HEADER OXIDOREDUCTASE 14-SEP-09 3JU8
TITLE CRYSTAL STRUCTURE OF SUCCINYLGLUTAMIC SEMIALDEHYDE DEHYDROGENASE FROM
TITLE 2 PSEUDOMONAS AERUGINOSA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINYLGLUTAMIC SEMIALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: N-SUCCINYLGLUTAMATE 5-SEMIALDEHYDE DEHYDROGENASE, SGSD;
COMPND 5 EC: 1.2.1.71;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: PA01;
SOURCE 5 GENE: ARUD, ASTD, PA0898;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG9
KEYWDS ALPHA-BETA STRUCTURE, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, ARGININE
KEYWDS 3 METABOLISM, NAD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,H.LI,K.BUCK,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS
AUTHOR 2 (MCSG)
REVDAT 3 16-NOV-11 3JU8 1 HETATM
REVDAT 2 13-JUL-11 3JU8 1 VERSN
REVDAT 1 22-SEP-09 3JU8 0
JRNL AUTH Y.KIM,H.LI,K.BUCK,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF SUCCINYLGLUTAMIC SEMIALDEHYDE
JRNL TITL 2 DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_138)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 104285
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5214
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 32.7807 - 3.9191 0.98 10090 516 0.1414 0.1650
REMARK 3 2 3.9191 - 3.1115 0.99 9981 522 0.1441 0.1694
REMARK 3 3 3.1115 - 2.7184 1.00 9977 555 0.1663 0.2141
REMARK 3 4 2.7184 - 2.4699 1.00 9952 511 0.1632 0.2217
REMARK 3 5 2.4699 - 2.2930 1.00 9887 488 0.1484 0.1879
REMARK 3 6 2.2930 - 2.1578 1.00 9910 534 0.1511 0.1974
REMARK 3 7 2.1578 - 2.0497 1.00 9976 497 0.1582 0.2183
REMARK 3 8 2.0497 - 1.9605 1.00 9839 532 0.1752 0.2162
REMARK 3 9 1.9605 - 1.8851 1.00 9908 539 0.1923 0.2409
REMARK 3 10 1.8851 - 1.8200 0.98 9551 520 0.2296 0.2648
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 59.84
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.21470
REMARK 3 B22 (A**2) : 13.07340
REMARK 3 B33 (A**2) : -8.85870
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.52740
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 8121
REMARK 3 ANGLE : 1.464 11141
REMARK 3 CHIRALITY : 0.102 1233
REMARK 3 PLANARITY : 0.007 1481
REMARK 3 DIHEDRAL : 18.816 3039
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain B
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7164 19.9414 33.2851
REMARK 3 T TENSOR
REMARK 3 T11: 0.1120 T22: 0.0877
REMARK 3 T33: 0.1270 T12: -0.0194
REMARK 3 T13: 0.0094 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 0.5350 L22: 0.1620
REMARK 3 L33: 0.6065 L12: 0.0313
REMARK 3 L13: -0.2072 L23: -0.0564
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: 0.0264 S13: -0.0605
REMARK 3 S21: 0.0142 S22: 0.0136 S23: -0.0202
REMARK 3 S31: 0.0417 S32: 0.0696 S33: 0.0006
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3JU8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB055165.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104456
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 32.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000,SHELXD,MLPHARE,DM,RESOLVE,COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M MAGNESIUM SULFATE 0.1 M MES PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 68.55850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.01650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.55850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.01650
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: 13650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -167.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 773 LIES ON A SPECIAL POSITION.
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 SER A 487
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 SER B 487
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 424 O HOH A 926 2.06
REMARK 500 O HOH A 799 O HOH B 798 2.19
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 THR A 4 -81.16 -110.58
REMARK 500 VAL A 25 -66.97 -93.22
REMARK 500 ALA A 126 -126.00 52.08
REMARK 500 ALA A 371 -71.94 -57.50
REMARK 500 GLU A 372 78.50 -109.47
REMARK 500 ASP A 375 76.46 -106.03
REMARK 500 SER A 456 -148.22 -109.02
REMARK 500 ALA A 457 -125.33 51.54
REMARK 500 VAL B 25 -66.24 -93.10
REMARK 500 ALA B 126 -126.22 51.52
REMARK 500 ALA B 371 -71.31 -57.73
REMARK 500 SER B 456 -154.17 -101.77
REMARK 500 ALA B 457 -127.02 56.06
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 510 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 631 O
REMARK 620 2 HOH B 630 O 91.2
REMARK 620 3 HOH B 904 O 94.3 87.1
REMARK 620 4 HOH B 632 O 171.4 88.6 77.1
REMARK 620 5 HOH B 633 O 94.0 94.7 171.5 94.6
REMARK 620 6 HOH B 896 O 96.3 171.6 88.5 83.4 88.6
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 NAD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 510
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC37529.1 RELATED DB: TARGETDB
DBREF 3JU8 A 2 487 UNP O50174 ASTD_PSEAE 1 486
DBREF 3JU8 B 2 487 UNP O50174 ASTD_PSEAE 1 486
SEQADV 3JU8 SER A -2 UNP O50174 EXPRESSION TAG
SEQADV 3JU8 ASN A -1 UNP O50174 EXPRESSION TAG
SEQADV 3JU8 ALA A 0 UNP O50174 EXPRESSION TAG
SEQADV 3JU8 MSE A 1 UNP O50174 EXPRESSION TAG
SEQADV 3JU8 SER B -2 UNP O50174 EXPRESSION TAG
SEQADV 3JU8 ASN B -1 UNP O50174 EXPRESSION TAG
SEQADV 3JU8 ALA B 0 UNP O50174 EXPRESSION TAG
SEQADV 3JU8 MSE B 1 UNP O50174 EXPRESSION TAG
SEQRES 1 A 490 SER ASN ALA MSE MSE SER THR HIS TYR ILE ALA GLY GLN
SEQRES 2 A 490 TRP LEU ALA GLY GLN GLY GLU THR LEU GLU SER LEU ASP
SEQRES 3 A 490 PRO VAL GLY GLN GLY VAL VAL TRP SER GLY ARG GLY ALA
SEQRES 4 A 490 ASP ALA THR GLN VAL ASP ALA ALA VAL CYS ALA ALA ARG
SEQRES 5 A 490 GLU ALA PHE PRO ALA TRP ALA ARG ARG PRO LEU GLU GLN
SEQRES 6 A 490 ARG ILE GLU LEU LEU GLU ARG PHE ALA ALA THR LEU LYS
SEQRES 7 A 490 SER ARG ALA ASP GLU LEU ALA ARG VAL ILE GLY GLU GLU
SEQRES 8 A 490 THR GLY LYS PRO LEU TRP GLU SER ALA THR GLU VAL THR
SEQRES 9 A 490 SER MSE VAL ASN LYS VAL ALA ILE SER VAL GLN ALA PHE
SEQRES 10 A 490 ARG GLU ARG THR GLY GLU LYS SER GLY PRO LEU ALA ASP
SEQRES 11 A 490 ALA THR ALA VAL LEU ARG HIS LYS PRO HIS GLY VAL VAL
SEQRES 12 A 490 ALA VAL PHE GLY PRO TYR ASN PHE PRO GLY HIS LEU PRO
SEQRES 13 A 490 ASN GLY HIS ILE VAL PRO ALA LEU LEU ALA GLY ASN CYS
SEQRES 14 A 490 VAL VAL PHE LYS PRO SER GLU LEU THR PRO LYS VAL ALA
SEQRES 15 A 490 GLU LEU THR LEU LYS ALA TRP ILE GLN ALA GLY LEU PRO
SEQRES 16 A 490 ALA GLY VAL LEU ASN LEU VAL GLN GLY GLY ARG GLU THR
SEQRES 17 A 490 GLY VAL ALA LEU ALA ALA HIS ARG GLY LEU ASP GLY LEU
SEQRES 18 A 490 PHE PHE THR GLY SER SER ARG THR GLY ASN LEU LEU HIS
SEQRES 19 A 490 SER GLN PHE GLY GLY GLN PRO GLN LYS ILE LEU ALA LEU
SEQRES 20 A 490 GLU MSE GLY GLY ASN ASN PRO LEU VAL VAL GLU GLU VAL
SEQRES 21 A 490 ALA ASP LEU ASP ALA ALA VAL TYR THR ILE ILE GLN SER
SEQRES 22 A 490 ALA PHE ILE SER ALA GLY GLN ARG CYS THR CYS ALA ARG
SEQRES 23 A 490 ARG LEU LEU VAL PRO GLN GLY ALA TRP GLY ASP ALA LEU
SEQRES 24 A 490 LEU ALA ARG LEU VAL ALA VAL SER ALA THR LEU ARG VAL
SEQRES 25 A 490 GLY ARG PHE ASP GLU GLN PRO ALA PRO PHE MSE GLY ALA
SEQRES 26 A 490 VAL ILE SER LEU SER ALA ALA GLU HIS LEU LEU LYS ALA
SEQRES 27 A 490 GLN GLU HIS LEU ILE GLY LYS GLY ALA GLN PRO LEU LEU
SEQRES 28 A 490 ALA MSE THR GLN PRO ILE ASP GLY ALA ALA LEU LEU THR
SEQRES 29 A 490 PRO GLY ILE LEU ASP VAL SER ALA VAL ALA GLU ARG PRO
SEQRES 30 A 490 ASP GLU GLU PHE PHE GLY PRO LEU LEU GLN VAL ILE ARG
SEQRES 31 A 490 TYR SER ASP PHE ALA ALA ALA ILE ARG GLU ALA ASN ALA
SEQRES 32 A 490 THR GLN TYR GLY LEU ALA ALA GLY LEU LEU SER ASP SER
SEQRES 33 A 490 ARG GLU ARG PHE GLU GLN PHE LEU VAL GLU SER ARG ALA
SEQRES 34 A 490 GLY ILE VAL ASN TRP ASN LYS GLN LEU THR GLY ALA ALA
SEQRES 35 A 490 SER SER ALA PRO PHE GLY GLY ILE GLY ALA SER GLY ASN
SEQRES 36 A 490 HIS ARG PRO SER ALA TYR TYR ALA ALA ASP TYR CYS ALA
SEQRES 37 A 490 TYR PRO VAL ALA SER LEU GLU SER PRO SER VAL SER LEU
SEQRES 38 A 490 PRO ALA THR LEU THR PRO GLY ILE SER
SEQRES 1 B 490 SER ASN ALA MSE MSE SER THR HIS TYR ILE ALA GLY GLN
SEQRES 2 B 490 TRP LEU ALA GLY GLN GLY GLU THR LEU GLU SER LEU ASP
SEQRES 3 B 490 PRO VAL GLY GLN GLY VAL VAL TRP SER GLY ARG GLY ALA
SEQRES 4 B 490 ASP ALA THR GLN VAL ASP ALA ALA VAL CYS ALA ALA ARG
SEQRES 5 B 490 GLU ALA PHE PRO ALA TRP ALA ARG ARG PRO LEU GLU GLN
SEQRES 6 B 490 ARG ILE GLU LEU LEU GLU ARG PHE ALA ALA THR LEU LYS
SEQRES 7 B 490 SER ARG ALA ASP GLU LEU ALA ARG VAL ILE GLY GLU GLU
SEQRES 8 B 490 THR GLY LYS PRO LEU TRP GLU SER ALA THR GLU VAL THR
SEQRES 9 B 490 SER MSE VAL ASN LYS VAL ALA ILE SER VAL GLN ALA PHE
SEQRES 10 B 490 ARG GLU ARG THR GLY GLU LYS SER GLY PRO LEU ALA ASP
SEQRES 11 B 490 ALA THR ALA VAL LEU ARG HIS LYS PRO HIS GLY VAL VAL
SEQRES 12 B 490 ALA VAL PHE GLY PRO TYR ASN PHE PRO GLY HIS LEU PRO
SEQRES 13 B 490 ASN GLY HIS ILE VAL PRO ALA LEU LEU ALA GLY ASN CYS
SEQRES 14 B 490 VAL VAL PHE LYS PRO SER GLU LEU THR PRO LYS VAL ALA
SEQRES 15 B 490 GLU LEU THR LEU LYS ALA TRP ILE GLN ALA GLY LEU PRO
SEQRES 16 B 490 ALA GLY VAL LEU ASN LEU VAL GLN GLY GLY ARG GLU THR
SEQRES 17 B 490 GLY VAL ALA LEU ALA ALA HIS ARG GLY LEU ASP GLY LEU
SEQRES 18 B 490 PHE PHE THR GLY SER SER ARG THR GLY ASN LEU LEU HIS
SEQRES 19 B 490 SER GLN PHE GLY GLY GLN PRO GLN LYS ILE LEU ALA LEU
SEQRES 20 B 490 GLU MSE GLY GLY ASN ASN PRO LEU VAL VAL GLU GLU VAL
SEQRES 21 B 490 ALA ASP LEU ASP ALA ALA VAL TYR THR ILE ILE GLN SER
SEQRES 22 B 490 ALA PHE ILE SER ALA GLY GLN ARG CYS THR CYS ALA ARG
SEQRES 23 B 490 ARG LEU LEU VAL PRO GLN GLY ALA TRP GLY ASP ALA LEU
SEQRES 24 B 490 LEU ALA ARG LEU VAL ALA VAL SER ALA THR LEU ARG VAL
SEQRES 25 B 490 GLY ARG PHE ASP GLU GLN PRO ALA PRO PHE MSE GLY ALA
SEQRES 26 B 490 VAL ILE SER LEU SER ALA ALA GLU HIS LEU LEU LYS ALA
SEQRES 27 B 490 GLN GLU HIS LEU ILE GLY LYS GLY ALA GLN PRO LEU LEU
SEQRES 28 B 490 ALA MSE THR GLN PRO ILE ASP GLY ALA ALA LEU LEU THR
SEQRES 29 B 490 PRO GLY ILE LEU ASP VAL SER ALA VAL ALA GLU ARG PRO
SEQRES 30 B 490 ASP GLU GLU PHE PHE GLY PRO LEU LEU GLN VAL ILE ARG
SEQRES 31 B 490 TYR SER ASP PHE ALA ALA ALA ILE ARG GLU ALA ASN ALA
SEQRES 32 B 490 THR GLN TYR GLY LEU ALA ALA GLY LEU LEU SER ASP SER
SEQRES 33 B 490 ARG GLU ARG PHE GLU GLN PHE LEU VAL GLU SER ARG ALA
SEQRES 34 B 490 GLY ILE VAL ASN TRP ASN LYS GLN LEU THR GLY ALA ALA
SEQRES 35 B 490 SER SER ALA PRO PHE GLY GLY ILE GLY ALA SER GLY ASN
SEQRES 36 B 490 HIS ARG PRO SER ALA TYR TYR ALA ALA ASP TYR CYS ALA
SEQRES 37 B 490 TYR PRO VAL ALA SER LEU GLU SER PRO SER VAL SER LEU
SEQRES 38 B 490 PRO ALA THR LEU THR PRO GLY ILE SER
MODRES 3JU8 MSE A 1 MET SELENOMETHIONINE
MODRES 3JU8 MSE A 2 MET SELENOMETHIONINE
MODRES 3JU8 MSE A 103 MET SELENOMETHIONINE
MODRES 3JU8 MSE A 246 MET SELENOMETHIONINE
MODRES 3JU8 MSE A 320 MET SELENOMETHIONINE
MODRES 3JU8 MSE A 350 MET SELENOMETHIONINE
MODRES 3JU8 MSE B 2 MET SELENOMETHIONINE
MODRES 3JU8 MSE B 103 MET SELENOMETHIONINE
MODRES 3JU8 MSE B 246 MET SELENOMETHIONINE
MODRES 3JU8 MSE B 320 MET SELENOMETHIONINE
MODRES 3JU8 MSE B 350 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 2 8
HET MSE A 103 8
HET MSE A 246 8
HET MSE A 320 8
HET MSE A 350 8
HET MSE B 2 8
HET MSE B 103 8
HET MSE B 246 8
HET MSE B 320 8
HET MSE B 350 8
HET NAD A 501 44
HET SO4 A 502 5
HET SO4 A 503 5
HET SIN A 504 8
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET GOL A 508 6
HET GOL A 509 6
HET GOL A 510 6
HET GOL A 511 6
HET GOL A 512 6
HET GOL A 488 6
HET GOL A 489 6
HET NAD B 501 44
HET SO4 B 502 5
HET SO4 B 503 5
HET SO4 B 504 5
HET CL B 505 1
HET CL B 506 1
HET GOL B 509 6
HET MG B 510 1
HETNAM MSE SELENOMETHIONINE
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM SO4 SULFATE ION
HETNAM SIN SUCCINIC ACID
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 4 SO4 8(O4 S 2-)
FORMUL 6 SIN C4 H6 O4
FORMUL 10 GOL 8(C3 H8 O3)
FORMUL 21 CL 2(CL 1-)
FORMUL 24 MG MG 2+
FORMUL 25 HOH *929(H2 O)
HELIX 1 1 ASP A 37 ARG A 58 1 22
HELIX 2 2 PRO A 59 ARG A 77 1 19
HELIX 3 3 ARG A 77 GLY A 90 1 14
HELIX 4 4 PRO A 92 THR A 118 1 27
HELIX 5 5 GLY A 150 GLY A 164 1 15
HELIX 6 6 THR A 175 ALA A 189 1 15
HELIX 7 7 GLY A 202 ALA A 211 1 10
HELIX 8 8 SER A 223 PHE A 234 1 12
HELIX 9 9 ASP A 259 ILE A 273 1 15
HELIX 10 10 SER A 274 GLN A 277 5 4
HELIX 11 11 GLY A 290 LEU A 307 1 18
HELIX 12 12 SER A 325 LYS A 342 1 18
HELIX 13 13 ASP A 390 ALA A 400 1 11
HELIX 14 14 SER A 413 SER A 424 1 12
HELIX 15 15 ILE A 447 GLY A 451 5 5
HELIX 16 16 TYR A 459 CYS A 464 1 6
HELIX 17 17 ASP B 37 ARG B 58 1 22
HELIX 18 18 PRO B 59 ARG B 77 1 19
HELIX 19 19 ARG B 77 GLY B 90 1 14
HELIX 20 20 PRO B 92 THR B 118 1 27
HELIX 21 21 GLY B 150 GLY B 164 1 15
HELIX 22 22 THR B 175 ALA B 189 1 15
HELIX 23 23 GLY B 202 ALA B 211 1 10
HELIX 24 24 SER B 223 GLY B 235 1 13
HELIX 25 25 ASP B 259 PHE B 272 1 14
HELIX 26 26 ILE B 273 GLN B 277 5 5
HELIX 27 27 GLY B 290 ALA B 305 1 16
HELIX 28 28 SER B 325 LYS B 342 1 18
HELIX 29 29 ASP B 390 ALA B 400 1 11
HELIX 30 30 SER B 413 SER B 424 1 12
HELIX 31 31 ILE B 447 GLY B 451 5 5
HELIX 32 32 TYR B 459 CYS B 464 1 6
SHEET 1 A 2 HIS A 5 ILE A 7 0
SHEET 2 A 2 GLN A 10 LEU A 12 -1 O LEU A 12 N HIS A 5
SHEET 1 B 2 THR A 18 LEU A 22 0
SHEET 2 B 2 VAL A 29 ARG A 34 -1 O GLY A 33 N LEU A 19
SHEET 1 C 3 LYS A 121 LEU A 125 0
SHEET 2 C 3 ALA A 128 PRO A 136 -1 O ALA A 130 N GLY A 123
SHEET 3 C 3 ALA A 465 GLU A 472 -1 O VAL A 468 N ARG A 133
SHEET 1 D 5 LEU A 196 LEU A 198 0
SHEET 2 D 5 CYS A 166 LYS A 170 1 N PHE A 169 O ASN A 197
SHEET 3 D 5 VAL A 139 PHE A 143 1 N VAL A 142 O LYS A 170
SHEET 4 D 5 GLY A 217 THR A 221 1 O PHE A 219 N ALA A 141
SHEET 5 D 5 ILE A 241 GLU A 245 1 O ALA A 243 N PHE A 220
SHEET 1 E 7 GLN A 345 LEU A 348 0
SHEET 2 E 7 GLY A 363 ASP A 366 -1 O ASP A 366 N GLN A 345
SHEET 3 E 7 LEU A 382 TYR A 388 1 O VAL A 385 N LEU A 365
SHEET 4 E 7 ALA A 282 PRO A 288 1 N LEU A 285 O GLN A 384
SHEET 5 E 7 ASN A 250 VAL A 254 1 N ASN A 250 O ARG A 283
SHEET 6 E 7 ALA A 406 LEU A 410 1 O GLY A 408 N VAL A 253
SHEET 7 E 7 ILE A 428 TRP A 431 1 O ASN A 430 N LEU A 409
SHEET 1 F 2 PRO A 443 PHE A 444 0
SHEET 2 F 2 SER A 456 ALA A 457 -1 O SER A 456 N PHE A 444
SHEET 1 G 2 HIS B 5 ILE B 7 0
SHEET 2 G 2 GLN B 10 LEU B 12 -1 O LEU B 12 N HIS B 5
SHEET 1 H 2 THR B 18 LEU B 22 0
SHEET 2 H 2 VAL B 29 ARG B 34 -1 O VAL B 30 N SER B 21
SHEET 1 I 3 LYS B 121 LEU B 125 0
SHEET 2 I 3 ALA B 128 PRO B 136 -1 O LEU B 132 N LYS B 121
SHEET 3 I 3 ALA B 465 GLU B 472 -1 O VAL B 468 N ARG B 133
SHEET 1 J 5 LEU B 196 LEU B 198 0
SHEET 2 J 5 CYS B 166 LYS B 170 1 N PHE B 169 O ASN B 197
SHEET 3 J 5 VAL B 139 PHE B 143 1 N VAL B 142 O LYS B 170
SHEET 4 J 5 GLY B 217 THR B 221 1 O PHE B 219 N ALA B 141
SHEET 5 J 5 ILE B 241 GLU B 245 1 O ALA B 243 N PHE B 220
SHEET 1 K 7 GLN B 345 LEU B 348 0
SHEET 2 K 7 GLY B 363 ASP B 366 -1 O ASP B 366 N GLN B 345
SHEET 3 K 7 LEU B 382 TYR B 388 1 O LEU B 383 N GLY B 363
SHEET 4 K 7 ALA B 282 PRO B 288 1 N LEU B 285 O GLN B 384
SHEET 5 K 7 ASN B 250 VAL B 254 1 N VAL B 254 O LEU B 286
SHEET 6 K 7 ALA B 406 LEU B 410 1 O GLY B 408 N VAL B 253
SHEET 7 K 7 ILE B 428 TRP B 431 1 O ASN B 430 N LEU B 409
SHEET 1 L 2 PRO B 443 PHE B 444 0
SHEET 2 L 2 SER B 456 ALA B 457 -1 O SER B 456 N PHE B 444
LINK C MSE A 1 N MSE A 2 1555 1555 1.32
LINK C MSE A 2 N SER A 3 1555 1555 1.34
LINK C SER A 102 N MSE A 103 1555 1555 1.34
LINK C MSE A 103 N VAL A 104 1555 1555 1.32
LINK C GLU A 245 N MSE A 246 1555 1555 1.34
LINK C MSE A 246 N GLY A 247 1555 1555 1.32
LINK C PHE A 319 N MSE A 320 1555 1555 1.33
LINK C MSE A 320 N GLY A 321 1555 1555 1.33
LINK C ALA A 349 N MSE A 350 1555 1555 1.33
LINK C MSE A 350 N THR A 351 1555 1555 1.34
LINK C MSE B 2 N SER B 3 1555 1555 1.33
LINK C SER B 102 N MSE B 103 1555 1555 1.34
LINK C MSE B 103 N VAL B 104 1555 1555 1.32
LINK C GLU B 245 N MSE B 246 1555 1555 1.34
LINK C MSE B 246 N GLY B 247 1555 1555 1.33
LINK C PHE B 319 N MSE B 320 1555 1555 1.32
LINK C MSE B 320 N GLY B 321 1555 1555 1.32
LINK C ALA B 349 N MSE B 350 1555 1555 1.33
LINK C MSE B 350 N THR B 351 1555 1555 1.33
LINK MG MG B 510 O HOH B 631 1555 1555 2.23
LINK MG MG B 510 O HOH B 630 1555 1555 2.23
LINK MG MG B 510 O HOH B 904 1555 1555 2.32
LINK MG MG B 510 O HOH B 632 1555 1555 2.30
LINK MG MG B 510 O HOH B 633 1555 1555 2.14
LINK MG MG B 510 O HOH B 896 1555 1555 2.19
CISPEP 1 GLN A 315 PRO A 316 0 -1.30
CISPEP 2 GLN B 315 PRO B 316 0 0.68
SITE 1 AC1 29 GLY A 144 PRO A 145 TYR A 146 ASN A 147
SITE 2 AC1 29 LEU A 152 LYS A 170 PRO A 171 SER A 172
SITE 3 AC1 29 GLU A 173 ARG A 203 PHE A 220 THR A 221
SITE 4 AC1 29 GLY A 222 SER A 223 THR A 226 GLU A 245
SITE 5 AC1 29 MSE A 246 GLY A 247 CYS A 279 GLU A 377
SITE 6 AC1 29 PHE A 379 PHE A 444 SIN A 504 HOH A 514
SITE 7 AC1 29 HOH A 590 HOH A 689 HOH A 691 HOH A 719
SITE 8 AC1 29 HOH A 984
SITE 1 AC2 3 ARG A 77 HOH A 573 HOH A 994
SITE 1 AC3 3 SER A 102 ASN A 105 HOH A 693
SITE 1 AC4 8 ASN A 147 PHE A 148 ARG A 278 CYS A 279
SITE 2 AC4 8 THR A 280 GLY A 437 ALA A 438 NAD A 501
SITE 1 AC5 5 ASP A 390 PHE A 391 ARG A 416 HOH A 860
SITE 2 AC5 5 HOH A 911
SITE 1 AC6 3 SER A 413 ARG A 414 GLU A 415
SITE 1 AC7 3 PRO A 53 ARG A 57 HOH A 534
SITE 1 AC8 3 ASP A 261 HOH A 983 LEU B 482
SITE 1 AC9 5 PHE A 114 ARG A 115 GLY A 119 GLU A 120
SITE 2 AC9 5 HOH A 947
SITE 1 BC1 3 THR A 306 LEU A 307 HOH A 954
SITE 1 BC2 6 GLN A 289 GLY A 290 ASP A 294 ARG A 387
SITE 2 BC2 6 HOH A 757 HOH A 908
SITE 1 BC3 4 ASP A 375 ALA A 400 THR A 401 HOH A 818
SITE 1 BC4 10 HIS A 231 ASN A 452 ARG A 454 HOH A 613
SITE 2 BC4 10 HOH A 703 HOH A 758 HIS B 231 ASN B 452
SITE 3 BC4 10 ARG B 454 HOH B 924
SITE 1 BC5 3 LEU A 482 ASP B 261 HOH B 645
SITE 1 BC6 29 PHE B 143 GLY B 144 PRO B 145 TYR B 146
SITE 2 BC6 29 ASN B 147 LEU B 152 LYS B 170 PRO B 171
SITE 3 BC6 29 SER B 172 ARG B 203 PHE B 220 THR B 221
SITE 4 BC6 29 GLY B 222 SER B 223 THR B 226 GLU B 245
SITE 5 BC6 29 MSE B 246 GLY B 247 CYS B 279 GLU B 377
SITE 6 BC6 29 PHE B 379 PHE B 444 HOH B 607 HOH B 636
SITE 7 BC6 29 HOH B 639 HOH B 642 HOH B 663 HOH B 671
SITE 8 BC6 29 HOH B 901
SITE 1 BC7 6 GLN A 10 ARG B 77 LYS B 184 HOH B 635
SITE 2 BC7 6 HOH B 745 HOH B 896
SITE 1 BC8 4 SER B 102 ASN B 105 HOH B 599 HOH B 637
SITE 1 BC9 3 PRO B 53 ARG B 57 HOH B 842
SITE 1 CC1 3 THR B 280 GLY B 437 HOH B 927
SITE 1 CC2 3 ARG B 414 GLU B 415 HOH B 893
SITE 1 CC3 7 PHE B 114 ARG B 115 GLY B 119 GLU B 120
SITE 2 CC3 7 HOH B 619 HOH B 699 HOH B 861
SITE 1 CC4 6 HOH B 630 HOH B 631 HOH B 632 HOH B 633
SITE 2 CC4 6 HOH B 896 HOH B 904
CRYST1 137.117 48.033 187.130 90.00 107.43 90.00 C 1 2 1 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 0.007293 0.000000 0.002290 0.00000
SCALE2 0.000000 0.020819 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005601 0.00000
HETATM 1 N MSE A 1 41.572 35.790 59.331 1.00 54.00 N
ANISOU 1 N MSE A 1 6164 7712 6639 -933 72 -395 N
HETATM 2 CA MSE A 1 41.066 35.645 57.955 1.00 52.75 C
ANISOU 2 CA MSE A 1 6032 7507 6506 -901 93 -377 C
HETATM 3 C MSE A 1 39.621 35.177 58.003 1.00 49.80 C
ANISOU 3 C MSE A 1 5719 7043 6158 -845 93 -368 C
HETATM 4 O MSE A 1 39.236 34.400 58.881 1.00 57.49 O
ANISOU 4 O MSE A 1 6698 8016 7132 -801 73 -369 O
HETATM 5 CB MSE A 1 41.892 34.640 57.133 1.00 55.74 C
ANISOU 5 CB MSE A 1 6350 7955 6874 -849 91 -361 C
HETATM 6 CG MSE A 1 43.412 34.866 57.161 1.00 65.49 C
ANISOU 6 CG MSE A 1 7509 9296 8077 -891 88 -366 C
HETATM 7 SE MSE A 1 44.025 36.065 55.753 0.38 45.55 SE
ANISOU 7 SE MSE A 1 4975 6779 5553 -967 122 -363 SE
HETATM 8 CE MSE A 1 45.817 36.353 56.306 1.00 36.15 C
ANISOU 8 CE MSE A 1 3691 5725 4320 -1028 110 -376 C
HETATM 9 N MSE A 2 38.812 35.655 57.071 1.00 37.97 N
ANISOU 9 N MSE A 2 4268 5475 4683 -848 116 -359 N
HETATM 10 CA MSE A 2 37.411 35.206 57.004 1.00 34.42 C
ANISOU 10 CA MSE A 2 3873 4947 4258 -796 116 -350 C
HETATM 11 C MSE A 2 36.967 34.887 55.580 1.00 34.97 C
ANISOU 11 C MSE A 2 3954 4991 4342 -760 133 -331 C
HETATM 12 O MSE A 2 37.569 35.341 54.611 1.00 33.33 O
ANISOU 12 O MSE A 2 3727 4809 4129 -788 150 -324 O
HETATM 13 CB MSE A 2 36.471 36.221 57.682 1.00 46.33 C
ANISOU 13 CB MSE A 2 5442 6380 5780 -836 124 -359 C
HETATM 14 CG MSE A 2 36.481 37.629 57.082 1.00 53.19 C
ANISOU 14 CG MSE A 2 6339 7213 6658 -903 152 -359 C
HETATM 15 SE MSE A 2 35.648 38.943 58.305 0.73 58.53 SE
ANISOU 15 SE MSE A 2 7082 7810 7347 -960 162 -381 SE
HETATM 16 CE MSE A 2 36.405 38.208 59.931 1.00 59.88 C
ANISOU 16 CE MSE A 2 7207 8059 7486 -959 126 -407 C
(ATOM LINES ARE NOT SHOWN.)
END
