| content |
HEADER HYDROLASE 24-JAN-18 6FKX
TITLE CRYSTAL STRUCTURE OF AN ACETYL XYLAN ESTERASE FROM A DESERT METAGENOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.72;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 8 CHAIN: B, D, E, F;
COMPND 9 EC: 3.1.1.72;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: 1X HIS-TAG AT N-TERMINI;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 14 CHAIN: C;
COMPND 15 EC: 3.1.1.72;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 11 ORGANISM_TAXID: 256318;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 19 ORGANISM_TAXID: 256318;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CARBOHYDRATE-ACTIVE ENZYME, ACETYL XYLAN ESTERASE, ALPHA-BETA
KEYWDS 2 HYDROLASE, 7-ACA DEACETYLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.A.ADESIOYE,T.P.MAKHALANYANE,S.VIKRAM,B.T.SEWELL,W.SCHUBERT,
AUTHOR 2 D.A.COWAN
REVDAT 1 28-FEB-18 6FKX 0
JRNL AUTH F.A.ADESIOYE,T.P.MAKHALANYANE,S.VIKRAM,B.T.SEWELL,
JRNL AUTH 2 W.D.SCHUBERT,D.A.COWAN
JRNL TITL STRUCTURAL CHARACTERIZATION AND DIRECTED EVOLUTION OF A
JRNL TITL 2 NOVEL ACETYL XYLAN ESTERASE REVEALS THERMOSTABILITY
JRNL TITL 3 DETERMINANTS OF THE CARBOHYDRATE ESTERASE 7 FAMILY.
JRNL REF APPL. ENVIRON. MICROBIOL. 2018
JRNL REFN ESSN 1098-5336
JRNL PMID 29453256
JRNL DOI 10.1128/AEM.02695-17
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 130719
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6FKX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200006957.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 130734
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.026
REMARK 200 RESOLUTION RANGE LOW (A) : 89.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.06564
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34790
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: PHENIX
REMARK 200 STARTING MODEL: 3FCY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M 2-(N-MORPHOLINO) ETHANESULFONIC
REMARK 280 ACID (MES) BUFFERS PH 8.5 AND 25% PEG 8000 (W/V), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 53.84000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.71000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.41000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.71000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.84000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.41000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C, E, 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 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 HIS A -2 N CA CB CG ND1 CD2 CE1
REMARK 470 HIS A -2 NE2
REMARK 470 LEU C 3 CB CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP A 99 NH2 ARG A 103 2.12
REMARK 500 O GLU B 10 O HOH B 501 2.14
REMARK 500 O HOH B 761 O HOH B 850 2.15
REMARK 500 OE1 GLU C 11 O HOH C 501 2.16
REMARK 500 O HOH C 523 O HOH C 751 2.17
REMARK 500 O HOH C 557 O HOH C 747 2.17
REMARK 500 O HOH C 507 O HOH C 508 2.17
REMARK 500 OD2 ASP B 24 O HOH B 502 2.18
REMARK 500 O HOH E 589 O HOH E 608 2.18
REMARK 500 O HOH F 702 O HOH F 795 2.19
REMARK 500 OD1 ASP B 221 O HOH B 503 2.19
REMARK 500 OD2 ASP A 173 O HOH A 501 2.19
REMARK 500 O HOH F 777 O HOH F 828 2.19
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 LYS C 224 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 VAL F 81 CA - CB - CG2 ANGL. DEV. = 9.8 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 HIS A -1 -142.08 23.28
REMARK 500 ASP A 6 -151.28 -111.61
REMARK 500 ARG A 18 27.65 -142.05
REMARK 500 ALA A 79 72.72 48.54
REMARK 500 THR A 94 -1.36 73.06
REMARK 500 GLN A 121 -156.71 -90.54
REMARK 500 SER A 185 -117.03 60.86
REMARK 500 TYR A 208 73.74 18.41
REMARK 500 LEU A 211 33.87 73.67
REMARK 500 ASP A 221 74.57 52.72
REMARK 500 ASP A 238 63.77 -157.84
REMARK 500 ALA A 303 -142.61 -109.92
REMARK 500 ASP B 6 -145.95 -111.81
REMARK 500 VAL B 81 -63.84 -107.47
REMARK 500 GLN B 121 -156.59 -90.89
REMARK 500 SER B 185 -115.44 60.75
REMARK 500 TYR B 208 75.95 19.66
REMARK 500 LEU B 211 33.75 74.05
REMARK 500 ASP B 221 73.40 51.80
REMARK 500 ASP B 221 76.37 48.17
REMARK 500 ASP B 238 62.58 -155.40
REMARK 500 ALA B 303 -140.92 -111.10
REMARK 500 ASP D 6 -143.66 -112.69
REMARK 500 VAL D 81 -112.73 -110.92
REMARK 500 THR D 94 -0.58 71.97
REMARK 500 GLN D 121 -156.81 -91.81
REMARK 500 SER D 185 -116.90 61.61
REMARK 500 TYR D 208 75.47 18.21
REMARK 500 LEU D 211 34.17 72.19
REMARK 500 ASP D 221 84.16 57.25
REMARK 500 ASP D 238 63.33 -157.82
REMARK 500 ALA D 303 -142.95 -109.88
REMARK 500 THR C 4 91.07 -169.63
REMARK 500 ASP C 6 -146.22 -118.32
REMARK 500 VAL C 81 -69.65 -104.16
REMARK 500 THR C 94 -0.54 72.21
REMARK 500 GLN C 121 -157.41 -90.51
REMARK 500 SER C 185 -116.62 61.23
REMARK 500 TYR C 208 75.20 18.27
REMARK 500 LEU C 211 34.52 72.87
REMARK 500 LYS C 224 127.00 -176.16
REMARK 500 ASP C 238 65.28 -157.59
REMARK 500 ALA C 303 -142.82 -109.30
REMARK 500 VAL E 1 75.21 53.59
REMARK 500 ASP E 6 -145.40 -111.94
REMARK 500 ALA E 79 73.24 55.60
REMARK 500 GLN E 121 -156.90 -91.21
REMARK 500 SER E 185 -116.12 60.69
REMARK 500 TYR E 208 77.04 18.58
REMARK 500 LEU E 211 33.73 73.07
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
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 GLU C 223 LYS C 224 -138.03
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 846 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 847 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A 848 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 849 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A 850 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH B 862 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B 863 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B 864 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH B 865 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH B 866 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH D 872 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH D 873 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH D 874 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH D 875 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH D 876 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH D 877 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH D 878 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH D 879 DISTANCE = 7.86 ANGSTROMS
REMARK 525 HOH C 874 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH C 875 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH C 876 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH C 877 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH E 866 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH E 867 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH F 912 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH F 913 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH F 914 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH F 915 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH F 916 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH F 917 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH F 918 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH F 919 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH F 920 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH F 921 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH F 922 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH F 923 DISTANCE = 8.12 ANGSTROMS
REMARK 525 HOH F 924 DISTANCE = 8.13 ANGSTROMS
REMARK 525 HOH F 925 DISTANCE = 8.20 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MES A 402
REMARK 610 MES B 402
REMARK 610 MES B 403
REMARK 610 MES D 402
REMARK 610 MES D 404
REMARK 610 MES C 402
REMARK 610 MES C 403
REMARK 610 MES C 404
REMARK 610 MES E 402
REMARK 610 MES E 403
REMARK 610 MES F 402
REMARK 610 MES F 403
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 169 O
REMARK 620 2 MET A 171 O 100.6
REMARK 620 3 VAL A 174 O 103.0 84.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 169 O
REMARK 620 2 MET B 171 O 107.3
REMARK 620 3 VAL B 174 O 111.7 99.1
REMARK 620 4 HOH B 512 O 166.9 77.0 79.1
REMARK 620 5 HOH B 720 O 81.9 123.1 130.2 85.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU D 169 O
REMARK 620 2 MET D 171 O 107.2
REMARK 620 3 VAL D 174 O 109.0 86.1
REMARK 620 4 HOH D 531 O 174.8 77.6 73.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU C 169 O
REMARK 620 2 MET C 171 O 112.8
REMARK 620 3 VAL C 174 O 115.1 97.3
REMARK 620 4 HOH C 691 O 156.7 83.6 77.0
REMARK 620 5 HOH F 719 O 80.8 116.4 134.2 76.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU E 169 O
REMARK 620 2 MET E 171 O 98.5
REMARK 620 3 VAL E 174 O 96.9 81.1
REMARK 620 4 HOH E 654 O 164.8 84.9 68.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA F 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU F 169 O
REMARK 620 2 MET F 171 O 103.6
REMARK 620 3 VAL F 174 O 110.6 95.8
REMARK 620 4 HOH F 707 O 77.4 129.9 131.5
REMARK 620 5 HOH F 722 O 162.3 92.1 75.4 86.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES F 403
DBREF 6FKX A -2 321 PDB 6FKX 6FKX -2 321
DBREF 6FKX B 0 321 PDB 6FKX 6FKX 0 321
DBREF 6FKX D 0 321 PDB 6FKX 6FKX 0 321
DBREF 6FKX C 3 321 PDB 6FKX 6FKX 3 321
DBREF 6FKX E 0 321 PDB 6FKX 6FKX 0 321
DBREF 6FKX F 0 321 PDB 6FKX 6FKX 0 321
SEQRES 1 A 324 HIS HIS HIS VAL PRO LEU THR PHE ASP LEU PRO PHE GLU
SEQRES 2 A 324 GLU LEU LEU THR TYR PRO GLY ARG THR PRO ARG PRO ALA
SEQRES 3 A 324 ASP HIS ASP GLU TYR TRP ASP ARG GLY LEU ALA ASP LEU
SEQRES 4 A 324 ALA ALA VAL PRO ALA ASP VAL VAL ILE GLU PRO ALA GLU
SEQRES 5 A 324 PHE THR THR PRO LEU ALA ARG CYS SER HIS LEU TRP PHE
SEQRES 6 A 324 THR GLY THR GLY GLY VAL ARG VAL HIS ALA LYS LEU LEU
SEQRES 7 A 324 ARG PRO VAL ALA PRO VAL GLU PRO HIS PRO ALA LEU LEU
SEQRES 8 A 324 GLN PHE HIS GLY TYR THR GLY ASN SER GLY ASP TRP SER
SEQRES 9 A 324 SER ARG LEU HIS TYR VAL ALA LEU GLY TYR THR VAL ALA
SEQRES 10 A 324 ALA LEU ASP CYS ARG GLY GLN ALA GLY LEU SER VAL GLY
SEQRES 11 A 324 GLU ALA PRO VAL GLU ASN TRP SER MET ALA SER TYR LEU
SEQRES 12 A 324 LEU ARG GLY ILE ASP ASP ASP ALA ALA ASP ASN LEU ALA
SEQRES 13 A 324 LEU ARG HIS LEU PHE LEU ASP THR ALA ARG LEU ALA GLN
SEQRES 14 A 324 ILE VAL LEU ALA MET ASP ASP VAL ASP PRO ASP ARG VAL
SEQRES 15 A 324 ALA ALA THR GLY TYR SER GLN GLY GLY GLY LEU THR LEU
SEQRES 16 A 324 ALA CYS ALA ALA LEU GLU PRO ARG ILE ARG LEU ALA ALA
SEQRES 17 A 324 PRO VAL TYR PRO PHE LEU CYS ASP PHE ARG ARG ALA TRP
SEQRES 18 A 324 GLU MET ASP LEU GLU LYS GLY PRO TYR ASN GLU ILE THR
SEQRES 19 A 324 THR TYR PHE ARG ALA ARG ASP PRO ARG HIS LEU ARG GLU
SEQRES 20 A 324 GLU GLU ILE PHE SER ARG LEU GLY TYR VAL ASP VAL GLN
SEQRES 21 A 324 HIS LEU ALA PRO ARG VAL ARG ALA GLU VAL LEU MET THR
SEQRES 22 A 324 VAL SER LEU ALA ASP LYS ILE CYS PRO PRO SER THR GLN
SEQRES 23 A 324 PHE ALA ALA TYR ASN LYS LEU GLY GLY PRO LYS ASP TYR
SEQRES 24 A 324 ARG LEU TYR PRO ASP PHE ALA HIS GLU THR LEU PRO GLY
SEQRES 25 A 324 THR ASP ASP ALA ILE PHE THR PHE LEU GLN GLY LEU
SEQRES 1 B 322 HIS VAL PRO LEU THR PHE ASP LEU PRO PHE GLU GLU LEU
SEQRES 2 B 322 LEU THR TYR PRO GLY ARG THR PRO ARG PRO ALA ASP HIS
SEQRES 3 B 322 ASP GLU TYR TRP ASP ARG GLY LEU ALA ASP LEU ALA ALA
SEQRES 4 B 322 VAL PRO ALA ASP VAL VAL ILE GLU PRO ALA GLU PHE THR
SEQRES 5 B 322 THR PRO LEU ALA ARG CYS SER HIS LEU TRP PHE THR GLY
SEQRES 6 B 322 THR GLY GLY VAL ARG VAL HIS ALA LYS LEU LEU ARG PRO
SEQRES 7 B 322 VAL ALA PRO VAL GLU PRO HIS PRO ALA LEU LEU GLN PHE
SEQRES 8 B 322 HIS GLY TYR THR GLY ASN SER GLY ASP TRP SER SER ARG
SEQRES 9 B 322 LEU HIS TYR VAL ALA LEU GLY TYR THR VAL ALA ALA LEU
SEQRES 10 B 322 ASP CYS ARG GLY GLN ALA GLY LEU SER VAL GLY GLU ALA
SEQRES 11 B 322 PRO VAL GLU ASN TRP SER MET ALA SER TYR LEU LEU ARG
SEQRES 12 B 322 GLY ILE ASP ASP ASP ALA ALA ASP ASN LEU ALA LEU ARG
SEQRES 13 B 322 HIS LEU PHE LEU ASP THR ALA ARG LEU ALA GLN ILE VAL
SEQRES 14 B 322 LEU ALA MET ASP ASP VAL ASP PRO ASP ARG VAL ALA ALA
SEQRES 15 B 322 THR GLY TYR SER GLN GLY GLY GLY LEU THR LEU ALA CYS
SEQRES 16 B 322 ALA ALA LEU GLU PRO ARG ILE ARG LEU ALA ALA PRO VAL
SEQRES 17 B 322 TYR PRO PHE LEU CYS ASP PHE ARG ARG ALA TRP GLU MET
SEQRES 18 B 322 ASP LEU GLU LYS GLY PRO TYR ASN GLU ILE THR THR TYR
SEQRES 19 B 322 PHE ARG ALA ARG ASP PRO ARG HIS LEU ARG GLU GLU GLU
SEQRES 20 B 322 ILE PHE SER ARG LEU GLY TYR VAL ASP VAL GLN HIS LEU
SEQRES 21 B 322 ALA PRO ARG VAL ARG ALA GLU VAL LEU MET THR VAL SER
SEQRES 22 B 322 LEU ALA ASP LYS ILE CYS PRO PRO SER THR GLN PHE ALA
SEQRES 23 B 322 ALA TYR ASN LYS LEU GLY GLY PRO LYS ASP TYR ARG LEU
SEQRES 24 B 322 TYR PRO ASP PHE ALA HIS GLU THR LEU PRO GLY THR ASP
SEQRES 25 B 322 ASP ALA ILE PHE THR PHE LEU GLN GLY LEU
SEQRES 1 D 322 HIS VAL PRO LEU THR PHE ASP LEU PRO PHE GLU GLU LEU
SEQRES 2 D 322 LEU THR TYR PRO GLY ARG THR PRO ARG PRO ALA ASP HIS
SEQRES 3 D 322 ASP GLU TYR TRP ASP ARG GLY LEU ALA ASP LEU ALA ALA
SEQRES 4 D 322 VAL PRO ALA ASP VAL VAL ILE GLU PRO ALA GLU PHE THR
SEQRES 5 D 322 THR PRO LEU ALA ARG CYS SER HIS LEU TRP PHE THR GLY
SEQRES 6 D 322 THR GLY GLY VAL ARG VAL HIS ALA LYS LEU LEU ARG PRO
SEQRES 7 D 322 VAL ALA PRO VAL GLU PRO HIS PRO ALA LEU LEU GLN PHE
SEQRES 8 D 322 HIS GLY TYR THR GLY ASN SER GLY ASP TRP SER SER ARG
SEQRES 9 D 322 LEU HIS TYR VAL ALA LEU GLY TYR THR VAL ALA ALA LEU
SEQRES 10 D 322 ASP CYS ARG GLY GLN ALA GLY LEU SER VAL GLY GLU ALA
SEQRES 11 D 322 PRO VAL GLU ASN TRP SER MET ALA SER TYR LEU LEU ARG
SEQRES 12 D 322 GLY ILE ASP ASP ASP ALA ALA ASP ASN LEU ALA LEU ARG
SEQRES 13 D 322 HIS LEU PHE LEU ASP THR ALA ARG LEU ALA GLN ILE VAL
SEQRES 14 D 322 LEU ALA MET ASP ASP VAL ASP PRO ASP ARG VAL ALA ALA
SEQRES 15 D 322 THR GLY TYR SER GLN GLY GLY GLY LEU THR LEU ALA CYS
SEQRES 16 D 322 ALA ALA LEU GLU PRO ARG ILE ARG LEU ALA ALA PRO VAL
SEQRES 17 D 322 TYR PRO PHE LEU CYS ASP PHE ARG ARG ALA TRP GLU MET
SEQRES 18 D 322 ASP LEU GLU LYS GLY PRO TYR ASN GLU ILE THR THR TYR
SEQRES 19 D 322 PHE ARG ALA ARG ASP PRO ARG HIS LEU ARG GLU GLU GLU
SEQRES 20 D 322 ILE PHE SER ARG LEU GLY TYR VAL ASP VAL GLN HIS LEU
SEQRES 21 D 322 ALA PRO ARG VAL ARG ALA GLU VAL LEU MET THR VAL SER
SEQRES 22 D 322 LEU ALA ASP LYS ILE CYS PRO PRO SER THR GLN PHE ALA
SEQRES 23 D 322 ALA TYR ASN LYS LEU GLY GLY PRO LYS ASP TYR ARG LEU
SEQRES 24 D 322 TYR PRO ASP PHE ALA HIS GLU THR LEU PRO GLY THR ASP
SEQRES 25 D 322 ASP ALA ILE PHE THR PHE LEU GLN GLY LEU
SEQRES 1 C 319 LEU THR PHE ASP LEU PRO PHE GLU GLU LEU LEU THR TYR
SEQRES 2 C 319 PRO GLY ARG THR PRO ARG PRO ALA ASP HIS ASP GLU TYR
SEQRES 3 C 319 TRP ASP ARG GLY LEU ALA ASP LEU ALA ALA VAL PRO ALA
SEQRES 4 C 319 ASP VAL VAL ILE GLU PRO ALA GLU PHE THR THR PRO LEU
SEQRES 5 C 319 ALA ARG CYS SER HIS LEU TRP PHE THR GLY THR GLY GLY
SEQRES 6 C 319 VAL ARG VAL HIS ALA LYS LEU LEU ARG PRO VAL ALA PRO
SEQRES 7 C 319 VAL GLU PRO HIS PRO ALA LEU LEU GLN PHE HIS GLY TYR
SEQRES 8 C 319 THR GLY ASN SER GLY ASP TRP SER SER ARG LEU HIS TYR
SEQRES 9 C 319 VAL ALA LEU GLY TYR THR VAL ALA ALA LEU ASP CYS ARG
SEQRES 10 C 319 GLY GLN ALA GLY LEU SER VAL GLY GLU ALA PRO VAL GLU
SEQRES 11 C 319 ASN TRP SER MET ALA SER TYR LEU LEU ARG GLY ILE ASP
SEQRES 12 C 319 ASP ASP ALA ALA ASP ASN LEU ALA LEU ARG HIS LEU PHE
SEQRES 13 C 319 LEU ASP THR ALA ARG LEU ALA GLN ILE VAL LEU ALA MET
SEQRES 14 C 319 ASP ASP VAL ASP PRO ASP ARG VAL ALA ALA THR GLY TYR
SEQRES 15 C 319 SER GLN GLY GLY GLY LEU THR LEU ALA CYS ALA ALA LEU
SEQRES 16 C 319 GLU PRO ARG ILE ARG LEU ALA ALA PRO VAL TYR PRO PHE
SEQRES 17 C 319 LEU CYS ASP PHE ARG ARG ALA TRP GLU MET ASP LEU GLU
SEQRES 18 C 319 LYS GLY PRO TYR ASN GLU ILE THR THR TYR PHE ARG ALA
SEQRES 19 C 319 ARG ASP PRO ARG HIS LEU ARG GLU GLU GLU ILE PHE SER
SEQRES 20 C 319 ARG LEU GLY TYR VAL ASP VAL GLN HIS LEU ALA PRO ARG
SEQRES 21 C 319 VAL ARG ALA GLU VAL LEU MET THR VAL SER LEU ALA ASP
SEQRES 22 C 319 LYS ILE CYS PRO PRO SER THR GLN PHE ALA ALA TYR ASN
SEQRES 23 C 319 LYS LEU GLY GLY PRO LYS ASP TYR ARG LEU TYR PRO ASP
SEQRES 24 C 319 PHE ALA HIS GLU THR LEU PRO GLY THR ASP ASP ALA ILE
SEQRES 25 C 319 PHE THR PHE LEU GLN GLY LEU
SEQRES 1 E 322 HIS VAL PRO LEU THR PHE ASP LEU PRO PHE GLU GLU LEU
SEQRES 2 E 322 LEU THR TYR PRO GLY ARG THR PRO ARG PRO ALA ASP HIS
SEQRES 3 E 322 ASP GLU TYR TRP ASP ARG GLY LEU ALA ASP LEU ALA ALA
SEQRES 4 E 322 VAL PRO ALA ASP VAL VAL ILE GLU PRO ALA GLU PHE THR
SEQRES 5 E 322 THR PRO LEU ALA ARG CYS SER HIS LEU TRP PHE THR GLY
SEQRES 6 E 322 THR GLY GLY VAL ARG VAL HIS ALA LYS LEU LEU ARG PRO
SEQRES 7 E 322 VAL ALA PRO VAL GLU PRO HIS PRO ALA LEU LEU GLN PHE
SEQRES 8 E 322 HIS GLY TYR THR GLY ASN SER GLY ASP TRP SER SER ARG
SEQRES 9 E 322 LEU HIS TYR VAL ALA LEU GLY TYR THR VAL ALA ALA LEU
SEQRES 10 E 322 ASP CYS ARG GLY GLN ALA GLY LEU SER VAL GLY GLU ALA
SEQRES 11 E 322 PRO VAL GLU ASN TRP SER MET ALA SER TYR LEU LEU ARG
SEQRES 12 E 322 GLY ILE ASP ASP ASP ALA ALA ASP ASN LEU ALA LEU ARG
SEQRES 13 E 322 HIS LEU PHE LEU ASP THR ALA ARG LEU ALA GLN ILE VAL
SEQRES 14 E 322 LEU ALA MET ASP ASP VAL ASP PRO ASP ARG VAL ALA ALA
SEQRES 15 E 322 THR GLY TYR SER GLN GLY GLY GLY LEU THR LEU ALA CYS
SEQRES 16 E 322 ALA ALA LEU GLU PRO ARG ILE ARG LEU ALA ALA PRO VAL
SEQRES 17 E 322 TYR PRO PHE LEU CYS ASP PHE ARG ARG ALA TRP GLU MET
SEQRES 18 E 322 ASP LEU GLU LYS GLY PRO TYR ASN GLU ILE THR THR TYR
SEQRES 19 E 322 PHE ARG ALA ARG ASP PRO ARG HIS LEU ARG GLU GLU GLU
SEQRES 20 E 322 ILE PHE SER ARG LEU GLY TYR VAL ASP VAL GLN HIS LEU
SEQRES 21 E 322 ALA PRO ARG VAL ARG ALA GLU VAL LEU MET THR VAL SER
SEQRES 22 E 322 LEU ALA ASP LYS ILE CYS PRO PRO SER THR GLN PHE ALA
SEQRES 23 E 322 ALA TYR ASN LYS LEU GLY GLY PRO LYS ASP TYR ARG LEU
SEQRES 24 E 322 TYR PRO ASP PHE ALA HIS GLU THR LEU PRO GLY THR ASP
SEQRES 25 E 322 ASP ALA ILE PHE THR PHE LEU GLN GLY LEU
SEQRES 1 F 322 HIS VAL PRO LEU THR PHE ASP LEU PRO PHE GLU GLU LEU
SEQRES 2 F 322 LEU THR TYR PRO GLY ARG THR PRO ARG PRO ALA ASP HIS
SEQRES 3 F 322 ASP GLU TYR TRP ASP ARG GLY LEU ALA ASP LEU ALA ALA
SEQRES 4 F 322 VAL PRO ALA ASP VAL VAL ILE GLU PRO ALA GLU PHE THR
SEQRES 5 F 322 THR PRO LEU ALA ARG CYS SER HIS LEU TRP PHE THR GLY
SEQRES 6 F 322 THR GLY GLY VAL ARG VAL HIS ALA LYS LEU LEU ARG PRO
SEQRES 7 F 322 VAL ALA PRO VAL GLU PRO HIS PRO ALA LEU LEU GLN PHE
SEQRES 8 F 322 HIS GLY TYR THR GLY ASN SER GLY ASP TRP SER SER ARG
SEQRES 9 F 322 LEU HIS TYR VAL ALA LEU GLY TYR THR VAL ALA ALA LEU
SEQRES 10 F 322 ASP CYS ARG GLY GLN ALA GLY LEU SER VAL GLY GLU ALA
SEQRES 11 F 322 PRO VAL GLU ASN TRP SER MET ALA SER TYR LEU LEU ARG
SEQRES 12 F 322 GLY ILE ASP ASP ASP ALA ALA ASP ASN LEU ALA LEU ARG
SEQRES 13 F 322 HIS LEU PHE LEU ASP THR ALA ARG LEU ALA GLN ILE VAL
SEQRES 14 F 322 LEU ALA MET ASP ASP VAL ASP PRO ASP ARG VAL ALA ALA
SEQRES 15 F 322 THR GLY TYR SER GLN GLY GLY GLY LEU THR LEU ALA CYS
SEQRES 16 F 322 ALA ALA LEU GLU PRO ARG ILE ARG LEU ALA ALA PRO VAL
SEQRES 17 F 322 TYR PRO PHE LEU CYS ASP PHE ARG ARG ALA TRP GLU MET
SEQRES 18 F 322 ASP LEU GLU LYS GLY PRO TYR ASN GLU ILE THR THR TYR
SEQRES 19 F 322 PHE ARG ALA ARG ASP PRO ARG HIS LEU ARG GLU GLU GLU
SEQRES 20 F 322 ILE PHE SER ARG LEU GLY TYR VAL ASP VAL GLN HIS LEU
SEQRES 21 F 322 ALA PRO ARG VAL ARG ALA GLU VAL LEU MET THR VAL SER
SEQRES 22 F 322 LEU ALA ASP LYS ILE CYS PRO PRO SER THR GLN PHE ALA
SEQRES 23 F 322 ALA TYR ASN LYS LEU GLY GLY PRO LYS ASP TYR ARG LEU
SEQRES 24 F 322 TYR PRO ASP PHE ALA HIS GLU THR LEU PRO GLY THR ASP
SEQRES 25 F 322 ASP ALA ILE PHE THR PHE LEU GLN GLY LEU
HET NA A 401 1
HET MES A 402 8
HET SO4 A 403 5
HET NA B 401 1
HET MES B 402 7
HET MES B 403 5
HET FMT B 404 3
HET NA D 401 1
HET MES D 402 8
HET MES D 403 12
HET MES D 404 11
HET NA C 401 1
HET MES C 402 6
HET MES C 403 7
HET MES C 404 6
HET NA E 401 1
HET MES E 402 7
HET MES E 403 6
HET NA F 401 1
HET MES F 402 7
HET MES F 403 8
HETNAM NA SODIUM ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM SO4 SULFATE ION
HETNAM FMT FORMIC ACID
FORMUL 7 NA 6(NA 1+)
FORMUL 8 MES 13(C6 H13 N O4 S)
FORMUL 9 SO4 O4 S 2-
FORMUL 13 FMT C H2 O2
FORMUL 28 HOH *2264(H2 O)
HELIX 1 AA1 PRO A 8 LEU A 13 1 6
HELIX 2 AA2 ASP A 24 ALA A 38 1 15
HELIX 3 AA3 ASP A 99 SER A 102 5 4
HELIX 4 AA4 ARG A 103 LEU A 109 1 7
HELIX 5 AA5 ALA A 148 ASN A 151 5 4
HELIX 6 AA6 LEU A 152 ALA A 170 1 19
HELIX 7 AA7 SER A 185 GLU A 198 1 14
HELIX 8 AA8 ASP A 213 MET A 220 1 8
HELIX 9 AA9 TYR A 227 ASP A 238 1 12
HELIX 10 AB1 ARG A 243 GLY A 252 1 10
HELIX 11 AB2 ASP A 255 ALA A 260 1 6
HELIX 12 AB3 PRO A 261 VAL A 263 5 3
HELIX 13 AB4 PRO A 279 ASN A 288 1 10
HELIX 14 AB5 GLY A 309 GLY A 320 1 12
HELIX 15 AB6 PRO B 8 LEU B 13 1 6
HELIX 16 AB7 ASP B 24 ALA B 38 1 15
HELIX 17 AB8 THR B 65 GLY B 67 5 3
HELIX 18 AB9 ASP B 99 SER B 102 5 4
HELIX 19 AC1 ARG B 103 LEU B 109 1 7
HELIX 20 AC2 ALA B 148 ASN B 151 5 4
HELIX 21 AC3 LEU B 152 MET B 171 1 20
HELIX 22 AC4 SER B 185 GLU B 198 1 14
HELIX 23 AC5 ASP B 213 ASP B 221 1 9
HELIX 24 AC6 TYR B 227 ASP B 238 1 12
HELIX 25 AC7 ARG B 243 GLY B 252 1 10
HELIX 26 AC8 ASP B 255 ALA B 260 1 6
HELIX 27 AC9 PRO B 261 VAL B 263 5 3
HELIX 28 AD1 PRO B 279 ASN B 288 1 10
HELIX 29 AD2 GLY B 309 GLN B 319 1 11
HELIX 30 AD3 PRO D 8 LEU D 13 1 6
HELIX 31 AD4 ASP D 24 ALA D 38 1 15
HELIX 32 AD5 ASP D 99 SER D 102 5 4
HELIX 33 AD6 ARG D 103 LEU D 109 1 7
HELIX 34 AD7 ALA D 148 ASN D 151 5 4
HELIX 35 AD8 LEU D 152 MET D 171 1 20
HELIX 36 AD9 SER D 185 GLU D 198 1 14
HELIX 37 AE1 ASP D 213 MET D 220 1 8
HELIX 38 AE2 TYR D 227 ASP D 238 1 12
HELIX 39 AE3 ARG D 243 VAL D 254 1 12
HELIX 40 AE4 ASP D 255 ALA D 260 1 6
HELIX 41 AE5 PRO D 261 VAL D 263 5 3
HELIX 42 AE6 PRO D 279 ASN D 288 1 10
HELIX 43 AE7 GLY D 309 GLN D 319 1 11
HELIX 44 AE8 PRO C 8 LEU C 13 1 6
HELIX 45 AE9 ASP C 24 ALA C 38 1 15
HELIX 46 AF1 THR C 65 GLY C 67 5 3
HELIX 47 AF2 ASP C 99 SER C 102 5 4
HELIX 48 AF3 ARG C 103 LEU C 109 1 7
HELIX 49 AF4 ALA C 148 ASN C 151 5 4
HELIX 50 AF5 LEU C 152 MET C 171 1 20
HELIX 51 AF6 SER C 185 GLU C 198 1 14
HELIX 52 AF7 ASP C 213 MET C 220 1 8
HELIX 53 AF8 TYR C 227 ASP C 238 1 12
HELIX 54 AF9 ARG C 243 GLY C 252 1 10
HELIX 55 AG1 ASP C 255 ALA C 260 1 6
HELIX 56 AG2 PRO C 261 VAL C 263 5 3
HELIX 57 AG3 PRO C 279 ASN C 288 1 10
HELIX 58 AG4 GLY C 309 GLY C 320 1 12
HELIX 59 AG5 PRO E 8 LEU E 13 1 6
HELIX 60 AG6 ASP E 24 ALA E 38 1 15
HELIX 61 AG7 ASP E 99 SER E 102 5 4
HELIX 62 AG8 ARG E 103 LEU E 109 1 7
HELIX 63 AG9 ALA E 148 ASN E 151 5 4
HELIX 64 AH1 LEU E 152 ALA E 170 1 19
HELIX 65 AH2 SER E 185 GLU E 198 1 14
HELIX 66 AH3 ASP E 213 MET E 220 1 8
HELIX 67 AH4 GLY E 225 TYR E 227 5 3
HELIX 68 AH5 ASN E 228 ASP E 238 1 11
HELIX 69 AH6 ARG E 243 GLY E 252 1 10
HELIX 70 AH7 ASP E 255 ALA E 260 1 6
HELIX 71 AH8 PRO E 261 VAL E 263 5 3
HELIX 72 AH9 PRO E 279 ASN E 288 1 10
HELIX 73 AI1 GLY E 309 GLY E 320 1 12
HELIX 74 AI2 PRO F 8 LEU F 13 1 6
HELIX 75 AI3 ASP F 24 ALA F 38 1 15
HELIX 76 AI4 ASP F 99 SER F 102 5 4
HELIX 77 AI5 ARG F 103 LEU F 109 1 7
HELIX 78 AI6 ALA F 148 ASN F 151 5 4
HELIX 79 AI7 LEU F 152 ALA F 170 1 19
HELIX 80 AI8 SER F 185 GLU F 198 1 14
HELIX 81 AI9 ASP F 213 MET F 220 1 8
HELIX 82 AJ1 TYR F 227 ASP F 238 1 12
HELIX 83 AJ2 ARG F 243 GLY F 252 1 10
HELIX 84 AJ3 ASP F 255 ALA F 260 1 6
HELIX 85 AJ4 PRO F 261 VAL F 263 5 3
HELIX 86 AJ5 PRO F 279 ASN F 288 1 10
HELIX 87 AJ6 GLY F 309 GLY F 320 1 12
SHEET 1 AA1 9 VAL A 44 PRO A 47 0
SHEET 2 AA1 9 ARG A 56 GLY A 64 -1 O HIS A 59 N GLU A 46
SHEET 3 AA1 9 VAL A 68 ARG A 76 -1 O VAL A 70 N PHE A 62
SHEET 4 AA1 9 THR A 112 LEU A 116 -1 O VAL A 113 N LEU A 75
SHEET 5 AA1 9 HIS A 84 PHE A 90 1 N LEU A 87 O THR A 112
SHEET 6 AA1 9 VAL A 174 TYR A 184 1 O ALA A 180 N LEU A 88
SHEET 7 AA1 9 LEU A 203 VAL A 207 1 O ALA A 205 N ALA A 181
SHEET 8 AA1 9 GLU A 266 SER A 272 1 O LEU A 268 N ALA A 204
SHEET 9 AA1 9 LYS A 294 TYR A 299 1 O ARG A 297 N VAL A 271
SHEET 1 AA2 9 VAL B 44 PRO B 47 0
SHEET 2 AA2 9 ARG B 56 THR B 63 -1 O HIS B 59 N GLU B 46
SHEET 3 AA2 9 ARG B 69 ARG B 76 -1 O ALA B 72 N LEU B 60
SHEET 4 AA2 9 THR B 112 LEU B 116 -1 O ALA B 115 N LYS B 73
SHEET 5 AA2 9 HIS B 84 PHE B 90 1 N GLN B 89 O ALA B 114
SHEET 6 AA2 9 VAL B 174 TYR B 184 1 O ALA B 180 N LEU B 88
SHEET 7 AA2 9 LEU B 203 VAL B 207 1 O ALA B 205 N ALA B 181
SHEET 8 AA2 9 GLU B 266 SER B 272 1 O LEU B 268 N ALA B 204
SHEET 9 AA2 9 LYS B 294 TYR B 299 1 O ARG B 297 N VAL B 271
SHEET 1 AA3 9 VAL D 44 PRO D 47 0
SHEET 2 AA3 9 ARG D 56 GLY D 64 -1 O HIS D 59 N GLU D 46
SHEET 3 AA3 9 VAL D 68 ARG D 76 -1 O VAL D 70 N PHE D 62
SHEET 4 AA3 9 THR D 112 LEU D 116 -1 O VAL D 113 N LEU D 75
SHEET 5 AA3 9 HIS D 84 PHE D 90 1 N LEU D 87 O THR D 112
SHEET 6 AA3 9 VAL D 174 TYR D 184 1 O ALA D 180 N LEU D 88
SHEET 7 AA3 9 LEU D 203 VAL D 207 1 O ALA D 205 N ALA D 181
SHEET 8 AA3 9 GLU D 266 SER D 272 1 O GLU D 266 N ALA D 204
SHEET 9 AA3 9 LYS D 294 TYR D 299 1 O ARG D 297 N VAL D 271
SHEET 1 AA4 9 VAL C 44 PRO C 47 0
SHEET 2 AA4 9 ARG C 56 THR C 63 -1 O HIS C 59 N GLU C 46
SHEET 3 AA4 9 ARG C 69 ARG C 76 -1 O VAL C 70 N PHE C 62
SHEET 4 AA4 9 THR C 112 LEU C 116 -1 O VAL C 113 N LEU C 75
SHEET 5 AA4 9 HIS C 84 PHE C 90 1 N GLN C 89 O ALA C 114
SHEET 6 AA4 9 VAL C 174 TYR C 184 1 O ALA C 180 N LEU C 88
SHEET 7 AA4 9 LEU C 203 VAL C 207 1 O ALA C 205 N ALA C 181
SHEET 8 AA4 9 GLU C 266 SER C 272 1 O LEU C 268 N ALA C 204
SHEET 9 AA4 9 LYS C 294 TYR C 299 1 O ARG C 297 N VAL C 271
SHEET 1 AA5 9 VAL E 44 PRO E 47 0
SHEET 2 AA5 9 ARG E 56 GLY E 64 -1 O HIS E 59 N GLU E 46
SHEET 3 AA5 9 VAL E 68 ARG E 76 -1 O VAL E 70 N PHE E 62
SHEET 4 AA5 9 THR E 112 LEU E 116 -1 O VAL E 113 N LEU E 75
SHEET 5 AA5 9 HIS E 84 PHE E 90 1 N LEU E 87 O THR E 112
SHEET 6 AA5 9 VAL E 174 TYR E 184 1 O ALA E 180 N LEU E 88
SHEET 7 AA5 9 LEU E 203 VAL E 207 1 O ALA E 205 N ALA E 181
SHEET 8 AA5 9 GLU E 266 SER E 272 1 O LEU E 268 N ALA E 204
SHEET 9 AA5 9 LYS E 294 TYR E 299 1 O ARG E 297 N VAL E 271
SHEET 1 AA6 9 VAL F 44 PRO F 47 0
SHEET 2 AA6 9 ARG F 56 GLY F 64 -1 O HIS F 59 N GLU F 46
SHEET 3 AA6 9 VAL F 68 ARG F 76 -1 O VAL F 70 N PHE F 62
SHEET 4 AA6 9 THR F 112 LEU F 116 -1 O VAL F 113 N LEU F 75
SHEET 5 AA6 9 HIS F 84 PHE F 90 1 N LEU F 87 O THR F 112
SHEET 6 AA6 9 VAL F 174 TYR F 184 1 O ASP F 175 N HIS F 84
SHEET 7 AA6 9 LEU F 203 VAL F 207 1 O ALA F 205 N ALA F 181
SHEET 8 AA6 9 GLU F 266 SER F 272 1 O GLU F 266 N ALA F 204
SHEET 9 AA6 9 LYS F 294 TYR F 299 1 O ARG F 297 N VAL F 271
LINK O LEU A 169 NA NA A 401 1555 1555 2.54
LINK O MET A 171 NA NA A 401 1555 1555 2.36
LINK O VAL A 174 NA NA A 401 1555 1555 2.56
LINK O LEU B 169 NA NA B 401 1555 1555 2.41
LINK O MET B 171 NA NA B 401 1555 1555 2.34
LINK O VAL B 174 NA NA B 401 1555 1555 2.30
LINK O LEU D 169 NA NA D 401 1555 1555 2.35
LINK O MET D 171 NA NA D 401 1555 1555 2.40
LINK O VAL D 174 NA NA D 401 1555 1555 2.51
LINK O LEU C 169 NA NA C 401 1555 1555 2.30
LINK O MET C 171 NA NA C 401 1555 1555 2.27
LINK O VAL C 174 NA NA C 401 1555 1555 2.32
LINK O LEU E 169 NA NA E 401 1555 1555 2.61
LINK O MET E 171 NA NA E 401 1555 1555 2.61
LINK O VAL E 174 NA NA E 401 1555 1555 2.66
LINK O LEU F 169 NA NA F 401 1555 1555 2.39
LINK O MET F 171 NA NA F 401 1555 1555 2.37
LINK O VAL F 174 NA NA F 401 1555 1555 2.37
LINK NA NA B 401 O HOH B 512 1555 1555 2.77
LINK NA NA B 401 O HOH B 720 1555 1555 2.57
LINK NA NA D 401 O HOH D 531 1555 1555 2.80
LINK NA NA C 401 O HOH C 691 1555 1555 2.63
LINK NA NA E 401 O HOH E 654 1555 1555 2.89
LINK NA NA F 401 O HOH F 707 1555 1555 2.37
LINK NA NA F 401 O HOH F 722 1555 1555 2.54
LINK NA NA C 401 O HOH F 719 1555 3646 2.54
SITE 1 AC1 4 LEU A 169 ALA A 170 MET A 171 VAL A 174
SITE 1 AC2 6 GLU A 49 PHE A 50 HIS A 59 LYS A 73
SITE 2 AC2 6 TRP A 100 HOH A 524
SITE 1 AC3 4 VAL A 44 TRP A 61 ARG A 69 HOH A 641
SITE 1 AC4 5 LEU B 169 MET B 171 VAL B 174 HOH B 512
SITE 2 AC4 5 HOH B 720
SITE 1 AC5 4 VAL B 44 TRP B 61 ARG B 69 HOH B 693
SITE 1 AC6 5 ALA B 48 GLU B 49 PHE B 50 HIS B 59
SITE 2 AC6 5 TRP B 100
SITE 1 AC7 5 PRO B 199 ILE B 201 ARG B 264 ALA B 265
SITE 2 AC7 5 HOH B 519
SITE 1 AC8 5 LEU D 169 ALA D 170 MET D 171 VAL D 174
SITE 2 AC8 5 HOH D 531
SITE 1 AC9 8 GLU D 49 PHE D 50 HIS D 59 LYS D 73
SITE 2 AC9 8 TRP D 100 HOH D 502 HOH D 538 HOH D 573
SITE 1 AD1 5 VAL D 44 GLU D 46 TRP D 61 ARG D 69
SITE 2 AD1 5 HOH D 510
SITE 1 AD2 5 TRP A 134 TRP D 134 MET D 136 HOH D 635
SITE 2 AD2 5 HOH D 782
SITE 1 AD3 6 LEU C 169 ALA C 170 MET C 171 VAL C 174
SITE 2 AD3 6 HOH C 691 HOH F 719
SITE 1 AD4 7 VAL C 44 GLU C 46 TRP C 61 ARG C 69
SITE 2 AD4 7 HOH C 630 HOH C 718 HOH C 763
SITE 1 AD5 6 ALA C 48 GLU C 49 PHE C 50 HIS C 59
SITE 2 AD5 6 TRP C 100 HOH C 574
SITE 1 AD6 2 TRP C 134 TRP E 134
SITE 1 AD7 4 LEU E 169 MET E 171 VAL E 174 HOH E 654
SITE 1 AD8 6 ALA E 48 GLU E 49 PHE E 50 HIS E 59
SITE 2 AD8 6 TRP E 100 HOH E 658
SITE 1 AD9 7 HIS B 0 VAL E 44 GLU E 46 TRP E 61
SITE 2 AD9 7 ARG E 69 HOH E 624 HOH E 822
SITE 1 AE1 5 LEU F 169 MET F 171 VAL F 174 HOH F 707
SITE 2 AE1 5 HOH F 722
SITE 1 AE2 6 ALA F 48 GLU F 49 PHE F 50 HIS F 59
SITE 2 AE2 6 TRP F 100 HOH F 712
SITE 1 AE3 7 TRP B 134 MET B 136 TRP F 134 SER F 135
SITE 2 AE3 7 ARG F 142 HOH F 621 HOH F 643
CRYST1 107.680 116.820 159.420 90.00 90.00 90.00 P 21 21 21 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 0.009287 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006273 0.00000
TER 2567 LEU A 321
TER 5159 LEU B 321
TER 7720 LEU D 321
TER 10269 LEU C 321
TER 12824 LEU E 321
TER 15429 LEU F 321
MASTER 536 0 21 87 54 0 37 617510 6 139 150
END |