HEADER BIOSYNTHETIC PROTEIN 16-MAY-07 2PYX
TITLE CRYSTAL STRUCTURE OF TRYPTOPHAN HALOGENASE (YP_750003.1) FROM
TITLE 2 SHEWANELLA FRIGIDIMARINA NCIMB 400 AT 1.50 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHAN HALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA FRIGIDIMARINA;
SOURCE 3 ORGANISM_TAXID: 318167;
SOURCE 4 STRAIN: NCIMB 400;
SOURCE 5 GENE: YP_750003.1, SFRI_1312;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS YP_750003.1, TRYPTOPHAN HALOGENASE, STRUCTURAL GENOMICS, JOINT CENTER
KEYWDS 2 FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2,
KEYWDS 3 BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 7 25-JAN-23 2PYX 1 REMARK SEQADV
REVDAT 6 24-JUL-19 2PYX 1 REMARK LINK
REVDAT 5 25-OCT-17 2PYX 1 REMARK
REVDAT 4 18-OCT-17 2PYX 1 REMARK
REVDAT 3 13-JUL-11 2PYX 1 VERSN
REVDAT 2 24-FEB-09 2PYX 1 VERSN
REVDAT 1 29-MAY-07 2PYX 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF TRYPTOPHAN HALOGENASE (YP_750003.1)
JRNL TITL 2 FROM SHEWANELLA FRIGIDIMARINA NCIMB 400 AT 1.50 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 184358
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9258
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7145
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 394
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8214
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 1587
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : 0.11000
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): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.069
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.007
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8824 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7769 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12091 ; 1.443 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18208 ; 0.833 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1161 ; 5.549 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 422 ;40.335 ;24.976
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1453 ;11.028 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;12.078 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1336 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10027 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1726 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1769 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8083 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4427 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5006 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1201 ; 0.154 ; 0.200
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): 19 ; 0.299 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 79 ; 0.275 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 48 ; 0.145 ; 0.200
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): 5522 ; 1.709 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2175 ; 0.430 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8792 ; 2.530 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3724 ; 3.803 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3242 ; 5.659 ;11.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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:
REMARK 3 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 3 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
REMARK 3 INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY
REMARK 3 OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION.
REMARK 3 3. CL, TARTRATE, AND PEG WERE MODELED BASED ON CRYSTALLIZATION
REMARK 3 AND CRYOPROTECTION CONDITIONS.
REMARK 4
REMARK 4 2PYX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042938.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837, 0.97916, 0.97885
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 184436
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.775
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31300
REMARK 200 R SYM FOR SHELL (I) : 0.31300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.2M NA TARTRATE, 20.0% PEG
REMARK 280 3350, NO BUFFER PH 7.2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 48.77250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.01800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.80650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.01800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.77250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.80650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1,2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT
REMARK 300 OF A MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE
REMARK 300 IN SOLUTION.
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 33 CE NZ
REMARK 470 HIS A 38 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 52 CG1 CG2
REMARK 470 ILE A 55 CG1 CG2 CD1
REMARK 470 GLN A 119 CD OE1 NE2
REMARK 470 GLN A 204 CD OE1 NE2
REMARK 470 LYS A 231 CD CE NZ
REMARK 470 ASN A 266 CG OD1 ND2
REMARK 470 LYS A 325 CG CD CE NZ
REMARK 470 GLU A 327 CG CD OE1 OE2
REMARK 470 ARG A 329 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 331 CG CD1 CD2
REMARK 470 GLN A 449 CG CD OE1 NE2
REMARK 470 LYS A 524 CG CD CE NZ
REMARK 470 LEU A 525 CG CD1 CD2
REMARK 470 ILE B 55 CG1 CG2 CD1
REMARK 470 GLN B 204 CG CD OE1 NE2
REMARK 470 LYS B 214 CD CE NZ
REMARK 470 ASN B 266 CG OD1 ND2
REMARK 470 LYS B 325 CG CD CE NZ
REMARK 470 ARG B 329 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 501 CD OE1 NE2
REMARK 470 LYS B 505 CD CE NZ
REMARK 470 ASN B 506 CG OD1 ND2
REMARK 470 LYS B 524 CG CD CE NZ
REMARK 470 LEU B 525 C O CB CG CD1 CD2
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 OD1 ASP A 84 O HOH A 1296 2.04
REMARK 500 OE1 GLN B 398 O HOH B 1318 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 MSE A 351 SE MSE A 351 CE -0.473
REMARK 500 MSE A 438 SE MSE A 438 CE -0.531
REMARK 500 MSE B 351 SE MSE B 351 CE -0.532
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 TYR A 161 -5.96 72.79
REMARK 500 GLN A 215 13.12 -140.49
REMARK 500 PHE A 251 -42.33 73.52
REMARK 500 ASP A 253 18.70 -143.49
REMARK 500 ASN A 344 -123.94 51.47
REMARK 500 PRO A 358 27.02 -78.22
REMARK 500 TYR B 161 -2.45 70.22
REMARK 500 PHE B 251 -43.96 73.86
REMARK 500 ASN B 344 -124.37 50.20
REMARK 500 PRO B 358 27.18 -78.06
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 CL A 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA B 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA B 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 529
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 528
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 374311 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV
REMARK 999 PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE
REMARK 999 TARGET SEQUENCE.
DBREF 2PYX A 1 525 UNP Q085A0 Q085A0_SHEFN 1 525
DBREF 2PYX B 1 525 UNP Q085A0 Q085A0_SHEFN 1 525
SEQADV 2PYX GLY A 0 UNP Q085A0 EXPRESSION TAG
SEQADV 2PYX MSE A 1 UNP Q085A0 MET 1 MODIFIED RESIDUE
SEQADV 2PYX MSE A 2 UNP Q085A0 MET 2 MODIFIED RESIDUE
SEQADV 2PYX MSE A 65 UNP Q085A0 MET 65 MODIFIED RESIDUE
SEQADV 2PYX MSE A 351 UNP Q085A0 MET 351 MODIFIED RESIDUE
SEQADV 2PYX MSE A 383 UNP Q085A0 MET 383 MODIFIED RESIDUE
SEQADV 2PYX MSE A 385 UNP Q085A0 MET 385 MODIFIED RESIDUE
SEQADV 2PYX MSE A 438 UNP Q085A0 MET 438 MODIFIED RESIDUE
SEQADV 2PYX MSE A 471 UNP Q085A0 MET 471 MODIFIED RESIDUE
SEQADV 2PYX MSE A 485 UNP Q085A0 MET 485 MODIFIED RESIDUE
SEQADV 2PYX GLY B 0 UNP Q085A0 EXPRESSION TAG
SEQADV 2PYX MSE B 1 UNP Q085A0 MET 1 MODIFIED RESIDUE
SEQADV 2PYX MSE B 2 UNP Q085A0 MET 2 MODIFIED RESIDUE
SEQADV 2PYX MSE B 65 UNP Q085A0 MET 65 MODIFIED RESIDUE
SEQADV 2PYX MSE B 351 UNP Q085A0 MET 351 MODIFIED RESIDUE
SEQADV 2PYX MSE B 383 UNP Q085A0 MET 383 MODIFIED RESIDUE
SEQADV 2PYX MSE B 385 UNP Q085A0 MET 385 MODIFIED RESIDUE
SEQADV 2PYX MSE B 438 UNP Q085A0 MET 438 MODIFIED RESIDUE
SEQADV 2PYX MSE B 471 UNP Q085A0 MET 471 MODIFIED RESIDUE
SEQADV 2PYX MSE B 485 UNP Q085A0 MET 485 MODIFIED RESIDUE
SEQRES 1 A 526 GLY MSE MSE GLN LYS PRO ILE THR GLU ILE ILE ILE VAL
SEQRES 2 A 526 GLY GLY GLY THR ALA GLY TRP ILE THR ALA GLY LEU LEU
SEQRES 3 A 526 ALA ALA GLU HIS ASN VAL ASP LYS GLY VAL LEU ALA HIS
SEQRES 4 A 526 SER PRO LYS LEU ASN ILE THR LEU ILE GLU SER PRO ASP
SEQRES 5 A 526 VAL ALA THR ILE GLY VAL GLY GLU GLY THR TRP PRO SER
SEQRES 6 A 526 MSE ARG SER THR LEU SER LYS ILE GLY ILE ASP GLU ASN
SEQRES 7 A 526 ASP PHE ILE ARG GLN CYS ASP ALA SER PHE LYS GLN GLY
SEQRES 8 A 526 SER ARG PHE ILE ASN TRP CYS LYS ASP PRO GLN SER ASN
SEQRES 9 A 526 VAL ALA ASP SER TYR LEU HIS PRO PHE SER LEU PRO HIS
SEQRES 10 A 526 GLY HIS GLN GLU LEU ASP LEU CYS PRO TYR TRP LEU PRO
SEQRES 11 A 526 HIS ALA GLU GLN VAL SER PHE ALA GLU ALA VAL CYS SER
SEQRES 12 A 526 GLN GLN VAL LEU THR GLN LEU GLY LEU ALA PRO LYS SER
SEQRES 13 A 526 ILE VAL THR ALA GLN TYR HIS PHE GLN ASN ASN TYR GLY
SEQRES 14 A 526 TYR HIS LEU ASN ALA ALA LYS PHE SER GLN LEU LEU THR
SEQRES 15 A 526 GLU HIS CYS THR GLN LYS LEU GLY VAL THR HIS ILE ARG
SEQRES 16 A 526 ASP HIS VAL SER GLN ILE ILE ASN ASN GLN HIS GLY ASP
SEQRES 17 A 526 ILE GLU LYS LEU ILE THR LYS GLN ASN GLY GLU ILE SER
SEQRES 18 A 526 GLY GLN LEU PHE ILE ASP CYS THR GLY ALA LYS SER LEU
SEQRES 19 A 526 LEU LEU GLY GLU HIS LEU GLN VAL PRO PHE LEU SER GLN
SEQRES 20 A 526 LYS SER VAL LEU PHE ASN ASP ARG ALA LEU ALA ILE GLN
SEQRES 21 A 526 VAL PRO TYR SER ASP ALA ASN SER PRO ILE ALA SER CYS
SEQRES 22 A 526 THR HIS SER THR ALA GLN PRO ASN GLY TRP ILE TRP ASP
SEQRES 23 A 526 ILE GLY LEU PRO THR ARG LYS GLY VAL GLY TYR VAL TYR
SEQRES 24 A 526 SER SER SER HIS THR ASN ASP ILE ASP ALA GLN LYS THR
SEQRES 25 A 526 LEU PHE ASN TYR LEU GLY VAL ASP GLY ALA ALA ALA ASP
SEQRES 26 A 526 LYS LEU GLU PRO ARG GLN LEU ALA ILE ASN PRO GLY TYR
SEQRES 27 A 526 ARG ALA LYS CYS TRP GLN ASN ASN CYS ILE ALA ILE GLY
SEQRES 28 A 526 MSE ALA ALA GLY PHE ILE GLU PRO LEU GLU ALA SER ALA
SEQRES 29 A 526 LEU ALA LEU ILE GLU TRP THR ALA SER THR LEU ALA GLN
SEQRES 30 A 526 GLN LEU PRO PRO ASN ARG MSE VAL MSE ASP THR ILE SER
SEQRES 31 A 526 ALA ARG VAL ASN GLU ARG TYR GLN GLN HIS TRP GLN GLN
SEQRES 32 A 526 ILE ILE ASP PHE LEU LYS LEU HIS TYR VAL ILE SER GLN
SEQRES 33 A 526 ARG GLN GLU ASP ARG TYR TRP ARG ASP HIS ARG GLU SER
SEQRES 34 A 526 ASN SER ILE PRO ASP SER LEU GLN ALA MSE LEU GLU LEU
SEQRES 35 A 526 TRP ARG TYR GLN THR PRO SER GLN GLN ASP ILE SER TYR
SEQRES 36 A 526 LYS GLU ALA LEU PHE PRO ALA ALA SER PHE GLN TYR VAL
SEQRES 37 A 526 LEU TYR GLY MSE SER PHE ASN THR GLN LEU PRO THR HIS
SEQRES 38 A 526 VAL LYS PRO SER MSE GLN GLN LEU ALA GLN ARG LEU PHE
SEQRES 39 A 526 ASN ASP ASN GLN GLN ARG THR GLN ALA LEU SER LYS ASN
SEQRES 40 A 526 LEU PRO THR ASN ARG GLU LEU LEU ASP LYS VAL ALA GLN
SEQRES 41 A 526 TYR GLY PHE PRO LYS LEU
SEQRES 1 B 526 GLY MSE MSE GLN LYS PRO ILE THR GLU ILE ILE ILE VAL
SEQRES 2 B 526 GLY GLY GLY THR ALA GLY TRP ILE THR ALA GLY LEU LEU
SEQRES 3 B 526 ALA ALA GLU HIS ASN VAL ASP LYS GLY VAL LEU ALA HIS
SEQRES 4 B 526 SER PRO LYS LEU ASN ILE THR LEU ILE GLU SER PRO ASP
SEQRES 5 B 526 VAL ALA THR ILE GLY VAL GLY GLU GLY THR TRP PRO SER
SEQRES 6 B 526 MSE ARG SER THR LEU SER LYS ILE GLY ILE ASP GLU ASN
SEQRES 7 B 526 ASP PHE ILE ARG GLN CYS ASP ALA SER PHE LYS GLN GLY
SEQRES 8 B 526 SER ARG PHE ILE ASN TRP CYS LYS ASP PRO GLN SER ASN
SEQRES 9 B 526 VAL ALA ASP SER TYR LEU HIS PRO PHE SER LEU PRO HIS
SEQRES 10 B 526 GLY HIS GLN GLU LEU ASP LEU CYS PRO TYR TRP LEU PRO
SEQRES 11 B 526 HIS ALA GLU GLN VAL SER PHE ALA GLU ALA VAL CYS SER
SEQRES 12 B 526 GLN GLN VAL LEU THR GLN LEU GLY LEU ALA PRO LYS SER
SEQRES 13 B 526 ILE VAL THR ALA GLN TYR HIS PHE GLN ASN ASN TYR GLY
SEQRES 14 B 526 TYR HIS LEU ASN ALA ALA LYS PHE SER GLN LEU LEU THR
SEQRES 15 B 526 GLU HIS CYS THR GLN LYS LEU GLY VAL THR HIS ILE ARG
SEQRES 16 B 526 ASP HIS VAL SER GLN ILE ILE ASN ASN GLN HIS GLY ASP
SEQRES 17 B 526 ILE GLU LYS LEU ILE THR LYS GLN ASN GLY GLU ILE SER
SEQRES 18 B 526 GLY GLN LEU PHE ILE ASP CYS THR GLY ALA LYS SER LEU
SEQRES 19 B 526 LEU LEU GLY GLU HIS LEU GLN VAL PRO PHE LEU SER GLN
SEQRES 20 B 526 LYS SER VAL LEU PHE ASN ASP ARG ALA LEU ALA ILE GLN
SEQRES 21 B 526 VAL PRO TYR SER ASP ALA ASN SER PRO ILE ALA SER CYS
SEQRES 22 B 526 THR HIS SER THR ALA GLN PRO ASN GLY TRP ILE TRP ASP
SEQRES 23 B 526 ILE GLY LEU PRO THR ARG LYS GLY VAL GLY TYR VAL TYR
SEQRES 24 B 526 SER SER SER HIS THR ASN ASP ILE ASP ALA GLN LYS THR
SEQRES 25 B 526 LEU PHE ASN TYR LEU GLY VAL ASP GLY ALA ALA ALA ASP
SEQRES 26 B 526 LYS LEU GLU PRO ARG GLN LEU ALA ILE ASN PRO GLY TYR
SEQRES 27 B 526 ARG ALA LYS CYS TRP GLN ASN ASN CYS ILE ALA ILE GLY
SEQRES 28 B 526 MSE ALA ALA GLY PHE ILE GLU PRO LEU GLU ALA SER ALA
SEQRES 29 B 526 LEU ALA LEU ILE GLU TRP THR ALA SER THR LEU ALA GLN
SEQRES 30 B 526 GLN LEU PRO PRO ASN ARG MSE VAL MSE ASP THR ILE SER
SEQRES 31 B 526 ALA ARG VAL ASN GLU ARG TYR GLN GLN HIS TRP GLN GLN
SEQRES 32 B 526 ILE ILE ASP PHE LEU LYS LEU HIS TYR VAL ILE SER GLN
SEQRES 33 B 526 ARG GLN GLU ASP ARG TYR TRP ARG ASP HIS ARG GLU SER
SEQRES 34 B 526 ASN SER ILE PRO ASP SER LEU GLN ALA MSE LEU GLU LEU
SEQRES 35 B 526 TRP ARG TYR GLN THR PRO SER GLN GLN ASP ILE SER TYR
SEQRES 36 B 526 LYS GLU ALA LEU PHE PRO ALA ALA SER PHE GLN TYR VAL
SEQRES 37 B 526 LEU TYR GLY MSE SER PHE ASN THR GLN LEU PRO THR HIS
SEQRES 38 B 526 VAL LYS PRO SER MSE GLN GLN LEU ALA GLN ARG LEU PHE
SEQRES 39 B 526 ASN ASP ASN GLN GLN ARG THR GLN ALA LEU SER LYS ASN
SEQRES 40 B 526 LEU PRO THR ASN ARG GLU LEU LEU ASP LYS VAL ALA GLN
SEQRES 41 B 526 TYR GLY PHE PRO LYS LEU
MODRES 2PYX MSE A 1 MET SELENOMETHIONINE
MODRES 2PYX MSE A 2 MET SELENOMETHIONINE
MODRES 2PYX MSE A 65 MET SELENOMETHIONINE
MODRES 2PYX MSE A 351 MET SELENOMETHIONINE
MODRES 2PYX MSE A 383 MET SELENOMETHIONINE
MODRES 2PYX MSE A 385 MET SELENOMETHIONINE
MODRES 2PYX MSE A 438 MET SELENOMETHIONINE
MODRES 2PYX MSE A 471 MET SELENOMETHIONINE
MODRES 2PYX MSE A 485 MET SELENOMETHIONINE
MODRES 2PYX MSE B 1 MET SELENOMETHIONINE
MODRES 2PYX MSE B 2 MET SELENOMETHIONINE
MODRES 2PYX MSE B 65 MET SELENOMETHIONINE
MODRES 2PYX MSE B 351 MET SELENOMETHIONINE
MODRES 2PYX MSE B 383 MET SELENOMETHIONINE
MODRES 2PYX MSE B 385 MET SELENOMETHIONINE
MODRES 2PYX MSE B 438 MET SELENOMETHIONINE
MODRES 2PYX MSE B 471 MET SELENOMETHIONINE
MODRES 2PYX MSE B 485 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 2 8
HET MSE A 65 8
HET MSE A 351 13
HET MSE A 383 13
HET MSE A 385 8
HET MSE A 438 8
HET MSE A 471 8
HET MSE A 485 13
HET MSE B 1 8
HET MSE B 2 8
HET MSE B 65 8
HET MSE B 351 13
HET MSE B 383 18
HET MSE B 385 8
HET MSE B 438 13
HET MSE B 471 8
HET MSE B 485 13
HET CL A 526 1
HET TLA A 527 10
HET TLA A 528 10
HET PG4 A 529 13
HET TLA B 526 10
HET TLA B 527 10
HET PG4 B 528 13
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM TLA L(+)-TARTARIC ACID
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 3 CL CL 1-
FORMUL 4 TLA 4(C4 H6 O6)
FORMUL 6 PG4 2(C8 H18 O5)
FORMUL 10 HOH *1587(H2 O)
HELIX 1 1 GLY A 0 LYS A 4 5 5
HELIX 2 2 GLY A 14 ASN A 30 1 17
HELIX 3 3 PRO A 63 GLY A 73 1 11
HELIX 4 4 ASP A 75 CYS A 83 1 9
HELIX 5 5 LEU A 123 LEU A 128 1 6
HELIX 6 6 PRO A 129 ALA A 131 5 3
HELIX 7 7 SER A 135 CYS A 141 1 7
HELIX 8 8 SER A 142 LEU A 149 1 8
HELIX 9 9 ASN A 172 LYS A 187 1 16
HELIX 10 10 THR A 228 SER A 232 5 5
HELIX 11 11 GLN A 246 PHE A 251 1 6
HELIX 12 12 ASN A 304 GLY A 317 1 14
HELIX 13 13 ASP A 319 LEU A 326 1 8
HELIX 14 14 GLY A 350 ALA A 352 5 3
HELIX 15 15 ALA A 361 GLN A 377 1 17
HELIX 16 16 ASN A 381 ILE A 413 1 33
HELIX 17 17 ASP A 419 HIS A 425 1 7
HELIX 18 18 ARG A 426 ILE A 431 5 6
HELIX 19 19 PRO A 432 ARG A 443 1 12
HELIX 20 20 SER A 448 ILE A 452 5 5
HELIX 21 21 PRO A 460 MSE A 471 1 12
HELIX 22 22 LYS A 482 LEU A 507 1 26
HELIX 23 23 THR A 509 TYR A 520 1 12
HELIX 24 24 GLY B 0 LYS B 4 5 5
HELIX 25 25 GLY B 14 ASN B 30 1 17
HELIX 26 26 PRO B 63 GLY B 73 1 11
HELIX 27 27 ASP B 75 CYS B 83 1 9
HELIX 28 28 LEU B 123 LEU B 128 1 6
HELIX 29 29 PRO B 129 ALA B 131 5 3
HELIX 30 30 SER B 135 CYS B 141 1 7
HELIX 31 31 SER B 142 LEU B 149 1 8
HELIX 32 32 ASN B 172 LYS B 187 1 16
HELIX 33 33 THR B 228 SER B 232 5 5
HELIX 34 34 GLN B 246 PHE B 251 1 6
HELIX 35 35 ASN B 304 GLY B 317 1 14
HELIX 36 36 ASP B 319 LEU B 326 1 8
HELIX 37 37 ALA B 361 GLN B 377 1 17
HELIX 38 38 VAL B 384 ILE B 413 1 30
HELIX 39 39 ASP B 419 ARG B 426 1 8
HELIX 40 40 GLU B 427 ILE B 431 5 5
HELIX 41 41 PRO B 432 ARG B 443 1 12
HELIX 42 42 SER B 448 ILE B 452 5 5
HELIX 43 43 PRO B 460 MSE B 471 1 12
HELIX 44 44 LYS B 482 ASN B 506 1 25
HELIX 45 45 THR B 509 TYR B 520 1 12
SHEET 1 A 6 THR A 191 ARG A 194 0
SHEET 2 A 6 ASN A 43 GLU A 48 1 N LEU A 46 O THR A 191
SHEET 3 A 6 GLU A 8 VAL A 12 1 N ILE A 11 O THR A 45
SHEET 4 A 6 LEU A 223 ASP A 226 1 O ILE A 225 N VAL A 12
SHEET 5 A 6 CYS A 346 ALA A 348 1 O ILE A 347 N ASP A 226
SHEET 6 A 6 TRP A 342 GLN A 343 -1 N GLN A 343 O CYS A 346
SHEET 1 B 2 VAL A 31 ASP A 32 0
SHEET 2 B 2 VAL A 35 LEU A 36 -1 O VAL A 35 N ASP A 32
SHEET 1 C 3 GLU A 59 GLY A 60 0
SHEET 2 C 3 GLY A 168 LEU A 171 -1 O LEU A 171 N GLU A 59
SHEET 3 C 3 SER A 86 LYS A 88 -1 N LYS A 88 O GLY A 168
SHEET 1 D 7 SER A 107 PRO A 111 0
SHEET 2 D 7 GLY A 90 ILE A 94 -1 N SER A 91 O HIS A 110
SHEET 3 D 7 THR A 273 GLN A 278 1 O THR A 273 N ARG A 92
SHEET 4 D 7 GLY A 281 GLY A 287 -1 O GLY A 281 N GLN A 278
SHEET 5 D 7 ARG A 291 TYR A 298 -1 O VAL A 297 N TRP A 282
SHEET 6 D 7 ARG A 254 PRO A 261 -1 N VAL A 260 O LYS A 292
SHEET 7 D 7 ARG A 329 ALA A 332 -1 O ARG A 329 N ALA A 257
SHEET 1 E 3 VAL A 197 ASN A 202 0
SHEET 2 E 3 ILE A 208 THR A 213 -1 O GLU A 209 N ILE A 201
SHEET 3 E 3 GLU A 218 SER A 220 -1 O ILE A 219 N LEU A 211
SHEET 1 F 3 PHE A 243 SER A 245 0
SHEET 2 F 3 GLY A 336 ARG A 338 -1 O TYR A 337 N LEU A 244
SHEET 3 F 3 GLY A 354 PHE A 355 -1 O PHE A 355 N GLY A 336
SHEET 1 G 6 THR B 191 ARG B 194 0
SHEET 2 G 6 ASN B 43 GLU B 48 1 N LEU B 46 O THR B 191
SHEET 3 G 6 GLU B 8 VAL B 12 1 N ILE B 11 O THR B 45
SHEET 4 G 6 LEU B 223 ASP B 226 1 O ILE B 225 N VAL B 12
SHEET 5 G 6 CYS B 346 ALA B 348 1 O ILE B 347 N ASP B 226
SHEET 6 G 6 TRP B 342 GLN B 343 -1 N GLN B 343 O CYS B 346
SHEET 1 H 2 VAL B 31 ASP B 32 0
SHEET 2 H 2 VAL B 35 LEU B 36 -1 O VAL B 35 N ASP B 32
SHEET 1 I 3 GLU B 59 GLY B 60 0
SHEET 2 I 3 GLY B 168 LEU B 171 -1 O LEU B 171 N GLU B 59
SHEET 3 I 3 SER B 86 LYS B 88 -1 N LYS B 88 O GLY B 168
SHEET 1 J 7 SER B 107 PRO B 111 0
SHEET 2 J 7 GLY B 90 ILE B 94 -1 N SER B 91 O HIS B 110
SHEET 3 J 7 THR B 273 GLN B 278 1 O THR B 273 N ARG B 92
SHEET 4 J 7 GLY B 281 GLY B 287 -1 O GLY B 281 N GLN B 278
SHEET 5 J 7 ARG B 291 TYR B 298 -1 O VAL B 297 N TRP B 282
SHEET 6 J 7 ARG B 254 PRO B 261 -1 N VAL B 260 O LYS B 292
SHEET 7 J 7 ARG B 329 ALA B 332 -1 O LEU B 331 N ALA B 255
SHEET 1 K 3 VAL B 197 ASN B 202 0
SHEET 2 K 3 ILE B 208 THR B 213 -1 O GLU B 209 N ILE B 201
SHEET 3 K 3 GLU B 218 SER B 220 -1 O ILE B 219 N LEU B 211
SHEET 1 L 3 PHE B 243 SER B 245 0
SHEET 2 L 3 GLY B 336 ARG B 338 -1 O TYR B 337 N LEU B 244
SHEET 3 L 3 GLY B 354 PHE B 355 -1 O PHE B 355 N GLY B 336
LINK C GLY A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N MSE A 2 1555 1555 1.32
LINK C MSE A 2 N GLN A 3 1555 1555 1.34
LINK C SER A 64 N MSE A 65 1555 1555 1.34
LINK C MSE A 65 N ARG A 66 1555 1555 1.33
LINK C GLY A 350 N MSE A 351 1555 1555 1.33
LINK C MSE A 351 N ALA A 352 1555 1555 1.34
LINK C ARG A 382 N MSE A 383 1555 1555 1.33
LINK C MSE A 383 N VAL A 384 1555 1555 1.33
LINK C VAL A 384 N MSE A 385 1555 1555 1.34
LINK C MSE A 385 N ASP A 386 1555 1555 1.33
LINK C ALA A 437 N MSE A 438 1555 1555 1.33
LINK C MSE A 438 N LEU A 439 1555 1555 1.32
LINK C GLY A 470 N MSE A 471 1555 1555 1.32
LINK C MSE A 471 N SER A 472 1555 1555 1.34
LINK C SER A 484 N MSE A 485 1555 1555 1.33
LINK C MSE A 485 N GLN A 486 1555 1555 1.32
LINK C GLY B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N MSE B 2 1555 1555 1.32
LINK C MSE B 2 N GLN B 3 1555 1555 1.34
LINK C SER B 64 N MSE B 65 1555 1555 1.34
LINK C MSE B 65 N ARG B 66 1555 1555 1.34
LINK C GLY B 350 N MSE B 351 1555 1555 1.33
LINK C MSE B 351 N ALA B 352 1555 1555 1.33
LINK C ARG B 382 N MSE B 383 1555 1555 1.33
LINK C MSE B 383 N VAL B 384 1555 1555 1.33
LINK C VAL B 384 N MSE B 385 1555 1555 1.34
LINK C MSE B 385 N ASP B 386 1555 1555 1.33
LINK C ALA B 437 N MSE B 438 1555 1555 1.33
LINK C MSE B 438 N LEU B 439 1555 1555 1.32
LINK C GLY B 470 N MSE B 471 1555 1555 1.32
LINK C MSE B 471 N SER B 472 1555 1555 1.33
LINK C SER B 484 N MSE B 485 1555 1555 1.33
LINK C MSE B 485 N GLN B 486 1555 1555 1.34
SITE 1 AC1 3 GLY A 58 ALA A 173 HOH A 730
SITE 1 AC2 14 GLY A 15 THR A 16 ALA A 17 GLY A 229
SITE 2 AC2 14 GLY A 350 MSE A 351 HOH A 602 HOH A 610
SITE 3 AC2 14 HOH A 644 HOH A 829 HOH A 931 HOH A 987
SITE 4 AC2 14 HOH A 995 HOH A1301
SITE 1 AC3 14 LYS A 247 ASP A 253 ARG A 254 ILE A 333
SITE 2 AC3 14 ASN A 334 HOH A 695 LYS B 247 ASP B 253
SITE 3 AC3 14 ARG B 254 ILE B 333 ASN B 334 HOH B 719
SITE 4 AC3 14 HOH B1263 HOH B1283
SITE 1 AC4 15 GLY B 15 THR B 16 ALA B 17 GLY B 229
SITE 2 AC4 15 GLY B 350 MSE B 351 HOH B 611 HOH B 659
SITE 3 AC4 15 HOH B 739 HOH B 746 HOH B 955 HOH B1055
SITE 4 AC4 15 HOH B1133 HOH B1154 HOH B1332
SITE 1 AC5 6 LYS A 516 GLN A 519 HOH A1023 ARG B 81
SITE 2 AC5 6 TYR B 520 HOH B 832
SITE 1 AC6 11 LEU A 24 GLU A 28 SER A 67 THR A 68
SITE 2 AC6 11 LYS A 71 GLU A 368 SER A 372 ALA A 375
SITE 3 AC6 11 GLN A 376 HOH A 553 HOH A 999
SITE 1 AC7 9 LEU B 24 GLU B 28 SER B 67 THR B 68
SITE 2 AC7 9 LYS B 71 GLU B 368 SER B 372 GLN B 376
SITE 3 AC7 9 HOH B 568
CRYST1 97.545 109.613 120.036 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010252 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009123 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
