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HEADER HYDROLASE 31-MAY-13 4L0C
TITLE CRYTAL STRUCTURE OF THE N-FOPMYLMALEAMIC ACID DEFORMYLASE NFO(S94A)
TITLE 2 FROM PSEUDOMONAS PUTIDA S16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEFORMYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: N-FORMYLMALEAMATE DEFORMYLASE, NFO;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 1042876;
SOURCE 4 STRAIN: S16;
SOURCE 5 GENE: PPS_4059;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS DEFORMYLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.CHEN,Y.LU,Z.ZHANG,G.WU,P.XU
REVDAT 1 04-JUN-14 4L0C 0
JRNL AUTH D.CHEN,Y.LU,Z.ZHANG,G.WU,P.XU
JRNL TITL CRYTAL STRUCTURE OF THE N-FOPMYLMALEAMIC ACID DEFORMYLASE
JRNL TITL 2 NFO FROM PSEUDOMONAS PUTIDA S16
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 226522
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11941
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 16459
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 821
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15728
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 2104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.34000
REMARK 3 B22 (A**2) : 0.99000
REMARK 3 B33 (A**2) : 0.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16325 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22305 ; 1.284 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2077 ; 5.389 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 715 ;29.087 ;23.063
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2382 ;12.409 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 128 ;14.988 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2518 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12548 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4L0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB080020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 239055
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 44.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG8000, 0.3M NABR, 0.1M TRIS PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 43.63400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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 ASN C 254
REMARK 465 ARG C 255
REMARK 465 ASN D 254
REMARK 465 ARG D 255
REMARK 465 MSE F 1
REMARK 465 GLU F 235
REMARK 465 ARG F 255
REMARK 465 MSE G 1
REMARK 465 ASN G 254
REMARK 465 ARG G 255
REMARK 465 MSE H 1
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 MSE A 85 CG SE CE
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 GLU C 235 CG CD OE1 OE2
REMARK 470 GLU D 235 CG CD OE1 OE2
REMARK 470 GLU F 234 CG CD OE1 OE2
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 O HOH G 453 O HOH H 696 2.17
REMARK 500 O HOH B 402 O HOH B 652 2.18
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 G 105 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 MSE H 74 CA - CB - CG ANGL. DEV. = -10.3 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 SER A 64 -158.46 -131.67
REMARK 500 ALA A 94 -112.66 64.66
REMARK 500 GLU A 235 -3.64 71.40
REMARK 500 ASN A 244 82.81 -152.22
REMARK 500 SER B 64 -158.75 -131.43
REMARK 500 ALA B 94 -111.46 62.43
REMARK 500 GLU B 235 -4.32 68.78
REMARK 500 ASN B 244 81.95 -151.72
REMARK 500 SER C 64 -159.92 -127.99
REMARK 500 ALA C 94 -115.62 62.51
REMARK 500 GLU C 235 -18.16 65.16
REMARK 500 ASN C 244 79.62 -154.71
REMARK 500 SER D 64 -162.81 -129.59
REMARK 500 ALA D 94 -113.59 59.66
REMARK 500 ASN D 244 82.02 -150.29
REMARK 500 SER E 64 -158.03 -128.84
REMARK 500 ALA E 94 -114.71 61.05
REMARK 500 ASP E 107 75.10 -157.31
REMARK 500 GLU E 235 -7.40 73.43
REMARK 500 ASN E 244 82.77 -150.11
REMARK 500 ASN E 254 17.37 59.06
REMARK 500 SER F 64 -155.49 -130.66
REMARK 500 ALA F 94 -116.47 63.05
REMARK 500 ASP F 107 87.78 -156.68
REMARK 500 ALA G 94 -113.23 63.42
REMARK 500 GLU G 235 -11.33 70.85
REMARK 500 ASN G 244 82.42 -153.66
REMARK 500 SER H 64 -159.18 -131.97
REMARK 500 ALA H 94 -114.31 59.17
REMARK 500 ASP H 107 73.98 -156.73
REMARK 500 GLU H 235 -6.65 72.22
REMARK 500 ASN H 254 19.37 53.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MSE B 85 -26.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 612 DISTANCE = 9.17 ANGSTROMS
REMARK 525 HOH B 455 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH D 406 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH H 408 DISTANCE = 12.05 ANGSTROMS
REMARK 525 HOH H 490 DISTANCE = 8.09 ANGSTROMS
REMARK 525 HOH H 684 DISTANCE = 10.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG H 302
DBREF 4L0C A 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
DBREF 4L0C B 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
DBREF 4L0C C 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
DBREF 4L0C D 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
DBREF 4L0C E 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
DBREF 4L0C F 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
DBREF 4L0C G 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
DBREF 4L0C H 1 255 UNP F8G0M2 F8G0M2_PSEPU 1 255
SEQADV 4L0C ALA A 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQADV 4L0C ALA B 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQADV 4L0C ALA C 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQADV 4L0C ALA D 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQADV 4L0C ALA E 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQADV 4L0C ALA F 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQADV 4L0C ALA G 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQADV 4L0C ALA H 94 UNP F8G0M2 SER 94 ENGINEERED MUTATION
SEQRES 1 A 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 A 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 A 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 A 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 A 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 A 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 A 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 A 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 A 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 A 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 A 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 A 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 A 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 A 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 A 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 A 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 A 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 A 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 A 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 A 255 PHE ILE THR ALA VAL SER ASN ARG
SEQRES 1 B 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 B 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 B 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 B 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 B 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 B 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 B 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 B 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 B 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 B 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 B 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 B 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 B 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 B 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 B 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 B 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 B 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 B 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 B 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 B 255 PHE ILE THR ALA VAL SER ASN ARG
SEQRES 1 C 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 C 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 C 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 C 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 C 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 C 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 C 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 C 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 C 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 C 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 C 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 C 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 C 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 C 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 C 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 C 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 C 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 C 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 C 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 C 255 PHE ILE THR ALA VAL SER ASN ARG
SEQRES 1 D 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 D 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 D 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 D 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 D 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 D 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 D 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 D 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 D 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 D 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 D 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 D 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 D 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 D 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 D 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 D 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 D 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 D 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 D 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 D 255 PHE ILE THR ALA VAL SER ASN ARG
SEQRES 1 E 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 E 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 E 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 E 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 E 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 E 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 E 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 E 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 E 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 E 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 E 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 E 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 E 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 E 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 E 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 E 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 E 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 E 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 E 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 E 255 PHE ILE THR ALA VAL SER ASN ARG
SEQRES 1 F 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 F 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 F 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 F 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 F 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 F 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 F 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 F 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 F 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 F 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 F 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 F 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 F 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 F 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 F 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 F 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 F 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 F 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 F 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 F 255 PHE ILE THR ALA VAL SER ASN ARG
SEQRES 1 G 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 G 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 G 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 G 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 G 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 G 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 G 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 G 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 G 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 G 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 G 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 G 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 G 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 G 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 G 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 G 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 G 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 G 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 G 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 G 255 PHE ILE THR ALA VAL SER ASN ARG
SEQRES 1 H 255 MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES 2 H 255 HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES 3 H 255 LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES 4 H 255 PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES 5 H 255 VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES 6 H 255 ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES 7 H 255 VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES 8 H 255 GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES 9 H 255 ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES 10 H 255 ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES 11 H 255 ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES 12 H 255 GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES 13 H 255 PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES 14 H 255 TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES 15 H 255 PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES 16 H 255 ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES 17 H 255 GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES 18 H 255 ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES 19 H 255 GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES 20 H 255 PHE ILE THR ALA VAL SER ASN ARG
MODRES 4L0C MSE A 1 MET SELENOMETHIONINE
MODRES 4L0C MSE A 74 MET SELENOMETHIONINE
MODRES 4L0C MSE A 85 MET SELENOMETHIONINE
MODRES 4L0C MSE A 95 MET SELENOMETHIONINE
MODRES 4L0C MSE A 150 MET SELENOMETHIONINE
MODRES 4L0C MSE A 152 MET SELENOMETHIONINE
MODRES 4L0C MSE A 239 MET SELENOMETHIONINE
MODRES 4L0C MSE B 1 MET SELENOMETHIONINE
MODRES 4L0C MSE B 74 MET SELENOMETHIONINE
MODRES 4L0C MSE B 85 MET SELENOMETHIONINE
MODRES 4L0C MSE B 95 MET SELENOMETHIONINE
MODRES 4L0C MSE B 150 MET SELENOMETHIONINE
MODRES 4L0C MSE B 152 MET SELENOMETHIONINE
MODRES 4L0C MSE B 239 MET SELENOMETHIONINE
MODRES 4L0C MSE C 1 MET SELENOMETHIONINE
MODRES 4L0C MSE C 74 MET SELENOMETHIONINE
MODRES 4L0C MSE C 85 MET SELENOMETHIONINE
MODRES 4L0C MSE C 95 MET SELENOMETHIONINE
MODRES 4L0C MSE C 150 MET SELENOMETHIONINE
MODRES 4L0C MSE C 152 MET SELENOMETHIONINE
MODRES 4L0C MSE C 239 MET SELENOMETHIONINE
MODRES 4L0C MSE D 1 MET SELENOMETHIONINE
MODRES 4L0C MSE D 74 MET SELENOMETHIONINE
MODRES 4L0C MSE D 85 MET SELENOMETHIONINE
MODRES 4L0C MSE D 95 MET SELENOMETHIONINE
MODRES 4L0C MSE D 150 MET SELENOMETHIONINE
MODRES 4L0C MSE D 152 MET SELENOMETHIONINE
MODRES 4L0C MSE D 239 MET SELENOMETHIONINE
MODRES 4L0C MSE E 1 MET SELENOMETHIONINE
MODRES 4L0C MSE E 74 MET SELENOMETHIONINE
MODRES 4L0C MSE E 85 MET SELENOMETHIONINE
MODRES 4L0C MSE E 95 MET SELENOMETHIONINE
MODRES 4L0C MSE E 150 MET SELENOMETHIONINE
MODRES 4L0C MSE E 152 MET SELENOMETHIONINE
MODRES 4L0C MSE E 239 MET SELENOMETHIONINE
MODRES 4L0C MSE F 74 MET SELENOMETHIONINE
MODRES 4L0C MSE F 85 MET SELENOMETHIONINE
MODRES 4L0C MSE F 95 MET SELENOMETHIONINE
MODRES 4L0C MSE F 150 MET SELENOMETHIONINE
MODRES 4L0C MSE F 152 MET SELENOMETHIONINE
MODRES 4L0C MSE F 239 MET SELENOMETHIONINE
MODRES 4L0C MSE G 74 MET SELENOMETHIONINE
MODRES 4L0C MSE G 85 MET SELENOMETHIONINE
MODRES 4L0C MSE G 95 MET SELENOMETHIONINE
MODRES 4L0C MSE G 150 MET SELENOMETHIONINE
MODRES 4L0C MSE G 152 MET SELENOMETHIONINE
MODRES 4L0C MSE G 239 MET SELENOMETHIONINE
MODRES 4L0C MSE H 74 MET SELENOMETHIONINE
MODRES 4L0C MSE H 85 MET SELENOMETHIONINE
MODRES 4L0C MSE H 95 MET SELENOMETHIONINE
MODRES 4L0C MSE H 150 MET SELENOMETHIONINE
MODRES 4L0C MSE H 152 MET SELENOMETHIONINE
MODRES 4L0C MSE H 239 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 74 8
HET MSE A 85 5
HET MSE A 95 8
HET MSE A 150 8
HET MSE A 152 8
HET MSE A 239 8
HET MSE B 1 13
HET MSE B 74 8
HET MSE B 85 8
HET MSE B 95 8
HET MSE B 150 8
HET MSE B 152 8
HET MSE B 239 8
HET MSE C 1 8
HET MSE C 74 8
HET MSE C 85 13
HET MSE C 95 8
HET MSE C 150 8
HET MSE C 152 8
HET MSE C 239 8
HET MSE D 1 8
HET MSE D 74 8
HET MSE D 85 8
HET MSE D 95 8
HET MSE D 150 8
HET MSE D 152 8
HET MSE D 239 8
HET MSE E 1 8
HET MSE E 74 8
HET MSE E 85 8
HET MSE E 95 8
HET MSE E 150 8
HET MSE E 152 8
HET MSE E 239 8
HET MSE F 74 8
HET MSE F 85 8
HET MSE F 95 8
HET MSE F 150 8
HET MSE F 152 8
HET MSE F 239 8
HET MSE G 74 8
HET MSE G 85 8
HET MSE G 95 8
HET MSE G 150 8
HET MSE G 152 8
HET MSE G 239 8
HET MSE H 74 8
HET MSE H 85 8
HET MSE H 95 8
HET MSE H 150 8
HET MSE H 152 8
HET MSE H 239 8
HET ACY A 301 4
HET ACY A 302 4
HET ACY B 301 4
HET ACY C 301 4
HET ACY D 301 4
HET ACY E 301 4
HET ACY F 301 4
HET ACY G 301 4
HET ACY G 302 4
HET ACY H 301 4
HET PEG H 302 7
HETNAM MSE SELENOMETHIONINE
HETNAM ACY ACETIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 1 MSE 53(C5 H11 N O2 SE)
FORMUL 9 ACY 10(C2 H4 O2)
FORMUL 19 PEG C4 H10 O3
FORMUL 20 HOH *2104(H2 O)
HELIX 1 1 PRO A 34 THR A 37 5 4
HELIX 2 2 TRP A 38 ALA A 46 1 9
HELIX 3 3 SER A 70 ARG A 84 1 15
HELIX 4 4 ALA A 94 ASP A 107 1 14
HELIX 5 5 LYS A 132 GLY A 146 1 15
HELIX 6 6 THR A 148 SER A 154 1 7
HELIX 7 7 THR A 160 LEU A 171 1 12
HELIX 8 8 HIS A 172 CYS A 174 5 3
HELIX 9 9 GLN A 175 ASP A 189 1 15
HELIX 10 10 ILE A 191 ALA A 196 1 6
HELIX 11 11 GLN A 214 ALA A 225 1 12
HELIX 12 12 MSE A 239 ASN A 244 1 6
HELIX 13 13 ASN A 244 SER A 253 1 10
HELIX 14 14 PRO B 34 THR B 37 5 4
HELIX 15 15 TRP B 38 ALA B 46 1 9
HELIX 16 16 SER B 70 GLN B 83 1 14
HELIX 17 17 ALA B 94 ASP B 107 1 14
HELIX 18 18 LYS B 132 GLY B 146 1 15
HELIX 19 19 THR B 148 SER B 154 1 7
HELIX 20 20 THR B 160 LEU B 171 1 12
HELIX 21 21 HIS B 172 CYS B 174 5 3
HELIX 22 22 GLN B 175 ASP B 189 1 15
HELIX 23 23 ILE B 191 ALA B 196 1 6
HELIX 24 24 GLN B 214 ALA B 225 1 12
HELIX 25 25 MSE B 239 ASN B 244 1 6
HELIX 26 26 ASN B 244 VAL B 252 1 9
HELIX 27 27 PRO C 34 THR C 37 5 4
HELIX 28 28 TRP C 38 ALA C 46 1 9
HELIX 29 29 SER C 70 GLN C 83 1 14
HELIX 30 30 ALA C 94 ASP C 107 1 14
HELIX 31 31 LYS C 132 GLY C 146 1 15
HELIX 32 32 THR C 148 SER C 154 1 7
HELIX 33 33 THR C 160 LEU C 171 1 12
HELIX 34 34 HIS C 172 CYS C 174 5 3
HELIX 35 35 GLN C 175 ASP C 189 1 15
HELIX 36 36 ILE C 191 ALA C 196 1 6
HELIX 37 37 GLN C 214 ALA C 225 1 12
HELIX 38 38 MSE C 239 ASN C 244 1 6
HELIX 39 39 ASN C 244 SER C 253 1 10
HELIX 40 40 PRO D 34 THR D 37 5 4
HELIX 41 41 TRP D 38 ALA D 46 1 9
HELIX 42 42 SER D 70 GLN D 83 1 14
HELIX 43 43 ALA D 94 ASP D 107 1 14
HELIX 44 44 LYS D 132 GLY D 146 1 15
HELIX 45 45 THR D 148 SER D 154 1 7
HELIX 46 46 THR D 160 LEU D 171 1 12
HELIX 47 47 HIS D 172 CYS D 174 5 3
HELIX 48 48 GLN D 175 ASP D 189 1 15
HELIX 49 49 ILE D 191 ALA D 196 1 6
HELIX 50 50 GLN D 214 ALA D 225 1 12
HELIX 51 51 MSE D 239 ASN D 244 1 6
HELIX 52 52 ASN D 244 SER D 253 1 10
HELIX 53 53 PRO E 34 THR E 37 5 4
HELIX 54 54 TRP E 38 ALA E 46 1 9
HELIX 55 55 SER E 70 GLN E 83 1 14
HELIX 56 56 ALA E 94 ASP E 107 1 14
HELIX 57 57 LYS E 132 GLY E 146 1 15
HELIX 58 58 THR E 148 SER E 154 1 7
HELIX 59 59 THR E 160 LEU E 171 1 12
HELIX 60 60 HIS E 172 CYS E 174 5 3
HELIX 61 61 GLN E 175 ASP E 189 1 15
HELIX 62 62 ILE E 191 ALA E 196 1 6
HELIX 63 63 GLN E 214 ALA E 225 1 12
HELIX 64 64 MSE E 239 ASN E 244 1 6
HELIX 65 65 ASN E 244 ASN E 254 1 11
HELIX 66 66 PRO F 34 THR F 37 5 4
HELIX 67 67 TRP F 38 ALA F 46 1 9
HELIX 68 68 SER F 70 GLN F 83 1 14
HELIX 69 69 ALA F 94 ASP F 107 1 14
HELIX 70 70 LYS F 132 GLY F 146 1 15
HELIX 71 71 THR F 148 SER F 154 1 7
HELIX 72 72 THR F 160 LEU F 171 1 12
HELIX 73 73 HIS F 172 CYS F 174 5 3
HELIX 74 74 GLN F 175 ASP F 189 1 15
HELIX 75 75 ILE F 191 ALA F 196 1 6
HELIX 76 76 GLN F 214 ALA F 225 1 12
HELIX 77 77 MSE F 239 ASN F 244 1 6
HELIX 78 78 ASN F 244 SER F 253 1 10
HELIX 79 79 PRO G 34 THR G 37 5 4
HELIX 80 80 TRP G 38 ALA G 46 1 9
HELIX 81 81 SER G 70 GLN G 83 1 14
HELIX 82 82 ALA G 94 ASP G 107 1 14
HELIX 83 83 LYS G 132 GLY G 146 1 15
HELIX 84 84 THR G 148 SER G 154 1 7
HELIX 85 85 THR G 160 LEU G 171 1 12
HELIX 86 86 HIS G 172 CYS G 174 5 3
HELIX 87 87 GLN G 175 ASP G 189 1 15
HELIX 88 88 ILE G 191 ALA G 196 1 6
HELIX 89 89 GLN G 214 ALA G 225 1 12
HELIX 90 90 MSE G 239 ASN G 244 1 6
HELIX 91 91 ASN G 244 SER G 253 1 10
HELIX 92 92 PRO H 34 THR H 37 5 4
HELIX 93 93 TRP H 38 ALA H 46 1 9
HELIX 94 94 SER H 70 GLN H 83 1 14
HELIX 95 95 ALA H 94 ASP H 107 1 14
HELIX 96 96 LYS H 132 GLY H 146 1 15
HELIX 97 97 THR H 148 SER H 154 1 7
HELIX 98 98 THR H 160 LEU H 171 1 12
HELIX 99 99 HIS H 172 CYS H 174 5 3
HELIX 100 100 GLN H 175 ASP H 189 1 15
HELIX 101 101 ILE H 191 ALA H 196 1 6
HELIX 102 102 GLN H 214 ALA H 225 1 12
HELIX 103 103 MSE H 239 ASN H 244 1 6
HELIX 104 104 ASN H 244 ASN H 254 1 11
SHEET 1 A 8 LYS A 2 ALA A 8 0
SHEET 2 A 8 ILE A 11 PHE A 18 -1 O HIS A 17 N LYS A 2
SHEET 3 A 8 ASP A 50 VAL A 54 -1 O VAL A 51 N PHE A 18
SHEET 4 A 8 PRO A 24 ILE A 28 1 N LEU A 27 O VAL A 54
SHEET 5 A 8 VAL A 88 HIS A 93 1 O HIS A 93 N ILE A 28
SHEET 6 A 8 PHE A 111 VAL A 117 1 O VAL A 117 N GLY A 92
SHEET 7 A 8 ILE A 202 ALA A 207 1 O GLN A 203 N LEU A 116
SHEET 8 A 8 THR A 229 VAL A 233 1 O THR A 229 N LEU A 204
SHEET 1 B 8 LYS B 2 ALA B 8 0
SHEET 2 B 8 ILE B 11 PHE B 18 -1 O GLN B 13 N VAL B 6
SHEET 3 B 8 PHE B 49 VAL B 54 -1 O VAL B 51 N PHE B 18
SHEET 4 B 8 SER B 23 ILE B 28 1 N LEU B 27 O VAL B 54
SHEET 5 B 8 VAL B 88 HIS B 93 1 O HIS B 93 N ILE B 28
SHEET 6 B 8 PHE B 111 VAL B 117 1 O VAL B 117 N GLY B 92
SHEET 7 B 8 ILE B 202 ALA B 207 1 O VAL B 205 N LEU B 116
SHEET 8 B 8 THR B 229 VAL B 233 1 O THR B 229 N LEU B 204
SHEET 1 C 8 LYS C 2 ALA C 8 0
SHEET 2 C 8 ILE C 11 PHE C 18 -1 O GLN C 13 N VAL C 6
SHEET 3 C 8 ASP C 50 VAL C 54 -1 O VAL C 51 N PHE C 18
SHEET 4 C 8 PRO C 24 ILE C 28 1 N LEU C 25 O HIS C 52
SHEET 5 C 8 VAL C 88 HIS C 93 1 O HIS C 93 N ILE C 28
SHEET 6 C 8 PHE C 111 VAL C 117 1 O VAL C 117 N GLY C 92
SHEET 7 C 8 ILE C 202 ALA C 207 1 O GLN C 203 N LEU C 116
SHEET 8 C 8 THR C 229 VAL C 233 1 O THR C 229 N LEU C 204
SHEET 1 D 8 LYS D 2 ALA D 8 0
SHEET 2 D 8 ILE D 11 PHE D 18 -1 O ILE D 15 N TYR D 4
SHEET 3 D 8 PHE D 49 VAL D 54 -1 O VAL D 51 N PHE D 18
SHEET 4 D 8 SER D 23 ILE D 28 1 N LEU D 25 O ASP D 50
SHEET 5 D 8 VAL D 88 HIS D 93 1 O HIS D 93 N ILE D 28
SHEET 6 D 8 PHE D 111 VAL D 117 1 O VAL D 117 N GLY D 92
SHEET 7 D 8 ILE D 202 ALA D 207 1 O VAL D 205 N LEU D 116
SHEET 8 D 8 THR D 229 VAL D 233 1 O THR D 229 N LEU D 204
SHEET 1 E 8 LYS E 2 ALA E 8 0
SHEET 2 E 8 ILE E 11 PHE E 18 -1 O ILE E 15 N TYR E 4
SHEET 3 E 8 ASP E 50 VAL E 54 -1 O VAL E 51 N PHE E 18
SHEET 4 E 8 PRO E 24 ILE E 28 1 N LEU E 25 O HIS E 52
SHEET 5 E 8 VAL E 88 HIS E 93 1 O HIS E 93 N ILE E 28
SHEET 6 E 8 PHE E 111 VAL E 117 1 O VAL E 117 N GLY E 92
SHEET 7 E 8 ILE E 202 ALA E 207 1 O VAL E 205 N LEU E 116
SHEET 8 E 8 THR E 229 VAL E 233 1 O THR E 229 N LEU E 204
SHEET 1 F 8 GLY F 3 ALA F 8 0
SHEET 2 F 8 ILE F 11 PHE F 18 -1 O GLN F 13 N VAL F 6
SHEET 3 F 8 ASP F 50 VAL F 54 -1 O VAL F 51 N PHE F 18
SHEET 4 F 8 PRO F 24 ILE F 28 1 N LEU F 25 O HIS F 52
SHEET 5 F 8 VAL F 88 HIS F 93 1 O VAL F 89 N LEU F 26
SHEET 6 F 8 PHE F 111 VAL F 117 1 O VAL F 117 N GLY F 92
SHEET 7 F 8 ILE F 202 ALA F 207 1 O GLN F 203 N LEU F 116
SHEET 8 F 8 THR F 229 VAL F 233 1 O VAL F 233 N VAL F 206
SHEET 1 G 8 GLY G 3 ALA G 8 0
SHEET 2 G 8 ILE G 11 PHE G 18 -1 O ILE G 15 N TYR G 4
SHEET 3 G 8 ASP G 50 VAL G 54 -1 O VAL G 51 N PHE G 18
SHEET 4 G 8 PRO G 24 ILE G 28 1 N LEU G 25 O HIS G 52
SHEET 5 G 8 VAL G 88 HIS G 93 1 O LEU G 91 N ILE G 28
SHEET 6 G 8 PHE G 111 VAL G 117 1 O VAL G 117 N GLY G 92
SHEET 7 G 8 ILE G 202 ALA G 207 1 O GLN G 203 N LEU G 116
SHEET 8 G 8 THR G 229 VAL G 233 1 O THR G 229 N LEU G 204
SHEET 1 H 8 GLY H 3 ALA H 8 0
SHEET 2 H 8 ILE H 11 PHE H 18 -1 O GLN H 13 N VAL H 6
SHEET 3 H 8 ASP H 50 VAL H 54 -1 O VAL H 51 N PHE H 18
SHEET 4 H 8 PRO H 24 ILE H 28 1 N LEU H 25 O HIS H 52
SHEET 5 H 8 VAL H 88 HIS H 93 1 O HIS H 93 N ILE H 28
SHEET 6 H 8 PHE H 111 VAL H 117 1 O ILE H 115 N VAL H 90
SHEET 7 H 8 ILE H 202 ALA H 207 1 O VAL H 205 N LEU H 116
SHEET 8 H 8 THR H 229 VAL H 233 1 O THR H 229 N LEU H 204
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C ALA A 73 N MSE A 74 1555 1555 1.33
LINK C MSE A 74 N ALA A 75 1555 1555 1.33
LINK C ARG A 84 N MSE A 85 1555 1555 1.31
LINK C MSE A 85 N GLU A 86 1555 1555 1.32
LINK C ALA A 94 N MSE A 95 1555 1555 1.34
LINK C MSE A 95 N GLY A 96 1555 1555 1.34
LINK C ALA A 149 N MSE A 150 1555 1555 1.33
LINK C MSE A 150 N GLU A 151 1555 1555 1.34
LINK C GLU A 151 N MSE A 152 1555 1555 1.33
LINK C MSE A 152 N ARG A 153 1555 1555 1.33
LINK C HIS A 238 N MSE A 239 1555 1555 1.33
LINK C MSE A 239 N ILE A 240 1555 1555 1.34
LINK C MSE B 1 N LYS B 2 1555 1555 1.34
LINK C ALA B 73 N MSE B 74 1555 1555 1.33
LINK C MSE B 74 N ALA B 75 1555 1555 1.33
LINK C ARG B 84 N MSE B 85 1555 1555 1.22
LINK C MSE B 85 N GLU B 86 1555 1555 1.29
LINK C ALA B 94 N MSE B 95 1555 1555 1.34
LINK C MSE B 95 N GLY B 96 1555 1555 1.34
LINK C ALA B 149 N MSE B 150 1555 1555 1.34
LINK C MSE B 150 N GLU B 151 1555 1555 1.34
LINK C GLU B 151 N MSE B 152 1555 1555 1.33
LINK C MSE B 152 N ARG B 153 1555 1555 1.33
LINK C HIS B 238 N MSE B 239 1555 1555 1.34
LINK C MSE B 239 N ILE B 240 1555 1555 1.34
LINK C MSE C 1 N LYS C 2 1555 1555 1.33
LINK C ALA C 73 N MSE C 74 1555 1555 1.34
LINK C MSE C 74 N ALA C 75 1555 1555 1.34
LINK C ARG C 84 N MSE C 85 1555 1555 1.33
LINK C MSE C 85 N GLU C 86 1555 1555 1.32
LINK C ALA C 94 N MSE C 95 1555 1555 1.34
LINK C MSE C 95 N GLY C 96 1555 1555 1.34
LINK C ALA C 149 N MSE C 150 1555 1555 1.34
LINK C MSE C 150 N GLU C 151 1555 1555 1.33
LINK C GLU C 151 N MSE C 152 1555 1555 1.33
LINK C MSE C 152 N ARG C 153 1555 1555 1.33
LINK C HIS C 238 N MSE C 239 1555 1555 1.33
LINK C MSE C 239 N ILE C 240 1555 1555 1.33
LINK C MSE D 1 N LYS D 2 1555 1555 1.33
LINK C ALA D 73 N MSE D 74 1555 1555 1.34
LINK C MSE D 74 N ALA D 75 1555 1555 1.33
LINK C ARG D 84 N MSE D 85 1555 1555 1.33
LINK C MSE D 85 N GLU D 86 1555 1555 1.33
LINK C ALA D 94 N MSE D 95 1555 1555 1.33
LINK C MSE D 95 N GLY D 96 1555 1555 1.34
LINK C ALA D 149 N MSE D 150 1555 1555 1.33
LINK C MSE D 150 N GLU D 151 1555 1555 1.34
LINK C GLU D 151 N MSE D 152 1555 1555 1.33
LINK C MSE D 152 N ARG D 153 1555 1555 1.33
LINK C HIS D 238 N MSE D 239 1555 1555 1.33
LINK C MSE D 239 N ILE D 240 1555 1555 1.34
LINK C MSE E 1 N LYS E 2 1555 1555 1.33
LINK C ALA E 73 N MSE E 74 1555 1555 1.33
LINK C MSE E 74 N ALA E 75 1555 1555 1.21
LINK C ARG E 84 N MSE E 85 1555 1555 1.33
LINK C MSE E 85 N GLU E 86 1555 1555 1.33
LINK C ALA E 94 N MSE E 95 1555 1555 1.34
LINK C MSE E 95 N GLY E 96 1555 1555 1.34
LINK C ALA E 149 N MSE E 150 1555 1555 1.33
LINK C MSE E 150 N GLU E 151 1555 1555 1.33
LINK C GLU E 151 N MSE E 152 1555 1555 1.34
LINK C MSE E 152 N ARG E 153 1555 1555 1.33
LINK C HIS E 238 N MSE E 239 1555 1555 1.27
LINK C MSE E 239 N ILE E 240 1555 1555 1.34
LINK C ALA F 73 N MSE F 74 1555 1555 1.34
LINK C MSE F 74 N ALA F 75 1555 1555 1.33
LINK C ARG F 84 N MSE F 85 1555 1555 1.34
LINK C MSE F 85 N GLU F 86 1555 1555 1.33
LINK C ALA F 94 N MSE F 95 1555 1555 1.34
LINK C MSE F 95 N GLY F 96 1555 1555 1.33
LINK C ALA F 149 N MSE F 150 1555 1555 1.33
LINK C MSE F 150 N GLU F 151 1555 1555 1.34
LINK C GLU F 151 N MSE F 152 1555 1555 1.33
LINK C MSE F 152 N ARG F 153 1555 1555 1.33
LINK C HIS F 238 N MSE F 239 1555 1555 1.33
LINK C MSE F 239 N ILE F 240 1555 1555 1.33
LINK C ALA G 73 N MSE G 74 1555 1555 1.34
LINK C MSE G 74 N ALA G 75 1555 1555 1.35
LINK C ARG G 84 N MSE G 85 1555 1555 1.34
LINK C MSE G 85 N GLU G 86 1555 1555 1.33
LINK C ALA G 94 N MSE G 95 1555 1555 1.33
LINK C MSE G 95 N GLY G 96 1555 1555 1.33
LINK C ALA G 149 N MSE G 150 1555 1555 1.33
LINK C MSE G 150 N GLU G 151 1555 1555 1.33
LINK C GLU G 151 N MSE G 152 1555 1555 1.33
LINK C MSE G 152 N ARG G 153 1555 1555 1.33
LINK C HIS G 238 N MSE G 239 1555 1555 1.33
LINK C MSE G 239 N ILE G 240 1555 1555 1.33
LINK C ALA H 73 N MSE H 74 1555 1555 1.34
LINK C MSE H 74 N ALA H 75 1555 1555 1.33
LINK C ARG H 84 N MSE H 85 1555 1555 1.33
LINK C MSE H 85 N GLU H 86 1555 1555 1.33
LINK C ALA H 94 N MSE H 95 1555 1555 1.34
LINK C MSE H 95 N GLY H 96 1555 1555 1.33
LINK C ALA H 149 N MSE H 150 1555 1555 1.34
LINK C MSE H 150 N GLU H 151 1555 1555 1.33
LINK C GLU H 151 N MSE H 152 1555 1555 1.34
LINK C MSE H 152 N ARG H 153 1555 1555 1.33
LINK C HIS H 238 N MSE H 239 1555 1555 1.33
LINK C MSE H 239 N ILE H 240 1555 1555 1.34
SITE 1 AC1 5 GLY A 30 THR A 32 SER A 33 MSE A 239
SITE 2 AC1 5 HOH A 682
SITE 1 AC2 4 ARG A 12 GLU A 63 SER A 64 HOH A 575
SITE 1 AC3 5 GLY B 30 THR B 32 SER B 33 MSE B 239
SITE 2 AC3 5 HOH B 651
SITE 1 AC4 5 GLY C 30 THR C 32 SER C 33 MSE C 239
SITE 2 AC4 5 HOH C 409
SITE 1 AC5 4 THR D 32 SER D 33 MSE D 239 HOH D 465
SITE 1 AC6 5 GLY E 30 THR E 32 SER E 33 MSE E 239
SITE 2 AC6 5 HOH E 436
SITE 1 AC7 5 GLY F 30 THR F 32 SER F 33 MSE F 239
SITE 2 AC7 5 HOH F 599
SITE 1 AC8 5 GLY G 30 THR G 32 SER G 33 MSE G 239
SITE 2 AC8 5 HOH G 465
SITE 1 AC9 5 ARG D 153 HOH D 544 SER G 23 VAL G 89
SITE 2 AC9 5 ARG G 113
SITE 1 BC1 5 GLY H 30 THR H 32 SER H 33 MSE H 239
SITE 2 BC1 5 HOH H 688
SITE 1 BC2 2 ALA H 131 LYS H 132
CRYST1 89.412 87.268 130.879 90.00 94.42 90.00 P 1 21 1 16
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 0.011184 0.000000 0.000865 0.00000
SCALE2 0.000000 0.011459 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007663 0.00000
TER 1997 ARG A 255
TER 4021 ARG B 255
TER 5992 SER C 253
TER 7976 SER D 253
TER 9968 ARG E 255
TER 11929 ASN F 254
TER 13884 SER G 253
TER 15881 ARG H 255
MASTER 460 0 64 104 64 0 19 617879 8 579 160
END |