HEADER UNKNOWN FUNCTION 18-JAN-05 1YKW
TITLE CRYSTAL STRUCTURE OF A NOVEL RUBISCO-LIKE PROTEIN FROM THE GREEN
TITLE 2 SULFUR BACTERIUM CHLOROBIUM TEPIDUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBISCO-LIKE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLOROBACULUM TEPIDUM;
SOURCE 3 ORGANISM_TAXID: 1097;
SOURCE 4 GENE: CT1772;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS BETA-ALPHA-BARREL, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,M.R.SAWAYA,F.R.TABITA,D.EISENBERG
REVDAT 5 23-AUG-23 1YKW 1 REMARK
REVDAT 4 20-OCT-21 1YKW 1 SEQADV
REVDAT 3 13-JUL-11 1YKW 1 VERSN
REVDAT 2 24-FEB-09 1YKW 1 VERSN
REVDAT 1 17-MAY-05 1YKW 0
JRNL AUTH H.LI,M.R.SAWAYA,F.R.TABITA,D.EISENBERG
JRNL TITL CRYSTAL STRUCTURE OF A RUBISCO-LIKE PROTEIN FROM THE GREEN
JRNL TITL 2 SULFUR BACTERIUM CHLOROBIUM TEPIDUM.
JRNL REF STRUCTURE V. 13 779 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15893668
JRNL DOI 10.1016/J.STR.2005.02.017
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 57608
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2956
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3019
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6398
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.18000
REMARK 3 B22 (A**2) : -0.74000
REMARK 3 B33 (A**2) : 3.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.67000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.193
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.172
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.954
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6573 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8916 ; 1.626 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 825 ; 6.703 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 290 ;37.166 ;24.310
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1094 ;17.018 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;17.645 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 984 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5009 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2874 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4451 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 338 ; 0.166 ; 0.200
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): 31 ; 0.155 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.151 ; 0.200
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): 4224 ; 1.018 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6639 ; 1.598 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2637 ; 2.460 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2277 ; 3.820 ; 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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 40 3
REMARK 3 1 B 7 B 40 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 136 ; 0.03 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 139 ; 0.21 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 136 ; 0.12 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 139 ; 0.85 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 90 A 160 3
REMARK 3 1 B 90 B 160 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 280 ; 0.04 ; 0.05
REMARK 3 LOOSE POSITIONAL 2 A (A): 259 ; 0.23 ; 5.00
REMARK 3 TIGHT THERMAL 2 A (A**2): 280 ; 0.17 ; 0.50
REMARK 3 LOOSE THERMAL 2 A (A**2): 259 ; 0.99 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 225 A 320 3
REMARK 3 1 B 225 B 320 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 384 ; 0.04 ; 0.05
REMARK 3 LOOSE POSITIONAL 3 A (A): 351 ; 0.32 ; 5.00
REMARK 3 TIGHT THERMAL 3 A (A**2): 384 ; 0.17 ; 0.50
REMARK 3 LOOSE THERMAL 3 A (A**2): 351 ; 1.10 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 333 A 375 3
REMARK 3 1 B 333 B 375 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 168 ; 0.03 ; 0.05
REMARK 3 LOOSE POSITIONAL 4 A (A): 141 ; 0.47 ; 5.00
REMARK 3 TIGHT THERMAL 4 A (A**2): 168 ; 0.18 ; 0.50
REMARK 3 LOOSE THERMAL 4 A (A**2): 141 ; 1.38 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 47
REMARK 3 RESIDUE RANGE : A 59 A 144
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1884 25.0597 61.1763
REMARK 3 T TENSOR
REMARK 3 T11: -0.0393 T22: -0.0026
REMARK 3 T33: 0.0308 T12: 0.0500
REMARK 3 T13: 0.0174 T23: 0.1331
REMARK 3 L TENSOR
REMARK 3 L11: 1.8163 L22: 0.9839
REMARK 3 L33: 3.5280 L12: 0.1362
REMARK 3 L13: 0.7262 L23: -0.2174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0248 S12: 0.4554 S13: 0.4528
REMARK 3 S21: -0.0916 S22: 0.0108 S23: -0.0258
REMARK 3 S31: -0.2571 S32: -0.1322 S33: -0.0357
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 145 A 428
REMARK 3 ORIGIN FOR THE GROUP (A): 54.3272 -3.4221 73.7012
REMARK 3 T TENSOR
REMARK 3 T11: -0.0497 T22: -0.0803
REMARK 3 T33: -0.0369 T12: 0.0182
REMARK 3 T13: -0.0170 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 1.9732 L22: 0.5813
REMARK 3 L33: 1.0973 L12: -0.1111
REMARK 3 L13: -0.3589 L23: 0.0207
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: 0.2262 S13: -0.3297
REMARK 3 S21: -0.0117 S22: 0.0318 S23: -0.0434
REMARK 3 S31: 0.2217 S32: 0.0961 S33: 0.0161
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 47
REMARK 3 RESIDUE RANGE : B 59 B 144
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6991 -11.2262 61.2429
REMARK 3 T TENSOR
REMARK 3 T11: -0.0389 T22: 0.0282
REMARK 3 T33: 0.0118 T12: 0.0313
REMARK 3 T13: 0.0025 T23: -0.1425
REMARK 3 L TENSOR
REMARK 3 L11: 1.5708 L22: 1.2555
REMARK 3 L33: 3.5267 L12: 0.1927
REMARK 3 L13: -0.8214 L23: 0.0587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0349 S12: 0.4798 S13: -0.4892
REMARK 3 S21: -0.1173 S22: 0.0217 S23: -0.0612
REMARK 3 S31: 0.3271 S32: 0.0781 S33: 0.0133
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 145 B 174
REMARK 3 RESIDUE RANGE : B 177 B 428
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4417 17.2069 73.7040
REMARK 3 T TENSOR
REMARK 3 T11: -0.0558 T22: -0.0734
REMARK 3 T33: -0.0269 T12: 0.0197
REMARK 3 T13: 0.0104 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 1.8287 L22: 0.6061
REMARK 3 L33: 1.1205 L12: -0.2019
REMARK 3 L13: 0.3141 L23: -0.0959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0379 S12: 0.2228 S13: 0.3409
REMARK 3 S21: 0.0339 S22: 0.0330 S23: 0.0464
REMARK 3 S31: -0.2073 S32: -0.0925 S33: 0.0050
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 1YKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031632.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1271
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL 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 : 60951
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 90.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 5RUB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM FORMATE , PH 5.9,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
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 39.22550
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 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 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 48
REMARK 465 GLN A 49
REMARK 465 TRP A 50
REMARK 465 LYS A 51
REMARK 465 ARG A 52
REMARK 465 VAL A 53
REMARK 465 GLY A 54
REMARK 465 VAL A 55
REMARK 465 ASP A 56
REMARK 465 GLU A 57
REMARK 465 ASP A 58
REMARK 465 SER A 429
REMARK 465 LEU A 430
REMARK 465 LEU A 431
REMARK 465 LYS A 432
REMARK 465 LYS A 433
REMARK 465 GLN A 434
REMARK 465 ASP A 435
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 48
REMARK 465 GLN B 49
REMARK 465 TRP B 50
REMARK 465 LYS B 51
REMARK 465 ARG B 52
REMARK 465 VAL B 53
REMARK 465 GLY B 54
REMARK 465 VAL B 55
REMARK 465 ASP B 56
REMARK 465 GLU B 57
REMARK 465 ASP B 58
REMARK 465 ILE B 175
REMARK 465 GLY B 176
REMARK 465 SER B 429
REMARK 465 LEU B 430
REMARK 465 LEU B 431
REMARK 465 LYS B 432
REMARK 465 LYS B 433
REMARK 465 GLN B 434
REMARK 465 ASP B 435
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 46 -104.03 -151.69
REMARK 500 CYS A 117 46.54 -145.57
REMARK 500 ASN A 160 51.91 38.69
REMARK 500 ALA A 204 -126.55 -104.84
REMARK 500 SER A 209 78.77 -151.50
REMARK 500 PHE A 290 -33.09 91.68
REMARK 500 MET A 329 33.95 -80.36
REMARK 500 SER B 46 -110.11 -141.12
REMARK 500 ASP B 69 149.01 -176.22
REMARK 500 CYS B 117 53.04 -143.38
REMARK 500 PRO B 179 -37.25 -36.17
REMARK 500 ALA B 204 -119.15 -114.25
REMARK 500 SER B 209 75.86 -151.52
REMARK 500 PHE B 290 -35.35 86.80
REMARK 500 MET B 329 32.72 -94.14
REMARK 500 VAL B 385 -66.49 -96.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
DBREF 1YKW A 1 435 UNP Q8KBL4 Q8KBL4_CHLTE 1 435
DBREF 1YKW B 1 435 UNP Q8KBL4 Q8KBL4_CHLTE 1 435
SEQADV 1YKW VAL A 328 UNP Q8KBL4 MET 328 ENGINEERED MUTATION
SEQADV 1YKW VAL B 328 UNP Q8KBL4 MET 328 ENGINEERED MUTATION
SEQRES 1 A 435 MET ASN ALA GLU ASP VAL LYS GLY PHE PHE ALA SER ARG
SEQRES 2 A 435 GLU SER LEU ASP MET GLU GLN TYR LEU VAL LEU ASP TYR
SEQRES 3 A 435 TYR LEU GLU SER VAL GLY ASP ILE GLU THR ALA LEU ALA
SEQRES 4 A 435 HIS PHE CYS SER GLU GLN SER THR ALA GLN TRP LYS ARG
SEQRES 5 A 435 VAL GLY VAL ASP GLU ASP PHE ARG LEU VAL HIS ALA ALA
SEQRES 6 A 435 LYS VAL ILE ASP TYR GLU VAL ILE GLU GLU LEU GLU GLN
SEQRES 7 A 435 LEU SER TYR PRO VAL LYS HIS SER GLU THR GLY LYS ILE
SEQRES 8 A 435 HIS ALA CYS ARG VAL THR ILE ALA HIS PRO HIS CYS ASN
SEQRES 9 A 435 PHE GLY PRO LYS ILE PRO ASN LEU LEU THR ALA VAL CYS
SEQRES 10 A 435 GLY GLU GLY THR TYR PHE THR PRO GLY VAL PRO VAL VAL
SEQRES 11 A 435 LYS LEU MET ASP ILE HIS PHE PRO ASP THR TYR LEU ALA
SEQRES 12 A 435 ASP PHE GLU GLY PRO LYS PHE GLY ILE GLU GLY LEU ARG
SEQRES 13 A 435 ASP ILE LEU ASN ALA HIS GLY ARG PRO ILE PHE PHE GLY
SEQRES 14 A 435 VAL VAL LYS PRO ASN ILE GLY LEU SER PRO GLY GLU PHE
SEQRES 15 A 435 ALA GLU ILE ALA TYR GLN SER TRP LEU GLY GLY LEU ASP
SEQRES 16 A 435 ILE ALA LYS ASP ASP GLU MET LEU ALA ASP VAL THR TRP
SEQRES 17 A 435 SER SER ILE GLU GLU ARG ALA ALA HIS LEU GLY LYS ALA
SEQRES 18 A 435 ARG ARG LYS ALA GLU ALA GLU THR GLY GLU PRO LYS ILE
SEQRES 19 A 435 TYR LEU ALA ASN ILE THR ASP GLU VAL ASP SER LEU MET
SEQRES 20 A 435 GLU LYS HIS ASP VAL ALA VAL ARG ASN GLY ALA ASN ALA
SEQRES 21 A 435 LEU LEU ILE ASN ALA LEU PRO VAL GLY LEU SER ALA VAL
SEQRES 22 A 435 ARG MET LEU SER ASN TYR THR GLN VAL PRO LEU ILE GLY
SEQRES 23 A 435 HIS PHE PRO PHE ILE ALA SER PHE SER ARG MET GLU LYS
SEQRES 24 A 435 TYR GLY ILE HIS SER LYS VAL MET THR LYS LEU GLN ARG
SEQRES 25 A 435 LEU ALA GLY LEU ASP ALA VAL ILE MET PRO GLY PHE GLY
SEQRES 26 A 435 ASP ARG VAL MET THR PRO GLU GLU GLU VAL LEU GLU ASN
SEQRES 27 A 435 VAL ILE GLU CYS THR LYS PRO MET GLY ARG ILE LYS PRO
SEQRES 28 A 435 CYS LEU PRO VAL PRO GLY GLY SER ASP SER ALA LEU THR
SEQRES 29 A 435 LEU GLN THR VAL TYR GLU LYS VAL GLY ASN VAL ASP PHE
SEQRES 30 A 435 GLY PHE VAL PRO GLY ARG GLY VAL PHE GLY HIS PRO MET
SEQRES 31 A 435 GLY PRO LYS ALA GLY ALA LYS SER ILE ARG GLN ALA TRP
SEQRES 32 A 435 GLU ALA ILE GLU GLN GLY ILE SER ILE GLU THR TRP ALA
SEQRES 33 A 435 GLU THR HIS PRO GLU LEU GLN ALA MET VAL ASP GLN SER
SEQRES 34 A 435 LEU LEU LYS LYS GLN ASP
SEQRES 1 B 435 MET ASN ALA GLU ASP VAL LYS GLY PHE PHE ALA SER ARG
SEQRES 2 B 435 GLU SER LEU ASP MET GLU GLN TYR LEU VAL LEU ASP TYR
SEQRES 3 B 435 TYR LEU GLU SER VAL GLY ASP ILE GLU THR ALA LEU ALA
SEQRES 4 B 435 HIS PHE CYS SER GLU GLN SER THR ALA GLN TRP LYS ARG
SEQRES 5 B 435 VAL GLY VAL ASP GLU ASP PHE ARG LEU VAL HIS ALA ALA
SEQRES 6 B 435 LYS VAL ILE ASP TYR GLU VAL ILE GLU GLU LEU GLU GLN
SEQRES 7 B 435 LEU SER TYR PRO VAL LYS HIS SER GLU THR GLY LYS ILE
SEQRES 8 B 435 HIS ALA CYS ARG VAL THR ILE ALA HIS PRO HIS CYS ASN
SEQRES 9 B 435 PHE GLY PRO LYS ILE PRO ASN LEU LEU THR ALA VAL CYS
SEQRES 10 B 435 GLY GLU GLY THR TYR PHE THR PRO GLY VAL PRO VAL VAL
SEQRES 11 B 435 LYS LEU MET ASP ILE HIS PHE PRO ASP THR TYR LEU ALA
SEQRES 12 B 435 ASP PHE GLU GLY PRO LYS PHE GLY ILE GLU GLY LEU ARG
SEQRES 13 B 435 ASP ILE LEU ASN ALA HIS GLY ARG PRO ILE PHE PHE GLY
SEQRES 14 B 435 VAL VAL LYS PRO ASN ILE GLY LEU SER PRO GLY GLU PHE
SEQRES 15 B 435 ALA GLU ILE ALA TYR GLN SER TRP LEU GLY GLY LEU ASP
SEQRES 16 B 435 ILE ALA LYS ASP ASP GLU MET LEU ALA ASP VAL THR TRP
SEQRES 17 B 435 SER SER ILE GLU GLU ARG ALA ALA HIS LEU GLY LYS ALA
SEQRES 18 B 435 ARG ARG LYS ALA GLU ALA GLU THR GLY GLU PRO LYS ILE
SEQRES 19 B 435 TYR LEU ALA ASN ILE THR ASP GLU VAL ASP SER LEU MET
SEQRES 20 B 435 GLU LYS HIS ASP VAL ALA VAL ARG ASN GLY ALA ASN ALA
SEQRES 21 B 435 LEU LEU ILE ASN ALA LEU PRO VAL GLY LEU SER ALA VAL
SEQRES 22 B 435 ARG MET LEU SER ASN TYR THR GLN VAL PRO LEU ILE GLY
SEQRES 23 B 435 HIS PHE PRO PHE ILE ALA SER PHE SER ARG MET GLU LYS
SEQRES 24 B 435 TYR GLY ILE HIS SER LYS VAL MET THR LYS LEU GLN ARG
SEQRES 25 B 435 LEU ALA GLY LEU ASP ALA VAL ILE MET PRO GLY PHE GLY
SEQRES 26 B 435 ASP ARG VAL MET THR PRO GLU GLU GLU VAL LEU GLU ASN
SEQRES 27 B 435 VAL ILE GLU CYS THR LYS PRO MET GLY ARG ILE LYS PRO
SEQRES 28 B 435 CYS LEU PRO VAL PRO GLY GLY SER ASP SER ALA LEU THR
SEQRES 29 B 435 LEU GLN THR VAL TYR GLU LYS VAL GLY ASN VAL ASP PHE
SEQRES 30 B 435 GLY PHE VAL PRO GLY ARG GLY VAL PHE GLY HIS PRO MET
SEQRES 31 B 435 GLY PRO LYS ALA GLY ALA LYS SER ILE ARG GLN ALA TRP
SEQRES 32 B 435 GLU ALA ILE GLU GLN GLY ILE SER ILE GLU THR TRP ALA
SEQRES 33 B 435 GLU THR HIS PRO GLU LEU GLN ALA MET VAL ASP GLN SER
SEQRES 34 B 435 LEU LEU LYS LYS GLN ASP
FORMUL 3 HOH *317(H2 O)
HELIX 1 1 ASP A 5 PHE A 9 5 5
HELIX 2 2 SER A 12 SER A 15 5 4
HELIX 3 3 ASP A 17 GLN A 20 5 4
HELIX 4 4 ASP A 33 GLU A 44 1 12
HELIX 5 5 HIS A 102 GLY A 106 5 5
HELIX 6 6 LYS A 108 CYS A 117 1 10
HELIX 7 7 GLU A 119 PHE A 123 1 5
HELIX 8 8 PRO A 138 ALA A 143 1 6
HELIX 9 9 PHE A 150 ASN A 160 1 11
HELIX 10 10 SER A 178 GLY A 192 1 15
HELIX 11 11 SER A 210 GLY A 230 1 21
HELIX 12 12 GLU A 242 SER A 245 5 4
HELIX 13 13 SER A 245 GLY A 257 1 13
HELIX 14 14 ALA A 265 GLY A 269 1 5
HELIX 15 15 GLY A 269 THR A 280 1 12
HELIX 16 16 ILE A 291 PHE A 294 1 4
HELIX 17 17 HIS A 303 GLY A 315 1 13
HELIX 18 18 PRO A 331 LYS A 344 1 14
HELIX 19 19 THR A 364 GLY A 373 1 10
HELIX 20 20 GLY A 391 GLN A 408 1 18
HELIX 21 21 SER A 411 GLU A 417 1 7
HELIX 22 22 HIS A 419 GLN A 428 1 10
HELIX 23 23 ASP B 5 PHE B 9 5 5
HELIX 24 24 SER B 12 SER B 15 5 4
HELIX 25 25 ASP B 17 GLN B 20 5 4
HELIX 26 26 ASP B 33 GLU B 44 1 12
HELIX 27 27 HIS B 102 GLY B 106 5 5
HELIX 28 28 LYS B 108 CYS B 117 1 10
HELIX 29 29 GLU B 119 PHE B 123 1 5
HELIX 30 30 PRO B 138 ALA B 143 1 6
HELIX 31 31 PHE B 150 ASN B 160 1 11
HELIX 32 32 SER B 178 GLY B 192 1 15
HELIX 33 33 SER B 210 GLY B 230 1 21
HELIX 34 34 GLU B 242 SER B 245 5 4
HELIX 35 35 SER B 245 GLY B 257 1 13
HELIX 36 36 ALA B 265 GLY B 269 1 5
HELIX 37 37 GLY B 269 THR B 280 1 12
HELIX 38 38 ILE B 291 PHE B 294 1 4
HELIX 39 39 HIS B 303 GLY B 315 1 13
HELIX 40 40 PRO B 331 LYS B 344 1 14
HELIX 41 41 THR B 364 GLY B 373 1 10
HELIX 42 42 GLY B 391 GLN B 408 1 18
HELIX 43 43 SER B 411 GLU B 417 1 7
HELIX 44 44 HIS B 419 GLN B 428 1 10
SHEET 1 A 5 LYS A 66 LEU A 76 0
SHEET 2 A 5 ILE A 91 PRO A 101 -1 O ARG A 95 N GLU A 71
SHEET 3 A 5 TYR A 21 VAL A 31 -1 N LEU A 22 O HIS A 100
SHEET 4 A 5 VAL A 129 HIS A 136 -1 O LYS A 131 N TYR A 27
SHEET 5 A 5 GLY A 301 ILE A 302 1 O GLY A 301 N VAL A 130
SHEET 1 B 8 LEU A 353 GLY A 357 0
SHEET 2 B 8 ALA A 318 PRO A 322 1 N MET A 321 O GLY A 357
SHEET 3 B 8 LEU A 284 HIS A 287 1 N GLY A 286 O ILE A 320
SHEET 4 B 8 ALA A 260 ASN A 264 1 N LEU A 261 O ILE A 285
SHEET 5 B 8 ILE A 234 ASN A 238 1 N ALA A 237 O LEU A 262
SHEET 6 B 8 ILE A 196 LYS A 198 1 N ALA A 197 O ILE A 234
SHEET 7 B 8 ILE A 166 VAL A 170 1 N GLY A 169 O ILE A 196
SHEET 8 B 8 GLY A 378 PHE A 379 1 O PHE A 379 N PHE A 168
SHEET 1 C 5 LYS B 66 LEU B 76 0
SHEET 2 C 5 ILE B 91 PRO B 101 -1 O ARG B 95 N GLU B 71
SHEET 3 C 5 TYR B 21 VAL B 31 -1 N LEU B 22 O HIS B 100
SHEET 4 C 5 VAL B 129 HIS B 136 -1 O LYS B 131 N TYR B 27
SHEET 5 C 5 GLY B 301 ILE B 302 1 O GLY B 301 N VAL B 130
SHEET 1 D 8 LEU B 353 GLY B 357 0
SHEET 2 D 8 ALA B 318 PRO B 322 1 N MET B 321 O GLY B 357
SHEET 3 D 8 LEU B 284 HIS B 287 1 N GLY B 286 O ILE B 320
SHEET 4 D 8 ALA B 260 ASN B 264 1 N LEU B 261 O ILE B 285
SHEET 5 D 8 ILE B 234 ASN B 238 1 N ALA B 237 O LEU B 262
SHEET 6 D 8 ILE B 196 LYS B 198 1 N ALA B 197 O ILE B 234
SHEET 7 D 8 ILE B 166 VAL B 170 1 N GLY B 169 O LYS B 198
SHEET 8 D 8 GLY B 378 PHE B 379 1 O PHE B 379 N PHE B 168
CISPEP 1 LYS A 172 PRO A 173 0 10.14
CISPEP 2 LYS B 172 PRO B 173 0 -2.17
CRYST1 67.348 78.451 90.369 90.00 99.95 90.00 P 1 21 1 4
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 0.014848 0.000000 0.002605 0.00000
SCALE2 0.000000 0.012747 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011235 0.00000
(ATOM LINES ARE NOT SHOWN.)
END