HEADER TRANSFERASE 09-MAR-09 3GJY
TITLE CRYSTAL STRUCTURE OF A PROBABLE SPERMIDINE SYNTHASE FROM
TITLE 2 CORYNEBACTERIUM GLUTAMICUM ATCC 13032
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPERMIDINE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM ATCC 13032;
SOURCE 3 ORGANISM_TAXID: 196627;
SOURCE 4 STRAIN: DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
SOURCE 5 ATCC: 13032;
SOURCE 6 GENE: CGL1237, CG1394;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS APC62791, SPERMIDINE SYNTHASE, CORYNEBACTERIUM GLUTAMICUM
KEYWDS 2 ATCC 13032, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,H.LI,L.FREEMAN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 24-MAR-09 3GJY 0
JRNL AUTH K.TAN,H.LI,L.FREEMAN,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A PROBABLE SPERMIDINE
JRNL TITL 2 SYNTHASE FROM CORYNEBACTERIUM GLUTAMICUM ATCC
JRNL TITL 3 13032.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0054
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 48639
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2614
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3414
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 162
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2251
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 388
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.02000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.077
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.067
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.035
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.009
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2323 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3181 ; 1.459 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 315 ; 6.159 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;34.834 ;23.274
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 379 ;12.740 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;17.204 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 348 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1832 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1445 ; 1.454 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2340 ; 2.231 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 878 ; 3.140 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 821 ; 4.535 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2323 ; 1.702 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 385 ; 6.758 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2254 ; 4.150 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3GJY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB051954.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
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 : SI(111) CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51371
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 23.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 43.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, ARP/WARP, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE, 20%
REMARK 280 PEG 3350, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
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 26.45450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.65400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.50450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.65400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.45450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.50450
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: AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN
REMARK 300 IS EXPERIMENTALLY UNKNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 ALA A 2
REMARK 465 ARG A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 ASN A 6
REMARK 465 THR A 7
REMARK 465 SER A 8
REMARK 465 ASP A 9
REMARK 465 GLN A 10
REMARK 465 SER A 11
REMARK 465 ARG A 12
REMARK 465 SER A 13
REMARK 465 GLN A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 ASN A 17
REMARK 465 SER A 297
REMARK 465 ASP A 298
REMARK 465 THR A 299
REMARK 465 PRO A 300
REMARK 465 GLN A 301
REMARK 465 HIS A 302
REMARK 465 PRO A 303
REMARK 465 ALA A 304
REMARK 465 GLU A 305
REMARK 465 THR A 306
REMARK 465 PRO A 307
REMARK 465 GLU A 308
REMARK 465 HIS A 309
REMARK 465 SER A 310
REMARK 465 ASN A 311
REMARK 465 THR A 312
REMARK 465 GLN A 313
REMARK 465 PRO A 314
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 OG SER A 151 O HOH A 394 1.83
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 ARG A 157 NE - CZ - NH2 ANGL. DEV. = 4.0 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 97 11.48 58.41
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 HIS A 200 SER A 201 -148.81
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 FMT A 315
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC62791 RELATED DB: TARGETDB
DBREF 3GJY A 1 314 UNP Q8NR27 Q8NR27_CORGL 1 314
SEQADV 3GJY SER A -2 UNP Q8NR27 EXPRESSION TAG
SEQADV 3GJY ASN A -1 UNP Q8NR27 EXPRESSION TAG
SEQADV 3GJY ALA A 0 UNP Q8NR27 EXPRESSION TAG
SEQRES 1 A 317 SER ASN ALA MSE ALA ARG LYS LYS ASN THR SER ASP GLN
SEQRES 2 A 317 SER ARG SER GLN ALA ALA ASN THR PRO ILE ALA GLY THR
SEQRES 3 A 317 TYR GLU GLY GLU TYR SER VAL ILE GLU LEU GLU ALA ASP
SEQRES 4 A 317 SER TYR THR THR ASP GLY TRP LEU ILE SER ILE ASN GLY
SEQRES 5 A 317 VAL PRO SER SER HIS ILE VAL LEU GLY GLN PRO GLN ALA
SEQRES 6 A 317 LEU GLU PHE GLU TYR MSE ARG TRP ILE ALA THR GLY ALA
SEQRES 7 A 317 ARG ALA PHE ILE ASP ALA HIS GLN ASP ALA SER LYS LEU
SEQRES 8 A 317 ARG ILE THR HIS LEU GLY GLY GLY ALA CYS THR MSE ALA
SEQRES 9 A 317 ARG TYR PHE ALA ASP VAL TYR PRO GLN SER ARG ASN THR
SEQRES 10 A 317 VAL VAL GLU LEU ASP ALA GLU LEU ALA ARG LEU SER ARG
SEQRES 11 A 317 GLU TRP PHE ASP ILE PRO ARG ALA PRO ARG VAL LYS ILE
SEQRES 12 A 317 ARG VAL ASP ASP ALA ARG MSE VAL ALA GLU SER PHE THR
SEQRES 13 A 317 PRO ALA SER ARG ASP VAL ILE ILE ARG ASP VAL PHE ALA
SEQRES 14 A 317 GLY ALA ILE THR PRO GLN ASN PHE THR THR VAL GLU PHE
SEQRES 15 A 317 PHE GLU HIS CYS HIS ARG GLY LEU ALA PRO GLY GLY LEU
SEQRES 16 A 317 TYR VAL ALA ASN CYS GLY ASP HIS SER ASP LEU ARG GLY
SEQRES 17 A 317 ALA LYS SER GLU LEU ALA GLY MSE MSE GLU VAL PHE GLU
SEQRES 18 A 317 HIS VAL ALA VAL ILE ALA ASP PRO PRO MSE LEU LYS GLY
SEQRES 19 A 317 ARG ARG TYR GLY ASN ILE ILE LEU MSE GLY SER ASP THR
SEQRES 20 A 317 GLU PHE PHE SER SER ASN SER THR GLU ALA SER ALA ILE
SEQRES 21 A 317 THR ARG GLU LEU LEU GLY GLY GLY VAL PRO ALA GLN TYR
SEQRES 22 A 317 LYS ASP GLU SER TRP VAL ARG LYS PHE ALA SER GLY ALA
SEQRES 23 A 317 GLN ALA ARG HIS ASP GLY VAL SER THR LEU GLN MSE PRO
SEQRES 24 A 317 SER ASP THR PRO GLN HIS PRO ALA GLU THR PRO GLU HIS
SEQRES 25 A 317 SER ASN THR GLN PRO
MODRES 3GJY MSE A 68 MET SELENOMETHIONINE
MODRES 3GJY MSE A 100 MET SELENOMETHIONINE
MODRES 3GJY MSE A 147 MET SELENOMETHIONINE
MODRES 3GJY MSE A 213 MET SELENOMETHIONINE
MODRES 3GJY MSE A 214 MET SELENOMETHIONINE
MODRES 3GJY MSE A 228 MET SELENOMETHIONINE
MODRES 3GJY MSE A 240 MET SELENOMETHIONINE
MODRES 3GJY MSE A 295 MET SELENOMETHIONINE
HET MSE A 68 8
HET MSE A 100 13
HET MSE A 147 13
HET MSE A 213 8
HET MSE A 214 8
HET MSE A 228 8
HET MSE A 240 8
HET MSE A 295 8
HET FMT A 315 3
HETNAM MSE SELENOMETHIONINE
HETNAM FMT FORMIC ACID
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 FMT C H2 O2
FORMUL 3 HOH *385(H2 O)
HELIX 1 1 PHE A 65 GLN A 83 1 19
HELIX 2 2 ASP A 84 LYS A 87 5 4
HELIX 3 3 GLY A 95 ALA A 97 5 3
HELIX 4 4 CYS A 98 TYR A 108 1 11
HELIX 5 5 ASP A 119 PHE A 130 1 12
HELIX 6 6 ASP A 144 SER A 151 1 8
HELIX 7 7 PRO A 171 THR A 175 5 5
HELIX 8 8 THR A 176 GLY A 186 1 11
HELIX 9 9 LEU A 203 PHE A 217 1 15
HELIX 10 10 ASP A 225 LYS A 230 1 6
HELIX 11 11 SER A 251 LEU A 262 1 12
HELIX 12 12 ASP A 272 ALA A 280 1 9
SHEET 1 A 4 GLY A 22 GLU A 25 0
SHEET 2 A 4 VAL A 30 ALA A 35 -1 O ILE A 31 N TYR A 24
SHEET 3 A 4 GLY A 42 ILE A 47 -1 O LEU A 44 N GLU A 34
SHEET 4 A 4 VAL A 50 VAL A 56 -1 O SER A 52 N ILE A 45
SHEET 1 B 8 VAL A 138 VAL A 142 0
SHEET 2 B 8 ARG A 112 GLU A 117 1 N VAL A 115 O ARG A 141
SHEET 3 B 8 ARG A 89 LEU A 93 1 N HIS A 92 O THR A 114
SHEET 4 B 8 ARG A 157 ARG A 162 1 O ILE A 161 N LEU A 93
SHEET 5 B 8 LEU A 187 ASP A 199 1 O ASN A 196 N ARG A 162
SHEET 6 B 8 GLY A 235 SER A 242 -1 O GLY A 241 N TYR A 193
SHEET 7 B 8 HIS A 219 ALA A 224 -1 N ILE A 223 O ILE A 238
SHEET 8 B 8 GLN A 269 LYS A 271 -1 O LYS A 271 N VAL A 222
LINK C TYR A 67 N MSE A 68 1555 1555 1.34
LINK C MSE A 68 N ARG A 69 1555 1555 1.35
LINK C THR A 99 N MSE A 100 1555 1555 1.34
LINK C MSE A 100 N ALA A 101 1555 1555 1.34
LINK C ARG A 146 N MSE A 147 1555 1555 1.33
LINK C MSE A 147 N VAL A 148 1555 1555 1.33
LINK C GLY A 212 N MSE A 213 1555 1555 1.33
LINK C MSE A 213 N MSE A 214 1555 1555 1.34
LINK C MSE A 214 N GLU A 215 1555 1555 1.33
LINK C PRO A 227 N MSE A 228 1555 1555 1.33
LINK C MSE A 228 N LEU A 229 1555 1555 1.33
LINK C LEU A 239 N MSE A 240 1555 1555 1.34
LINK C MSE A 240 N GLY A 241 1555 1555 1.33
LINK C GLN A 294 N MSE A 295 1555 1555 1.33
LINK C MSE A 295 N PRO A 296 1555 1555 1.36
CISPEP 1 ALA A 135 PRO A 136 0 9.20
SITE 1 AC1 7 GLY A 95 ALA A 97 CYS A 98 VAL A 115
SITE 2 AC1 7 GLU A 117 LEU A 122 SER A 126
CRYST1 52.909 65.009 87.308 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018900 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015382 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011454 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
