HEADER LIGAND BINDING PROTEIN 17-JUL-06 2HPG
TITLE THE CRYSTAL STRUCTURE OF A THERMOPHILIC TRAP PERIPLASMIC
TITLE 2 BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABC TRANSPORTER, PERIPLASMIC SUBSTRATE-BINDING
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: TRAP-PERIPLASMIC BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM0322;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS PERIPLASMIC BINDING PROTEIN, THERMOPHILIC PROTEINS, TRAP-
KEYWDS 2 TRANSPORT, LIGAND BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.CUNEO,H.W.HELLINGA
REVDAT 2 23-DEC-08 2HPG 1 JRNL VERSN
REVDAT 1 20-MAR-07 2HPG 0
JRNL AUTH M.J.CUNEO,A.CHANGELA,A.E.MIKLOS,L.S.BEESE,
JRNL AUTH 2 J.K.KRUEGER,H.W.HELLINGA
JRNL TITL STRUCTURAL ANALYSIS OF A PERIPLASMIC BINDING
JRNL TITL 2 PROTEIN IN THE TRIPARTITE ATP-INDEPENDENT
JRNL TITL 3 TRANSPORTER FAMILY REVEALS A TETRAMERIC ASSEMBLY
JRNL TITL 4 THAT MAY HAVE A ROLE IN LIGAND TRANSPORT.
JRNL REF J.BIOL.CHEM. V. 283 32812 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18723845
JRNL DOI 10.1074/JBC.M803595200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 142411
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7152
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9847
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 486
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10353
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 529
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.10000
REMARK 3 B22 (A**2) : 1.10000
REMARK 3 B33 (A**2) : -1.65000
REMARK 3 B12 (A**2) : 0.55000
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): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.131
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.906
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10615 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7372 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14375 ; 1.249 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18086 ; 0.872 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1335 ; 5.844 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 493 ;36.398 ;25.071
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1985 ;14.701 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;17.595 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1540 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11780 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2092 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2276 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7653 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5128 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5333 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 511 ; 0.162 ; 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): 27 ; 0.263 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 41 ; 0.241 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.154 ; 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): 8058 ; 0.875 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2614 ; 0.130 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10365 ; 1.017 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4895 ; 1.751 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3980 ; 2.561 ; 4.500
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 : 1.40
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 2HPG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038607.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97167, 0.97934, 0.97920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 142555
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 103.282
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : 0.09400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.40500
REMARK 200 R SYM FOR SHELL (I) : 0.40500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PHOSPHATE/CITRATE PH4.2, 2.5M
REMARK 280 AMMONIUM SULFATE , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 286.06667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 143.03333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 214.55000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.51667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 357.58333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 286.06667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 143.03333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 71.51667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 214.55000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 357.58333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: THE BIOLOGICAL ASSEMBLY IS A MONOMER.
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 MSE A 16
REMARK 465 SER A 17
REMARK 465 ALA A 18
REMARK 465 HIS A 337
REMARK 465 HIS A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 MSE B 16
REMARK 465 SER B 17
REMARK 465 ALA B 18
REMARK 465 VAL B 19
REMARK 465 GLU B 336
REMARK 465 HIS B 337
REMARK 465 HIS B 338
REMARK 465 HIS B 339
REMARK 465 HIS B 340
REMARK 465 HIS B 341
REMARK 465 HIS B 342
REMARK 465 MSE C 16
REMARK 465 SER C 17
REMARK 465 ALA C 18
REMARK 465 VAL C 19
REMARK 465 PHE C 20
REMARK 465 ILE C 77
REMARK 465 ARG C 78
REMARK 465 MSE C 79
REMARK 465 HIS C 337
REMARK 465 HIS C 338
REMARK 465 HIS C 339
REMARK 465 HIS C 340
REMARK 465 HIS C 341
REMARK 465 HIS C 342
REMARK 465 MSE D 16
REMARK 465 SER D 17
REMARK 465 ALA D 18
REMARK 465 VAL D 19
REMARK 465 GLU D 336
REMARK 465 HIS D 337
REMARK 465 HIS D 338
REMARK 465 HIS D 339
REMARK 465 HIS D 340
REMARK 465 HIS D 341
REMARK 465 HIS D 342
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 GLU B 216 CB GLU B 216 CG -0.122
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 177 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 177 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG C 177 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG C 177 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG D 177 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG D 177 NE - CZ - NH2 ANGL. DEV. = -3.3 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 LEU A 32 -157.02 72.76
REMARK 500 THR A 87 -154.48 -125.89
REMARK 500 TYR A 151 39.14 -91.20
REMARK 500 GLU A 282 -48.93 -132.26
REMARK 500 LYS A 334 10.37 -59.37
REMARK 500 ALA B 33 83.71 -167.85
REMARK 500 PRO B 37 45.44 -81.79
REMARK 500 THR B 87 -150.72 -125.95
REMARK 500 TYR B 151 31.24 -98.15
REMARK 500 GLU B 282 -51.37 -121.77
REMARK 500 LEU C 32 -158.97 70.07
REMARK 500 LEU C 67 -44.62 -164.66
REMARK 500 GLU C 70 -117.72 -90.29
REMARK 500 GLU C 71 159.17 65.17
REMARK 500 ASP C 72 -165.89 -105.22
REMARK 500 ILE C 74 61.82 -160.01
REMARK 500 GLU C 75 40.54 -88.86
REMARK 500 ALA D 33 -100.21 66.59
REMARK 500 THR D 87 -156.15 -128.15
REMARK 500 TYR D 151 30.34 -96.83
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 ILE C 74 GLU C 75 148.55
REMARK 500 LEU D 32 ALA D 33 70.06
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HPG A 17 336 UNP Q9WYF8 Q9WYF8_THEMA 17 336
DBREF 2HPG B 17 336 UNP Q9WYF8 Q9WYF8_THEMA 17 336
DBREF 2HPG C 17 336 UNP Q9WYF8 Q9WYF8_THEMA 17 336
DBREF 2HPG D 17 336 UNP Q9WYF8 Q9WYF8_THEMA 17 336
SEQADV 2HPG MSE A 16 UNP Q9WYF8 INITIATING METHIONINE
SEQADV 2HPG MSE A 79 UNP Q9WYF8 MET 79 MODIFIED RESIDUE
SEQADV 2HPG MSE A 94 UNP Q9WYF8 MET 94 MODIFIED RESIDUE
SEQADV 2HPG MSE A 102 UNP Q9WYF8 MET 102 MODIFIED RESIDUE
SEQADV 2HPG MSE A 111 UNP Q9WYF8 MET 111 MODIFIED RESIDUE
SEQADV 2HPG MSE A 132 UNP Q9WYF8 MET 132 MODIFIED RESIDUE
SEQADV 2HPG MSE A 234 UNP Q9WYF8 MET 234 MODIFIED RESIDUE
SEQADV 2HPG MSE A 268 UNP Q9WYF8 MET 268 MODIFIED RESIDUE
SEQADV 2HPG MSE A 280 UNP Q9WYF8 MET 280 MODIFIED RESIDUE
SEQADV 2HPG MSE A 296 UNP Q9WYF8 MET 296 MODIFIED RESIDUE
SEQADV 2HPG MSE A 310 UNP Q9WYF8 MET 310 MODIFIED RESIDUE
SEQADV 2HPG HIS A 337 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS A 338 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS A 339 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS A 340 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS A 341 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS A 342 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG MSE B 16 UNP Q9WYF8 INITIATING METHIONINE
SEQADV 2HPG MSE B 79 UNP Q9WYF8 MET 79 MODIFIED RESIDUE
SEQADV 2HPG MSE B 94 UNP Q9WYF8 MET 94 MODIFIED RESIDUE
SEQADV 2HPG MSE B 102 UNP Q9WYF8 MET 102 MODIFIED RESIDUE
SEQADV 2HPG MSE B 111 UNP Q9WYF8 MET 111 MODIFIED RESIDUE
SEQADV 2HPG MSE B 132 UNP Q9WYF8 MET 132 MODIFIED RESIDUE
SEQADV 2HPG MSE B 234 UNP Q9WYF8 MET 234 MODIFIED RESIDUE
SEQADV 2HPG MSE B 268 UNP Q9WYF8 MET 268 MODIFIED RESIDUE
SEQADV 2HPG MSE B 280 UNP Q9WYF8 MET 280 MODIFIED RESIDUE
SEQADV 2HPG MSE B 296 UNP Q9WYF8 MET 296 MODIFIED RESIDUE
SEQADV 2HPG MSE B 310 UNP Q9WYF8 MET 310 MODIFIED RESIDUE
SEQADV 2HPG HIS B 337 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS B 338 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS B 339 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS B 340 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS B 341 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS B 342 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG MSE C 16 UNP Q9WYF8 INITIATING METHIONINE
SEQADV 2HPG MSE C 79 UNP Q9WYF8 MET 79 MODIFIED RESIDUE
SEQADV 2HPG MSE C 94 UNP Q9WYF8 MET 94 MODIFIED RESIDUE
SEQADV 2HPG MSE C 102 UNP Q9WYF8 MET 102 MODIFIED RESIDUE
SEQADV 2HPG MSE C 111 UNP Q9WYF8 MET 111 MODIFIED RESIDUE
SEQADV 2HPG MSE C 132 UNP Q9WYF8 MET 132 MODIFIED RESIDUE
SEQADV 2HPG MSE C 234 UNP Q9WYF8 MET 234 MODIFIED RESIDUE
SEQADV 2HPG MSE C 268 UNP Q9WYF8 MET 268 MODIFIED RESIDUE
SEQADV 2HPG MSE C 280 UNP Q9WYF8 MET 280 MODIFIED RESIDUE
SEQADV 2HPG MSE C 296 UNP Q9WYF8 MET 296 MODIFIED RESIDUE
SEQADV 2HPG MSE C 310 UNP Q9WYF8 MET 310 MODIFIED RESIDUE
SEQADV 2HPG HIS C 337 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS C 338 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS C 339 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS C 340 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS C 341 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS C 342 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG MSE D 16 UNP Q9WYF8 INITIATING METHIONINE
SEQADV 2HPG MSE D 79 UNP Q9WYF8 MET 79 MODIFIED RESIDUE
SEQADV 2HPG MSE D 94 UNP Q9WYF8 MET 94 MODIFIED RESIDUE
SEQADV 2HPG MSE D 102 UNP Q9WYF8 MET 102 MODIFIED RESIDUE
SEQADV 2HPG MSE D 111 UNP Q9WYF8 MET 111 MODIFIED RESIDUE
SEQADV 2HPG MSE D 132 UNP Q9WYF8 MET 132 MODIFIED RESIDUE
SEQADV 2HPG MSE D 234 UNP Q9WYF8 MET 234 MODIFIED RESIDUE
SEQADV 2HPG MSE D 268 UNP Q9WYF8 MET 268 MODIFIED RESIDUE
SEQADV 2HPG MSE D 280 UNP Q9WYF8 MET 280 MODIFIED RESIDUE
SEQADV 2HPG MSE D 296 UNP Q9WYF8 MET 296 MODIFIED RESIDUE
SEQADV 2HPG MSE D 310 UNP Q9WYF8 MET 310 MODIFIED RESIDUE
SEQADV 2HPG HIS D 337 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS D 338 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS D 339 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS D 340 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS D 341 UNP Q9WYF8 EXPRESSION TAG
SEQADV 2HPG HIS D 342 UNP Q9WYF8 EXPRESSION TAG
SEQRES 1 A 327 MSE SER ALA VAL PHE GLY ALA LYS TYR THR LEU ARG PHE
SEQRES 2 A 327 GLY HIS VAL LEU ALA PRO GLY GLU PRO TYR HIS GLN ALA
SEQRES 3 A 327 PHE LEU LYS TRP ALA LYS ALA VAL GLU GLU LYS THR ASN
SEQRES 4 A 327 GLY ASP VAL ARG ILE GLU VAL PHE PRO SER SER GLN LEU
SEQRES 5 A 327 GLY VAL GLU GLU ASP ILE ILE GLU GLN ILE ARG MSE GLY
SEQRES 6 A 327 ALA PRO VAL GLY TRP ASN THR ASP SER ALA ARG LEU GLY
SEQRES 7 A 327 MSE TYR VAL LYS ASP ILE GLY VAL MSE ASN LEU ALA TYR
SEQRES 8 A 327 PHE ILE ASP PHE MSE GLY ALA LYS THR PRO GLU GLU ALA
SEQRES 9 A 327 ILE GLU VAL LEU LYS LYS ILE LYS GLN SER PRO THR MSE
SEQRES 10 A 327 GLN LYS TRP LEU LYS GLU LEU GLU GLN ARG PHE GLY ILE
SEQRES 11 A 327 LYS VAL LEU SER PHE TYR TRP VAL GLN GLY TYR ARG HIS
SEQRES 12 A 327 PHE VAL THR ASN LYS PRO ILE ARG LYS PRO GLU ASP LEU
SEQRES 13 A 327 ASN GLY LEU ARG ILE ARG THR PRO GLY ALA PRO ALA TRP
SEQRES 14 A 327 GLN GLU SER ILE ARG SER LEU GLY ALA ILE PRO VAL ALA
SEQRES 15 A 327 VAL ASN PHE GLY GLU ILE TYR THR ALA VAL GLN THR ARG
SEQRES 16 A 327 ALA VAL ASP GLY ALA GLU LEU THR TYR ALA ASN VAL TYR
SEQRES 17 A 327 ASN GLY GLY LEU TYR GLU VAL LEU LYS TYR MSE SER GLU
SEQRES 18 A 327 THR GLY HIS PHE LEU LEU ILE ASN PHE GLU ILE VAL SER
SEQRES 19 A 327 ALA ASP TRP PHE ASN SER LEU PRO LYS GLU TYR GLN LYS
SEQRES 20 A 327 ILE ILE GLU GLU GLU MSE ASP LYS ALA GLY ILE GLU VAL
SEQRES 21 A 327 SER LEU LYS ILE MSE LYS GLU LEU GLU GLU GLU TYR LYS
SEQRES 22 A 327 GLN LYS CYS ILE GLU LYS GLY MSE ALA VAL ILE PRO ALA
SEQRES 23 A 327 SER GLU ILE ASP LYS GLU ALA PHE MSE GLU LYS ALA LYS
SEQRES 24 A 327 GLN ALA TYR LYS ASN LEU GLY LEU GLU ASN ALA LEU ASN
SEQRES 25 A 327 GLN LEU ILE LYS GLU VAL LYS GLY GLU HIS HIS HIS HIS
SEQRES 26 A 327 HIS HIS
SEQRES 1 B 327 MSE SER ALA VAL PHE GLY ALA LYS TYR THR LEU ARG PHE
SEQRES 2 B 327 GLY HIS VAL LEU ALA PRO GLY GLU PRO TYR HIS GLN ALA
SEQRES 3 B 327 PHE LEU LYS TRP ALA LYS ALA VAL GLU GLU LYS THR ASN
SEQRES 4 B 327 GLY ASP VAL ARG ILE GLU VAL PHE PRO SER SER GLN LEU
SEQRES 5 B 327 GLY VAL GLU GLU ASP ILE ILE GLU GLN ILE ARG MSE GLY
SEQRES 6 B 327 ALA PRO VAL GLY TRP ASN THR ASP SER ALA ARG LEU GLY
SEQRES 7 B 327 MSE TYR VAL LYS ASP ILE GLY VAL MSE ASN LEU ALA TYR
SEQRES 8 B 327 PHE ILE ASP PHE MSE GLY ALA LYS THR PRO GLU GLU ALA
SEQRES 9 B 327 ILE GLU VAL LEU LYS LYS ILE LYS GLN SER PRO THR MSE
SEQRES 10 B 327 GLN LYS TRP LEU LYS GLU LEU GLU GLN ARG PHE GLY ILE
SEQRES 11 B 327 LYS VAL LEU SER PHE TYR TRP VAL GLN GLY TYR ARG HIS
SEQRES 12 B 327 PHE VAL THR ASN LYS PRO ILE ARG LYS PRO GLU ASP LEU
SEQRES 13 B 327 ASN GLY LEU ARG ILE ARG THR PRO GLY ALA PRO ALA TRP
SEQRES 14 B 327 GLN GLU SER ILE ARG SER LEU GLY ALA ILE PRO VAL ALA
SEQRES 15 B 327 VAL ASN PHE GLY GLU ILE TYR THR ALA VAL GLN THR ARG
SEQRES 16 B 327 ALA VAL ASP GLY ALA GLU LEU THR TYR ALA ASN VAL TYR
SEQRES 17 B 327 ASN GLY GLY LEU TYR GLU VAL LEU LYS TYR MSE SER GLU
SEQRES 18 B 327 THR GLY HIS PHE LEU LEU ILE ASN PHE GLU ILE VAL SER
SEQRES 19 B 327 ALA ASP TRP PHE ASN SER LEU PRO LYS GLU TYR GLN LYS
SEQRES 20 B 327 ILE ILE GLU GLU GLU MSE ASP LYS ALA GLY ILE GLU VAL
SEQRES 21 B 327 SER LEU LYS ILE MSE LYS GLU LEU GLU GLU GLU TYR LYS
SEQRES 22 B 327 GLN LYS CYS ILE GLU LYS GLY MSE ALA VAL ILE PRO ALA
SEQRES 23 B 327 SER GLU ILE ASP LYS GLU ALA PHE MSE GLU LYS ALA LYS
SEQRES 24 B 327 GLN ALA TYR LYS ASN LEU GLY LEU GLU ASN ALA LEU ASN
SEQRES 25 B 327 GLN LEU ILE LYS GLU VAL LYS GLY GLU HIS HIS HIS HIS
SEQRES 26 B 327 HIS HIS
SEQRES 1 C 327 MSE SER ALA VAL PHE GLY ALA LYS TYR THR LEU ARG PHE
SEQRES 2 C 327 GLY HIS VAL LEU ALA PRO GLY GLU PRO TYR HIS GLN ALA
SEQRES 3 C 327 PHE LEU LYS TRP ALA LYS ALA VAL GLU GLU LYS THR ASN
SEQRES 4 C 327 GLY ASP VAL ARG ILE GLU VAL PHE PRO SER SER GLN LEU
SEQRES 5 C 327 GLY VAL GLU GLU ASP ILE ILE GLU GLN ILE ARG MSE GLY
SEQRES 6 C 327 ALA PRO VAL GLY TRP ASN THR ASP SER ALA ARG LEU GLY
SEQRES 7 C 327 MSE TYR VAL LYS ASP ILE GLY VAL MSE ASN LEU ALA TYR
SEQRES 8 C 327 PHE ILE ASP PHE MSE GLY ALA LYS THR PRO GLU GLU ALA
SEQRES 9 C 327 ILE GLU VAL LEU LYS LYS ILE LYS GLN SER PRO THR MSE
SEQRES 10 C 327 GLN LYS TRP LEU LYS GLU LEU GLU GLN ARG PHE GLY ILE
SEQRES 11 C 327 LYS VAL LEU SER PHE TYR TRP VAL GLN GLY TYR ARG HIS
SEQRES 12 C 327 PHE VAL THR ASN LYS PRO ILE ARG LYS PRO GLU ASP LEU
SEQRES 13 C 327 ASN GLY LEU ARG ILE ARG THR PRO GLY ALA PRO ALA TRP
SEQRES 14 C 327 GLN GLU SER ILE ARG SER LEU GLY ALA ILE PRO VAL ALA
SEQRES 15 C 327 VAL ASN PHE GLY GLU ILE TYR THR ALA VAL GLN THR ARG
SEQRES 16 C 327 ALA VAL ASP GLY ALA GLU LEU THR TYR ALA ASN VAL TYR
SEQRES 17 C 327 ASN GLY GLY LEU TYR GLU VAL LEU LYS TYR MSE SER GLU
SEQRES 18 C 327 THR GLY HIS PHE LEU LEU ILE ASN PHE GLU ILE VAL SER
SEQRES 19 C 327 ALA ASP TRP PHE ASN SER LEU PRO LYS GLU TYR GLN LYS
SEQRES 20 C 327 ILE ILE GLU GLU GLU MSE ASP LYS ALA GLY ILE GLU VAL
SEQRES 21 C 327 SER LEU LYS ILE MSE LYS GLU LEU GLU GLU GLU TYR LYS
SEQRES 22 C 327 GLN LYS CYS ILE GLU LYS GLY MSE ALA VAL ILE PRO ALA
SEQRES 23 C 327 SER GLU ILE ASP LYS GLU ALA PHE MSE GLU LYS ALA LYS
SEQRES 24 C 327 GLN ALA TYR LYS ASN LEU GLY LEU GLU ASN ALA LEU ASN
SEQRES 25 C 327 GLN LEU ILE LYS GLU VAL LYS GLY GLU HIS HIS HIS HIS
SEQRES 26 C 327 HIS HIS
SEQRES 1 D 327 MSE SER ALA VAL PHE GLY ALA LYS TYR THR LEU ARG PHE
SEQRES 2 D 327 GLY HIS VAL LEU ALA PRO GLY GLU PRO TYR HIS GLN ALA
SEQRES 3 D 327 PHE LEU LYS TRP ALA LYS ALA VAL GLU GLU LYS THR ASN
SEQRES 4 D 327 GLY ASP VAL ARG ILE GLU VAL PHE PRO SER SER GLN LEU
SEQRES 5 D 327 GLY VAL GLU GLU ASP ILE ILE GLU GLN ILE ARG MSE GLY
SEQRES 6 D 327 ALA PRO VAL GLY TRP ASN THR ASP SER ALA ARG LEU GLY
SEQRES 7 D 327 MSE TYR VAL LYS ASP ILE GLY VAL MSE ASN LEU ALA TYR
SEQRES 8 D 327 PHE ILE ASP PHE MSE GLY ALA LYS THR PRO GLU GLU ALA
SEQRES 9 D 327 ILE GLU VAL LEU LYS LYS ILE LYS GLN SER PRO THR MSE
SEQRES 10 D 327 GLN LYS TRP LEU LYS GLU LEU GLU GLN ARG PHE GLY ILE
SEQRES 11 D 327 LYS VAL LEU SER PHE TYR TRP VAL GLN GLY TYR ARG HIS
SEQRES 12 D 327 PHE VAL THR ASN LYS PRO ILE ARG LYS PRO GLU ASP LEU
SEQRES 13 D 327 ASN GLY LEU ARG ILE ARG THR PRO GLY ALA PRO ALA TRP
SEQRES 14 D 327 GLN GLU SER ILE ARG SER LEU GLY ALA ILE PRO VAL ALA
SEQRES 15 D 327 VAL ASN PHE GLY GLU ILE TYR THR ALA VAL GLN THR ARG
SEQRES 16 D 327 ALA VAL ASP GLY ALA GLU LEU THR TYR ALA ASN VAL TYR
SEQRES 17 D 327 ASN GLY GLY LEU TYR GLU VAL LEU LYS TYR MSE SER GLU
SEQRES 18 D 327 THR GLY HIS PHE LEU LEU ILE ASN PHE GLU ILE VAL SER
SEQRES 19 D 327 ALA ASP TRP PHE ASN SER LEU PRO LYS GLU TYR GLN LYS
SEQRES 20 D 327 ILE ILE GLU GLU GLU MSE ASP LYS ALA GLY ILE GLU VAL
SEQRES 21 D 327 SER LEU LYS ILE MSE LYS GLU LEU GLU GLU GLU TYR LYS
SEQRES 22 D 327 GLN LYS CYS ILE GLU LYS GLY MSE ALA VAL ILE PRO ALA
SEQRES 23 D 327 SER GLU ILE ASP LYS GLU ALA PHE MSE GLU LYS ALA LYS
SEQRES 24 D 327 GLN ALA TYR LYS ASN LEU GLY LEU GLU ASN ALA LEU ASN
SEQRES 25 D 327 GLN LEU ILE LYS GLU VAL LYS GLY GLU HIS HIS HIS HIS
SEQRES 26 D 327 HIS HIS
MODRES 2HPG MSE A 79 MET SELENOMETHIONINE
MODRES 2HPG MSE A 94 MET SELENOMETHIONINE
MODRES 2HPG MSE A 102 MET SELENOMETHIONINE
MODRES 2HPG MSE A 111 MET SELENOMETHIONINE
MODRES 2HPG MSE A 132 MET SELENOMETHIONINE
MODRES 2HPG MSE A 234 MET SELENOMETHIONINE
MODRES 2HPG MSE A 268 MET SELENOMETHIONINE
MODRES 2HPG MSE A 280 MET SELENOMETHIONINE
MODRES 2HPG MSE A 296 MET SELENOMETHIONINE
MODRES 2HPG MSE A 310 MET SELENOMETHIONINE
MODRES 2HPG MSE B 79 MET SELENOMETHIONINE
MODRES 2HPG MSE B 94 MET SELENOMETHIONINE
MODRES 2HPG MSE B 102 MET SELENOMETHIONINE
MODRES 2HPG MSE B 111 MET SELENOMETHIONINE
MODRES 2HPG MSE B 132 MET SELENOMETHIONINE
MODRES 2HPG MSE B 234 MET SELENOMETHIONINE
MODRES 2HPG MSE B 268 MET SELENOMETHIONINE
MODRES 2HPG MSE B 280 MET SELENOMETHIONINE
MODRES 2HPG MSE B 296 MET SELENOMETHIONINE
MODRES 2HPG MSE B 310 MET SELENOMETHIONINE
MODRES 2HPG MSE C 94 MET SELENOMETHIONINE
MODRES 2HPG MSE C 102 MET SELENOMETHIONINE
MODRES 2HPG MSE C 111 MET SELENOMETHIONINE
MODRES 2HPG MSE C 132 MET SELENOMETHIONINE
MODRES 2HPG MSE C 234 MET SELENOMETHIONINE
MODRES 2HPG MSE C 268 MET SELENOMETHIONINE
MODRES 2HPG MSE C 280 MET SELENOMETHIONINE
MODRES 2HPG MSE C 296 MET SELENOMETHIONINE
MODRES 2HPG MSE C 310 MET SELENOMETHIONINE
MODRES 2HPG MSE D 79 MET SELENOMETHIONINE
MODRES 2HPG MSE D 94 MET SELENOMETHIONINE
MODRES 2HPG MSE D 102 MET SELENOMETHIONINE
MODRES 2HPG MSE D 111 MET SELENOMETHIONINE
MODRES 2HPG MSE D 132 MET SELENOMETHIONINE
MODRES 2HPG MSE D 234 MET SELENOMETHIONINE
MODRES 2HPG MSE D 268 MET SELENOMETHIONINE
MODRES 2HPG MSE D 280 MET SELENOMETHIONINE
MODRES 2HPG MSE D 296 MET SELENOMETHIONINE
MODRES 2HPG MSE D 310 MET SELENOMETHIONINE
HET MSE A 79 16
HET MSE A 94 13
HET MSE A 102 8
HET MSE A 111 13
HET MSE A 132 8
HET MSE A 234 13
HET MSE A 268 16
HET MSE A 280 8
HET MSE A 296 8
HET MSE A 310 8
HET MSE B 79 8
HET MSE B 94 13
HET MSE B 102 8
HET MSE B 111 8
HET MSE B 132 8
HET MSE B 234 8
HET MSE B 268 8
HET MSE B 280 8
HET MSE B 296 8
HET MSE B 310 8
HET MSE C 94 16
HET MSE C 102 8
HET MSE C 111 8
HET MSE C 132 8
HET MSE C 234 13
HET MSE C 268 13
HET MSE C 280 8
HET MSE C 296 13
HET MSE C 310 8
HET MSE D 79 8
HET MSE D 94 8
HET MSE D 102 8
HET MSE D 111 8
HET MSE D 132 8
HET MSE D 234 8
HET MSE D 268 8
HET MSE D 280 8
HET MSE D 296 8
HET MSE D 310 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 39(C5 H11 N O2 SE)
FORMUL 5 HOH *529(H2 O)
HELIX 1 1 GLU A 36 THR A 53 1 18
HELIX 2 2 ASP A 72 GLY A 80 1 9
HELIX 3 3 SER A 89 GLY A 93 1 5
HELIX 4 4 MSE A 94 TYR A 95 5 2
HELIX 5 5 VAL A 96 LEU A 104 5 9
HELIX 6 6 TYR A 106 MSE A 111 1 6
HELIX 7 7 THR A 115 GLN A 128 1 14
HELIX 8 8 SER A 129 GLY A 144 1 16
HELIX 9 9 LYS A 167 ASN A 172 5 6
HELIX 10 10 ALA A 181 GLY A 192 1 12
HELIX 11 11 ASN A 199 GLY A 201 5 3
HELIX 12 12 GLU A 202 THR A 209 1 8
HELIX 13 13 THR A 218 GLY A 225 1 8
HELIX 14 14 GLY A 226 VAL A 230 5 5
HELIX 15 15 ALA A 250 LEU A 256 1 7
HELIX 16 16 PRO A 257 GLU A 282 1 26
HELIX 17 17 GLU A 282 LYS A 294 1 13
HELIX 18 18 PRO A 300 ILE A 304 5 5
HELIX 19 19 ASP A 305 GLY A 321 1 17
HELIX 20 20 LEU A 322 LYS A 334 1 13
HELIX 21 21 PRO B 37 THR B 53 1 17
HELIX 22 22 VAL B 69 MSE B 79 1 11
HELIX 23 23 SER B 89 GLY B 93 1 5
HELIX 24 24 MSE B 94 TYR B 95 5 2
HELIX 25 25 VAL B 96 LEU B 104 5 9
HELIX 26 26 TYR B 106 MSE B 111 1 6
HELIX 27 27 THR B 115 SER B 129 1 15
HELIX 28 28 SER B 129 GLY B 144 1 16
HELIX 29 29 LYS B 167 ASN B 172 5 6
HELIX 30 30 ALA B 181 GLY B 192 1 12
HELIX 31 31 ASN B 199 GLY B 201 5 3
HELIX 32 32 GLU B 202 THR B 209 1 8
HELIX 33 33 THR B 218 GLY B 225 1 8
HELIX 34 34 GLY B 226 VAL B 230 5 5
HELIX 35 35 ALA B 250 LEU B 256 1 7
HELIX 36 36 PRO B 257 GLU B 282 1 26
HELIX 37 37 GLU B 282 LYS B 294 1 13
HELIX 38 38 PRO B 300 ILE B 304 5 5
HELIX 39 39 ASP B 305 LEU B 320 1 16
HELIX 40 40 LEU B 322 GLY B 335 1 14
HELIX 41 41 GLU C 36 THR C 53 1 18
HELIX 42 42 SER C 89 GLY C 93 1 5
HELIX 43 43 MSE C 94 TYR C 95 5 2
HELIX 44 44 VAL C 96 LEU C 104 5 9
HELIX 45 45 TYR C 106 MSE C 111 1 6
HELIX 46 46 THR C 115 SER C 129 1 15
HELIX 47 47 SER C 129 GLY C 144 1 16
HELIX 48 48 LYS C 167 ASN C 172 5 6
HELIX 49 49 ALA C 181 GLY C 192 1 12
HELIX 50 50 ASN C 199 GLY C 201 5 3
HELIX 51 51 GLU C 202 THR C 209 1 8
HELIX 52 52 THR C 218 GLY C 225 1 8
HELIX 53 53 GLY C 226 VAL C 230 5 5
HELIX 54 54 ALA C 250 LEU C 256 1 7
HELIX 55 55 PRO C 257 GLU C 282 1 26
HELIX 56 56 GLU C 282 LYS C 294 1 13
HELIX 57 57 PRO C 300 ILE C 304 5 5
HELIX 58 58 ASP C 305 GLY C 321 1 17
HELIX 59 59 LEU C 322 GLU C 336 1 15
HELIX 60 60 GLY D 35 THR D 53 1 19
HELIX 61 61 VAL D 69 GLY D 80 1 12
HELIX 62 62 SER D 89 GLY D 93 1 5
HELIX 63 63 MSE D 94 TYR D 95 5 2
HELIX 64 64 VAL D 96 LEU D 104 5 9
HELIX 65 65 TYR D 106 MSE D 111 1 6
HELIX 66 66 THR D 115 SER D 129 1 15
HELIX 67 67 SER D 129 GLY D 144 1 16
HELIX 68 68 LYS D 167 ASN D 172 5 6
HELIX 69 69 ALA D 181 GLY D 192 1 12
HELIX 70 70 ASN D 199 GLY D 201 5 3
HELIX 71 71 GLU D 202 THR D 209 1 8
HELIX 72 72 THR D 218 GLY D 225 1 8
HELIX 73 73 GLY D 226 VAL D 230 5 5
HELIX 74 74 ALA D 250 LEU D 256 1 7
HELIX 75 75 PRO D 257 GLU D 282 1 26
HELIX 76 76 GLU D 282 LYS D 294 1 13
HELIX 77 77 PRO D 300 ILE D 304 5 5
HELIX 78 78 ASP D 305 LEU D 320 1 16
HELIX 79 79 LEU D 322 GLY D 335 1 14
SHEET 1 A 5 VAL A 57 PHE A 62 0
SHEET 2 A 5 TYR A 24 GLY A 29 1 N LEU A 26 O GLU A 60
SHEET 3 A 5 VAL A 83 ASP A 88 1 O GLY A 84 N GLY A 29
SHEET 4 A 5 ILE A 243 SER A 249 -1 O PHE A 245 N THR A 87
SHEET 5 A 5 ILE A 145 VAL A 153 -1 N TRP A 152 O ASN A 244
SHEET 1 B 6 ILE A 194 VAL A 196 0
SHEET 2 B 6 ARG A 175 ARG A 177 1 N ILE A 176 O ILE A 194
SHEET 3 B 6 GLY A 214 LEU A 217 1 O GLY A 214 N ARG A 177
SHEET 4 B 6 ARG A 157 THR A 161 -1 N VAL A 160 O ALA A 215
SHEET 5 B 6 TYR A 233 PHE A 240 -1 O TYR A 233 N THR A 161
SHEET 6 B 6 ALA A 297 ILE A 299 1 O ILE A 299 N MSE A 234
SHEET 1 C 5 VAL B 57 VAL B 61 0
SHEET 2 C 5 TYR B 24 GLY B 29 1 N PHE B 28 O GLU B 60
SHEET 3 C 5 VAL B 83 ASP B 88 1 O GLY B 84 N ARG B 27
SHEET 4 C 5 ILE B 243 SER B 249 -1 O PHE B 245 N THR B 87
SHEET 5 C 5 ILE B 145 VAL B 153 -1 N TRP B 152 O ASN B 244
SHEET 1 D 4 GLY B 214 LEU B 217 0
SHEET 2 D 4 ARG B 157 THR B 161 -1 N VAL B 160 O ALA B 215
SHEET 3 D 4 TYR B 233 PHE B 240 -1 O TYR B 233 N THR B 161
SHEET 4 D 4 ALA B 297 ILE B 299 1 O ILE B 299 N MSE B 234
SHEET 1 E 2 ARG B 175 ARG B 177 0
SHEET 2 E 2 ILE B 194 VAL B 196 1 O ILE B 194 N ILE B 176
SHEET 1 F 8 VAL C 57 VAL C 61 0
SHEET 2 F 8 TYR C 24 GLY C 29 1 N LEU C 26 O GLU C 60
SHEET 3 F 8 VAL C 83 ASP C 88 1 O GLY C 84 N GLY C 29
SHEET 4 F 8 TYR C 233 SER C 249 -1 O PHE C 245 N THR C 87
SHEET 5 F 8 ILE C 145 THR C 161 -1 N TRP C 152 O ASN C 244
SHEET 6 F 8 GLY C 214 LEU C 217 -1 O ALA C 215 N VAL C 160
SHEET 7 F 8 ARG C 175 ARG C 177 1 N ARG C 177 O GLY C 214
SHEET 8 F 8 ILE C 194 VAL C 196 1 O ILE C 194 N ILE C 176
SHEET 1 G 5 VAL C 57 VAL C 61 0
SHEET 2 G 5 TYR C 24 GLY C 29 1 N LEU C 26 O GLU C 60
SHEET 3 G 5 VAL C 83 ASP C 88 1 O GLY C 84 N GLY C 29
SHEET 4 G 5 TYR C 233 SER C 249 -1 O PHE C 245 N THR C 87
SHEET 5 G 5 ALA C 297 ILE C 299 1 O ILE C 299 N MSE C 234
SHEET 1 H 5 VAL D 57 PHE D 62 0
SHEET 2 H 5 TYR D 24 GLY D 29 1 N PHE D 28 O GLU D 60
SHEET 3 H 5 VAL D 83 ASP D 88 1 O GLY D 84 N ARG D 27
SHEET 4 H 5 ILE D 243 SER D 249 -1 O PHE D 245 N THR D 87
SHEET 5 H 5 ILE D 145 VAL D 153 -1 N TRP D 152 O ASN D 244
SHEET 1 I 4 GLY D 214 LEU D 217 0
SHEET 2 I 4 ARG D 157 THR D 161 -1 N HIS D 158 O LEU D 217
SHEET 3 I 4 TYR D 233 PHE D 240 -1 O TYR D 233 N THR D 161
SHEET 4 I 4 ALA D 297 ILE D 299 1 O ILE D 299 N GLU D 236
SHEET 1 J 2 ARG D 175 ARG D 177 0
SHEET 2 J 2 ILE D 194 VAL D 196 1 O ILE D 194 N ILE D 176
LINK C ARG A 78 N AMSE A 79 1555 1555 1.33
LINK C ARG A 78 N BMSE A 79 1555 1555 1.33
LINK C AMSE A 79 N GLY A 80 1555 1555 1.33
LINK C BMSE A 79 N GLY A 80 1555 1555 1.34
LINK C GLY A 93 N MSE A 94 1555 1555 1.34
LINK C MSE A 94 N TYR A 95 1555 1555 1.33
LINK C VAL A 101 N MSE A 102 1555 1555 1.34
LINK C MSE A 102 N ASN A 103 1555 1555 1.33
LINK C PHE A 110 N MSE A 111 1555 1555 1.33
LINK C MSE A 111 N GLY A 112 1555 1555 1.33
LINK C THR A 131 N MSE A 132 1555 1555 1.33
LINK C MSE A 132 N GLN A 133 1555 1555 1.33
LINK C TYR A 233 N MSE A 234 1555 1555 1.33
LINK C MSE A 234 N SER A 235 1555 1555 1.34
LINK C GLU A 267 N AMSE A 268 1555 1555 1.32
LINK C GLU A 267 N BMSE A 268 1555 1555 1.34
LINK C AMSE A 268 N ASP A 269 1555 1555 1.33
LINK C BMSE A 268 N ASP A 269 1555 1555 1.33
LINK C ILE A 279 N MSE A 280 1555 1555 1.33
LINK C MSE A 280 N LYS A 281 1555 1555 1.33
LINK C GLY A 295 N MSE A 296 1555 1555 1.33
LINK C MSE A 296 N ALA A 297 1555 1555 1.33
LINK C PHE A 309 N MSE A 310 1555 1555 1.33
LINK C MSE A 310 N GLU A 311 1555 1555 1.34
LINK C ARG B 78 N MSE B 79 1555 1555 1.33
LINK C MSE B 79 N GLY B 80 1555 1555 1.33
LINK C GLY B 93 N MSE B 94 1555 1555 1.34
LINK C MSE B 94 N TYR B 95 1555 1555 1.33
LINK C VAL B 101 N MSE B 102 1555 1555 1.33
LINK C MSE B 102 N ASN B 103 1555 1555 1.34
LINK C PHE B 110 N MSE B 111 1555 1555 1.33
LINK C MSE B 111 N GLY B 112 1555 1555 1.33
LINK C THR B 131 N MSE B 132 1555 1555 1.33
LINK C MSE B 132 N GLN B 133 1555 1555 1.32
LINK C TYR B 233 N MSE B 234 1555 1555 1.33
LINK C MSE B 234 N SER B 235 1555 1555 1.33
LINK C GLU B 267 N MSE B 268 1555 1555 1.33
LINK C MSE B 268 N ASP B 269 1555 1555 1.33
LINK C ILE B 279 N MSE B 280 1555 1555 1.34
LINK C MSE B 280 N LYS B 281 1555 1555 1.34
LINK C GLY B 295 N MSE B 296 1555 1555 1.33
LINK C MSE B 296 N ALA B 297 1555 1555 1.33
LINK C PHE B 309 N MSE B 310 1555 1555 1.33
LINK C MSE B 310 N GLU B 311 1555 1555 1.33
LINK C GLY C 93 N BMSE C 94 1555 1555 1.33
LINK C GLY C 93 N AMSE C 94 1555 1555 1.33
LINK C BMSE C 94 N TYR C 95 1555 1555 1.34
LINK C AMSE C 94 N TYR C 95 1555 1555 1.33
LINK C VAL C 101 N MSE C 102 1555 1555 1.33
LINK C MSE C 102 N ASN C 103 1555 1555 1.33
LINK C PHE C 110 N MSE C 111 1555 1555 1.33
LINK C MSE C 111 N GLY C 112 1555 1555 1.33
LINK C THR C 131 N MSE C 132 1555 1555 1.33
LINK C MSE C 132 N GLN C 133 1555 1555 1.33
LINK C TYR C 233 N MSE C 234 1555 1555 1.34
LINK C MSE C 234 N SER C 235 1555 1555 1.33
LINK C GLU C 267 N MSE C 268 1555 1555 1.34
LINK C MSE C 268 N ASP C 269 1555 1555 1.33
LINK C ILE C 279 N MSE C 280 1555 1555 1.32
LINK C MSE C 280 N LYS C 281 1555 1555 1.33
LINK C GLY C 295 N MSE C 296 1555 1555 1.33
LINK C MSE C 296 N ALA C 297 1555 1555 1.34
LINK C PHE C 309 N MSE C 310 1555 1555 1.33
LINK C MSE C 310 N GLU C 311 1555 1555 1.34
LINK C ARG D 78 N MSE D 79 1555 1555 1.32
LINK C MSE D 79 N GLY D 80 1555 1555 1.33
LINK C GLY D 93 N MSE D 94 1555 1555 1.33
LINK C MSE D 94 N TYR D 95 1555 1555 1.33
LINK C VAL D 101 N MSE D 102 1555 1555 1.33
LINK C MSE D 102 N ASN D 103 1555 1555 1.33
LINK C PHE D 110 N MSE D 111 1555 1555 1.33
LINK C MSE D 111 N GLY D 112 1555 1555 1.33
LINK C THR D 131 N MSE D 132 1555 1555 1.33
LINK C MSE D 132 N GLN D 133 1555 1555 1.33
LINK C TYR D 233 N MSE D 234 1555 1555 1.32
LINK C MSE D 234 N SER D 235 1555 1555 1.33
LINK C GLU D 267 N MSE D 268 1555 1555 1.34
LINK C MSE D 268 N ASP D 269 1555 1555 1.33
LINK C ILE D 279 N MSE D 280 1555 1555 1.33
LINK C MSE D 280 N LYS D 281 1555 1555 1.34
LINK C GLY D 295 N MSE D 296 1555 1555 1.33
LINK C MSE D 296 N ALA D 297 1555 1555 1.34
LINK C PHE D 309 N MSE D 310 1555 1555 1.33
LINK C MSE D 310 N GLU D 311 1555 1555 1.34
CISPEP 1 VAL A 19 PHE A 20 0 -6.23
CISPEP 2 GLY A 335 GLU A 336 0 14.52
CISPEP 3 GLU C 71 ASP C 72 0 -0.16
CRYST1 119.260 119.260 429.100 90.00 90.00 120.00 P 65 2 2 48
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 0.008385 0.004841 0.000000 0.00000
SCALE2 0.000000 0.009682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002330 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
