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HEADER HYDROLASE 04-APR-14 4Q1V
TITLE CRYSTAL STRUCTURE OF A PUTATIVE DIPEPTIDYL AMINOPEPTIDASE IV
TITLE 2 (BACOVA_01349) FROM BACTEROIDES OVATUS ATCC 8483 AT 2.48 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIPEPTIDYL AMINOPEPTIDASE IV;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PEPTIDASE, S9A/B/C FAMILY, CATALYTIC DOMAIN PROTEIN;
COMPND 5 EC: 3.4.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES OVATUS;
SOURCE 3 ORGANISM_TAXID: 411476;
SOURCE 4 STRAIN: ATCC 8483;
SOURCE 5 GENE: BACOVA_01349, ZP_02064383.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS TWO DOMAIN PROTEIN, DIPEPTIDYL-PEPTIDASE IV FAMILY (PF00930), PROLYL
KEYWDS 2 OLIGOPEPTIDASE FAMILY (PF00326), STRUCTURAL GENOMICS, JOINT CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 4 BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 07-MAY-14 4Q1V 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE DIPEPTIDYL AMINOPEPTIDASE IV
JRNL TITL 2 (BACOVA_01349) FROM BACTEROIDES OVATUS ATCC 8483 AT 2.48 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 70548
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3561
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.54
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5125
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1981
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4886
REMARK 3 BIN R VALUE (WORKING SET) : 0.1958
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.66
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 239
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11272
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 641
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.64940
REMARK 3 B22 (A**2) : -4.79360
REMARK 3 B33 (A**2) : 2.14420
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.260
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 11748 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 15965 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5360 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 314 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1718 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 11748 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1485 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 13169 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.65
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.84
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Q1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085499.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : VERTICAL FOCUSING MIRROR; DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70624
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 49.304
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.15200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.91900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD,SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10.0% POLYETHYLENE GLYCOL 6000, 0.1M
REMARK 280 MES PH 6.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 46.24350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.56350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.85150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.56350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.24350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.85150
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: 5200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 GLY A 0
REMARK 465 GLN A 24
REMARK 465 GLU A 25
REMARK 465 GLY B 0
REMARK 465 GLN B 24
REMARK 465 GLU B 25
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 290 CE
REMARK 470 ALA A 508 CB
REMARK 470 LYS A 509 CE NZ
REMARK 470 LYS A 667 NZ
REMARK 470 GLU B 470 CD OE1 OE2
REMARK 470 LYS B 667 CE NZ
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 ASP A 157 -116.49 62.23
REMARK 500 ASN A 163 -119.58 60.24
REMARK 500 LYS A 312 -82.08 -86.62
REMARK 500 ALA A 464 142.58 -170.34
REMARK 500 TYR A 518 -78.99 -123.03
REMARK 500 ARG A 570 55.62 -143.48
REMARK 500 SER A 603 -111.45 70.24
REMARK 500 ASP A 645 -155.07 60.81
REMARK 500 LYS A 709 -158.46 -84.86
REMARK 500 VAL B 78 -63.98 -101.47
REMARK 500 ASP B 157 -117.00 60.83
REMARK 500 ASN B 163 -119.47 61.38
REMARK 500 LYS B 312 -82.37 -88.67
REMARK 500 TYR B 518 -78.93 -123.31
REMARK 500 ARG B 570 47.35 -141.55
REMARK 500 SER B 603 -111.63 71.33
REMARK 500 ASP B 645 -155.14 60.89
REMARK 500 LYS B 709 -159.41 -84.40
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 B 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1171 O
REMARK 620 2 HOH B1024 O 88.6
REMARK 620 3 ASP B 285 OD1 89.8 173.6
REMARK 620 4 ASP B 285 O 77.7 91.2 82.4
REMARK 620 5 ASP B 645 OD1 88.7 88.2 98.0 166.4
REMARK 620 6 HOH B1056 O 173.0 84.6 96.9 101.0 92.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 925 O
REMARK 620 2 ASP A 285 OD1 98.7
REMARK 620 3 HOH A 924 O 74.4 167.2
REMARK 620 4 ASP A 285 O 79.7 84.4 83.8
REMARK 620 5 HOH A1235 O 164.5 96.7 90.1 99.5
REMARK 620 6 ASP A 645 OD1 89.7 97.8 93.0 169.4 90.6
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 PEG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-420002 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 24-732 OF THE TARGET
REMARK 999 SEQUENCE.
DBREF 4Q1V A 24 732 UNP A7LU53 A7LU53_BACO1 24 732
DBREF 4Q1V B 24 732 UNP A7LU53 A7LU53_BACO1 24 732
SEQADV 4Q1V GLY A 0 UNP A7LU53 LEADER SEQUENCE
SEQADV 4Q1V GLY B 0 UNP A7LU53 LEADER SEQUENCE
SEQRES 1 A 710 GLY GLN GLU THR LYS LYS PRO THR LEU GLU GLU LEU ILE
SEQRES 2 A 710 PRO GLY GLY GLU SER TYR LEU TYR ALA GLU ASN LEU TYR
SEQRES 3 A 710 GLY LEU GLN TRP TRP GLY ASP GLU CYS ILE LYS PRO GLY
SEQRES 4 A 710 VAL ASP THR LEU TYR SER ILE GLN PRO LYS THR GLY LYS
SEQRES 5 A 710 GLU THR MSE VAL ILE THR ARG GLU GLN ILE ASN LYS VAL
SEQRES 6 A 710 LEU GLU GLU ASN LYS ALA GLY LYS LEU SER HIS LEU TYR
SEQRES 7 A 710 SER VAL ARG PHE PRO TRP THR ASP LYS ALA GLN MSE LEU
SEQRES 8 A 710 PHE THR ILE ALA GLY LYS PHE ILE VAL TYR ASN PHE LYS
SEQRES 9 A 710 ASN ASN GLN VAL VAL SER THR PHE LYS PRO LYS ASP GLY
SEQRES 10 A 710 ALA ASN ASN GLU ASP TYR CYS ALA ALA SER GLY ASN VAL
SEQRES 11 A 710 ALA TYR THR ILE ASP ASN ASN LEU TYR VAL ASN GLU LYS
SEQRES 12 A 710 ALA VAL THR ASN GLU PRO GLU GLY ILE VAL CYS GLY GLN
SEQRES 13 A 710 THR VAL HIS ARG ASN GLU PHE GLY ILE ASN LYS GLY THR
SEQRES 14 A 710 PHE TRP SER PRO LYS GLY ASN LEU LEU ALA PHE TYR ARG
SEQRES 15 A 710 MSE ASP GLU SER MSE VAL THR GLN TYR PRO LEU VAL ASP
SEQRES 16 A 710 ILE THR ALA ARG VAL GLY GLU VAL ASN ASN VAL ARG TYR
SEQRES 17 A 710 PRO MSE ALA GLY MSE THR SER HIS GLN VAL LYS VAL GLY
SEQRES 18 A 710 ILE TYR ASN PRO ALA THR GLY LYS SER ILE TYR LEU ASN
SEQRES 19 A 710 ALA GLY ASP PRO THR ASP ARG TYR PHE THR ASN ILE SER
SEQRES 20 A 710 TRP ALA PRO ASP GLU LYS SER LEU TYR LEU ILE GLU VAL
SEQRES 21 A 710 ASN ARG ASP GLN ASN HIS ALA LYS LEU CYS GLN TYR ASN
SEQRES 22 A 710 ALA GLU THR GLY GLU PRO MSE GLY VAL LEU TYR GLU GLU
SEQRES 23 A 710 MSE HIS PRO LYS TYR VAL GLU PRO GLN ASN PRO ILE VAL
SEQRES 24 A 710 PHE LEU PRO TRP ASP PRO THR LYS PHE ILE TYR GLN SER
SEQRES 25 A 710 GLN ARG ASP GLY TYR ASN HIS LEU TYR LEU PHE GLU THR
SEQRES 26 A 710 ASN ALA ALA ASN MSE LYS GLY GLU THR TYR ASN SER ALA
SEQRES 27 A 710 ASN GLY GLY SER TYR PHE GLN ALA GLY LYS VAL LYS GLN
SEQRES 28 A 710 LEU THR LYS GLY ASN TRP LEU VAL SER GLU ILE LEU GLY
SEQRES 29 A 710 PHE ASN THR LYS ARG LYS GLU VAL ILE PHE THR ALA VAL
SEQRES 30 A 710 GLU GLY LEU ARG SER GLY HIS PHE ALA VAL ASN VAL SER
SEQRES 31 A 710 ASN GLY LYS ILE SER GLN PRO PHE GLU ASN CYS LYS GLU
SEQRES 32 A 710 SER GLU HIS SER GLY THR LEU SER ALA SER GLY THR TYR
SEQRES 33 A 710 LEU ILE ASP ARG TYR SER THR LYS ASP GLN PRO ARG VAL
SEQRES 34 A 710 ILE ASN LEU VAL ASP THR LYS ASN PHE LYS GLU THR ALA
SEQRES 35 A 710 ASN LEU LEU THR ALA GLU ASN PRO TYR ASP GLY TYR GLN
SEQRES 36 A 710 MSE PRO SER ILE GLU THR GLY THR ILE LYS ALA ALA ASP
SEQRES 37 A 710 GLY THR THR ASP LEU HIS TYR ARG LEU MSE LYS PRO ALA
SEQRES 38 A 710 ASN PHE ASP PRO ALA LYS LYS TYR PRO VAL ILE VAL TYR
SEQRES 39 A 710 VAL TYR GLY GLY PRO HIS ALA GLN CYS VAL THR GLY GLY
SEQRES 40 A 710 TRP GLN ASN GLY ALA ARG GLY TRP ASP THR TYR MSE ALA
SEQRES 41 A 710 SER LYS GLY TYR ILE MSE PHE THR ILE ASP ASN ARG GLY
SEQRES 42 A 710 SER SER ASN ARG GLY LEU THR PHE GLU ASN ALA THR PHE
SEQRES 43 A 710 ARG ARG LEU GLY ILE GLU GLU GLY LYS ASP GLN VAL LYS
SEQRES 44 A 710 GLY VAL GLU PHE LEU LYS SER LEU PRO TYR VAL ASP SER
SEQRES 45 A 710 GLU ARG ILE GLY VAL HIS GLY TRP SER PHE GLY GLY HIS
SEQRES 46 A 710 MSE THR THR ALA LEU MSE LEU ARG TYR PRO GLU ILE PHE
SEQRES 47 A 710 LYS VAL GLY VAL ALA GLY GLY PRO VAL ILE ASP TRP GLY
SEQRES 48 A 710 TYR TYR GLU ILE MSE TYR GLY GLU ARG TYR MSE ASP THR
SEQRES 49 A 710 PRO GLU SER ASN PRO GLU GLY TYR LYS GLU CYS ASN LEU
SEQRES 50 A 710 LYS ASN LEU ALA ASP GLN LEU LYS GLY HIS LEU LEU ILE
SEQRES 51 A 710 ILE HIS ASP ASP HIS ASP ASP THR CYS VAL PRO GLN HIS
SEQRES 52 A 710 THR LEU SER PHE MSE LYS ALA CYS VAL ASP ALA ARG THR
SEQRES 53 A 710 TYR PRO ASP LEU PHE ILE TYR PRO CYS HIS LYS HIS ASN
SEQRES 54 A 710 VAL ALA GLY ARG ASP ARG VAL HIS LEU HIS GLU LYS ILE
SEQRES 55 A 710 THR ARG TYR PHE GLU GLN ASN LEU
SEQRES 1 B 710 GLY GLN GLU THR LYS LYS PRO THR LEU GLU GLU LEU ILE
SEQRES 2 B 710 PRO GLY GLY GLU SER TYR LEU TYR ALA GLU ASN LEU TYR
SEQRES 3 B 710 GLY LEU GLN TRP TRP GLY ASP GLU CYS ILE LYS PRO GLY
SEQRES 4 B 710 VAL ASP THR LEU TYR SER ILE GLN PRO LYS THR GLY LYS
SEQRES 5 B 710 GLU THR MSE VAL ILE THR ARG GLU GLN ILE ASN LYS VAL
SEQRES 6 B 710 LEU GLU GLU ASN LYS ALA GLY LYS LEU SER HIS LEU TYR
SEQRES 7 B 710 SER VAL ARG PHE PRO TRP THR ASP LYS ALA GLN MSE LEU
SEQRES 8 B 710 PHE THR ILE ALA GLY LYS PHE ILE VAL TYR ASN PHE LYS
SEQRES 9 B 710 ASN ASN GLN VAL VAL SER THR PHE LYS PRO LYS ASP GLY
SEQRES 10 B 710 ALA ASN ASN GLU ASP TYR CYS ALA ALA SER GLY ASN VAL
SEQRES 11 B 710 ALA TYR THR ILE ASP ASN ASN LEU TYR VAL ASN GLU LYS
SEQRES 12 B 710 ALA VAL THR ASN GLU PRO GLU GLY ILE VAL CYS GLY GLN
SEQRES 13 B 710 THR VAL HIS ARG ASN GLU PHE GLY ILE ASN LYS GLY THR
SEQRES 14 B 710 PHE TRP SER PRO LYS GLY ASN LEU LEU ALA PHE TYR ARG
SEQRES 15 B 710 MSE ASP GLU SER MSE VAL THR GLN TYR PRO LEU VAL ASP
SEQRES 16 B 710 ILE THR ALA ARG VAL GLY GLU VAL ASN ASN VAL ARG TYR
SEQRES 17 B 710 PRO MSE ALA GLY MSE THR SER HIS GLN VAL LYS VAL GLY
SEQRES 18 B 710 ILE TYR ASN PRO ALA THR GLY LYS SER ILE TYR LEU ASN
SEQRES 19 B 710 ALA GLY ASP PRO THR ASP ARG TYR PHE THR ASN ILE SER
SEQRES 20 B 710 TRP ALA PRO ASP GLU LYS SER LEU TYR LEU ILE GLU VAL
SEQRES 21 B 710 ASN ARG ASP GLN ASN HIS ALA LYS LEU CYS GLN TYR ASN
SEQRES 22 B 710 ALA GLU THR GLY GLU PRO MSE GLY VAL LEU TYR GLU GLU
SEQRES 23 B 710 MSE HIS PRO LYS TYR VAL GLU PRO GLN ASN PRO ILE VAL
SEQRES 24 B 710 PHE LEU PRO TRP ASP PRO THR LYS PHE ILE TYR GLN SER
SEQRES 25 B 710 GLN ARG ASP GLY TYR ASN HIS LEU TYR LEU PHE GLU THR
SEQRES 26 B 710 ASN ALA ALA ASN MSE LYS GLY GLU THR TYR ASN SER ALA
SEQRES 27 B 710 ASN GLY GLY SER TYR PHE GLN ALA GLY LYS VAL LYS GLN
SEQRES 28 B 710 LEU THR LYS GLY ASN TRP LEU VAL SER GLU ILE LEU GLY
SEQRES 29 B 710 PHE ASN THR LYS ARG LYS GLU VAL ILE PHE THR ALA VAL
SEQRES 30 B 710 GLU GLY LEU ARG SER GLY HIS PHE ALA VAL ASN VAL SER
SEQRES 31 B 710 ASN GLY LYS ILE SER GLN PRO PHE GLU ASN CYS LYS GLU
SEQRES 32 B 710 SER GLU HIS SER GLY THR LEU SER ALA SER GLY THR TYR
SEQRES 33 B 710 LEU ILE ASP ARG TYR SER THR LYS ASP GLN PRO ARG VAL
SEQRES 34 B 710 ILE ASN LEU VAL ASP THR LYS ASN PHE LYS GLU THR ALA
SEQRES 35 B 710 ASN LEU LEU THR ALA GLU ASN PRO TYR ASP GLY TYR GLN
SEQRES 36 B 710 MSE PRO SER ILE GLU THR GLY THR ILE LYS ALA ALA ASP
SEQRES 37 B 710 GLY THR THR ASP LEU HIS TYR ARG LEU MSE LYS PRO ALA
SEQRES 38 B 710 ASN PHE ASP PRO ALA LYS LYS TYR PRO VAL ILE VAL TYR
SEQRES 39 B 710 VAL TYR GLY GLY PRO HIS ALA GLN CYS VAL THR GLY GLY
SEQRES 40 B 710 TRP GLN ASN GLY ALA ARG GLY TRP ASP THR TYR MSE ALA
SEQRES 41 B 710 SER LYS GLY TYR ILE MSE PHE THR ILE ASP ASN ARG GLY
SEQRES 42 B 710 SER SER ASN ARG GLY LEU THR PHE GLU ASN ALA THR PHE
SEQRES 43 B 710 ARG ARG LEU GLY ILE GLU GLU GLY LYS ASP GLN VAL LYS
SEQRES 44 B 710 GLY VAL GLU PHE LEU LYS SER LEU PRO TYR VAL ASP SER
SEQRES 45 B 710 GLU ARG ILE GLY VAL HIS GLY TRP SER PHE GLY GLY HIS
SEQRES 46 B 710 MSE THR THR ALA LEU MSE LEU ARG TYR PRO GLU ILE PHE
SEQRES 47 B 710 LYS VAL GLY VAL ALA GLY GLY PRO VAL ILE ASP TRP GLY
SEQRES 48 B 710 TYR TYR GLU ILE MSE TYR GLY GLU ARG TYR MSE ASP THR
SEQRES 49 B 710 PRO GLU SER ASN PRO GLU GLY TYR LYS GLU CYS ASN LEU
SEQRES 50 B 710 LYS ASN LEU ALA ASP GLN LEU LYS GLY HIS LEU LEU ILE
SEQRES 51 B 710 ILE HIS ASP ASP HIS ASP ASP THR CYS VAL PRO GLN HIS
SEQRES 52 B 710 THR LEU SER PHE MSE LYS ALA CYS VAL ASP ALA ARG THR
SEQRES 53 B 710 TYR PRO ASP LEU PHE ILE TYR PRO CYS HIS LYS HIS ASN
SEQRES 54 B 710 VAL ALA GLY ARG ASP ARG VAL HIS LEU HIS GLU LYS ILE
SEQRES 55 B 710 THR ARG TYR PHE GLU GLN ASN LEU
MODRES 4Q1V MSE A 77 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 112 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 205 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 209 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 232 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 235 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 302 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 309 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 352 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 478 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 500 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 541 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 548 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 608 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 613 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 638 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 644 MET SELENOMETHIONINE
MODRES 4Q1V MSE A 690 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 77 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 112 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 205 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 209 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 232 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 235 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 302 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 309 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 352 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 478 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 500 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 541 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 548 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 608 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 613 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 638 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 644 MET SELENOMETHIONINE
MODRES 4Q1V MSE B 690 MET SELENOMETHIONINE
HET MSE A 77 8
HET MSE A 112 8
HET MSE A 205 8
HET MSE A 209 8
HET MSE A 232 8
HET MSE A 235 8
HET MSE A 302 8
HET MSE A 309 8
HET MSE A 352 8
HET MSE A 478 8
HET MSE A 500 8
HET MSE A 541 8
HET MSE A 548 8
HET MSE A 608 8
HET MSE A 613 8
HET MSE A 638 8
HET MSE A 644 8
HET MSE A 690 8
HET MSE B 77 8
HET MSE B 112 8
HET MSE B 205 8
HET MSE B 209 8
HET MSE B 232 8
HET MSE B 235 8
HET MSE B 302 8
HET MSE B 309 8
HET MSE B 352 8
HET MSE B 478 8
HET MSE B 500 8
HET MSE B 541 8
HET MSE B 548 8
HET MSE B 608 8
HET MSE B 613 8
HET MSE B 638 8
HET MSE B 644 8
HET MSE B 690 8
HET PEG A 801 7
HET PEG A 802 7
HET MG A 803 1
HET PEG B 801 7
HET MG B 802 1
HETNAM MSE SELENOMETHIONINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM MG MAGNESIUM ION
FORMUL 1 MSE 36(C5 H11 N O2 SE)
FORMUL 3 PEG 3(C4 H10 O3)
FORMUL 5 MG 2(MG 2+)
FORMUL 8 HOH *641(H2 O)
HELIX 1 1 THR A 30 ILE A 35 1 6
HELIX 2 2 ARG A 81 ASN A 91 1 11
HELIX 3 3 VAL A 180 GLU A 184 5 5
HELIX 4 4 ASN A 348 MSE A 352 5 5
HELIX 5 5 PRO A 419 CYS A 423 5 5
HELIX 6 6 GLY A 529 ALA A 534 5 6
HELIX 7 7 ARG A 535 LYS A 544 1 10
HELIX 8 8 GLY A 560 ASN A 565 1 6
HELIX 9 9 ALA A 566 PHE A 568 5 3
HELIX 10 10 GLY A 572 SER A 588 1 17
HELIX 11 11 SER A 603 TYR A 616 1 14
HELIX 12 12 ASP A 631 TYR A 635 5 5
HELIX 13 13 GLU A 636 ASP A 645 1 10
HELIX 14 14 ASN A 650 CYS A 657 1 8
HELIX 15 15 ASN A 658 LEU A 666 5 9
HELIX 16 16 PRO A 683 ARG A 697 1 15
HELIX 17 17 ARG A 715 LEU A 732 1 18
HELIX 18 18 THR B 30 ILE B 35 1 6
HELIX 19 19 ARG B 81 ASN B 91 1 11
HELIX 20 20 VAL B 180 GLU B 184 5 5
HELIX 21 21 ASN B 348 MSE B 352 5 5
HELIX 22 22 PRO B 419 CYS B 423 5 5
HELIX 23 23 GLY B 529 ALA B 534 5 6
HELIX 24 24 ARG B 535 LYS B 544 1 10
HELIX 25 25 GLY B 560 ALA B 566 1 7
HELIX 26 26 GLY B 572 SER B 588 1 17
HELIX 27 27 SER B 603 TYR B 616 1 14
HELIX 28 28 ASP B 631 TYR B 635 5 5
HELIX 29 29 GLU B 636 ASP B 645 1 10
HELIX 30 30 ASN B 650 CYS B 657 1 8
HELIX 31 31 ASN B 658 LEU B 666 5 9
HELIX 32 32 PRO B 683 ARG B 697 1 15
HELIX 33 33 ARG B 715 LEU B 732 1 18
SHEET 1 A 4 GLN A 51 TRP A 53 0
SHEET 2 A 4 GLU A 56 PRO A 60 -1 O GLU A 56 N TRP A 53
SHEET 3 A 4 THR A 64 ILE A 68 -1 O ILE A 68 N CYS A 57
SHEET 4 A 4 GLU A 75 THR A 80 -1 O THR A 76 N SER A 67
SHEET 1 B 3 GLN A 111 ILE A 116 0
SHEET 2 B 3 LYS A 119 ASN A 124 -1 O ILE A 121 N PHE A 114
SHEET 3 B 3 GLN A 129 PHE A 134 -1 O PHE A 134 N PHE A 120
SHEET 1 C 4 ASN A 141 TYR A 145 0
SHEET 2 C 4 VAL A 152 ILE A 156 -1 O ALA A 153 N ASP A 144
SHEET 3 C 4 ASN A 159 VAL A 162 -1 O TYR A 161 N TYR A 154
SHEET 4 C 4 LYS A 165 ALA A 166 -1 O LYS A 165 N VAL A 162
SHEET 1 D 3 ILE A 174 CYS A 176 0
SHEET 2 D 3 LEU A 200 ASP A 206 -1 O MSE A 205 N VAL A 175
SHEET 3 D 3 THR A 191 TRP A 193 -1 N PHE A 192 O ALA A 201
SHEET 1 E 4 ILE A 174 CYS A 176 0
SHEET 2 E 4 LEU A 200 ASP A 206 -1 O MSE A 205 N VAL A 175
SHEET 3 E 4 GLN A 239 TYR A 245 -1 O TYR A 245 N LEU A 200
SHEET 4 E 4 SER A 252 TYR A 254 -1 O ILE A 253 N ILE A 244
SHEET 1 F 2 GLN A 212 ASP A 217 0
SHEET 2 F 2 GLU A 224 ARG A 229 -1 O ASN A 226 N LEU A 215
SHEET 1 G 6 ARG A 263 TRP A 270 0
SHEET 2 G 6 SER A 276 ASN A 283 -1 O TYR A 278 N SER A 269
SHEET 3 G 6 HIS A 288 ASN A 295 -1 O TYR A 294 N LEU A 277
SHEET 4 G 6 PRO A 301 MSE A 309 -1 O GLU A 308 N ALA A 289
SHEET 5 G 6 SER A 364 ALA A 368 -1 O SER A 364 N MSE A 309
SHEET 6 G 6 GLY A 354 ASN A 358 -1 N GLU A 355 O GLN A 367
SHEET 1 H 4 VAL A 321 LEU A 323 0
SHEET 2 H 4 ASP A 326 SER A 334 -1 O ILE A 331 N VAL A 321
SHEET 3 H 4 HIS A 341 GLU A 346 -1 O PHE A 345 N PHE A 330
SHEET 4 H 4 LYS A 372 GLN A 373 -1 O LYS A 372 N LEU A 344
SHEET 1 I 3 LEU A 380 ASN A 388 0
SHEET 2 I 3 GLU A 393 GLU A 400 -1 O ILE A 395 N GLY A 386
SHEET 3 I 3 ARG A 403 ASN A 410 -1 O PHE A 407 N PHE A 396
SHEET 1 J 4 GLU A 427 LEU A 432 0
SHEET 2 J 4 TYR A 438 THR A 445 -1 O ILE A 440 N THR A 431
SHEET 3 J 4 GLN A 448 ASP A 456 -1 O ASN A 453 N ASP A 441
SHEET 4 J 4 GLU A 462 THR A 468 -1 O THR A 463 N LEU A 454
SHEET 1 K 8 SER A 480 LYS A 487 0
SHEET 2 K 8 ASP A 494 LYS A 501 -1 O LEU A 499 N GLU A 482
SHEET 3 K 8 ILE A 547 ILE A 551 -1 O MSE A 548 N MSE A 500
SHEET 4 K 8 TYR A 511 TYR A 516 1 N TYR A 516 O PHE A 549
SHEET 5 K 8 VAL A 592 TRP A 602 1 O GLY A 598 N VAL A 513
SHEET 6 K 8 VAL A 622 GLY A 626 1 O GLY A 626 N GLY A 601
SHEET 7 K 8 HIS A 669 ASP A 675 1 O ILE A 673 N ALA A 625
SHEET 8 K 8 ASP A 701 TYR A 705 1 O ASP A 701 N LEU A 670
SHEET 1 L 4 GLN B 51 TRP B 53 0
SHEET 2 L 4 GLU B 56 PRO B 60 -1 O ILE B 58 N GLN B 51
SHEET 3 L 4 THR B 64 ILE B 68 -1 O ILE B 68 N CYS B 57
SHEET 4 L 4 GLU B 75 THR B 80 -1 O THR B 76 N SER B 67
SHEET 1 M 3 GLN B 111 ILE B 116 0
SHEET 2 M 3 LYS B 119 ASN B 124 -1 O ILE B 121 N PHE B 114
SHEET 3 M 3 GLN B 129 PHE B 134 -1 O PHE B 134 N PHE B 120
SHEET 1 N 4 ASN B 141 TYR B 145 0
SHEET 2 N 4 VAL B 152 ILE B 156 -1 O ALA B 153 N ASP B 144
SHEET 3 N 4 ASN B 159 VAL B 162 -1 O TYR B 161 N TYR B 154
SHEET 4 N 4 LYS B 165 ALA B 166 -1 O LYS B 165 N VAL B 162
SHEET 1 O 3 ILE B 174 CYS B 176 0
SHEET 2 O 3 LEU B 200 ASP B 206 -1 O MSE B 205 N VAL B 175
SHEET 3 O 3 THR B 191 TRP B 193 -1 N PHE B 192 O ALA B 201
SHEET 1 P 4 ILE B 174 CYS B 176 0
SHEET 2 P 4 LEU B 200 ASP B 206 -1 O MSE B 205 N VAL B 175
SHEET 3 P 4 GLN B 239 TYR B 245 -1 O TYR B 245 N LEU B 200
SHEET 4 P 4 SER B 252 TYR B 254 -1 O ILE B 253 N ILE B 244
SHEET 1 Q 2 GLN B 212 ASP B 217 0
SHEET 2 Q 2 GLU B 224 ARG B 229 -1 O ASN B 226 N LEU B 215
SHEET 1 R 6 ARG B 263 TRP B 270 0
SHEET 2 R 6 SER B 276 ASN B 283 -1 O TYR B 278 N SER B 269
SHEET 3 R 6 HIS B 288 ASN B 295 -1 O TYR B 294 N LEU B 277
SHEET 4 R 6 PRO B 301 MSE B 309 -1 O GLU B 308 N ALA B 289
SHEET 5 R 6 SER B 364 ALA B 368 -1 O SER B 364 N MSE B 309
SHEET 6 R 6 GLY B 354 ASN B 358 -1 N GLU B 355 O GLN B 367
SHEET 1 S 4 VAL B 321 LEU B 323 0
SHEET 2 S 4 ASP B 326 SER B 334 -1 O ILE B 331 N VAL B 321
SHEET 3 S 4 HIS B 341 GLU B 346 -1 O PHE B 345 N PHE B 330
SHEET 4 S 4 LYS B 372 GLN B 373 -1 O LYS B 372 N LEU B 344
SHEET 1 T 3 LEU B 380 ASN B 388 0
SHEET 2 T 3 GLU B 393 GLU B 400 -1 O ILE B 395 N GLY B 386
SHEET 3 T 3 ARG B 403 ASN B 410 -1 O PHE B 407 N PHE B 396
SHEET 1 U 4 GLU B 427 LEU B 432 0
SHEET 2 U 4 TYR B 438 SER B 444 -1 O ILE B 440 N THR B 431
SHEET 3 U 4 VAL B 451 ASP B 456 -1 O ASN B 453 N ASP B 441
SHEET 4 U 4 GLU B 462 THR B 468 -1 O THR B 463 N LEU B 454
SHEET 1 V 8 SER B 480 LYS B 487 0
SHEET 2 V 8 ASP B 494 LYS B 501 -1 O LEU B 499 N GLU B 482
SHEET 3 V 8 ILE B 547 ILE B 551 -1 O THR B 550 N ARG B 498
SHEET 4 V 8 TYR B 511 TYR B 516 1 N TYR B 516 O PHE B 549
SHEET 5 V 8 VAL B 592 TRP B 602 1 O ARG B 596 N VAL B 513
SHEET 6 V 8 VAL B 622 GLY B 626 1 O GLY B 626 N GLY B 601
SHEET 7 V 8 HIS B 669 ASP B 675 1 O LEU B 671 N ALA B 625
SHEET 8 V 8 ASP B 701 TYR B 705 1 O ASP B 701 N LEU B 670
LINK C THR A 76 N MSE A 77 1555 1555 1.33
LINK C MSE A 77 N VAL A 78 1555 1555 1.33
LINK C GLN A 111 N MSE A 112 1555 1555 1.35
LINK C MSE A 112 N LEU A 113 1555 1555 1.34
LINK C ARG A 204 N MSE A 205 1555 1555 1.32
LINK C MSE A 205 N ASP A 206 1555 1555 1.33
LINK C SER A 208 N MSE A 209 1555 1555 1.34
LINK C MSE A 209 N VAL A 210 1555 1555 1.35
LINK C PRO A 231 N MSE A 232 1555 1555 1.34
LINK C MSE A 232 N ALA A 233 1555 1555 1.37
LINK C GLY A 234 N MSE A 235 1555 1555 1.33
LINK C MSE A 235 N THR A 236 1555 1555 1.34
LINK C PRO A 301 N MSE A 302 1555 1555 1.34
LINK C MSE A 302 N GLY A 303 1555 1555 1.32
LINK C GLU A 308 N MSE A 309 1555 1555 1.34
LINK C MSE A 309 N HIS A 310 1555 1555 1.34
LINK C ASN A 351 N MSE A 352 1555 1555 1.35
LINK C MSE A 352 N LYS A 353 1555 1555 1.35
LINK C GLN A 477 N MSE A 478 1555 1555 1.33
LINK C MSE A 478 N PRO A 479 1555 1555 1.34
LINK C LEU A 499 N MSE A 500 1555 1555 1.33
LINK C MSE A 500 N LYS A 501 1555 1555 1.34
LINK C TYR A 540 N MSE A 541 1555 1555 1.34
LINK C MSE A 541 N ALA A 542 1555 1555 1.35
LINK C ILE A 547 N MSE A 548 1555 1555 1.32
LINK C MSE A 548 N PHE A 549 1555 1555 1.33
LINK C HIS A 607 N MSE A 608 1555 1555 1.34
LINK C MSE A 608 N THR A 609 1555 1555 1.34
LINK C LEU A 612 N MSE A 613 1555 1555 1.35
LINK C MSE A 613 N LEU A 614 1555 1555 1.36
LINK C ILE A 637 N MSE A 638 1555 1555 1.36
LINK C MSE A 638 N TYR A 639 1555 1555 1.34
LINK C TYR A 643 N MSE A 644 1555 1555 1.34
LINK C MSE A 644 N ASP A 645 1555 1555 1.35
LINK C PHE A 689 N MSE A 690 1555 1555 1.35
LINK C MSE A 690 N LYS A 691 1555 1555 1.36
LINK C THR B 76 N MSE B 77 1555 1555 1.33
LINK C MSE B 77 N VAL B 78 1555 1555 1.33
LINK C GLN B 111 N MSE B 112 1555 1555 1.32
LINK C MSE B 112 N LEU B 113 1555 1555 1.34
LINK C ARG B 204 N MSE B 205 1555 1555 1.33
LINK C MSE B 205 N ASP B 206 1555 1555 1.34
LINK C SER B 208 N MSE B 209 1555 1555 1.34
LINK C MSE B 209 N VAL B 210 1555 1555 1.34
LINK C PRO B 231 N MSE B 232 1555 1555 1.33
LINK C MSE B 232 N ALA B 233 1555 1555 1.35
LINK C GLY B 234 N MSE B 235 1555 1555 1.33
LINK C MSE B 235 N THR B 236 1555 1555 1.33
LINK C PRO B 301 N MSE B 302 1555 1555 1.34
LINK C MSE B 302 N GLY B 303 1555 1555 1.33
LINK C GLU B 308 N MSE B 309 1555 1555 1.34
LINK C MSE B 309 N HIS B 310 1555 1555 1.35
LINK C ASN B 351 N MSE B 352 1555 1555 1.35
LINK C MSE B 352 N LYS B 353 1555 1555 1.34
LINK C GLN B 477 N MSE B 478 1555 1555 1.33
LINK C MSE B 478 N PRO B 479 1555 1555 1.34
LINK C LEU B 499 N MSE B 500 1555 1555 1.33
LINK C MSE B 500 N LYS B 501 1555 1555 1.34
LINK C TYR B 540 N MSE B 541 1555 1555 1.34
LINK C MSE B 541 N ALA B 542 1555 1555 1.35
LINK C ILE B 547 N MSE B 548 1555 1555 1.32
LINK C MSE B 548 N PHE B 549 1555 1555 1.34
LINK C HIS B 607 N MSE B 608 1555 1555 1.34
LINK C MSE B 608 N THR B 609 1555 1555 1.37
LINK C LEU B 612 N MSE B 613 1555 1555 1.35
LINK C MSE B 613 N LEU B 614 1555 1555 1.37
LINK C ILE B 637 N MSE B 638 1555 1555 1.34
LINK C MSE B 638 N TYR B 639 1555 1555 1.34
LINK C TYR B 643 N MSE B 644 1555 1555 1.34
LINK C MSE B 644 N ASP B 645 1555 1555 1.35
LINK C PHE B 689 N MSE B 690 1555 1555 1.35
LINK C MSE B 690 N LYS B 691 1555 1555 1.35
LINK MG MG B 802 O HOH B1171 1555 1555 1.95
LINK MG MG B 802 O HOH B1024 1555 1555 2.04
LINK MG MG A 803 O HOH A 925 1555 1555 2.05
LINK OD1 ASP A 285 MG MG A 803 1555 1555 2.08
LINK OD1 ASP B 285 MG MG B 802 1555 1555 2.12
LINK MG MG A 803 O HOH A 924 1555 1555 2.15
LINK O ASP A 285 MG MG A 803 1555 1555 2.23
LINK MG MG A 803 O HOH A1235 1555 1555 2.24
LINK O ASP B 285 MG MG B 802 1555 1555 2.25
LINK OD1 ASP B 645 MG MG B 802 1555 1555 2.26
LINK OD1 ASP A 645 MG MG A 803 1555 1555 2.32
LINK MG MG B 802 O HOH B1056 1555 1555 2.52
SITE 1 AC1 1 GLN A 524
SITE 1 AC2 3 ARG A 204 LYS A 241 TYR A 254
SITE 1 AC3 5 ASP A 285 ASP A 645 HOH A 924 HOH A 925
SITE 2 AC3 5 HOH A1235
SITE 1 AC4 6 HIS B 406 GLN B 418 HIS B 428 ASP B 441
SITE 2 AC4 6 PHE B 460 GLU B 462
SITE 1 AC5 5 ASP B 285 ASP B 645 HOH B1024 HOH B1056
SITE 2 AC5 5 HOH B1171
CRYST1 92.487 133.703 159.127 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 0.010812 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006284 0.00000
TER 5727 LEU A 732
TER 11413 LEU B 732
MASTER 334 0 41 33 90 0 8 611936 2 397 110
END |