 BC8 17 ALA F 325 ALA F 326 GLY F 347 ASN F 349
SITE 5 BC8 17 ASN F 374
SITE 1 BC9 7 HIS F 209 SER F 213 ARG F 261 TYR F 262
SITE 2 BC9 7 ARG F 265 GLU F 292 HIS F 450
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
