HEADER HYDROLASE 13-SEP-14 4V0B
TITLE ESCHERICHIA COLI FTSH HEXAMERIC N-DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT ZINC METALLOPROTEASE FTSH;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, UNP RESIDUES 25-96;
COMPND 5 SYNONYM: CELL DIVISION PROTEASE FTSH;
COMPND 6 EC: 3.4.24.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 ATCC: 27325;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, MEMBRANE PROTEIN, PERIPLASMIC DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SEREK-HEUBERGER,J.MARTIN,A.N.LUPAS,M.D.HARTMANN
REVDAT 3 10-JAN-24 4V0B 1 REMARK
REVDAT 2 04-MAR-15 4V0B 1 JRNL
REVDAT 1 21-JAN-15 4V0B 0
JRNL AUTH F.SCHARFENBERG,J.SEREK-HEUBERGER,M.COLES,M.D.HARTMANN,
JRNL AUTH 2 M.HABECK,J.MARTIN,A.N.LUPAS,V.ALVA
JRNL TITL STRUCTURE AND EVOLUTION OF N-DOMAINS IN AAA
JRNL TITL 2 METALLOPROTEASES.
JRNL REF J.MOL.BIOL. V. 427 910 2015
JRNL REFN ISSN 0022-2836
JRNL PMID 25576874
JRNL DOI 10.1016/J.JMB.2014.12.024
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 9199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 643
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.9924 - 4.3589 0.98 1792 136 0.1870 0.2105
REMARK 3 2 4.3589 - 3.4605 1.00 1746 131 0.1976 0.2439
REMARK 3 3 3.4605 - 3.0232 1.00 1752 132 0.2138 0.2907
REMARK 3 4 3.0232 - 2.7469 1.00 1732 128 0.2494 0.3350
REMARK 3 5 2.7469 - 2.5500 0.89 1534 116 0.3098 0.3196
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.27
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 : 0.003 1555
REMARK 3 ANGLE : 0.774 2107
REMARK 3 CHIRALITY : 0.059 246
REMARK 3 PLANARITY : 0.005 277
REMARK 3 DIHEDRAL : 16.154 608
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -50.5709 59.1306 -0.3037
REMARK 3 T TENSOR
REMARK 3 T11: 0.4703 T22: 0.3958
REMARK 3 T33: 0.6902 T12: 0.0498
REMARK 3 T13: -0.0800 T23: -0.0762
REMARK 3 L TENSOR
REMARK 3 L11: 0.2490 L22: 8.2787
REMARK 3 L33: 0.2616 L12: -2.2613
REMARK 3 L13: -0.6184 L23: 1.6656
REMARK 3 S TENSOR
REMARK 3 S11: -0.1265 S12: -0.1070 S13: 0.1566
REMARK 3 S21: 0.1615 S22: 0.2401 S23: -0.7301
REMARK 3 S31: 0.1740 S32: 0.2430 S33: -0.0870
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 4V0B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1290061749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9209
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 39.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 5.120
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.98
REMARK 200 R MERGE FOR SHELL (I) : 0.78000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.010
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: PDB ENTRY 2MUY
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M HEPES PH
REMARK 280 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 -0.500000 -0.866025 0.000000 -59.55500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 103.15229
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -119.11000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.1 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 206.30457
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 -119.11000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 206.30457
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.500000 0.866025 0.000000 -119.11000
REMARK 350 BIOMT2 4 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -0.500000 0.866025 0.000000 -178.66500
REMARK 350 BIOMT2 5 -0.866025 -0.500000 0.000000 103.15229
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 59.55500
REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 103.15229
REMARK 350 BIOMT3 6 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 23
REMARK 465 ALA A 24
REMARK 465 SER A 25
REMARK 465 GLU A 26
REMARK 465 SER A 27
REMARK 465 ASN A 28
REMARK 465 GLY A 29
REMARK 465 PRO A 93
REMARK 465 GLU A 94
REMARK 465 GLU A 95
REMARK 465 PRO A 96
REMARK 465 LEU A 97
REMARK 465 GLU A 98
REMARK 465 HIS A 99
REMARK 465 HIS A 100
REMARK 465 HIS A 101
REMARK 465 HIS A 102
REMARK 465 HIS A 103
REMARK 465 HIS A 104
REMARK 465 MET B 23
REMARK 465 ALA B 24
REMARK 465 SER B 25
REMARK 465 GLU B 26
REMARK 465 SER B 27
REMARK 465 ASN B 28
REMARK 465 GLY B 29
REMARK 465 PRO B 93
REMARK 465 GLU B 94
REMARK 465 GLU B 95
REMARK 465 PRO B 96
REMARK 465 LEU B 97
REMARK 465 GLU B 98
REMARK 465 HIS B 99
REMARK 465 HIS B 100
REMARK 465 HIS B 101
REMARK 465 HIS B 102
REMARK 465 HIS B 103
REMARK 465 HIS B 104
REMARK 465 MET C 23
REMARK 465 ALA C 24
REMARK 465 SER C 25
REMARK 465 GLU C 26
REMARK 465 SER C 27
REMARK 465 ASN C 28
REMARK 465 GLY C 29
REMARK 465 PRO C 93
REMARK 465 GLU C 94
REMARK 465 GLU C 95
REMARK 465 PRO C 96
REMARK 465 LEU C 97
REMARK 465 GLU C 98
REMARK 465 HIS C 99
REMARK 465 HIS C 100
REMARK 465 HIS C 101
REMARK 465 HIS C 102
REMARK 465 HIS C 103
REMARK 465 HIS C 104
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 31 CD CE NZ
REMARK 470 GLN A 39 CG CD OE1 NE2
REMARK 470 GLN A 73 CG CD OE1 NE2
REMARK 470 LYS B 76 CG CD CE NZ
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 GLU A 91 NH2 ARG B 54 2.17
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 63 -0.59 73.13
REMARK 500 SER B 63 -0.03 72.48
REMARK 500 SER C 63 -0.31 72.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1093
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UZR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYROCOCCUS HORIKOSHII PH1500
DBREF 4V0B A 25 96 UNP P0AAI3 FTSH_ECOLI 25 96
DBREF 4V0B B 25 96 UNP P0AAI3 FTSH_ECOLI 25 96
DBREF 4V0B C 25 96 UNP P0AAI3 FTSH_ECOLI 25 96
SEQADV 4V0B MET A 23 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B ALA A 24 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B LEU A 97 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B GLU A 98 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS A 99 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS A 100 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS A 101 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS A 102 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS A 103 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS A 104 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B MET B 23 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B ALA B 24 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B LEU B 97 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B GLU B 98 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS B 99 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS B 100 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS B 101 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS B 102 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS B 103 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS B 104 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B MET C 23 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B ALA C 24 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B LEU C 97 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B GLU C 98 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS C 99 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS C 100 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS C 101 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS C 102 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS C 103 UNP P0AAI3 EXPRESSION TAG
SEQADV 4V0B HIS C 104 UNP P0AAI3 EXPRESSION TAG
SEQRES 1 A 82 MET ALA SER GLU SER ASN GLY ARG LYS VAL ASP TYR SER
SEQRES 2 A 82 THR PHE LEU GLN GLU VAL ASN ASN ASP GLN VAL ARG GLU
SEQRES 3 A 82 ALA ARG ILE ASN GLY ARG GLU ILE ASN VAL THR LYS LYS
SEQRES 4 A 82 ASP SER ASN ARG TYR THR THR TYR ILE PRO VAL GLN ASP
SEQRES 5 A 82 PRO LYS LEU LEU ASP ASN LEU LEU THR LYS ASN VAL LYS
SEQRES 6 A 82 VAL VAL GLY GLU PRO PRO GLU GLU PRO LEU GLU HIS HIS
SEQRES 7 A 82 HIS HIS HIS HIS
SEQRES 1 B 82 MET ALA SER GLU SER ASN GLY ARG LYS VAL ASP TYR SER
SEQRES 2 B 82 THR PHE LEU GLN GLU VAL ASN ASN ASP GLN VAL ARG GLU
SEQRES 3 B 82 ALA ARG ILE ASN GLY ARG GLU ILE ASN VAL THR LYS LYS
SEQRES 4 B 82 ASP SER ASN ARG TYR THR THR TYR ILE PRO VAL GLN ASP
SEQRES 5 B 82 PRO LYS LEU LEU ASP ASN LEU LEU THR LYS ASN VAL LYS
SEQRES 6 B 82 VAL VAL GLY GLU PRO PRO GLU GLU PRO LEU GLU HIS HIS
SEQRES 7 B 82 HIS HIS HIS HIS
SEQRES 1 C 82 MET ALA SER GLU SER ASN GLY ARG LYS VAL ASP TYR SER
SEQRES 2 C 82 THR PHE LEU GLN GLU VAL ASN ASN ASP GLN VAL ARG GLU
SEQRES 3 C 82 ALA ARG ILE ASN GLY ARG GLU ILE ASN VAL THR LYS LYS
SEQRES 4 C 82 ASP SER ASN ARG TYR THR THR TYR ILE PRO VAL GLN ASP
SEQRES 5 C 82 PRO LYS LEU LEU ASP ASN LEU LEU THR LYS ASN VAL LYS
SEQRES 6 C 82 VAL VAL GLY GLU PRO PRO GLU GLU PRO LEU GLU HIS HIS
SEQRES 7 C 82 HIS HIS HIS HIS
HET SO4 B1093 5
HETNAM SO4 SULFATE ION
FORMUL 4 SO4 O4 S 2-
HELIX 1 1 ASP A 33 ASN A 43 1 11
HELIX 2 2 LYS A 76 LYS A 84 1 9
HELIX 3 3 ASP B 33 ASN B 43 1 11
HELIX 4 4 LYS B 76 LYS B 84 1 9
HELIX 5 5 ASP C 33 ASN C 43 1 11
HELIX 6 6 LYS C 76 LYS C 84 1 9
SHEET 1 AA 4 ARG A 65 TYR A 69 0
SHEET 2 AA 4 GLU A 55 LYS A 60 -1 O ILE A 56 N THR A 68
SHEET 3 AA 4 VAL A 46 ASN A 52 -1 N ARG A 47 O THR A 59
SHEET 4 AA 4 LYS A 87 GLY A 90 1 O LYS A 87 N ALA A 49
SHEET 1 BA 4 ARG B 65 TYR B 69 0
SHEET 2 BA 4 GLU B 55 LYS B 60 -1 O ILE B 56 N THR B 68
SHEET 3 BA 4 VAL B 46 ASN B 52 -1 N ARG B 47 O THR B 59
SHEET 4 BA 4 LYS B 87 GLY B 90 1 O LYS B 87 N ALA B 49
SHEET 1 CA 4 ARG C 65 TYR C 69 0
SHEET 2 CA 4 GLU C 55 LYS C 60 -1 O ILE C 56 N THR C 68
SHEET 3 CA 4 VAL C 46 ASN C 52 -1 N ARG C 47 O THR C 59
SHEET 4 CA 4 LYS C 87 GLY C 90 1 O LYS C 87 N ALA C 49
SITE 1 AC1 3 ARG B 47 LYS B 61 ARG C 65
CRYST1 119.110 119.110 34.540 90.00 90.00 120.00 P 6 18
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 0.008396 0.004847 0.000000 0.00000
SCALE2 0.000000 0.009694 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028952 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
