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HEADER HYDROLASE 03-OCT-13 3WJ2
TITLE CRYSTAL STRUCTURE OF ESTFA (FE-LACKING APO FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FERROPLASMA ACIDIPHILUM;
SOURCE 3 ORGANISM_TAXID: 74969;
SOURCE 4 GENE: EST;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA-HYDRORASE FOLD, CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.OHARA,H.UNNO,Y.OSHIMA,K.FURUKAWA,N.FUJINO,K.HIROOKA,H.HEMMI,
AUTHOR 2 S.TAKAHASHI,T.NISHINO,M.KUSUNOKI,T.NAKAYAMA
REVDAT 1 30-JUL-14 3WJ2 0
JRNL AUTH K.OHARA,H.UNNO,Y.OSHIMA,M.HOSOYA,N.FUJINO,K.HIROOKA,
JRNL AUTH 2 S.TAKAHASHI,S.YAMASHITA,M.KUSUNOKI,T.NAKAYAMA
JRNL TITL STRUCTURAL INSIGHTS INTO THE LOW-PH ADAPTATION OF A UNIQUE
JRNL TITL 2 CARBOXYLESTERASE FROM FERROPLASMA: ALTERING THE PH OPTIMA OF
JRNL TITL 3 TWO CARBOXYLESTERASES
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M113.521856
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 158320
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8382
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) : 1.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10768
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 546
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9444
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 983
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.17000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.095
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.751
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9648 ; 0.029 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13013 ; 2.395 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1191 ; 6.378 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 455 ;31.951 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1659 ;15.117 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;17.974 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1383 ; 0.171 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7400 ; 0.014 ; 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): 5959 ; 1.532 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9564 ; 2.418 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3689 ; 3.551 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3449 ; 5.332 ; 4.500
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 : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3WJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB096397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
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 : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 166739
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.05800
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) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 3350, 100MM SODIUM ACETATE, PH
REMARK 280 8.0, VAPOR DIFFUSION, TEMPERATURE 293K
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 68.68000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, 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 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 MET A 1
REMARK 465 HIS A 2
REMARK 465 LEU A 3
REMARK 465 MET A 4
REMARK 465 ASN A 5
REMARK 465 MET A 221
REMARK 465 GLN A 222
REMARK 465 ASP A 223
REMARK 465 LEU A 224
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 LEU B 3
REMARK 465 MET B 4
REMARK 465 MET B 221
REMARK 465 GLN B 222
REMARK 465 ASP B 223
REMARK 465 LEU B 224
REMARK 465 MET C 1
REMARK 465 HIS C 2
REMARK 465 LEU C 3
REMARK 465 MET C 4
REMARK 465 MET C 221
REMARK 465 GLN C 222
REMARK 465 ASP C 223
REMARK 465 LEU C 224
REMARK 465 MET D 1
REMARK 465 HIS D 2
REMARK 465 LEU D 3
REMARK 465 MET D 4
REMARK 465 MET D 221
REMARK 465 GLN D 222
REMARK 465 ASP D 223
REMARK 465 LEU D 224
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 CG MET B 69 O HOH B 449 1.80
REMARK 500 O HOH B 554 O HOH B 673 1.86
REMARK 500 O HOH B 456 O HOH B 517 1.86
REMARK 500 NH1 ARG C 116 OD1 ASP C 129 1.87
REMARK 500 O HOH C 476 O HOH C 617 1.88
REMARK 500 O HOH B 574 O HOH B 629 1.90
REMARK 500 O HOH D 512 O HOH D 557 1.92
REMARK 500 CD ARG A 116 OD2 ASP A 129 1.92
REMARK 500 O HOH C 429 O HOH C 474 1.92
REMARK 500 O HOH A 614 O HOH A 653 1.96
REMARK 500 NH2 ARG A 170 O ASP A 236 1.97
REMARK 500 N ASN B 5 O HOH B 661 1.99
REMARK 500 O ASP B 201 N TYR B 203 2.01
REMARK 500 NH1 ARG A 265 O HOH A 448 2.01
REMARK 500 O HOH A 504 O HOH C 607 2.02
REMARK 500 ND2 ASN D 128 O HOH D 577 2.02
REMARK 500 O HOH C 579 O HOH C 603 2.05
REMARK 500 O HOH C 417 O HOH C 601 2.05
REMARK 500 N ASN D 5 O HOH D 448 2.07
REMARK 500 O HOH B 543 O HOH B 579 2.07
REMARK 500 O HOH A 560 O HOH A 640 2.08
REMARK 500 O HOH A 460 O HOH A 612 2.09
REMARK 500 OH TYR A 217 O HOH A 652 2.09
REMARK 500 O HOH A 544 O HOH A 645 2.09
REMARK 500 O HOH D 456 O HOH D 570 2.10
REMARK 500 C ASN B 220 O HOH B 451 2.11
REMARK 500 O HOH B 586 O HOH C 612 2.12
REMARK 500 O HOH A 505 O HOH A 522 2.13
REMARK 500 OG SER B 200 O HOH B 545 2.14
REMARK 500 O HOH A 476 O HOH B 519 2.14
REMARK 500 O HOH A 591 O HOH A 675 2.14
REMARK 500 NZ LYS D 142 O HOH D 573 2.15
REMARK 500 O HOH D 444 O HOH D 580 2.17
REMARK 500 O HOH A 515 O HOH A 658 2.18
REMARK 500 OH TYR C 217 O HOH C 583 2.19
REMARK 500 O ASN B 202 O HOH B 663 2.19
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 GLU A 257 CD GLU A 257 OE2 0.072
REMARK 500 VAL A 261 CB VAL A 261 CG1 -0.164
REMARK 500 VAL A 261 CB VAL A 261 CG2 -0.160
REMARK 500 TYR B 95 CD1 TYR B 95 CE1 0.094
REMARK 500 PHE B 123 CE1 PHE B 123 CZ 0.118
REMARK 500 MET B 176 CB MET B 176 CG 0.259
REMARK 500 VAL B 261 CB VAL B 261 CG2 -0.158
REMARK 500 TYR C 70 CE1 TYR C 70 CZ 0.081
REMARK 500 TYR C 228 CE1 TYR C 228 CZ 0.091
REMARK 500 VAL C 261 CB VAL C 261 CG1 -0.176
REMARK 500 GLU C 288 CD GLU C 288 OE2 -0.068
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 TYR A 98 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 116 CG - CD - NE ANGL. DEV. = -12.8 DEGREES
REMARK 500 ARG A 116 CD - NE - CZ ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ASP A 132 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 265 CD - NE - CZ ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH1 ANGL. DEV. = -12.8 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 270 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 294 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 MET B 69 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU B 88 CB - CG - CD2 ANGL. DEV. = -11.0 DEGREES
REMARK 500 TYR B 98 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 TYR B 98 CD1 - CE1 - CZ ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG B 100 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 116 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 MET B 176 CB - CG - SD ANGL. DEV. = -23.7 DEGREES
REMARK 500 MET B 176 CG - SD - CE ANGL. DEV. = -11.8 DEGREES
REMARK 500 ASP B 251 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP B 251 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TYR B 260 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 275 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 MET B 299 CG - SD - CE ANGL. DEV. = -21.3 DEGREES
REMARK 500 ASP C 8 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 63 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 68 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP C 96 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 MET C 216 CG - SD - CE ANGL. DEV. = -12.4 DEGREES
REMARK 500 ASN C 220 N - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 ASN C 220 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 ARG C 270 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU D 80 CB - CG - CD1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG D 116 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG D 270 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG D 275 NE - CZ - NH1 ANGL. DEV. = -4.9 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 ASN A 73 24.76 -148.64
REMARK 500 ASN A 74 55.40 37.90
REMARK 500 SER A 156 -119.86 46.56
REMARK 500 TYR A 184 63.22 36.56
REMARK 500 PHE A 192 -10.42 -150.27
REMARK 500 ASN A 202 0.83 82.29
REMARK 500 VAL A 204 -65.19 69.67
REMARK 500 TYR A 250 73.50 -109.96
REMARK 500 ASN B 73 22.44 -150.13
REMARK 500 ASN B 74 50.77 34.67
REMARK 500 PHE B 87 0.08 80.03
REMARK 500 SER B 156 -127.56 55.22
REMARK 500 TYR B 184 64.59 37.46
REMARK 500 PHE B 192 -13.21 -151.74
REMARK 500 ASN B 202 43.44 -54.14
REMARK 500 TYR B 203 -39.73 73.55
REMARK 500 TYR B 250 69.57 -111.10
REMARK 500 ASP C 61 98.94 -64.15
REMARK 500 ASN C 73 26.89 -151.21
REMARK 500 ASN C 74 48.84 38.62
REMARK 500 SER C 156 -125.87 51.75
REMARK 500 TYR C 184 61.09 39.95
REMARK 500 PHE C 192 -7.56 -150.81
REMARK 500 ASP C 201 -50.61 -121.64
REMARK 500 VAL C 204 -59.60 69.17
REMARK 500 TYR C 250 70.08 -106.24
REMARK 500 MET D 6 50.80 -118.72
REMARK 500 SER D 42 -94.03 -65.08
REMARK 500 SER D 43 40.79 -74.51
REMARK 500 ASP D 61 99.17 -47.35
REMARK 500 ASN D 73 21.73 -150.80
REMARK 500 ASN D 74 58.93 37.56
REMARK 500 PHE D 89 -169.28 -124.82
REMARK 500 LYS D 140 41.38 -101.94
REMARK 500 SER D 156 -123.25 60.14
REMARK 500 TYR D 184 66.15 35.21
REMARK 500 PHE D 192 -4.64 -149.09
REMARK 500 ASN D 202 -3.35 84.79
REMARK 500 TYR D 203 43.44 -108.12
REMARK 500 VAL D 204 -61.90 73.37
REMARK 500 LYS D 219 -104.29 -88.48
REMARK 500 TYR D 250 77.00 -106.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE A 303 23.9 L L OUTSIDE RANGE
REMARK 500 TYR B 203 20.9 L L OUTSIDE RANGE
REMARK 500 ASP C 201 22.3 L L OUTSIDE RANGE
REMARK 500 ASN C 220 16.9 L L OUTSIDE RANGE
REMARK 500 ILE C 225 24.9 L L OUTSIDE RANGE
REMARK 500 SER D 42 24.1 L L OUTSIDE RANGE
REMARK 500 ILE D 225 23.9 L L OUTSIDE RANGE
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 651 DISTANCE = 5.47 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WJ1 RELATED DB: PDB
REMARK 900 RELATED ID: 4P9N RELATED DB: PDB
DBREF 3WJ2 A 1 308 UNP Q2PCE5 Q2PCE5_9EURY 1 308
DBREF 3WJ2 B 1 308 UNP Q2PCE5 Q2PCE5_9EURY 1 308
DBREF 3WJ2 C 1 308 UNP Q2PCE5 Q2PCE5_9EURY 1 308
DBREF 3WJ2 D 1 308 UNP Q2PCE5 Q2PCE5_9EURY 1 308
SEQRES 1 A 308 MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER
SEQRES 2 A 308 LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS
SEQRES 3 A 308 ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER
SEQRES 4 A 308 SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU
SEQRES 5 A 308 ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU
SEQRES 6 A 308 ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA
SEQRES 7 A 308 ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN
SEQRES 8 A 308 ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS
SEQRES 9 A 308 GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU
SEQRES 10 A 308 ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA
SEQRES 11 A 308 TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP
SEQRES 12 A 308 PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER
SEQRES 13 A 308 ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS
SEQRES 14 A 308 ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU
SEQRES 15 A 308 PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER
SEQRES 16 A 308 PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS
SEQRES 17 A 308 MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET
SEQRES 18 A 308 GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA
SEQRES 19 A 308 ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR
SEQRES 20 A 308 ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR
SEQRES 21 A 308 VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY
SEQRES 22 A 308 ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP
SEQRES 23 A 308 PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET
SEQRES 24 A 308 VAL ALA ARG ILE ILE PRO ASP TYR LEU
SEQRES 1 B 308 MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER
SEQRES 2 B 308 LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS
SEQRES 3 B 308 ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER
SEQRES 4 B 308 SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU
SEQRES 5 B 308 ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU
SEQRES 6 B 308 ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA
SEQRES 7 B 308 ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN
SEQRES 8 B 308 ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS
SEQRES 9 B 308 GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU
SEQRES 10 B 308 ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA
SEQRES 11 B 308 TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP
SEQRES 12 B 308 PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER
SEQRES 13 B 308 ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS
SEQRES 14 B 308 ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU
SEQRES 15 B 308 PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER
SEQRES 16 B 308 PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS
SEQRES 17 B 308 MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET
SEQRES 18 B 308 GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA
SEQRES 19 B 308 ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR
SEQRES 20 B 308 ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR
SEQRES 21 B 308 VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY
SEQRES 22 B 308 ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP
SEQRES 23 B 308 PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET
SEQRES 24 B 308 VAL ALA ARG ILE ILE PRO ASP TYR LEU
SEQRES 1 C 308 MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER
SEQRES 2 C 308 LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS
SEQRES 3 C 308 ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER
SEQRES 4 C 308 SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU
SEQRES 5 C 308 ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU
SEQRES 6 C 308 ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA
SEQRES 7 C 308 ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN
SEQRES 8 C 308 ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS
SEQRES 9 C 308 GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU
SEQRES 10 C 308 ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA
SEQRES 11 C 308 TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP
SEQRES 12 C 308 PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER
SEQRES 13 C 308 ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS
SEQRES 14 C 308 ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU
SEQRES 15 C 308 PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER
SEQRES 16 C 308 PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS
SEQRES 17 C 308 MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET
SEQRES 18 C 308 GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA
SEQRES 19 C 308 ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR
SEQRES 20 C 308 ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR
SEQRES 21 C 308 VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY
SEQRES 22 C 308 ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP
SEQRES 23 C 308 PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET
SEQRES 24 C 308 VAL ALA ARG ILE ILE PRO ASP TYR LEU
SEQRES 1 D 308 MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER
SEQRES 2 D 308 LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS
SEQRES 3 D 308 ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER
SEQRES 4 D 308 SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU
SEQRES 5 D 308 ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU
SEQRES 6 D 308 ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA
SEQRES 7 D 308 ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN
SEQRES 8 D 308 ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS
SEQRES 9 D 308 GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU
SEQRES 10 D 308 ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA
SEQRES 11 D 308 TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP
SEQRES 12 D 308 PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER
SEQRES 13 D 308 ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS
SEQRES 14 D 308 ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU
SEQRES 15 D 308 PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER
SEQRES 16 D 308 PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS
SEQRES 17 D 308 MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET
SEQRES 18 D 308 GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA
SEQRES 19 D 308 ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR
SEQRES 20 D 308 ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR
SEQRES 21 D 308 VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY
SEQRES 22 D 308 ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP
SEQRES 23 D 308 PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET
SEQRES 24 D 308 VAL ALA ARG ILE ILE PRO ASP TYR LEU
FORMUL 5 HOH *983(H2 O)
HELIX 1 1 ASP A 8 ASP A 10 5 3
HELIX 2 2 PHE A 11 GLY A 22 1 12
HELIX 3 3 GLU A 28 SER A 43 1 16
HELIX 4 4 ASN A 91 GLY A 107 1 17
HELIX 5 5 PRO A 124 LYS A 140 1 17
HELIX 6 6 LYS A 141 GLY A 145 5 5
HELIX 7 7 SER A 156 GLY A 172 1 17
HELIX 8 8 SER A 193 TYR A 199 1 7
HELIX 9 9 THR A 206 SER A 218 1 13
HELIX 10 10 SER A 230 ALA A 234 5 5
HELIX 11 11 LEU A 253 ALA A 267 1 15
HELIX 12 12 SER A 283 PHE A 287 5 5
HELIX 13 13 SER A 290 ILE A 304 1 15
HELIX 14 14 PRO A 305 LEU A 308 5 4
HELIX 15 15 ASP B 8 ASP B 10 5 3
HELIX 16 16 PHE B 11 ALA B 21 1 11
HELIX 17 17 GLU B 28 ARG B 44 1 17
HELIX 18 18 TYR B 95 GLY B 107 1 13
HELIX 19 19 PRO B 124 LYS B 140 1 17
HELIX 20 20 LYS B 141 GLY B 145 5 5
HELIX 21 21 SER B 156 LYS B 173 1 18
HELIX 22 22 SER B 193 TYR B 199 1 7
HELIX 23 23 THR B 206 SER B 218 1 13
HELIX 24 24 SER B 230 ALA B 234 5 5
HELIX 25 25 LEU B 253 ALA B 267 1 15
HELIX 26 26 GLY B 282 PHE B 287 5 6
HELIX 27 27 SER B 290 ILE B 304 1 15
HELIX 28 28 PRO B 305 LEU B 308 5 4
HELIX 29 29 ASP C 8 ASP C 10 5 3
HELIX 30 30 PHE C 11 ALA C 21 1 11
HELIX 31 31 ASP C 23 ILE C 27 5 5
HELIX 32 32 GLU C 28 ARG C 44 1 17
HELIX 33 33 ASN C 91 GLY C 107 1 17
HELIX 34 34 PRO C 124 LYS C 140 1 17
HELIX 35 35 LYS C 141 GLY C 145 5 5
HELIX 36 36 SER C 156 LYS C 173 1 18
HELIX 37 37 SER C 193 SER C 200 1 8
HELIX 38 38 THR C 206 SER C 218 1 13
HELIX 39 39 SER C 230 ALA C 234 5 5
HELIX 40 40 LEU C 253 ALA C 267 1 15
HELIX 41 41 SER C 283 PHE C 287 5 5
HELIX 42 42 SER C 290 ILE C 304 1 15
HELIX 43 43 PRO C 305 LEU C 308 5 4
HELIX 44 44 ASP D 8 ASP D 10 5 3
HELIX 45 45 PHE D 11 ALA D 21 1 11
HELIX 46 46 GLU D 28 SER D 42 1 15
HELIX 47 47 TYR D 95 GLY D 107 1 13
HELIX 48 48 PRO D 124 LYS D 140 1 17
HELIX 49 49 LYS D 141 GLY D 145 5 5
HELIX 50 50 SER D 156 GLY D 172 1 17
HELIX 51 51 SER D 193 TYR D 199 1 7
HELIX 52 52 THR D 206 SER D 218 1 13
HELIX 53 53 SER D 230 ALA D 234 5 5
HELIX 54 54 LEU D 253 ALA D 267 1 15
HELIX 55 55 SER D 290 ILE D 304 1 15
HELIX 56 56 PRO D 305 LEU D 308 5 4
SHEET 1 A16 GLU A 52 LEU A 60 0
SHEET 2 A16 ARG A 63 ASP A 71 -1 O MET A 69 N LYS A 54
SHEET 3 A16 LYS A 109 ILE A 113 -1 O ILE A 110 N TYR A 70
SHEET 4 A16 ALA A 78 TYR A 82 1 N ILE A 79 O ILE A 111
SHEET 5 A16 ILE A 150 ASP A 155 1 O GLY A 151 N LEU A 80
SHEET 6 A16 GLN A 180 PHE A 183 1 O PHE A 183 N GLY A 154
SHEET 7 A16 ALA A 243 TYR A 250 1 O ILE A 244 N LEU A 182
SHEET 8 A16 ALA A 271 ILE A 280 1 O GLY A 276 N THR A 247
SHEET 9 A16 ALA D 271 ILE D 280 -1 O GLY D 273 N ILE A 277
SHEET 10 A16 ALA D 243 TYR D 250 1 N TYR D 250 O MET D 279
SHEET 11 A16 GLN D 180 PHE D 183 1 N LEU D 182 O ILE D 244
SHEET 12 A16 ILE D 150 ASP D 155 1 N GLY D 154 O PHE D 183
SHEET 13 A16 ALA D 78 TYR D 82 1 N TYR D 82 O ALA D 153
SHEET 14 A16 LYS D 109 ILE D 113 1 O ILE D 111 N ILE D 79
SHEET 15 A16 ARG D 63 ASP D 71 -1 N ARG D 68 O SER D 112
SHEET 16 A16 GLU D 52 LEU D 60 -1 N LYS D 54 O MET D 69
SHEET 1 B16 GLU B 52 LEU B 60 0
SHEET 2 B16 ARG B 63 ASP B 71 -1 O MET B 69 N LYS B 54
SHEET 3 B16 LYS B 109 ILE B 113 -1 O SER B 112 N ARG B 68
SHEET 4 B16 ALA B 78 TYR B 82 1 N TYR B 81 O ILE B 111
SHEET 5 B16 ILE B 150 ASP B 155 1 O GLY B 151 N LEU B 80
SHEET 6 B16 GLN B 180 PHE B 183 1 O PHE B 183 N GLY B 154
SHEET 7 B16 ALA B 243 TYR B 250 1 O ILE B 244 N LEU B 182
SHEET 8 B16 ALA B 271 ILE B 280 1 O GLY B 276 N THR B 247
SHEET 9 B16 ALA C 271 ILE C 280 -1 O GLY C 273 N ILE B 277
SHEET 10 B16 ALA C 243 TYR C 250 1 N THR C 247 O GLY C 276
SHEET 11 B16 GLN C 180 PHE C 183 1 N LEU C 182 O ILE C 244
SHEET 12 B16 ILE C 150 ASP C 155 1 N GLY C 154 O PHE C 183
SHEET 13 B16 ALA C 78 TYR C 82 1 N LEU C 80 O GLY C 151
SHEET 14 B16 LYS C 109 ILE C 113 1 O ILE C 111 N TYR C 81
SHEET 15 B16 ARG C 63 ASP C 71 -1 N ARG C 68 O SER C 112
SHEET 16 B16 GLU C 52 LEU C 60 -1 N ILE C 58 O LEU C 65
CISPEP 1 ALA A 118 PRO A 119 0 -5.62
CISPEP 2 PHE A 123 PRO A 124 0 9.19
CISPEP 3 ALA B 118 PRO B 119 0 5.81
CISPEP 4 PHE B 123 PRO B 124 0 15.46
CISPEP 5 ALA C 118 PRO C 119 0 3.29
CISPEP 6 PHE C 123 PRO C 124 0 9.10
CISPEP 7 LYS C 219 ASN C 220 0 -18.17
CISPEP 8 ALA D 118 PRO D 119 0 3.01
CISPEP 9 PHE D 123 PRO D 124 0 2.69
CRYST1 62.804 137.360 76.878 90.00 91.47 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015923 0.000000 0.000408 0.00000
SCALE2 0.000000 0.007280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013012 0.00000
TER 2356 LEU A 308
TER 4720 LEU B 308
TER 7084 LEU C 308
TER 9448 LEU D 308
MASTER 502 0 0 56 32 0 0 610427 4 0 96
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