HEADER STRUCTURAL PROTEIN 02-JUN-14 4QIV
TITLE CRYSTAL STRUCTURE OF HEXAMERIC MICROCOMPARMENT SHELL PROTEIN FROM
TITLE 2 AEROMONAS HYDROPHILA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERIAL MICROCOMPARTMENTS FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROMONAS HYDROPHILA SUBSP. HYDROPHILA;
SOURCE 3 ORGANISM_TAXID: 380703;
SOURCE 4 STRAIN: ATCC 7966 / NCIB 9240;
SOURCE 5 GENE: AHA_1335;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS BMC DOMAIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.H.PANG,M.R.SAWAYA,T.O.YEATES
REVDAT 2 28-FEB-24 4QIV 1 SEQADV
REVDAT 1 12-AUG-15 4QIV 0
JRNL AUTH A.H.PANG,M.R.SAWAYA,T.O.YEATES
JRNL TITL CRYSTAL STRUCTURE OF A HEXAMERIC MICROCOMPARMENT PROTEIN
JRNL TITL 2 FROM AEROMONAS HYDROPHILA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 64.0
REMARK 3 NUMBER OF REFLECTIONS : 6508
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 327
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 115
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 14.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.1360
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1801
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.399
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.513
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.893
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.838
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1819 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1864 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2465 ; 1.421 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4276 ; 0.988 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 257 ; 6.642 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;42.862 ;26.429
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 314 ;18.005 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;32.091 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 319 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2076 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 329 ; 0.002 ; 0.020
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): 1034 ; 3.079 ; 1.804
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1033 ; 3.057 ; 1.796
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1289 ; 4.848 ; 2.675
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 785 ; 5.178 ; 2.543
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 88 B 3 88 4847 0.09 0.05
REMARK 3 2 A 3 88 C 3 88 4947 0.08 0.05
REMARK 3 3 B 3 88 C 3 88 4802 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .9792
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6835
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.298
REMARK 200 RESOLUTION RANGE LOW (A) : 61.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 64.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 14.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.19900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.850
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 (%): 25.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 1.5M AMMONIUM SULFATE, PH
REMARK 280 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.60500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 61.17500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.60500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.17500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.60500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.17500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.60500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 61.17500
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 61.17500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 61.17500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 61.17500
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 61.17500
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 57.60500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 57.60500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 57.60500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 33.23000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 57.60500
REMARK 290 SMTRY3 16 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -33.23000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 57.60500
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 111 LIES ON A SPECIAL POSITION.
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 HIS A 89
REMARK 465 TYR A 90
REMARK 465 LYS A 91
REMARK 465 ILE A 92
REMARK 465 ALA A 93
REMARK 465 GLU A 94
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 HIS B 89
REMARK 465 TYR B 90
REMARK 465 LYS B 91
REMARK 465 ILE B 92
REMARK 465 ALA B 93
REMARK 465 GLU B 94
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 HIS C 89
REMARK 465 TYR C 90
REMARK 465 LYS C 91
REMARK 465 ILE C 92
REMARK 465 ALA C 93
REMARK 465 GLU C 94
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 GLU B 69 CG CD OE1 OE2
REMARK 470 GLU C 69 CG CD OE1 OE2
DBREF 4QIV A 1 94 UNP A0KHX4 A0KHX4_AERHH 1 94
DBREF 4QIV B 1 94 UNP A0KHX4 A0KHX4_AERHH 1 94
DBREF 4QIV C 1 94 UNP A0KHX4 A0KHX4_AERHH 1 94
SEQADV 4QIV MET A -19 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY A -18 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER A -17 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER A -16 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS A -15 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS A -14 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS A -13 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS A -12 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS A -11 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS A -10 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER A -9 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER A -8 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY A -7 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV LEU A -6 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV VAL A -5 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV PRO A -4 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV ARG A -3 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY A -2 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER A -1 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS A 0 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV MET B -19 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY B -18 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER B -17 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER B -16 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS B -15 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS B -14 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS B -13 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS B -12 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS B -11 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS B -10 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER B -9 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER B -8 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY B -7 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV LEU B -6 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV VAL B -5 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV PRO B -4 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV ARG B -3 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY B -2 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER B -1 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS B 0 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV MET C -19 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY C -18 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER C -17 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER C -16 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS C -15 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS C -14 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS C -13 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS C -12 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS C -11 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS C -10 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER C -9 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER C -8 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY C -7 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV LEU C -6 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV VAL C -5 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV PRO C -4 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV ARG C -3 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV GLY C -2 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV SER C -1 UNP A0KHX4 EXPRESSION TAG
SEQADV 4QIV HIS C 0 UNP A0KHX4 EXPRESSION TAG
SEQRES 1 A 114 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 114 LEU VAL PRO ARG GLY SER HIS MET GLY ASP ALA LEU GLY
SEQRES 3 A 114 LEU ILE GLU THR LYS GLY LEU VAL ALA CYS ILE GLU ALA
SEQRES 4 A 114 ALA ASP ALA MET CYS LYS ALA ALA ASN VAL GLU LEU ILE
SEQRES 5 A 114 GLY TYR GLU ASN VAL GLY SER GLY LEU VAL THR ALA MET
SEQRES 6 A 114 VAL LYS GLY ASP VAL GLY ALA VAL LYS ALA ALA VAL ASP
SEQRES 7 A 114 SER GLY VAL GLU SER ALA GLN ARG ILE GLY GLU VAL VAL
SEQRES 8 A 114 THR SER LEU VAL ILE ALA ARG PRO HIS ASN ASP ILE SER
SEQRES 9 A 114 LYS ILE VAL ALA HIS TYR LYS ILE ALA GLU
SEQRES 1 B 114 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 114 LEU VAL PRO ARG GLY SER HIS MET GLY ASP ALA LEU GLY
SEQRES 3 B 114 LEU ILE GLU THR LYS GLY LEU VAL ALA CYS ILE GLU ALA
SEQRES 4 B 114 ALA ASP ALA MET CYS LYS ALA ALA ASN VAL GLU LEU ILE
SEQRES 5 B 114 GLY TYR GLU ASN VAL GLY SER GLY LEU VAL THR ALA MET
SEQRES 6 B 114 VAL LYS GLY ASP VAL GLY ALA VAL LYS ALA ALA VAL ASP
SEQRES 7 B 114 SER GLY VAL GLU SER ALA GLN ARG ILE GLY GLU VAL VAL
SEQRES 8 B 114 THR SER LEU VAL ILE ALA ARG PRO HIS ASN ASP ILE SER
SEQRES 9 B 114 LYS ILE VAL ALA HIS TYR LYS ILE ALA GLU
SEQRES 1 C 114 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 114 LEU VAL PRO ARG GLY SER HIS MET GLY ASP ALA LEU GLY
SEQRES 3 C 114 LEU ILE GLU THR LYS GLY LEU VAL ALA CYS ILE GLU ALA
SEQRES 4 C 114 ALA ASP ALA MET CYS LYS ALA ALA ASN VAL GLU LEU ILE
SEQRES 5 C 114 GLY TYR GLU ASN VAL GLY SER GLY LEU VAL THR ALA MET
SEQRES 6 C 114 VAL LYS GLY ASP VAL GLY ALA VAL LYS ALA ALA VAL ASP
SEQRES 7 C 114 SER GLY VAL GLU SER ALA GLN ARG ILE GLY GLU VAL VAL
SEQRES 8 C 114 THR SER LEU VAL ILE ALA ARG PRO HIS ASN ASP ILE SER
SEQRES 9 C 114 LYS ILE VAL ALA HIS TYR LYS ILE ALA GLU
FORMUL 4 HOH *46(H2 O)
HELIX 1 1 GLY A 12 ALA A 27 1 16
HELIX 2 2 ASP A 49 GLY A 68 1 20
HELIX 3 3 HIS A 80 ALA A 88 1 9
HELIX 4 4 LEU B 13 ALA B 27 1 15
HELIX 5 5 ASP B 49 GLY B 68 1 20
HELIX 6 6 HIS B 80 ALA B 88 1 9
HELIX 7 7 GLY C 12 ALA C 27 1 16
HELIX 8 8 ASP C 49 GLY C 68 1 20
HELIX 9 9 HIS C 80 ALA C 88 1 9
SHEET 1 A 4 VAL A 29 ASN A 36 0
SHEET 2 A 4 LEU A 41 GLY A 48 -1 O THR A 43 N GLU A 35
SHEET 3 A 4 ALA A 4 LYS A 11 -1 N THR A 10 O VAL A 42
SHEET 4 A 4 GLU A 69 ILE A 76 -1 O ILE A 76 N LEU A 5
SHEET 1 B 4 VAL B 29 ASN B 36 0
SHEET 2 B 4 LEU B 41 GLY B 48 -1 O THR B 43 N GLU B 35
SHEET 3 B 4 ALA B 4 LYS B 11 -1 N THR B 10 O VAL B 42
SHEET 4 B 4 GLU B 69 ILE B 76 -1 O THR B 72 N GLU B 9
SHEET 1 C 4 VAL C 29 ASN C 36 0
SHEET 2 C 4 LEU C 41 GLY C 48 -1 O THR C 43 N GLU C 35
SHEET 3 C 4 ALA C 4 LYS C 11 -1 N THR C 10 O VAL C 42
SHEET 4 C 4 GLU C 69 ILE C 76 -1 O ILE C 76 N LEU C 5
CRYST1 66.460 115.210 122.350 90.00 90.00 90.00 F 2 2 2 48
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015047 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008173 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
