HEADER SIGNALING PROTEIN,TRANSFERASE 15-AUG-05 2AP9
TITLE CRYSTAL STRUCTURE OF ACETYLGLUTAMATE KINASE FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS CDC1551
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLGLUTAMATE KINASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: ACETYLGLUTAMATE KINASE;
COMPND 5 SYNONYM: NAG KINASE; AGK; N-ACETYL-L-GLUTAMATE 5-PHOSPHOTRANSFERASE;
COMPND 6 EC: 2.7.2.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83331;
SOURCE 4 STRAIN: CDC1551;
SOURCE 5 GENE: ARGB, RV1654, MT1692;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834, DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET T7
KEYWDS STRUCTURAL GENOMICS; PROTEIN STRUCTURE INITIATIVE; NYSGXRC; T1702;
KEYWDS 2 ACETYLGLUTAMATE KINASE; PSI; NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, SIGNALING PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.RAJASHANKAR,R.KNIEWEL,K.LEE,C.D.LIMA,S.K.BURLEY,NEW YORK SGX
AUTHOR 2 RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 4 03-FEB-21 2AP9 1 AUTHOR REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2AP9 1 VERSN
REVDAT 2 24-FEB-09 2AP9 1 VERSN
REVDAT 1 30-AUG-05 2AP9 0
JRNL AUTH K.R.RAJASHANKAR,R.KNIEWEL,K.LEE,C.D.LIMA
JRNL TITL CRYSTAL STRUCTURE OF ACETYLGLUTAMATE KINASE FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS CDC1551
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 178264.750
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.9
REMARK 3 NUMBER OF REFLECTIONS : 88420
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 SET) : 0.258
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4316
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8966
REMARK 3 BIN R VALUE (WORKING SET) : 0.4640
REMARK 3 BIN FREE R VALUE : 0.4490
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 423
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13025
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 113
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.89000
REMARK 3 B22 (A**2) : 22.62000
REMARK 3 B33 (A**2) : -27.50000
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) : 0.50
REMARK 3 ESD FROM SIGMAA (A) : 0.95
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.82
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.350 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.680 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.650 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 31.49
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CERTAIN REGIONS OF THE MODEL DO NOT
REMARK 3 HAVE WELL DEFINED ELECTRON DENSITY. THESE ARE RESIDUES 143-152
REMARK 3 AND 222-231. TWO SOLVENT PEAKS HAVE BEEN REFINED AS MAGNESIUM
REMARK 3 IONS, AND ONE SOLVENT PEAK HAS BE REFINED AS A NICKLE ION (AS IT
REMARK 3 IS BOUND TO HIS6 RAG).
REMARK 4
REMARK 4 2AP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000034157.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.975
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : VERTICAL FOCUSSING MIRROR DOWN
REMARK 200 STREAM OF MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94360
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 3.170
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: MODEL BUILT BASED ON THE EXPERIMENTAL ELECTRON
REMARK 200 DENSITY MAP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% PEG 6000, 0.1M TRIS PH 8.5, 0.1M
REMARK 280 POTASSIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
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 44.01200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.29050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.49800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.29050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.01200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.49800
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 300 REMARK: POLYPEPTIDE CHAIN A, B, C, D, E AND F TOGETHER FORM A
REMARK 300 BIOLOGICAL ASSEMBLY
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
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 GLY B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 GLY C 298
REMARK 465 HIS C 299
REMARK 465 HIS C 300
REMARK 465 HIS C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
REMARK 465 HIS C 304
REMARK 465 GLY D 298
REMARK 465 HIS D 299
REMARK 465 HIS D 300
REMARK 465 HIS D 301
REMARK 465 HIS D 302
REMARK 465 HIS D 303
REMARK 465 HIS D 304
REMARK 465 HIS E 301
REMARK 465 HIS E 302
REMARK 465 HIS E 303
REMARK 465 HIS E 304
REMARK 465 GLY F 298
REMARK 465 HIS F 299
REMARK 465 HIS F 300
REMARK 465 HIS F 301
REMARK 465 HIS F 302
REMARK 465 HIS F 303
REMARK 465 HIS F 304
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 C TRP C 224 CD PRO C 225 1.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 VAL A 146 N - CA - C ANGL. DEV. = -23.8 DEGREES
REMARK 500 TRP B 224 N - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 PRO C 225 C - N - CA ANGL. DEV. = 60.4 DEGREES
REMARK 500 PRO C 225 C - N - CD ANGL. DEV. = -50.6 DEGREES
REMARK 500 PRO C 225 CA - N - CD ANGL. DEV. = -9.7 DEGREES
REMARK 500 PRO D 225 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 PRO D 225 N - CA - C ANGL. DEV. = -19.6 DEGREES
REMARK 500 GLY D 288 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 TRP E 224 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 ASP E 226 N - CA - C ANGL. DEV. = 20.7 DEGREES
REMARK 500 ASP E 228 N - CA - C ANGL. DEV. = 21.8 DEGREES
REMARK 500 PHE F 88 N - CA - C ANGL. DEV. = 17.5 DEGREES
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 ALA A 8 30.09 -84.89
REMARK 500 THR A 43 -70.12 -57.02
REMARK 500 VAL A 94 98.12 62.26
REMARK 500 GLN A 110 -67.19 -135.52
REMARK 500 ASN A 120 8.88 -65.86
REMARK 500 TYR A 125 -68.79 -104.70
REMARK 500 ALA A 134 18.58 53.20
REMARK 500 VAL A 146 -91.56 161.61
REMARK 500 ASP A 147 -21.68 -144.38
REMARK 500 VAL A 149 -14.49 65.43
REMARK 500 ALA A 150 29.59 -71.31
REMARK 500 ASP A 160 -74.06 -88.25
REMARK 500 THR A 181 79.24 -48.04
REMARK 500 ASP A 216 32.45 -94.00
REMARK 500 ARG A 223 80.03 -157.94
REMARK 500 TRP A 224 -68.61 -11.88
REMARK 500 PRO A 244 12.93 -69.32
REMARK 500 THR A 245 41.20 -144.58
REMARK 500 VAL A 265 109.65 -58.63
REMARK 500 ASP A 286 31.77 -85.66
REMARK 500 GLU B 20 -6.05 -55.57
REMARK 500 THR B 43 -70.12 -57.62
REMARK 500 VAL B 94 83.39 55.12
REMARK 500 THR B 95 91.97 -65.97
REMARK 500 GLN B 110 -67.72 -136.93
REMARK 500 ASN B 120 8.63 -65.53
REMARK 500 TYR B 125 -68.14 -104.61
REMARK 500 ALA B 134 18.42 53.80
REMARK 500 VAL B 146 59.42 -118.78
REMARK 500 VAL B 149 -31.02 -35.41
REMARK 500 ALA B 150 75.85 -57.20
REMARK 500 ILE B 153 31.87 -68.71
REMARK 500 ASP B 160 -74.90 -87.57
REMARK 500 THR B 181 77.55 -47.84
REMARK 500 ASP B 216 31.72 -93.55
REMARK 500 TYR B 221 99.11 -69.37
REMARK 500 ARG B 223 111.57 60.39
REMARK 500 TRP B 224 130.62 9.77
REMARK 500 PRO B 225 101.41 -1.01
REMARK 500 ASP B 226 104.91 -171.35
REMARK 500 ARG B 227 1.23 -67.68
REMARK 500 SER B 229 48.37 -79.02
REMARK 500 VAL B 231 174.58 -58.75
REMARK 500 GLU B 233 75.81 -163.07
REMARK 500 GLN B 241 38.74 -81.84
REMARK 500 ASP B 286 44.61 -77.02
REMARK 500 THR C 43 -70.19 -58.12
REMARK 500 GLN C 110 -67.03 -136.64
REMARK 500 ASN C 120 8.85 -65.60
REMARK 500 TYR C 125 -69.32 -103.88
REMARK 500
REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS.
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 A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 235 OD2
REMARK 620 2 HIS A 301 O 74.1
REMARK 620 3 HIS A 304 O 142.3 70.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T1702 RELATED DB: TARGETDB
DBREF 2AP9 A 6 296 UNP P0A4Y6 ARGB_MYCTU 4 294
DBREF 2AP9 B 6 296 UNP P0A4Y6 ARGB_MYCTU 4 294
DBREF 2AP9 C 6 296 UNP P0A4Y6 ARGB_MYCTU 4 294
DBREF 2AP9 D 6 296 UNP P0A4Y6 ARGB_MYCTU 4 294
DBREF 2AP9 E 6 296 UNP P0A4Y6 ARGB_MYCTU 4 294
DBREF 2AP9 F 6 296 UNP P0A4Y6 ARGB_MYCTU 4 294
SEQADV 2AP9 MSE A 42 UNP P0A4Y6 MET 40 MODIFIED RESIDUE
SEQADV 2AP9 MSE A 55 UNP P0A4Y6 MET 53 MODIFIED RESIDUE
SEQADV 2AP9 MSE A 78 UNP P0A4Y6 MET 76 MODIFIED RESIDUE
SEQADV 2AP9 MSE A 105 UNP P0A4Y6 MET 103 MODIFIED RESIDUE
SEQADV 2AP9 MSE A 167 UNP P0A4Y6 MET 165 MODIFIED RESIDUE
SEQADV 2AP9 MSE A 213 UNP P0A4Y6 MET 211 MODIFIED RESIDUE
SEQADV 2AP9 LEU A 248 UNP P0A4Y6 SER 246 CONFLICT
SEQADV 2AP9 MSE A 250 UNP P0A4Y6 MET 248 MODIFIED RESIDUE
SEQADV 2AP9 GLU A 297 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 GLY A 298 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS A 299 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS A 300 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS A 301 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS A 302 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS A 303 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS A 304 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 MSE B 42 UNP P0A4Y6 MET 40 MODIFIED RESIDUE
SEQADV 2AP9 MSE B 55 UNP P0A4Y6 MET 53 MODIFIED RESIDUE
SEQADV 2AP9 MSE B 78 UNP P0A4Y6 MET 76 MODIFIED RESIDUE
SEQADV 2AP9 MSE B 105 UNP P0A4Y6 MET 103 MODIFIED RESIDUE
SEQADV 2AP9 MSE B 167 UNP P0A4Y6 MET 165 MODIFIED RESIDUE
SEQADV 2AP9 MSE B 213 UNP P0A4Y6 MET 211 MODIFIED RESIDUE
SEQADV 2AP9 LEU B 248 UNP P0A4Y6 SER 246 CONFLICT
SEQADV 2AP9 MSE B 250 UNP P0A4Y6 MET 248 MODIFIED RESIDUE
SEQADV 2AP9 GLU B 297 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 GLY B 298 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS B 299 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS B 300 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS B 301 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS B 302 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS B 303 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS B 304 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 MSE C 42 UNP P0A4Y6 MET 40 MODIFIED RESIDUE
SEQADV 2AP9 MSE C 55 UNP P0A4Y6 MET 53 MODIFIED RESIDUE
SEQADV 2AP9 MSE C 78 UNP P0A4Y6 MET 76 MODIFIED RESIDUE
SEQADV 2AP9 MSE C 105 UNP P0A4Y6 MET 103 MODIFIED RESIDUE
SEQADV 2AP9 MSE C 167 UNP P0A4Y6 MET 165 MODIFIED RESIDUE
SEQADV 2AP9 MSE C 213 UNP P0A4Y6 MET 211 MODIFIED RESIDUE
SEQADV 2AP9 LEU C 248 UNP P0A4Y6 SER 246 CONFLICT
SEQADV 2AP9 MSE C 250 UNP P0A4Y6 MET 248 MODIFIED RESIDUE
SEQADV 2AP9 GLU C 297 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 GLY C 298 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS C 299 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS C 300 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS C 301 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS C 302 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS C 303 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS C 304 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 MSE D 42 UNP P0A4Y6 MET 40 MODIFIED RESIDUE
SEQADV 2AP9 MSE D 55 UNP P0A4Y6 MET 53 MODIFIED RESIDUE
SEQADV 2AP9 MSE D 78 UNP P0A4Y6 MET 76 MODIFIED RESIDUE
SEQADV 2AP9 MSE D 105 UNP P0A4Y6 MET 103 MODIFIED RESIDUE
SEQADV 2AP9 MSE D 167 UNP P0A4Y6 MET 165 MODIFIED RESIDUE
SEQADV 2AP9 MSE D 213 UNP P0A4Y6 MET 211 MODIFIED RESIDUE
SEQADV 2AP9 LEU D 248 UNP P0A4Y6 SER 246 CONFLICT
SEQADV 2AP9 MSE D 250 UNP P0A4Y6 MET 248 MODIFIED RESIDUE
SEQADV 2AP9 GLU D 297 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 GLY D 298 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS D 299 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS D 300 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS D 301 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS D 302 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS D 303 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS D 304 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 MSE E 42 UNP P0A4Y6 MET 40 MODIFIED RESIDUE
SEQADV 2AP9 MSE E 55 UNP P0A4Y6 MET 53 MODIFIED RESIDUE
SEQADV 2AP9 MSE E 78 UNP P0A4Y6 MET 76 MODIFIED RESIDUE
SEQADV 2AP9 MSE E 105 UNP P0A4Y6 MET 103 MODIFIED RESIDUE
SEQADV 2AP9 MSE E 167 UNP P0A4Y6 MET 165 MODIFIED RESIDUE
SEQADV 2AP9 MSE E 213 UNP P0A4Y6 MET 211 MODIFIED RESIDUE
SEQADV 2AP9 LEU E 248 UNP P0A4Y6 SER 246 CONFLICT
SEQADV 2AP9 MSE E 250 UNP P0A4Y6 MET 248 MODIFIED RESIDUE
SEQADV 2AP9 GLU E 297 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 GLY E 298 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS E 299 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS E 300 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS E 301 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS E 302 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS E 303 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS E 304 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 MSE F 42 UNP P0A4Y6 MET 40 MODIFIED RESIDUE
SEQADV 2AP9 MSE F 55 UNP P0A4Y6 MET 53 MODIFIED RESIDUE
SEQADV 2AP9 MSE F 78 UNP P0A4Y6 MET 76 MODIFIED RESIDUE
SEQADV 2AP9 MSE F 105 UNP P0A4Y6 MET 103 MODIFIED RESIDUE
SEQADV 2AP9 MSE F 167 UNP P0A4Y6 MET 165 MODIFIED RESIDUE
SEQADV 2AP9 MSE F 213 UNP P0A4Y6 MET 211 MODIFIED RESIDUE
SEQADV 2AP9 LEU F 248 UNP P0A4Y6 SER 246 CONFLICT
SEQADV 2AP9 MSE F 250 UNP P0A4Y6 MET 248 MODIFIED RESIDUE
SEQADV 2AP9 GLU F 297 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 GLY F 298 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS F 299 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS F 300 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS F 301 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS F 302 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS F 303 UNP P0A4Y6 EXPRESSION TAG
SEQADV 2AP9 HIS F 304 UNP P0A4Y6 EXPRESSION TAG
SEQRES 1 A 299 ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU
SEQRES 2 A 299 ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS
SEQRES 3 A 299 VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP
SEQRES 4 A 299 ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE
SEQRES 5 A 299 LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY
SEQRES 6 A 299 GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY
SEQRES 7 A 299 ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR
SEQRES 8 A 299 PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY
SEQRES 9 A 299 GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS
SEQRES 10 A 299 GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN
SEQRES 11 A 299 LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY
SEQRES 12 A 299 VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN
SEQRES 13 A 299 VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY
SEQRES 14 A 299 ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP
SEQRES 15 A 299 GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA
SEQRES 16 A 299 ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE
SEQRES 17 A 299 LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP
SEQRES 18 A 299 ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU
SEQRES 19 A 299 ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO
SEQRES 20 A 299 LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL
SEQRES 21 A 299 PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS
SEQRES 22 A 299 VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR
SEQRES 23 A 299 LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 299 ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU
SEQRES 2 B 299 ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS
SEQRES 3 B 299 VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP
SEQRES 4 B 299 ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE
SEQRES 5 B 299 LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY
SEQRES 6 B 299 GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY
SEQRES 7 B 299 ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR
SEQRES 8 B 299 PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY
SEQRES 9 B 299 GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS
SEQRES 10 B 299 GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN
SEQRES 11 B 299 LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY
SEQRES 12 B 299 VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN
SEQRES 13 B 299 VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY
SEQRES 14 B 299 ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP
SEQRES 15 B 299 GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA
SEQRES 16 B 299 ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE
SEQRES 17 B 299 LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP
SEQRES 18 B 299 ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU
SEQRES 19 B 299 ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO
SEQRES 20 B 299 LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL
SEQRES 21 B 299 PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS
SEQRES 22 B 299 VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR
SEQRES 23 B 299 LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 299 ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU
SEQRES 2 C 299 ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS
SEQRES 3 C 299 VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP
SEQRES 4 C 299 ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE
SEQRES 5 C 299 LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY
SEQRES 6 C 299 GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY
SEQRES 7 C 299 ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR
SEQRES 8 C 299 PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY
SEQRES 9 C 299 GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS
SEQRES 10 C 299 GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN
SEQRES 11 C 299 LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY
SEQRES 12 C 299 VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN
SEQRES 13 C 299 VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY
SEQRES 14 C 299 ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP
SEQRES 15 C 299 GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA
SEQRES 16 C 299 ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE
SEQRES 17 C 299 LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP
SEQRES 18 C 299 ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU
SEQRES 19 C 299 ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO
SEQRES 20 C 299 LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL
SEQRES 21 C 299 PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS
SEQRES 22 C 299 VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR
SEQRES 23 C 299 LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 D 299 ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU
SEQRES 2 D 299 ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS
SEQRES 3 D 299 VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP
SEQRES 4 D 299 ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE
SEQRES 5 D 299 LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY
SEQRES 6 D 299 GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY
SEQRES 7 D 299 ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR
SEQRES 8 D 299 PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY
SEQRES 9 D 299 GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS
SEQRES 10 D 299 GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN
SEQRES 11 D 299 LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY
SEQRES 12 D 299 VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN
SEQRES 13 D 299 VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY
SEQRES 14 D 299 ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP
SEQRES 15 D 299 GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA
SEQRES 16 D 299 ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE
SEQRES 17 D 299 LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP
SEQRES 18 D 299 ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU
SEQRES 19 D 299 ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO
SEQRES 20 D 299 LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL
SEQRES 21 D 299 PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS
SEQRES 22 D 299 VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR
SEQRES 23 D 299 LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 E 299 ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU
SEQRES 2 E 299 ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS
SEQRES 3 E 299 VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP
SEQRES 4 E 299 ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE
SEQRES 5 E 299 LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY
SEQRES 6 E 299 GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY
SEQRES 7 E 299 ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR
SEQRES 8 E 299 PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY
SEQRES 9 E 299 GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS
SEQRES 10 E 299 GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN
SEQRES 11 E 299 LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY
SEQRES 12 E 299 VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN
SEQRES 13 E 299 VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY
SEQRES 14 E 299 ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP
SEQRES 15 E 299 GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA
SEQRES 16 E 299 ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE
SEQRES 17 E 299 LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP
SEQRES 18 E 299 ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU
SEQRES 19 E 299 ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO
SEQRES 20 E 299 LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL
SEQRES 21 E 299 PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS
SEQRES 22 E 299 VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR
SEQRES 23 E 299 LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 F 299 ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU
SEQRES 2 F 299 ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS
SEQRES 3 F 299 VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP
SEQRES 4 F 299 ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE
SEQRES 5 F 299 LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY
SEQRES 6 F 299 GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY
SEQRES 7 F 299 ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR
SEQRES 8 F 299 PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY
SEQRES 9 F 299 GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS
SEQRES 10 F 299 GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN
SEQRES 11 F 299 LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY
SEQRES 12 F 299 VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN
SEQRES 13 F 299 VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY
SEQRES 14 F 299 ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP
SEQRES 15 F 299 GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA
SEQRES 16 F 299 ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE
SEQRES 17 F 299 LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP
SEQRES 18 F 299 ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU
SEQRES 19 F 299 ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO
SEQRES 20 F 299 LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL
SEQRES 21 F 299 PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS
SEQRES 22 F 299 VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR
SEQRES 23 F 299 LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS
MODRES 2AP9 MSE A 42 MET SELENOMETHIONINE
MODRES 2AP9 MSE A 55 MET SELENOMETHIONINE
MODRES 2AP9 MSE A 78 MET SELENOMETHIONINE
MODRES 2AP9 MSE A 105 MET SELENOMETHIONINE
MODRES 2AP9 MSE A 167 MET SELENOMETHIONINE
MODRES 2AP9 MSE A 213 MET SELENOMETHIONINE
MODRES 2AP9 MSE A 250 MET SELENOMETHIONINE
MODRES 2AP9 MSE B 42 MET SELENOMETHIONINE
MODRES 2AP9 MSE B 55 MET SELENOMETHIONINE
MODRES 2AP9 MSE B 78 MET SELENOMETHIONINE
MODRES 2AP9 MSE B 105 MET SELENOMETHIONINE
MODRES 2AP9 MSE B 167 MET SELENOMETHIONINE
MODRES 2AP9 MSE B 213 MET SELENOMETHIONINE
MODRES 2AP9 MSE B 250 MET SELENOMETHIONINE
MODRES 2AP9 MSE C 42 MET SELENOMETHIONINE
MODRES 2AP9 MSE C 55 MET SELENOMETHIONINE
MODRES 2AP9 MSE C 78 MET SELENOMETHIONINE
MODRES 2AP9 MSE C 105 MET SELENOMETHIONINE
MODRES 2AP9 MSE C 167 MET SELENOMETHIONINE
MODRES 2AP9 MSE C 213 MET SELENOMETHIONINE
MODRES 2AP9 MSE C 250 MET SELENOMETHIONINE
MODRES 2AP9 MSE D 42 MET SELENOMETHIONINE
MODRES 2AP9 MSE D 55 MET SELENOMETHIONINE
MODRES 2AP9 MSE D 78 MET SELENOMETHIONINE
MODRES 2AP9 MSE D 105 MET SELENOMETHIONINE
MODRES 2AP9 MSE D 167 MET SELENOMETHIONINE
MODRES 2AP9 MSE D 213 MET SELENOMETHIONINE
MODRES 2AP9 MSE D 250 MET SELENOMETHIONINE
MODRES 2AP9 MSE E 42 MET SELENOMETHIONINE
MODRES 2AP9 MSE E 55 MET SELENOMETHIONINE
MODRES 2AP9 MSE E 78 MET SELENOMETHIONINE
MODRES 2AP9 MSE E 105 MET SELENOMETHIONINE
MODRES 2AP9 MSE E 167 MET SELENOMETHIONINE
MODRES 2AP9 MSE E 213 MET SELENOMETHIONINE
MODRES 2AP9 MSE E 250 MET SELENOMETHIONINE
MODRES 2AP9 MSE F 42 MET SELENOMETHIONINE
MODRES 2AP9 MSE F 55 MET SELENOMETHIONINE
MODRES 2AP9 MSE F 78 MET SELENOMETHIONINE
MODRES 2AP9 MSE F 105 MET SELENOMETHIONINE
MODRES 2AP9 MSE F 167 MET SELENOMETHIONINE
MODRES 2AP9 MSE F 213 MET SELENOMETHIONINE
MODRES 2AP9 MSE F 250 MET SELENOMETHIONINE
HET MSE A 42 8
HET MSE A 55 8
HET MSE A 78 8
HET MSE A 105 8
HET MSE A 167 8
HET MSE A 213 8
HET MSE A 250 8
HET MSE B 42 8
HET MSE B 55 8
HET MSE B 78 8
HET MSE B 105 8
HET MSE B 167 8
HET MSE B 213 8
HET MSE B 250 8
HET MSE C 42 8
HET MSE C 55 8
HET MSE C 78 8
HET MSE C 105 8
HET MSE C 167 8
HET MSE C 213 8
HET MSE C 250 8
HET MSE D 42 8
HET MSE D 55 8
HET MSE D 78 8
HET MSE D 105 8
HET MSE D 167 8
HET MSE D 213 8
HET MSE D 250 8
HET MSE E 42 8
HET MSE E 55 8
HET MSE E 78 8
HET MSE E 105 8
HET MSE E 167 8
HET MSE E 213 8
HET MSE E 250 8
HET MSE F 42 8
HET MSE F 55 8
HET MSE F 78 8
HET MSE F 105 8
HET MSE F 167 8
HET MSE F 213 8
HET MSE F 250 8
HET MG A1002 1
HET NI A1003 1
HET MG D1001 1
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM NI NICKEL (II) ION
FORMUL 1 MSE 42(C5 H11 N O2 SE)
FORMUL 7 MG 2(MG 2+)
FORMUL 8 NI NI 2+
FORMUL 10 HOH *113(H2 O)
HELIX 1 1 PRO A 10 HIS A 29 1 20
HELIX 2 2 GLY A 39 ASP A 44 1 6
HELIX 3 3 ASP A 44 ASN A 60 1 17
HELIX 4 4 GLY A 72 GLY A 83 1 12
HELIX 5 5 THR A 96 GLN A 110 1 15
HELIX 6 6 GLN A 110 ASN A 120 1 11
HELIX 7 7 GLU A 132 GLN A 135 5 4
HELIX 8 8 ASN A 163 ALA A 173 1 11
HELIX 9 9 ASN A 194 LEU A 206 1 13
HELIX 10 10 THR A 236 LEU A 243 1 8
HELIX 11 11 PRO A 244 LEU A 246 5 3
HELIX 12 12 MSE A 250 GLY A 264 1 15
HELIX 13 13 HIS A 277 THR A 285 1 9
HELIX 14 14 GLY A 298 HIS A 304 1 7
HELIX 15 15 PRO B 10 GLU B 20 1 11
HELIX 16 16 ALA B 21 HIS B 29 1 9
HELIX 17 17 GLY B 39 ASP B 44 1 6
HELIX 18 18 ASP B 44 ASN B 60 1 17
HELIX 19 19 GLY B 72 LEU B 82 1 11
HELIX 20 20 THR B 96 GLN B 110 1 15
HELIX 21 21 GLN B 110 ASN B 120 1 11
HELIX 22 22 GLU B 132 GLN B 135 5 4
HELIX 23 23 ASN B 163 ALA B 173 1 11
HELIX 24 24 ASN B 194 LEU B 206 1 13
HELIX 25 25 LEU B 239 LEU B 246 5 8
HELIX 26 26 MSE B 250 ILE B 262 1 13
HELIX 27 27 HIS B 277 THR B 285 1 9
HELIX 28 28 PRO C 10 GLU C 20 1 11
HELIX 29 29 ALA C 21 HIS C 29 1 9
HELIX 30 30 GLY C 39 ASP C 44 1 6
HELIX 31 31 ASP C 44 ASN C 60 1 17
HELIX 32 32 GLY C 72 LEU C 82 1 11
HELIX 33 33 THR C 96 GLN C 110 1 15
HELIX 34 34 GLN C 110 ASN C 120 1 11
HELIX 35 35 GLU C 132 GLN C 135 5 4
HELIX 36 36 ASN C 163 ALA C 173 1 11
HELIX 37 37 ASN C 194 LEU C 206 1 13
HELIX 38 38 THR C 236 LEU C 242 1 7
HELIX 39 39 GLU C 247 GLY C 249 5 3
HELIX 40 40 MSE C 250 ILE C 262 1 13
HELIX 41 41 HIS C 277 THR C 285 1 9
HELIX 42 42 PRO D 10 GLU D 20 1 11
HELIX 43 43 ALA D 21 HIS D 29 1 9
HELIX 44 44 GLY D 39 ASP D 44 1 6
HELIX 45 45 ASP D 44 ASN D 60 1 17
HELIX 46 46 GLY D 72 GLY D 83 1 12
HELIX 47 47 THR D 96 GLN D 110 1 15
HELIX 48 48 GLN D 110 ASN D 120 1 11
HELIX 49 49 GLU D 132 GLN D 135 5 4
HELIX 50 50 ASN D 163 ALA D 173 1 11
HELIX 51 51 ASN D 194 LEU D 206 1 13
HELIX 52 52 LEU D 242 LEU D 246 5 5
HELIX 53 53 MSE D 250 GLY D 264 1 15
HELIX 54 54 HIS D 277 PHE D 284 1 8
HELIX 55 55 PRO E 10 GLU E 20 1 11
HELIX 56 56 ALA E 21 HIS E 29 1 9
HELIX 57 57 GLY E 39 ASP E 44 1 6
HELIX 58 58 ASP E 44 ASN E 60 1 17
HELIX 59 59 GLY E 72 LEU E 82 1 11
HELIX 60 60 THR E 96 GLN E 110 1 15
HELIX 61 61 GLN E 110 ASN E 120 1 11
HELIX 62 62 GLU E 132 GLN E 135 5 4
HELIX 63 63 ASN E 163 ALA E 173 1 11
HELIX 64 64 ASN E 194 LEU E 206 1 13
HELIX 65 65 GLU E 247 GLY E 249 5 3
HELIX 66 66 MSE E 250 ILE E 262 1 13
HELIX 67 67 HIS E 277 THR E 285 1 9
HELIX 68 68 PRO F 10 GLU F 20 1 11
HELIX 69 69 ALA F 21 HIS F 29 1 9
HELIX 70 70 GLY F 39 ASP F 44 1 6
HELIX 71 71 ASP F 44 ASN F 60 1 17
HELIX 72 72 GLY F 72 GLY F 83 1 12
HELIX 73 73 THR F 96 GLN F 110 1 15
HELIX 74 74 GLN F 110 ASN F 120 1 11
HELIX 75 75 GLU F 132 GLN F 135 5 4
HELIX 76 76 ASN F 163 ALA F 173 1 11
HELIX 77 77 ASN F 194 LEU F 206 1 13
HELIX 78 78 GLY F 237 LEU F 242 1 6
HELIX 79 79 MSE F 250 GLY F 263 1 14
HELIX 80 80 HIS F 277 THR F 285 1 9
SHEET 1 A 8 ALA A 126 THR A 130 0
SHEET 2 A 8 ILE A 176 SER A 180 1 O VAL A 178 N VAL A 127
SHEET 3 A 8 HIS A 64 HIS A 69 1 N VAL A 67 O VAL A 179
SHEET 4 A 8 VAL A 32 TYR A 37 1 N VAL A 35 O VAL A 68
SHEET 5 A 8 LYS A 210 THR A 215 1 O LEU A 212 N VAL A 34
SHEET 6 A 8 SER A 267 ASP A 272 1 O HIS A 269 N LEU A 211
SHEET 7 A 8 THR A 291 VAL A 294 -1 O VAL A 293 N ALA A 268
SHEET 8 A 8 GLU A 233 ASP A 235 1 N ILE A 234 O LYS A 292
SHEET 1 B 4 PHE A 137 ARG A 141 0
SHEET 2 B 4 VAL A 156 VAL A 162 -1 O ASP A 160 N THR A 138
SHEET 3 B 4 VAL A 190 ILE A 193 1 O ASN A 192 N GLY A 157
SHEET 4 B 4 LEU A 182 PRO A 184 -1 N ALA A 183 O HIS A 191
SHEET 1 C 2 LEU A 220 TYR A 221 0
SHEET 2 C 2 LEU A 230 VAL A 231 -1 O VAL A 231 N LEU A 220
SHEET 1 D 8 ALA B 126 THR B 130 0
SHEET 2 D 8 ILE B 176 SER B 180 1 O VAL B 178 N VAL B 127
SHEET 3 D 8 HIS B 64 HIS B 69 1 N VAL B 67 O VAL B 179
SHEET 4 D 8 VAL B 32 TYR B 37 1 N VAL B 35 O VAL B 68
SHEET 5 D 8 LYS B 210 THR B 215 1 O LEU B 212 N VAL B 34
SHEET 6 D 8 SER B 267 ASP B 272 1 O HIS B 269 N LEU B 211
SHEET 7 D 8 THR B 291 VAL B 294 -1 O THR B 291 N ILE B 270
SHEET 8 D 8 GLU B 233 ASP B 235 1 N ILE B 234 O LYS B 292
SHEET 1 E 4 PHE B 137 ARG B 141 0
SHEET 2 E 4 VAL B 156 VAL B 162 -1 O ASP B 160 N THR B 138
SHEET 3 E 4 HIS B 191 ILE B 193 1 O ASN B 192 N GLY B 157
SHEET 4 E 4 LEU B 182 ALA B 183 -1 N ALA B 183 O HIS B 191
SHEET 1 F 8 ALA C 126 THR C 130 0
SHEET 2 F 8 ILE C 176 SER C 180 1 O VAL C 178 N VAL C 127
SHEET 3 F 8 HIS C 64 HIS C 69 1 N VAL C 67 O VAL C 179
SHEET 4 F 8 VAL C 32 TYR C 37 1 N VAL C 35 O VAL C 68
SHEET 5 F 8 LYS C 210 THR C 215 1 O LEU C 212 N VAL C 34
SHEET 6 F 8 SER C 267 ASP C 272 1 O HIS C 269 N LEU C 211
SHEET 7 F 8 LYS C 292 VAL C 294 -1 O VAL C 293 N ALA C 268
SHEET 8 F 8 GLU C 233 ASP C 235 1 N ILE C 234 O LYS C 292
SHEET 1 G 4 PHE C 137 ARG C 141 0
SHEET 2 G 4 VAL C 156 VAL C 162 -1 O ASP C 160 N THR C 138
SHEET 3 G 4 HIS C 191 ILE C 193 1 O ASN C 192 N GLY C 157
SHEET 4 G 4 LEU C 182 ALA C 183 -1 N ALA C 183 O HIS C 191
SHEET 1 H 8 ALA D 126 ILE D 129 0
SHEET 2 H 8 ILE D 176 SER D 180 1 O VAL D 178 N VAL D 127
SHEET 3 H 8 HIS D 64 HIS D 69 1 N VAL D 67 O VAL D 179
SHEET 4 H 8 VAL D 32 TYR D 37 1 N VAL D 33 O HIS D 64
SHEET 5 H 8 LYS D 210 THR D 215 1 O LEU D 212 N LYS D 36
SHEET 6 H 8 SER D 267 ASP D 272 1 O HIS D 269 N MSE D 213
SHEET 7 H 8 THR D 291 VAL D 294 -1 O VAL D 293 N ALA D 268
SHEET 8 H 8 ILE D 234 ASP D 235 1 N ILE D 234 O VAL D 294
SHEET 1 I 2 PHE D 88 LYS D 89 0
SHEET 2 I 2 PHE D 92 ARG D 93 -1 O PHE D 92 N LYS D 89
SHEET 1 J 4 PHE D 137 THR D 145 0
SHEET 2 J 4 ALA D 150 VAL D 162 -1 O ASP D 158 N VAL D 140
SHEET 3 J 4 VAL D 190 ILE D 193 1 O ASN D 192 N LEU D 155
SHEET 4 J 4 LEU D 182 PRO D 184 -1 N ALA D 183 O HIS D 191
SHEET 1 K 7 ALA E 126 THR E 130 0
SHEET 2 K 7 ILE E 176 SER E 180 1 O VAL E 178 N VAL E 127
SHEET 3 K 7 HIS E 64 HIS E 69 1 N VAL E 67 O VAL E 179
SHEET 4 K 7 VAL E 32 TYR E 37 1 N VAL E 35 O VAL E 68
SHEET 5 K 7 LYS E 210 THR E 215 1 O LEU E 212 N VAL E 34
SHEET 6 K 7 SER E 267 ASP E 272 1 O HIS E 269 N LEU E 211
SHEET 7 K 7 THR E 291 VAL E 293 -1 O THR E 291 N ILE E 270
SHEET 1 L 4 PHE E 137 ARG E 141 0
SHEET 2 L 4 VAL E 156 VAL E 162 -1 O ASP E 160 N THR E 138
SHEET 3 L 4 HIS E 191 ILE E 193 1 O ASN E 192 N GLY E 157
SHEET 4 L 4 LEU E 182 ALA E 183 -1 N ALA E 183 O HIS E 191
SHEET 1 M 8 ALA F 126 THR F 130 0
SHEET 2 M 8 ILE F 176 SER F 180 1 O VAL F 178 N VAL F 127
SHEET 3 M 8 HIS F 64 HIS F 69 1 N VAL F 67 O VAL F 179
SHEET 4 M 8 VAL F 32 TYR F 37 1 N VAL F 35 O VAL F 68
SHEET 5 M 8 LYS F 210 THR F 215 1 O LEU F 212 N VAL F 34
SHEET 6 M 8 SER F 267 ASP F 272 1 O HIS F 269 N LEU F 211
SHEET 7 M 8 GLY F 290 VAL F 294 -1 O VAL F 293 N ALA F 268
SHEET 8 M 8 GLU F 233 ASP F 235 1 N ILE F 234 O LYS F 292
SHEET 1 N 4 PHE F 137 ARG F 141 0
SHEET 2 N 4 VAL F 156 VAL F 162 -1 O ASP F 160 N THR F 138
SHEET 3 N 4 VAL F 190 ILE F 193 1 O ASN F 192 N GLY F 157
SHEET 4 N 4 LEU F 182 PRO F 184 -1 N ALA F 183 O HIS F 191
LINK C ALA A 41 N MSE A 42 1555 1555 1.33
LINK C MSE A 42 N THR A 43 1555 1555 1.33
LINK C ASP A 54 N MSE A 55 1555 1555 1.33
LINK C MSE A 55 N ALA A 56 1555 1555 1.33
LINK C ALA A 77 N MSE A 78 1555 1555 1.33
LINK C MSE A 78 N LEU A 79 1555 1555 1.33
LINK C ARG A 104 N MSE A 105 1555 1555 1.33
LINK C MSE A 105 N VAL A 106 1555 1555 1.33
LINK C ALA A 166 N MSE A 167 1555 1555 1.33
LINK C MSE A 167 N LEU A 168 1555 1555 1.33
LINK C LEU A 212 N MSE A 213 1555 1555 1.33
LINK C MSE A 213 N LEU A 214 1555 1555 1.33
LINK C GLY A 249 N MSE A 250 1555 1555 1.33
LINK C MSE A 250 N VAL A 251 1555 1555 1.33
LINK C ALA B 41 N MSE B 42 1555 1555 1.33
LINK C MSE B 42 N THR B 43 1555 1555 1.33
LINK C ASP B 54 N MSE B 55 1555 1555 1.33
LINK C MSE B 55 N ALA B 56 1555 1555 1.33
LINK C ALA B 77 N MSE B 78 1555 1555 1.33
LINK C MSE B 78 N LEU B 79 1555 1555 1.33
LINK C ARG B 104 N MSE B 105 1555 1555 1.33
LINK C MSE B 105 N VAL B 106 1555 1555 1.33
LINK C ALA B 166 N MSE B 167 1555 1555 1.33
LINK C MSE B 167 N LEU B 168 1555 1555 1.33
LINK C LEU B 212 N MSE B 213 1555 1555 1.33
LINK C MSE B 213 N LEU B 214 1555 1555 1.33
LINK C GLY B 249 N MSE B 250 1555 1555 1.33
LINK C MSE B 250 N VAL B 251 1555 1555 1.33
LINK C ALA C 41 N MSE C 42 1555 1555 1.33
LINK C MSE C 42 N THR C 43 1555 1555 1.33
LINK C ASP C 54 N MSE C 55 1555 1555 1.33
LINK C MSE C 55 N ALA C 56 1555 1555 1.33
LINK C ALA C 77 N MSE C 78 1555 1555 1.33
LINK C MSE C 78 N LEU C 79 1555 1555 1.33
LINK C ARG C 104 N MSE C 105 1555 1555 1.33
LINK C MSE C 105 N VAL C 106 1555 1555 1.33
LINK C ALA C 166 N MSE C 167 1555 1555 1.33
LINK C MSE C 167 N LEU C 168 1555 1555 1.33
LINK C LEU C 212 N MSE C 213 1555 1555 1.33
LINK C MSE C 213 N LEU C 214 1555 1555 1.33
LINK C GLY C 249 N MSE C 250 1555 1555 1.33
LINK C MSE C 250 N VAL C 251 1555 1555 1.33
LINK C ALA D 41 N MSE D 42 1555 1555 1.33
LINK C MSE D 42 N THR D 43 1555 1555 1.33
LINK C ASP D 54 N MSE D 55 1555 1555 1.33
LINK C MSE D 55 N ALA D 56 1555 1555 1.33
LINK C ALA D 77 N MSE D 78 1555 1555 1.33
LINK C MSE D 78 N LEU D 79 1555 1555 1.33
LINK C ARG D 104 N MSE D 105 1555 1555 1.33
LINK C MSE D 105 N VAL D 106 1555 1555 1.33
LINK C ALA D 166 N MSE D 167 1555 1555 1.33
LINK C MSE D 167 N LEU D 168 1555 1555 1.33
LINK C LEU D 212 N MSE D 213 1555 1555 1.33
LINK C MSE D 213 N LEU D 214 1555 1555 1.33
LINK C GLY D 249 N MSE D 250 1555 1555 1.33
LINK C MSE D 250 N VAL D 251 1555 1555 1.33
LINK C ALA E 41 N MSE E 42 1555 1555 1.33
LINK C MSE E 42 N THR E 43 1555 1555 1.33
LINK C ASP E 54 N MSE E 55 1555 1555 1.33
LINK C MSE E 55 N ALA E 56 1555 1555 1.33
LINK C ALA E 77 N MSE E 78 1555 1555 1.33
LINK C MSE E 78 N LEU E 79 1555 1555 1.33
LINK C ARG E 104 N MSE E 105 1555 1555 1.33
LINK C MSE E 105 N VAL E 106 1555 1555 1.33
LINK C ALA E 166 N MSE E 167 1555 1555 1.33
LINK C MSE E 167 N LEU E 168 1555 1555 1.33
LINK C LEU E 212 N MSE E 213 1555 1555 1.33
LINK C MSE E 213 N LEU E 214 1555 1555 1.33
LINK C GLY E 249 N MSE E 250 1555 1555 1.33
LINK C MSE E 250 N VAL E 251 1555 1555 1.33
LINK C ALA F 41 N MSE F 42 1555 1555 1.33
LINK C MSE F 42 N THR F 43 1555 1555 1.33
LINK C ASP F 54 N MSE F 55 1555 1555 1.33
LINK C MSE F 55 N ALA F 56 1555 1555 1.33
LINK C ALA F 77 N MSE F 78 1555 1555 1.33
LINK C MSE F 78 N LEU F 79 1555 1555 1.33
LINK C ARG F 104 N MSE F 105 1555 1555 1.33
LINK C MSE F 105 N VAL F 106 1555 1555 1.33
LINK C ALA F 166 N MSE F 167 1555 1555 1.33
LINK C MSE F 167 N LEU F 168 1555 1555 1.33
LINK C LEU F 212 N MSE F 213 1555 1555 1.33
LINK C MSE F 213 N LEU F 214 1555 1555 1.33
LINK C GLY F 249 N MSE F 250 1555 1555 1.33
LINK C MSE F 250 N VAL F 251 1555 1555 1.33
LINK OD2 ASP A 235 MG MG A1002 1555 1555 2.09
LINK O HIS A 301 MG MG A1002 1555 1555 2.42
LINK NE2 HIS A 303 NI NI A1003 1555 1555 2.45
LINK O HIS A 304 MG MG A1002 1555 1555 2.47
CISPEP 1 TRP F 224 PRO F 225 0 0.60
SITE 1 AC1 1 GLU D 282
SITE 1 AC2 3 ASP A 235 HIS A 301 HIS A 304
SITE 1 AC3 1 HIS A 303
CRYST1 88.024 122.996 194.581 90.00 90.00 90.00 P 21 21 21 24
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 0.011361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008130 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005139 0.00000
(ATOM LINES ARE NOT SHOWN.)
END