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HEADER HYDROLASE/SIGNALING PROTEIN/PROTEIN BIND02-FEB-16 5HZG
TITLE THE CRYSTAL STRUCTURE OF THE STRIGOLACTONE-INDUCED ATD14-D3-ASK1
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRIGOLACTONE ESTERASE D14;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: PROTEIN DWARF 14,ATD14;
COMPND 5 EC: 3.1.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: F-BOX/LRR-REPEAT MAX2 HOMOLOG;
COMPND 9 CHAIN: B, F;
COMPND 10 SYNONYM: F-BOX AND LEUCINE-RICH REPEAT MAX2 HOMOLOG,PROTEIN DWARF 3;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: SKP1-LIKE PROTEIN 1A;
COMPND 14 CHAIN: C, G;
COMPND 15 SYNONYM: SKP1-LIKE 1,UFO-BINDING PROTEIN 1;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: D14, AT3G03990, T11I18.10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ORYZA SATIVA SUBSP. JAPONICA;
SOURCE 11 ORGANISM_COMMON: RICE;
SOURCE 12 ORGANISM_TAXID: 39947;
SOURCE 13 GENE: D3, OS06G0154200, LOC_OS06G06050, OSJNBA0085L11.6-1;
SOURCE 14 EXPRESSION_SYSTEM: INSECT CELL EXPRESSION VECTOR PTIE1;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 266783;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 19 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 20 ORGANISM_TAXID: 3702;
SOURCE 21 GENE: SKP1A, ASK1, SKP1, UIP1, AT1G75950, T4O12.17;
SOURCE 22 EXPRESSION_SYSTEM: INSECT CELL EXPRESSION VECTOR PTIE1;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 266783;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS F-BOX PROTEIN, RECEPTOR, HYDROLASE-SIGNALING PROTEIN-PROTEIN BINDING
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.F.YAO,Z.H.MING,L.M.YAN,Z.H.RAO,Z.Y.LOU,D.X.XIE
REVDAT 1 03-AUG-16 5HZG 0
JRNL AUTH R.F.YAO,Z.H.MING,L.M.YAN,Z.H.RAO,Z.Y.LOU,D.X.XIE
JRNL TITL DWARF14 IS A NON-CANONICAL HORMONE RECEPTOR FOR
JRNL TITL 2 STRIGOLACTONE
JRNL REF NATURE 2016
JRNL REFN ESSN 1476-4687
JRNL DOI 10.1038/NATURE19073
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 49674
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) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2669
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) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3640
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.3630
REMARK 3 BIN FREE R VALUE SET COUNT : 194
REMARK 3 BIN FREE R VALUE : 0.4090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15638
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.03000
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): 0.597
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.504
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.208
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.875
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.801
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15976 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 15363 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21701 ; 1.781 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35275 ; 1.151 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1985 ;10.662 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 700 ;37.930 ;23.014
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2628 ;22.179 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 134 ;17.013 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2506 ; 0.149 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17847 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3655 ; 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): 8000 ; 5.502 ; 8.852
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7999 ; 5.494 ; 8.853
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9965 ; 9.030 ;13.263
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 9966 ; 9.032 ;13.262
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7976 ; 4.868 ; 9.087
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7974 ; 4.867 ; 9.087
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 11736 ; 8.264 ;13.505
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 17662 ;13.773 ;69.377
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 17663 ;13.772 ;69.378
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 5HZG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000217974.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-SEP-14
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49674
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 19.82
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 3350, 16MM BICINE PH 9.0, 20MM
REMARK 280 HEPES PH 7.5, 4.4% W/V POLYACRYLIC ACID 5100 SODIUM SALT, 10MM
REMARK 280 PRASEODYMIUM (III) ACETATE HYDRATE, 100 MM NDSB-256, EVAPORATION,
REMARK 280 TEMPERATURE 291K
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 53.19850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.42250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.48950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.42250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.19850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 86.48950
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G
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 SER A 2
REMARK 465 GLN A 3
REMARK 465 HIS A 4
REMARK 465 ASP A 218
REMARK 465 VAL A 219
REMARK 465 SER A 220
REMARK 465 VAL A 221
REMARK 465 PRO A 222
REMARK 465 ARG A 267
REMARK 465 GLY B -19
REMARK 465 ALA B -18
REMARK 465 MET B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 ILE B -13
REMARK 465 GLN B -12
REMARK 465 ARG B -11
REMARK 465 PRO B -10
REMARK 465 THR B -9
REMARK 465 SER B -8
REMARK 465 THR B -7
REMARK 465 SER B -6
REMARK 465 SER B -5
REMARK 465 LEU B -4
REMARK 465 VAL B -3
REMARK 465 ALA B -2
REMARK 465 ALA B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 VAL B 7
REMARK 465 GLU B 8
REMARK 465 GLU B 9
REMARK 465 GLY B 10
REMARK 465 ARG B 11
REMARK 465 SER B 12
REMARK 465 SER B 13
REMARK 465 SER B 14
REMARK 465 SER B 15
REMARK 465 ALA B 16
REMARK 465 ILE B 17
REMARK 465 LEU B 18
REMARK 465 ASP B 19
REMARK 465 PRO B 102
REMARK 465 PRO B 103
REMARK 465 CYS B 104
REMARK 465 GLY B 105
REMARK 465 GLY B 106
REMARK 465 GLY B 107
REMARK 465 GLY B 108
REMARK 465 GLY B 109
REMARK 465 GLY B 110
REMARK 465 ALA B 111
REMARK 465 PRO B 112
REMARK 465 SER B 113
REMARK 465 ALA B 114
REMARK 465 SER B 115
REMARK 465 SER B 116
REMARK 465 SER B 117
REMARK 465 SER B 118
REMARK 465 GLY B 119
REMARK 465 MET B 120
REMARK 465 ASN B 121
REMARK 465 VAL B 122
REMARK 465 TYR B 123
REMARK 465 HIS B 124
REMARK 465 PRO B 125
REMARK 465 GLU B 126
REMARK 465 ALA B 127
REMARK 465 ALA B 302
REMARK 465 ALA B 303
REMARK 465 ALA B 304
REMARK 465 ASN B 305
REMARK 465 ILE B 306
REMARK 465 GLN B 307
REMARK 465 ARG B 308
REMARK 465 GLU B 309
REMARK 465 LEU B 467
REMARK 465 GLU B 468
REMARK 465 ILE B 469
REMARK 465 ASN B 470
REMARK 465 CYS B 471
REMARK 465 VAL B 472
REMARK 465 TRP B 473
REMARK 465 ASN B 474
REMARK 465 THR B 475
REMARK 465 THR B 476
REMARK 465 GLU B 477
REMARK 465 GLN B 478
REMARK 465 PRO B 479
REMARK 465 CYS B 480
REMARK 465 SER B 481
REMARK 465 VAL B 482
REMARK 465 ALA B 483
REMARK 465 ASN B 484
REMARK 465 GLY B 485
REMARK 465 THR B 486
REMARK 465 THR B 487
REMARK 465 THR B 488
REMARK 465 GLU B 489
REMARK 465 CYS B 490
REMARK 465 ASP B 491
REMARK 465 PRO B 492
REMARK 465 GLU B 493
REMARK 465 ASP B 494
REMARK 465 ASP B 495
REMARK 465 GLU B 496
REMARK 465 LEU B 497
REMARK 465 GLY B 498
REMARK 465 GLU B 499
REMARK 465 VAL B 500
REMARK 465 TYR B 501
REMARK 465 GLU B 502
REMARK 465 SER B 503
REMARK 465 ALA B 504
REMARK 465 ALA B 505
REMARK 465 LYS B 506
REMARK 465 LYS B 507
REMARK 465 CYS B 508
REMARK 465 ARG B 509
REMARK 465 TYR B 510
REMARK 465 MET B 511
REMARK 465 GLU B 512
REMARK 465 PHE B 513
REMARK 465 ASP B 514
REMARK 465 ASP B 515
REMARK 465 LEU B 516
REMARK 465 GLY B 517
REMARK 465 ASP B 720
REMARK 465 MET C -8
REMARK 465 ASP C -7
REMARK 465 TYR C -6
REMARK 465 LYS C -5
REMARK 465 ASP C -4
REMARK 465 ASP C -3
REMARK 465 ASP C -2
REMARK 465 ASP C -1
REMARK 465 LYS C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ALA C 3
REMARK 465 LYS C 4
REMARK 465 LYS C 5
REMARK 465 ILE C 6
REMARK 465 VAL C 7
REMARK 465 SER C 11
REMARK 465 ASP C 12
REMARK 465 GLY C 13
REMARK 465 GLU C 14
REMARK 465 SER C 15
REMARK 465 PHE C 16
REMARK 465 GLU C 17
REMARK 465 VAL C 18
REMARK 465 GLU C 19
REMARK 465 THR C 28
REMARK 465 ILE C 29
REMARK 465 HIS C 31
REMARK 465 MET C 32
REMARK 465 VAL C 33
REMARK 465 GLU C 34
REMARK 465 ASP C 35
REMARK 465 ASP C 36
REMARK 465 CYS C 37
REMARK 465 VAL C 38
REMARK 465 ASP C 39
REMARK 465 ASN C 40
REMARK 465 GLY C 41
REMARK 465 VAL C 42
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 GLN E 3
REMARK 465 HIS E 4
REMARK 465 ASP E 218
REMARK 465 VAL E 219
REMARK 465 SER E 220
REMARK 465 VAL E 221
REMARK 465 PRO E 222
REMARK 465 ARG E 267
REMARK 465 GLY F -19
REMARK 465 ALA F -18
REMARK 465 MET F -17
REMARK 465 GLY F -16
REMARK 465 SER F -15
REMARK 465 GLY F -14
REMARK 465 ILE F -13
REMARK 465 GLN F -12
REMARK 465 ARG F -11
REMARK 465 PRO F -10
REMARK 465 THR F -9
REMARK 465 SER F -8
REMARK 465 THR F -7
REMARK 465 SER F -6
REMARK 465 SER F -5
REMARK 465 LEU F -4
REMARK 465 VAL F -3
REMARK 465 ALA F -2
REMARK 465 ALA F -1
REMARK 465 ALA F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 GLU F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 6
REMARK 465 VAL F 7
REMARK 465 GLU F 8
REMARK 465 GLU F 9
REMARK 465 GLY F 10
REMARK 465 ARG F 11
REMARK 465 SER F 12
REMARK 465 SER F 13
REMARK 465 SER F 14
REMARK 465 SER F 15
REMARK 465 ALA F 16
REMARK 465 PRO F 102
REMARK 465 PRO F 103
REMARK 465 CYS F 104
REMARK 465 GLY F 105
REMARK 465 GLY F 106
REMARK 465 GLY F 107
REMARK 465 GLY F 108
REMARK 465 GLY F 109
REMARK 465 GLY F 110
REMARK 465 ALA F 111
REMARK 465 PRO F 112
REMARK 465 SER F 113
REMARK 465 ALA F 114
REMARK 465 SER F 115
REMARK 465 SER F 116
REMARK 465 SER F 117
REMARK 465 SER F 118
REMARK 465 GLY F 119
REMARK 465 MET F 120
REMARK 465 ASN F 121
REMARK 465 VAL F 122
REMARK 465 TYR F 123
REMARK 465 HIS F 124
REMARK 465 PRO F 125
REMARK 465 GLU F 126
REMARK 465 ALA F 127
REMARK 465 ALA F 302
REMARK 465 ALA F 303
REMARK 465 ALA F 304
REMARK 465 ASN F 305
REMARK 465 ILE F 306
REMARK 465 GLN F 307
REMARK 465 ARG F 308
REMARK 465 GLU F 309
REMARK 465 ALA F 370
REMARK 465 SER F 371
REMARK 465 TRP F 372
REMARK 465 LEU F 373
REMARK 465 LEU F 467
REMARK 465 GLU F 468
REMARK 465 ILE F 469
REMARK 465 ASN F 470
REMARK 465 CYS F 471
REMARK 465 VAL F 472
REMARK 465 TRP F 473
REMARK 465 ASN F 474
REMARK 465 THR F 475
REMARK 465 THR F 476
REMARK 465 GLU F 477
REMARK 465 GLN F 478
REMARK 465 PRO F 479
REMARK 465 CYS F 480
REMARK 465 SER F 481
REMARK 465 VAL F 482
REMARK 465 ALA F 483
REMARK 465 ASN F 484
REMARK 465 GLY F 485
REMARK 465 THR F 486
REMARK 465 THR F 487
REMARK 465 THR F 488
REMARK 465 GLU F 489
REMARK 465 CYS F 490
REMARK 465 ASP F 491
REMARK 465 PRO F 492
REMARK 465 GLU F 493
REMARK 465 ASP F 494
REMARK 465 ASP F 495
REMARK 465 GLU F 496
REMARK 465 LEU F 497
REMARK 465 GLY F 498
REMARK 465 GLU F 499
REMARK 465 VAL F 500
REMARK 465 TYR F 501
REMARK 465 GLU F 502
REMARK 465 SER F 503
REMARK 465 ALA F 504
REMARK 465 ALA F 505
REMARK 465 LYS F 506
REMARK 465 LYS F 507
REMARK 465 CYS F 508
REMARK 465 ARG F 509
REMARK 465 TYR F 510
REMARK 465 MET F 511
REMARK 465 GLU F 512
REMARK 465 PHE F 513
REMARK 465 ASP F 514
REMARK 465 ASP F 515
REMARK 465 LEU F 516
REMARK 465 GLY F 517
REMARK 465 ASP F 720
REMARK 465 MET G -8
REMARK 465 ASP G -7
REMARK 465 TYR G -6
REMARK 465 LYS G -5
REMARK 465 ASP G -4
REMARK 465 ASP G -3
REMARK 465 ASP G -2
REMARK 465 ASP G -1
REMARK 465 LYS G 0
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 ALA G 3
REMARK 465 LYS G 4
REMARK 465 LYS G 5
REMARK 465 ILE G 6
REMARK 465 VAL G 7
REMARK 465 SER G 11
REMARK 465 ASP G 12
REMARK 465 GLY G 13
REMARK 465 GLU G 14
REMARK 465 SER G 15
REMARK 465 PHE G 16
REMARK 465 GLU G 17
REMARK 465 VAL G 18
REMARK 465 GLU G 19
REMARK 465 HIS G 31
REMARK 465 MET G 32
REMARK 465 VAL G 33
REMARK 465 GLU G 34
REMARK 465 ASP G 35
REMARK 465 ASP G 36
REMARK 465 CYS G 37
REMARK 465 VAL G 38
REMARK 465 ASP G 39
REMARK 465 ASN G 40
REMARK 465 GLY G 41
REMARK 465 VAL G 42
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 TYR A 132 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS A 133 CG ND1 CD2 CE1 NE2
REMARK 470 TYR E 132 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS E 133 CG ND1 CD2 CE1 NE2
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 B 310 O ASN B 338 1.11
REMARK 500 OD1 ASP B 394 OG1 THR B 422 1.20
REMARK 500 OG SER E 97 C5 6OM E 301 1.58
REMARK 500 NE2 HIS E 247 C3 6OM E 301 1.61
REMARK 500 O CYS B 653 CD1 LEU B 656 1.66
REMARK 500 NH2 ARG B 36 NH1 ARG B 657 1.77
REMARK 500 CE MET B 389 N CYS B 392 1.77
REMARK 500 CE MET B 389 CB CYS B 392 1.88
REMARK 500 O ARG G 134 O PHE G 137 1.90
REMARK 500 O GLU B 310 C ASN B 338 1.96
REMARK 500 N VAL A 98 O2 6OM A 301 1.96
REMARK 500 OG SER A 97 O2 6OM A 301 1.97
REMARK 500 OE2 GLU F 58 O ALA F 81 1.99
REMARK 500 OG SER E 97 O2 6OM E 301 2.00
REMARK 500 C ALA E 170 N VAL E 172 2.00
REMARK 500 O SER F 99 OG1 THR F 157 2.02
REMARK 500 CE1 HIS A 247 O1 6OM A 301 2.06
REMARK 500 O GLN F 393 OG1 THR F 396 2.06
REMARK 500 O LEU C 98 N LEU C 101 2.07
REMARK 500 O ASP B 394 CG2 THR B 422 2.08
REMARK 500 O ASP F 187 OD1 ASP F 215 2.08
REMARK 500 O ARG B 53 O SER B 57 2.08
REMARK 500 CE1 HIS A 247 C3 6OM A 301 2.08
REMARK 500 CG ASP B 394 OG1 THR B 422 2.08
REMARK 500 O LEU B 230 O ASN B 258 2.09
REMARK 500 CE1 HIS E 247 C3 6OM E 301 2.10
REMARK 500 CE MET B 389 CA CYS B 392 2.11
REMARK 500 O ALA B 567 OG1 THR B 570 2.11
REMARK 500 CB ALA E 170 CB VAL E 172 2.12
REMARK 500 CG2 THR C 97 N GLU C 100 2.12
REMARK 500 CD2 LEU F 43 OD1 ASN G 155 2.14
REMARK 500 O ASP B 544 CE1 PHE B 580 2.14
REMARK 500 O PRO F 96 CG2 THR F 158 2.15
REMARK 500 CB PRO F 92 CD2 HIS F 95 2.17
REMARK 500 C GLU B 310 O ASN B 338 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO B 186 CD PRO B 186 N 0.097
REMARK 500 PRO B 435 CD PRO B 435 N 0.196
REMARK 500 PRO F 435 CD PRO F 435 N 0.097
REMARK 500 PRO F 568 CD PRO F 568 N 0.085
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 GLY A 165 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 PRO A 169 CB - CA - C ANGL. DEV. = -26.6 DEGREES
REMARK 500 ALA A 170 CB - CA - C ANGL. DEV. = 33.7 DEGREES
REMARK 500 ALA A 170 N - CA - CB ANGL. DEV. = 13.1 DEGREES
REMARK 500 ALA A 170 N - CA - C ANGL. DEV. = -22.8 DEGREES
REMARK 500 ALA A 171 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 PRO B 65 CB - CA - C ANGL. DEV. = -14.4 DEGREES
REMARK 500 PRO B 65 N - CA - C ANGL. DEV. = 29.3 DEGREES
REMARK 500 ARG B 66 N - CA - CB ANGL. DEV. = 18.7 DEGREES
REMARK 500 PRO B 186 C - N - CA ANGL. DEV. = 14.4 DEGREES
REMARK 500 PRO B 186 CA - N - CD ANGL. DEV. = -9.6 DEGREES
REMARK 500 LEU B 237 CB - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 ALA B 238 N - CA - CB ANGL. DEV. = 16.4 DEGREES
REMARK 500 SER B 371 CB - CA - C ANGL. DEV. = -24.6 DEGREES
REMARK 500 SER B 371 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 TRP B 372 N - CA - CB ANGL. DEV. = -18.5 DEGREES
REMARK 500 TRP B 372 N - CA - C ANGL. DEV. = 27.9 DEGREES
REMARK 500 TYR B 388 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 MET B 389 CB - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 MET B 389 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 ARG B 405 CB - CA - C ANGL. DEV. = 24.7 DEGREES
REMARK 500 ARG B 405 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 CYS B 407 CB - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 CYS B 407 N - CA - C ANGL. DEV. = -20.8 DEGREES
REMARK 500 VAL B 421 CB - CA - C ANGL. DEV. = -23.1 DEGREES
REMARK 500 VAL B 421 N - CA - C ANGL. DEV. = 28.1 DEGREES
REMARK 500 ARG B 434 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG B 434 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 PRO B 435 C - N - CD ANGL. DEV. = -27.0 DEGREES
REMARK 500 PRO B 435 CA - N - CD ANGL. DEV. = -10.7 DEGREES
REMARK 500 SER B 458 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 SER B 458 N - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500 SER B 540 N - CA - CB ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP B 544 CB - CA - C ANGL. DEV. = -23.1 DEGREES
REMARK 500 ASP B 544 N - CA - C ANGL. DEV. = 26.1 DEGREES
REMARK 500 SER B 545 N - CA - CB ANGL. DEV. = 23.1 DEGREES
REMARK 500 ALA B 691 CB - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 ALA B 691 N - CA - C ANGL. DEV. = 18.0 DEGREES
REMARK 500 PRO B 692 C - N - CD ANGL. DEV. = -28.1 DEGREES
REMARK 500 PRO B 692 N - CA - CB ANGL. DEV. = -21.9 DEGREES
REMARK 500 PRO B 692 N - CD - CG ANGL. DEV. = -19.8 DEGREES
REMARK 500 PRO B 692 N - CA - C ANGL. DEV. = 39.8 DEGREES
REMARK 500 GLU B 693 CB - CA - C ANGL. DEV. = -27.3 DEGREES
REMARK 500 ASN B 694 N - CA - CB ANGL. DEV. = -23.7 DEGREES
REMARK 500 ASN B 694 N - CA - C ANGL. DEV. = 40.5 DEGREES
REMARK 500 ASP C 94 N - CA - C ANGL. DEV. = -30.0 DEGREES
REMARK 500 GLN C 95 N - CA - C ANGL. DEV. = 33.6 DEGREES
REMARK 500 LYS C 126 N - CA - CB ANGL. DEV. = -13.4 DEGREES
REMARK 500 HIS E 96 CB - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 SER E 97 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 114 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 11 49.50 39.78
REMARK 500 VAL A 15 -53.81 -124.15
REMARK 500 PHE A 28 -72.82 -82.14
REMARK 500 ARG A 68 -51.47 -132.50
REMARK 500 TYR A 69 48.60 -79.99
REMARK 500 ARG A 110 77.66 -154.31
REMARK 500 HIS A 133 81.57 -65.38
REMARK 500 HIS A 157 67.47 -113.55
REMARK 500 VAL A 164 -87.41 -112.62
REMARK 500 ASP A 167 -167.00 -168.56
REMARK 500 ALA A 170 -72.05 -81.79
REMARK 500 ASN A 181 22.81 -74.77
REMARK 500 VAL A 225 -56.55 -138.89
REMARK 500 LEU A 248 79.81 -114.85
REMARK 500 ALA A 264 71.07 -112.21
REMARK 500 ARG B 40 -77.47 -74.35
REMARK 500 CYS B 45 -153.87 -152.75
REMARK 500 MET B 48 -9.69 -54.51
REMARK 500 THR B 55 -72.09 -87.06
REMARK 500 SER B 60 -3.96 62.56
REMARK 500 PHE B 70 -154.57 -122.84
REMARK 500 HIS B 75 -73.30 -134.81
REMARK 500 LEU B 98 60.31 36.26
REMARK 500 ARG B 171 -65.43 -97.85
REMARK 500 ASP B 187 16.85 -142.54
REMARK 500 ASP B 205 79.80 -111.02
REMARK 500 HIS B 223 50.44 -141.17
REMARK 500 ALA B 228 21.54 -77.40
REMARK 500 CYS B 256 78.75 -118.62
REMARK 500 ALA B 311 -53.51 -136.13
REMARK 500 LEU B 325 77.41 -117.49
REMARK 500 LEU B 340 -80.47 -85.82
REMARK 500 LYS B 357 -65.24 -125.25
REMARK 500 ALA B 370 171.87 170.08
REMARK 500 TRP B 372 -71.44 -94.69
REMARK 500 HIS B 374 -62.22 -123.33
REMARK 500 VAL B 378 95.48 -64.47
REMARK 500 LEU B 400 7.52 -67.35
REMARK 500 ALA B 402 32.07 -79.23
REMARK 500 GLU B 439 -152.76 -141.47
REMARK 500 LEU B 447 -1.48 66.13
REMARK 500 TRP B 519 73.89 -113.12
REMARK 500 ALA B 531 -128.59 55.47
REMARK 500 PRO B 547 1.47 -64.12
REMARK 500 GLU B 550 -63.12 -107.10
REMARK 500 PRO B 566 108.20 -43.34
REMARK 500 ALA B 567 122.35 -29.02
REMARK 500 PRO B 568 132.50 -37.18
REMARK 500 LYS B 587 86.72 -165.24
REMARK 500 ALA B 597 -69.34 -94.63
REMARK 500
REMARK 500 THIS ENTRY HAS 133 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 HIS A 96 SER A 97 -30.55
REMARK 500 TRP A 155 VAL A 156 141.29
REMARK 500 PRO B 186 ASP B 187 52.84
REMARK 500 THR B 241 ASP B 242 146.46
REMARK 500 LEU B 400 ALA B 401 146.39
REMARK 500 PHE B 431 THR B 432 143.23
REMARK 500 GLU B 439 VAL B 440 -123.92
REMARK 500 ALA B 451 GLU B 452 149.63
REMARK 500 CYS B 453 LEU B 454 -145.61
REMARK 500 ASP B 544 SER B 545 -142.96
REMARK 500 ASP B 636 VAL B 637 144.46
REMARK 500 ARG E 200 GLY E 201 141.72
REMARK 500 ALA F 41 ALA F 42 32.63
REMARK 500 ALA F 42 LEU F 43 -144.35
REMARK 500 GLN F 180 ARG F 181 147.59
REMARK 500 THR F 241 ASP F 242 147.76
REMARK 500 VAL F 339 LEU F 340 -148.77
REMARK 500 HIS F 374 LEU F 375 147.65
REMARK 500 GLY F 377 VAL F 378 141.17
REMARK 500 THR F 422 SER F 423 148.51
REMARK 500 PHE F 431 THR F 432 149.11
REMARK 500 GLU F 439 VAL F 440 -115.08
REMARK 500 GLU F 452 CYS F 453 -131.47
REMARK 500 LEU F 538 ILE F 539 139.57
REMARK 500 ALA F 541 GLY F 542 149.07
REMARK 500 LEU F 543 ASP F 544 -142.43
REMARK 500 ALA F 691 PRO F 692 -142.78
REMARK 500 LEU G 98 PHE G 99 149.25
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 6OM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6OM E 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HYW RELATED DB: PDB
DBREF 5HZG A 1 267 UNP Q9SQR3 D14_ARATH 1 267
DBREF 5HZG B 1 720 UNP Q5VMP0 MAX2_ORYSJ 1 720
DBREF 5HZG C 1 160 UNP Q39255 SKP1A_ARATH 1 160
DBREF 5HZG E 1 267 UNP Q9SQR3 D14_ARATH 1 267
DBREF 5HZG F 1 720 UNP Q5VMP0 MAX2_ORYSJ 1 720
DBREF 5HZG G 1 160 UNP Q39255 SKP1A_ARATH 1 160
SEQADV 5HZG GLY B -19 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA B -18 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG MET B -17 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG GLY B -16 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER B -15 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG GLY B -14 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ILE B -13 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG GLN B -12 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ARG B -11 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG PRO B -10 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG THR B -9 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER B -8 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG THR B -7 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER B -6 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER B -5 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG LEU B -4 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG VAL B -3 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA B -2 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA B -1 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA B 0 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG MET C -8 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP C -7 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG TYR C -6 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG LYS C -5 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP C -4 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP C -3 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP C -2 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP C -1 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG LYS C 0 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG GLY F -19 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA F -18 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG MET F -17 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG GLY F -16 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER F -15 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG GLY F -14 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ILE F -13 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG GLN F -12 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ARG F -11 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG PRO F -10 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG THR F -9 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER F -8 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG THR F -7 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER F -6 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG SER F -5 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG LEU F -4 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG VAL F -3 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA F -2 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA F -1 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG ALA F 0 UNP Q5VMP0 EXPRESSION TAG
SEQADV 5HZG MET G -8 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP G -7 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG TYR G -6 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG LYS G -5 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP G -4 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP G -3 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP G -2 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG ASP G -1 UNP Q39255 EXPRESSION TAG
SEQADV 5HZG LYS G 0 UNP Q39255 EXPRESSION TAG
SEQRES 1 A 267 MET SER GLN HIS ASN ILE LEU GLU ALA LEU ASN VAL ARG
SEQRES 2 A 267 VAL VAL GLY THR GLY ASP ARG ILE LEU PHE LEU ALA HIS
SEQRES 3 A 267 GLY PHE GLY THR ASP GLN SER ALA TRP HIS LEU ILE LEU
SEQRES 4 A 267 PRO TYR PHE THR GLN ASN TYR ARG VAL VAL LEU TYR ASP
SEQRES 5 A 267 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP
SEQRES 6 A 267 PHE ASN ARG TYR THR THR LEU ASP PRO TYR VAL ASP ASP
SEQRES 7 A 267 LEU LEU ASN ILE VAL ASP SER LEU GLY ILE GLN ASN CYS
SEQRES 8 A 267 ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 A 267 ILE ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS LEU
SEQRES 10 A 267 ILE LEU ILE GLY PHE SER PRO ARG PHE LEU ASN ASP GLU
SEQRES 11 A 267 ASP TYR HIS GLY GLY PHE GLU GLU GLY GLU ILE GLU LYS
SEQRES 12 A 267 VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP VAL
SEQRES 13 A 267 HIS GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 A 267 ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 A 267 ARG PRO ASP ILE SER LEU PHE VAL SER ARG THR VAL PHE
SEQRES 16 A 267 ASN SER ASP LEU ARG GLY VAL LEU GLY LEU VAL ARG VAL
SEQRES 17 A 267 PRO THR CYS VAL ILE GLN THR ALA LYS ASP VAL SER VAL
SEQRES 18 A 267 PRO ALA SER VAL ALA GLU TYR LEU ARG SER HIS LEU GLY
SEQRES 19 A 267 GLY ASP THR THR VAL GLU THR LEU LYS THR GLU GLY HIS
SEQRES 20 A 267 LEU PRO GLN LEU SER ALA PRO ALA GLN LEU ALA GLN PHE
SEQRES 21 A 267 LEU ARG ARG ALA LEU PRO ARG
SEQRES 1 B 740 GLY ALA MET GLY SER GLY ILE GLN ARG PRO THR SER THR
SEQRES 2 B 740 SER SER LEU VAL ALA ALA ALA MET ALA GLU GLU GLU GLU
SEQRES 3 B 740 VAL GLU GLU GLY ARG SER SER SER SER ALA ILE LEU ASP
SEQRES 4 B 740 LEU PRO GLU PRO LEU LEU LEU HIS ILE LEU SER PHE LEU
SEQRES 5 B 740 THR ASP VAL ARG SER ARG HIS ARG ALA ALA LEU ALA CYS
SEQRES 6 B 740 GLY ARG MET ARG ALA ALA GLU ARG ALA THR ARG SER GLU
SEQRES 7 B 740 LEU SER LEU ARG GLY ASP PRO ARG SER PRO GLY PHE LEU
SEQRES 8 B 740 PHE LEU SER HIS ALA PHE ARG PHE PRO ALA LEU GLU HIS
SEQRES 9 B 740 LEU ASP LEU SER LEU VAL SER PRO TRP GLY HIS PRO LEU
SEQRES 10 B 740 LEU SER SER VAL PRO PRO CYS GLY GLY GLY GLY GLY GLY
SEQRES 11 B 740 ALA PRO SER ALA SER SER SER SER GLY MET ASN VAL TYR
SEQRES 12 B 740 HIS PRO GLU ALA ILE SER GLU GLN ASN ALA PHE ILE ALA
SEQRES 13 B 740 ALA ARG LEU ALA GLY CYS PHE PRO ALA VAL THR SER LEU
SEQRES 14 B 740 ALA VAL TYR CYS ARG ASP PRO THR THR LEU ALA ASN LEU
SEQRES 15 B 740 THR PRO HIS TRP GLN ALA SER LEU ARG ARG VAL LYS LEU
SEQRES 16 B 740 VAL ARG TRP HIS GLN ARG PRO PRO THR LEU PRO ASP GLY
SEQRES 17 B 740 ALA ASP LEU GLU PRO LEU LEU GLU THR CYS ALA ALA LEU
SEQRES 18 B 740 ARG GLU LEU ASP LEU SER GLU PHE TYR CYS TRP THR GLU
SEQRES 19 B 740 ASP VAL VAL ARG ALA LEU THR THR HIS PRO SER ALA THR
SEQRES 20 B 740 ALA ALA LEU THR HIS LEU ASP LEU GLY LEU ALA ALA ALA
SEQRES 21 B 740 THR ASP GLY PHE LYS SER SER GLU LEU GLY PRO ILE ALA
SEQRES 22 B 740 ALA SER CYS PRO ASN LEU ARG LYS LEU VAL ALA PRO CYS
SEQRES 23 B 740 LEU PHE ASN PRO ARG PHE SER ASP CYS VAL GLY ASP ASP
SEQRES 24 B 740 ALA LEU LEU SER LEU ALA THR SER CYS PRO ARG LEU THR
SEQRES 25 B 740 VAL LEU ARG LEU SER GLU PRO PHE GLU ALA ALA ALA ASN
SEQRES 26 B 740 ILE GLN ARG GLU GLU ALA ALA ILE THR VAL ALA GLY LEU
SEQRES 27 B 740 VAL ALA PHE PHE ALA ALA LEU PRO ALA LEU GLU ASP PHE
SEQRES 28 B 740 THR MET ASP LEU GLN HIS ASN VAL LEU GLU ALA ALA PRO
SEQRES 29 B 740 ALA MET GLU ALA LEU ALA ARG ARG CYS PRO ARG ILE LYS
SEQRES 30 B 740 PHE LEU THR LEU GLY SER PHE GLN GLY LEU CYS LYS ALA
SEQRES 31 B 740 SER TRP LEU HIS LEU ASP GLY VAL ALA VAL CYS GLY GLY
SEQRES 32 B 740 LEU GLU SER LEU TYR MET LYS ASN CYS GLN ASP LEU THR
SEQRES 33 B 740 ASP ALA SER LEU ALA ALA ILE GLY ARG GLY CYS ARG ARG
SEQRES 34 B 740 LEU ALA LYS PHE GLY ILE HIS GLY CYS ASP LEU VAL THR
SEQRES 35 B 740 SER ALA GLY ILE ARG ARG LEU ALA PHE THR LEU ARG PRO
SEQRES 36 B 740 THR LEU LYS GLU VAL THR VAL LEU HIS CYS ARG LEU LEU
SEQRES 37 B 740 HIS THR ALA GLU CYS LEU THR ALA LEU SER PRO ILE ARG
SEQRES 38 B 740 ASP ARG ILE GLU SER LEU GLU ILE ASN CYS VAL TRP ASN
SEQRES 39 B 740 THR THR GLU GLN PRO CYS SER VAL ALA ASN GLY THR THR
SEQRES 40 B 740 THR GLU CYS ASP PRO GLU ASP ASP GLU LEU GLY GLU VAL
SEQRES 41 B 740 TYR GLU SER ALA ALA LYS LYS CYS ARG TYR MET GLU PHE
SEQRES 42 B 740 ASP ASP LEU GLY SER TRP GLU MET LEU ARG SER LEU SER
SEQRES 43 B 740 LEU TRP PHE SER ALA GLY GLN LEU LEU SER PRO LEU ILE
SEQRES 44 B 740 SER ALA GLY LEU ASP SER CYS PRO VAL LEU GLU GLU ILE
SEQRES 45 B 740 SER ILE LYS VAL GLU GLY ASP CYS ARG THR CYS PRO ARG
SEQRES 46 B 740 PRO ALA PRO ARG THR ILE PHE GLY LEU SER ASP LEU ALA
SEQRES 47 B 740 GLY PHE PRO VAL LEU ALA LYS MET LYS LEU ASP LEU SER
SEQRES 48 B 740 GLU ALA VAL GLY TYR ALA LEU THR ALA PRO THR GLY GLN
SEQRES 49 B 740 MET ASP LEU SER LEU TRP GLU ARG PHE TYR LEU HIS GLY
SEQRES 50 B 740 ILE GLU SER LEU GLN THR LEU TYR GLU LEU ASP TYR TRP
SEQRES 51 B 740 PRO PRO GLN ASP LYS ASP VAL HIS HIS ARG SER LEU THR
SEQRES 52 B 740 LEU PRO ALA VAL GLY LEU ILE GLN ARG CYS VAL GLY LEU
SEQRES 53 B 740 ARG LYS LEU PHE ILE HIS GLY THR THR HIS GLU HIS PHE
SEQRES 54 B 740 MET THR PHE PHE LEU SER ILE PRO ASN LEU ARG ASP MET
SEQRES 55 B 740 GLN LEU ARG GLU ASP TYR TYR PRO ALA PRO GLU ASN ASP
SEQRES 56 B 740 LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU ARG
SEQRES 57 B 740 PHE GLU VAL GLN LEU ASN SER ARG GLN ILE ASP ASP
SEQRES 1 C 169 MET ASP TYR LYS ASP ASP ASP ASP LYS MET SER ALA LYS
SEQRES 2 C 169 LYS ILE VAL LEU LYS SER SER ASP GLY GLU SER PHE GLU
SEQRES 3 C 169 VAL GLU GLU ALA VAL ALA LEU GLU SER GLN THR ILE ALA
SEQRES 4 C 169 HIS MET VAL GLU ASP ASP CYS VAL ASP ASN GLY VAL PRO
SEQRES 5 C 169 LEU PRO ASN VAL THR SER LYS ILE LEU ALA LYS VAL ILE
SEQRES 6 C 169 GLU TYR CYS LYS ARG HIS VAL GLU ALA ALA ALA SER LYS
SEQRES 7 C 169 ALA GLU ALA VAL GLU GLY ALA ALA THR SER ASP ASP ASP
SEQRES 8 C 169 LEU LYS ALA TRP ASP ALA ASP PHE MET LYS ILE ASP GLN
SEQRES 9 C 169 ALA THR LEU PHE GLU LEU ILE LEU ALA ALA ASN TYR LEU
SEQRES 10 C 169 ASN ILE LYS ASN LEU LEU ASP LEU THR CYS GLN THR VAL
SEQRES 11 C 169 ALA ASP MET ILE LYS GLY LYS THR PRO GLU GLU ILE ARG
SEQRES 12 C 169 THR THR PHE ASN ILE LYS ASN ASP PHE THR PRO GLU GLU
SEQRES 13 C 169 GLU GLU GLU VAL ARG ARG GLU ASN GLN TRP ALA PHE GLU
SEQRES 1 E 267 MET SER GLN HIS ASN ILE LEU GLU ALA LEU ASN VAL ARG
SEQRES 2 E 267 VAL VAL GLY THR GLY ASP ARG ILE LEU PHE LEU ALA HIS
SEQRES 3 E 267 GLY PHE GLY THR ASP GLN SER ALA TRP HIS LEU ILE LEU
SEQRES 4 E 267 PRO TYR PHE THR GLN ASN TYR ARG VAL VAL LEU TYR ASP
SEQRES 5 E 267 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP
SEQRES 6 E 267 PHE ASN ARG TYR THR THR LEU ASP PRO TYR VAL ASP ASP
SEQRES 7 E 267 LEU LEU ASN ILE VAL ASP SER LEU GLY ILE GLN ASN CYS
SEQRES 8 E 267 ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 E 267 ILE ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS LEU
SEQRES 10 E 267 ILE LEU ILE GLY PHE SER PRO ARG PHE LEU ASN ASP GLU
SEQRES 11 E 267 ASP TYR HIS GLY GLY PHE GLU GLU GLY GLU ILE GLU LYS
SEQRES 12 E 267 VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP VAL
SEQRES 13 E 267 HIS GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 E 267 ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 E 267 ARG PRO ASP ILE SER LEU PHE VAL SER ARG THR VAL PHE
SEQRES 16 E 267 ASN SER ASP LEU ARG GLY VAL LEU GLY LEU VAL ARG VAL
SEQRES 17 E 267 PRO THR CYS VAL ILE GLN THR ALA LYS ASP VAL SER VAL
SEQRES 18 E 267 PRO ALA SER VAL ALA GLU TYR LEU ARG SER HIS LEU GLY
SEQRES 19 E 267 GLY ASP THR THR VAL GLU THR LEU LYS THR GLU GLY HIS
SEQRES 20 E 267 LEU PRO GLN LEU SER ALA PRO ALA GLN LEU ALA GLN PHE
SEQRES 21 E 267 LEU ARG ARG ALA LEU PRO ARG
SEQRES 1 F 740 GLY ALA MET GLY SER GLY ILE GLN ARG PRO THR SER THR
SEQRES 2 F 740 SER SER LEU VAL ALA ALA ALA MET ALA GLU GLU GLU GLU
SEQRES 3 F 740 VAL GLU GLU GLY ARG SER SER SER SER ALA ILE LEU ASP
SEQRES 4 F 740 LEU PRO GLU PRO LEU LEU LEU HIS ILE LEU SER PHE LEU
SEQRES 5 F 740 THR ASP VAL ARG SER ARG HIS ARG ALA ALA LEU ALA CYS
SEQRES 6 F 740 GLY ARG MET ARG ALA ALA GLU ARG ALA THR ARG SER GLU
SEQRES 7 F 740 LEU SER LEU ARG GLY ASP PRO ARG SER PRO GLY PHE LEU
SEQRES 8 F 740 PHE LEU SER HIS ALA PHE ARG PHE PRO ALA LEU GLU HIS
SEQRES 9 F 740 LEU ASP LEU SER LEU VAL SER PRO TRP GLY HIS PRO LEU
SEQRES 10 F 740 LEU SER SER VAL PRO PRO CYS GLY GLY GLY GLY GLY GLY
SEQRES 11 F 740 ALA PRO SER ALA SER SER SER SER GLY MET ASN VAL TYR
SEQRES 12 F 740 HIS PRO GLU ALA ILE SER GLU GLN ASN ALA PHE ILE ALA
SEQRES 13 F 740 ALA ARG LEU ALA GLY CYS PHE PRO ALA VAL THR SER LEU
SEQRES 14 F 740 ALA VAL TYR CYS ARG ASP PRO THR THR LEU ALA ASN LEU
SEQRES 15 F 740 THR PRO HIS TRP GLN ALA SER LEU ARG ARG VAL LYS LEU
SEQRES 16 F 740 VAL ARG TRP HIS GLN ARG PRO PRO THR LEU PRO ASP GLY
SEQRES 17 F 740 ALA ASP LEU GLU PRO LEU LEU GLU THR CYS ALA ALA LEU
SEQRES 18 F 740 ARG GLU LEU ASP LEU SER GLU PHE TYR CYS TRP THR GLU
SEQRES 19 F 740 ASP VAL VAL ARG ALA LEU THR THR HIS PRO SER ALA THR
SEQRES 20 F 740 ALA ALA LEU THR HIS LEU ASP LEU GLY LEU ALA ALA ALA
SEQRES 21 F 740 THR ASP GLY PHE LYS SER SER GLU LEU GLY PRO ILE ALA
SEQRES 22 F 740 ALA SER CYS PRO ASN LEU ARG LYS LEU VAL ALA PRO CYS
SEQRES 23 F 740 LEU PHE ASN PRO ARG PHE SER ASP CYS VAL GLY ASP ASP
SEQRES 24 F 740 ALA LEU LEU SER LEU ALA THR SER CYS PRO ARG LEU THR
SEQRES 25 F 740 VAL LEU ARG LEU SER GLU PRO PHE GLU ALA ALA ALA ASN
SEQRES 26 F 740 ILE GLN ARG GLU GLU ALA ALA ILE THR VAL ALA GLY LEU
SEQRES 27 F 740 VAL ALA PHE PHE ALA ALA LEU PRO ALA LEU GLU ASP PHE
SEQRES 28 F 740 THR MET ASP LEU GLN HIS ASN VAL LEU GLU ALA ALA PRO
SEQRES 29 F 740 ALA MET GLU ALA LEU ALA ARG ARG CYS PRO ARG ILE LYS
SEQRES 30 F 740 PHE LEU THR LEU GLY SER PHE GLN GLY LEU CYS LYS ALA
SEQRES 31 F 740 SER TRP LEU HIS LEU ASP GLY VAL ALA VAL CYS GLY GLY
SEQRES 32 F 740 LEU GLU SER LEU TYR MET LYS ASN CYS GLN ASP LEU THR
SEQRES 33 F 740 ASP ALA SER LEU ALA ALA ILE GLY ARG GLY CYS ARG ARG
SEQRES 34 F 740 LEU ALA LYS PHE GLY ILE HIS GLY CYS ASP LEU VAL THR
SEQRES 35 F 740 SER ALA GLY ILE ARG ARG LEU ALA PHE THR LEU ARG PRO
SEQRES 36 F 740 THR LEU LYS GLU VAL THR VAL LEU HIS CYS ARG LEU LEU
SEQRES 37 F 740 HIS THR ALA GLU CYS LEU THR ALA LEU SER PRO ILE ARG
SEQRES 38 F 740 ASP ARG ILE GLU SER LEU GLU ILE ASN CYS VAL TRP ASN
SEQRES 39 F 740 THR THR GLU GLN PRO CYS SER VAL ALA ASN GLY THR THR
SEQRES 40 F 740 THR GLU CYS ASP PRO GLU ASP ASP GLU LEU GLY GLU VAL
SEQRES 41 F 740 TYR GLU SER ALA ALA LYS LYS CYS ARG TYR MET GLU PHE
SEQRES 42 F 740 ASP ASP LEU GLY SER TRP GLU MET LEU ARG SER LEU SER
SEQRES 43 F 740 LEU TRP PHE SER ALA GLY GLN LEU LEU SER PRO LEU ILE
SEQRES 44 F 740 SER ALA GLY LEU ASP SER CYS PRO VAL LEU GLU GLU ILE
SEQRES 45 F 740 SER ILE LYS VAL GLU GLY ASP CYS ARG THR CYS PRO ARG
SEQRES 46 F 740 PRO ALA PRO ARG THR ILE PHE GLY LEU SER ASP LEU ALA
SEQRES 47 F 740 GLY PHE PRO VAL LEU ALA LYS MET LYS LEU ASP LEU SER
SEQRES 48 F 740 GLU ALA VAL GLY TYR ALA LEU THR ALA PRO THR GLY GLN
SEQRES 49 F 740 MET ASP LEU SER LEU TRP GLU ARG PHE TYR LEU HIS GLY
SEQRES 50 F 740 ILE GLU SER LEU GLN THR LEU TYR GLU LEU ASP TYR TRP
SEQRES 51 F 740 PRO PRO GLN ASP LYS ASP VAL HIS HIS ARG SER LEU THR
SEQRES 52 F 740 LEU PRO ALA VAL GLY LEU ILE GLN ARG CYS VAL GLY LEU
SEQRES 53 F 740 ARG LYS LEU PHE ILE HIS GLY THR THR HIS GLU HIS PHE
SEQRES 54 F 740 MET THR PHE PHE LEU SER ILE PRO ASN LEU ARG ASP MET
SEQRES 55 F 740 GLN LEU ARG GLU ASP TYR TYR PRO ALA PRO GLU ASN ASP
SEQRES 56 F 740 LEU MET PHE THR GLU MET ARG ALA GLU SER TRP LEU ARG
SEQRES 57 F 740 PHE GLU VAL GLN LEU ASN SER ARG GLN ILE ASP ASP
SEQRES 1 G 169 MET ASP TYR LYS ASP ASP ASP ASP LYS MET SER ALA LYS
SEQRES 2 G 169 LYS ILE VAL LEU LYS SER SER ASP GLY GLU SER PHE GLU
SEQRES 3 G 169 VAL GLU GLU ALA VAL ALA LEU GLU SER GLN THR ILE ALA
SEQRES 4 G 169 HIS MET VAL GLU ASP ASP CYS VAL ASP ASN GLY VAL PRO
SEQRES 5 G 169 LEU PRO ASN VAL THR SER LYS ILE LEU ALA LYS VAL ILE
SEQRES 6 G 169 GLU TYR CYS LYS ARG HIS VAL GLU ALA ALA ALA SER LYS
SEQRES 7 G 169 ALA GLU ALA VAL GLU GLY ALA ALA THR SER ASP ASP ASP
SEQRES 8 G 169 LEU LYS ALA TRP ASP ALA ASP PHE MET LYS ILE ASP GLN
SEQRES 9 G 169 ALA THR LEU PHE GLU LEU ILE LEU ALA ALA ASN TYR LEU
SEQRES 10 G 169 ASN ILE LYS ASN LEU LEU ASP LEU THR CYS GLN THR VAL
SEQRES 11 G 169 ALA ASP MET ILE LYS GLY LYS THR PRO GLU GLU ILE ARG
SEQRES 12 G 169 THR THR PHE ASN ILE LYS ASN ASP PHE THR PRO GLU GLU
SEQRES 13 G 169 GLU GLU GLU VAL ARG ARG GLU ASN GLN TRP ALA PHE GLU
HET 6OM A 301 7
HET 6OM E 301 7
HETNAM 6OM (2Z)-2-METHYLBUT-2-ENE-1,4-DIOL
FORMUL 7 6OM 2(C5 H10 O2)
FORMUL 9 HOH *24(H2 O)
HELIX 1 AA1 ASN A 5 LEU A 10 1 6
HELIX 2 AA2 ASP A 31 HIS A 36 5 6
HELIX 3 AA3 ILE A 38 PHE A 42 5 5
HELIX 4 AA4 LEU A 72 GLY A 87 1 16
HELIX 5 AA5 SER A 97 ARG A 110 1 14
HELIX 6 AA6 GLU A 137 VAL A 156 1 20
HELIX 7 AA7 ALA A 171 THR A 178 1 8
HELIX 8 AA8 LEU A 179 MET A 182 5 4
HELIX 9 AA9 ARG A 183 ASN A 196 1 14
HELIX 10 AB1 VAL A 202 VAL A 206 5 5
HELIX 11 AB2 VAL A 225 LEU A 233 1 9
HELIX 12 AB3 ALA A 253 ALA A 264 1 12
HELIX 13 AB4 LEU B 24 SER B 30 1 7
HELIX 14 AB5 ASP B 34 ALA B 41 1 8
HELIX 15 AB6 GLY B 46 ALA B 51 1 6
HELIX 16 AB7 SER B 129 PHE B 143 1 15
HELIX 17 AB8 PRO B 156 ASN B 161 1 6
HELIX 18 AB9 LEU B 162 GLN B 167 1 6
HELIX 19 AC1 LEU B 191 CYS B 198 1 8
HELIX 20 AC2 TRP B 212 THR B 222 1 11
HELIX 21 AC3 HIS B 223 ALA B 228 1 6
HELIX 22 AC4 LYS B 245 CYS B 256 1 12
HELIX 23 AC5 GLY B 277 CYS B 288 1 12
HELIX 24 AC6 THR B 314 LEU B 325 1 12
HELIX 25 AC7 ALA B 342 CYS B 353 1 12
HELIX 26 AC8 GLN B 393 LEU B 400 1 8
HELIX 27 AC9 ALA B 401 GLY B 404 5 4
HELIX 28 AD1 VAL B 421 ALA B 430 1 10
HELIX 29 AD2 LEU B 535 SER B 540 1 6
HELIX 30 AD3 ASP B 559 CYS B 563 5 5
HELIX 31 AD4 GLY B 573 GLY B 579 5 7
HELIX 32 AD5 ASP B 606 HIS B 616 1 11
HELIX 33 AD6 GLY B 617 LEU B 621 5 5
HELIX 34 AD7 THR B 643 ARG B 652 1 10
HELIX 35 AD8 HIS B 666 THR B 671 1 6
HELIX 36 AD9 PHE B 672 ILE B 676 5 5
HELIX 37 AE1 ARG B 702 ASN B 714 1 13
HELIX 38 AE2 THR C 48 GLU C 71 1 24
HELIX 39 AE3 ALA C 85 MET C 91 1 7
HELIX 40 AE4 LEU C 98 LEU C 108 1 11
HELIX 41 AE5 ILE C 110 ASP C 123 1 14
HELIX 42 AE6 THR C 129 PHE C 137 1 9
HELIX 43 AE7 THR C 144 ARG C 153 1 10
HELIX 44 AE8 GLU C 154 ALA C 158 5 5
HELIX 45 AE9 ILE E 6 LEU E 10 1 5
HELIX 46 AF1 ASP E 31 PHE E 42 5 12
HELIX 47 AF2 ASN E 60 PHE E 64 5 5
HELIX 48 AF3 LEU E 72 LEU E 86 1 15
HELIX 49 AF4 VAL E 98 ARG E 110 1 13
HELIX 50 AF5 GLU E 138 HIS E 157 1 20
HELIX 51 AF6 ALA E 170 ARG E 177 1 8
HELIX 52 AF7 THR E 178 MET E 182 5 5
HELIX 53 AF8 ARG E 183 ASN E 196 1 14
HELIX 54 AF9 SER E 224 LEU E 233 1 10
HELIX 55 AG1 LEU E 248 ALA E 253 1 6
HELIX 56 AG2 ALA E 253 ARG E 263 1 11
HELIX 57 AG3 PRO F 21 SER F 30 1 10
HELIX 58 AG4 VAL F 35 ALA F 41 1 7
HELIX 59 AG5 GLY F 46 ALA F 51 1 6
HELIX 60 AG6 ALA F 51 ARG F 56 1 6
HELIX 61 AG7 SER F 88 VAL F 90 5 3
HELIX 62 AG8 GLU F 130 PHE F 143 1 14
HELIX 63 AG9 PRO F 156 THR F 163 1 8
HELIX 64 AH1 PRO F 164 GLN F 167 5 4
HELIX 65 AH2 LEU F 191 CYS F 198 1 8
HELIX 66 AH3 TRP F 212 HIS F 223 1 12
HELIX 67 AH4 HIS F 223 LEU F 230 1 8
HELIX 68 AH5 LYS F 245 CYS F 256 1 12
HELIX 69 AH6 GLY F 277 CYS F 288 1 12
HELIX 70 AH7 THR F 314 ALA F 324 1 11
HELIX 71 AH8 ALA F 342 CYS F 353 1 12
HELIX 72 AH9 GLN F 393 ALA F 398 1 6
HELIX 73 AI1 ASP F 419 ALA F 430 1 12
HELIX 74 AI2 LEU F 454 SER F 458 5 5
HELIX 75 AI3 LEU F 535 ALA F 541 1 7
HELIX 76 AI4 GLY F 573 ALA F 578 5 6
HELIX 77 AI5 ASP F 606 HIS F 616 1 11
HELIX 78 AI6 THR F 643 CYS F 653 1 11
HELIX 79 AI7 HIS F 666 THR F 671 1 6
HELIX 80 AI8 PHE F 672 SER F 675 5 4
HELIX 81 AI9 ARG F 702 ASN F 714 1 13
HELIX 82 AJ1 THR G 48 SER G 68 1 21
HELIX 83 AJ2 LYS G 84 MET G 91 1 8
HELIX 84 AJ3 PHE G 99 ASN G 109 1 11
HELIX 85 AJ4 ILE G 110 LYS G 126 1 17
HELIX 86 AJ5 THR G 129 PHE G 137 1 9
HELIX 87 AJ6 THR G 144 GLN G 156 1 13
SHEET 1 AA1 7 ARG A 13 VAL A 14 0
SHEET 2 AA1 7 ARG A 47 TYR A 51 -1 O LEU A 50 N ARG A 13
SHEET 3 AA1 7 ILE A 21 ALA A 25 1 N LEU A 22 O VAL A 49
SHEET 4 AA1 7 CYS A 91 GLY A 95 1 O VAL A 94 N ALA A 25
SHEET 5 AA1 7 PHE A 114 ILE A 120 1 O ILE A 118 N TYR A 93
SHEET 6 AA1 7 THR A 210 GLN A 214 1 O CYS A 211 N LEU A 119
SHEET 7 AA1 7 THR A 237 THR A 241 1 O THR A 238 N VAL A 212
SHEET 1 AA220 LEU B 61 GLY B 63 0
SHEET 2 AA220 HIS B 84 LEU B 87 1 O ASP B 86 N ARG B 62
SHEET 3 AA220 SER B 148 VAL B 151 1 O SER B 148 N LEU B 85
SHEET 4 AA220 ARG B 172 ARG B 177 1 O LYS B 174 N VAL B 151
SHEET 5 AA220 GLU B 203 PHE B 209 1 O GLU B 208 N ARG B 177
SHEET 6 AA220 HIS B 232 ASP B 234 1 O ASP B 234 N LEU B 204
SHEET 7 AA220 LYS B 261 PRO B 265 1 O VAL B 263 N LEU B 233
SHEET 8 AA220 VAL B 293 SER B 297 1 O ARG B 295 N ALA B 264
SHEET 9 AA220 ASP B 330 ASP B 334 1 O THR B 332 N LEU B 296
SHEET 10 AA220 LEU B 359 SER B 363 1 O GLY B 362 N MET B 333
SHEET 11 AA220 GLY B 383 TYR B 388 1 O GLY B 383 N LEU B 359
SHEET 12 AA220 ARG B 409 LYS B 412 1 O ALA B 411 N SER B 386
SHEET 13 AA220 PRO B 435 LYS B 438 1 O LEU B 437 N LYS B 412
SHEET 14 AA220 ARG B 461 GLU B 465 1 O ARG B 463 N THR B 436
SHEET 15 AA220 SER B 524 SER B 530 1 O SER B 526 N ASP B 462
SHEET 16 AA220 GLU B 551 GLU B 557 1 O SER B 553 N LEU B 527
SHEET 17 AA220 LEU B 588 ASP B 589 1 O ASP B 589 N ILE B 554
SHEET 18 AA220 GLU B 626 TRP B 630 1 O ASP B 628 N LEU B 588
SHEET 19 AA220 LYS B 658 ILE B 661 1 O PHE B 660 N TYR B 629
SHEET 20 AA220 ASP B 681 LEU B 684 1 O ASP B 681 N LEU B 659
SHEET 1 AA3 2 VAL B 594 GLY B 595 0
SHEET 2 AA3 2 GLN B 633 ASP B 634 1 O GLN B 633 N GLY B 595
SHEET 1 AA4 7 ARG E 13 VAL E 14 0
SHEET 2 AA4 7 ARG E 47 LEU E 50 -1 O LEU E 50 N ARG E 13
SHEET 3 AA4 7 ILE E 21 ALA E 25 1 N LEU E 22 O ARG E 47
SHEET 4 AA4 7 CYS E 91 GLY E 95 1 O VAL E 94 N PHE E 23
SHEET 5 AA4 7 PHE E 114 ILE E 120 1 O ILE E 120 N GLY E 95
SHEET 6 AA4 7 THR E 210 GLN E 214 1 O ILE E 213 N LEU E 119
SHEET 7 AA4 7 THR E 237 THR E 241 1 O GLU E 240 N GLN E 214
SHEET 1 AA5 2 LEU E 127 ASN E 128 0
SHEET 2 AA5 2 PHE E 136 GLU E 137 1 N PHE E 136 O ASN E 128
SHEET 1 AA6 5 LEU F 61 GLY F 63 0
SHEET 2 AA6 5 HIS F 84 ASP F 86 1 O ASP F 86 N ARG F 62
SHEET 3 AA6 5 LEU F 149 TYR F 152 1 O ALA F 150 N LEU F 85
SHEET 4 AA6 5 ARG F 172 ARG F 177 1 O LYS F 174 N LEU F 149
SHEET 5 AA6 5 GLU F 208 PHE F 209 1 O GLU F 208 N ARG F 177
SHEET 1 AA716 LEU F 61 GLY F 63 0
SHEET 2 AA716 HIS F 84 ASP F 86 1 O ASP F 86 N ARG F 62
SHEET 3 AA716 LEU F 149 TYR F 152 1 O ALA F 150 N LEU F 85
SHEET 4 AA716 ARG F 172 ARG F 177 1 O LYS F 174 N LEU F 149
SHEET 5 AA716 GLU F 203 ASP F 205 1 O ASP F 205 N VAL F 173
SHEET 6 AA716 HIS F 232 ASP F 234 1 O HIS F 232 N LEU F 204
SHEET 7 AA716 LYS F 261 PRO F 265 1 O VAL F 263 N LEU F 233
SHEET 8 AA716 VAL F 293 SER F 297 1 O ARG F 295 N ALA F 264
SHEET 9 AA716 ASP F 330 VAL F 339 1 O ASP F 334 N LEU F 296
SHEET 10 AA716 PHE F 358 PHE F 364 1 O GLY F 362 N MET F 333
SHEET 11 AA716 GLY F 383 SER F 386 1 O GLU F 385 N LEU F 361
SHEET 12 AA716 ARG F 409 LYS F 412 1 O ARG F 409 N LEU F 384
SHEET 13 AA716 PRO F 435 LYS F 438 1 O LEU F 437 N LYS F 412
SHEET 14 AA716 ARG F 461 GLU F 465 1 O ARG F 463 N THR F 436
SHEET 15 AA716 SER F 524 PHE F 529 1 O SER F 526 N ILE F 464
SHEET 16 AA716 ILE F 554 VAL F 556 1 O LYS F 555 N PHE F 529
SHEET 1 AA8 2 GLY F 558 ASP F 559 0
SHEET 2 AA8 2 ALA F 593 VAL F 594 1 O VAL F 594 N GLY F 558
SHEET 1 AA9 4 MET F 586 ASP F 589 0
SHEET 2 AA9 4 GLU F 626 TRP F 630 1 O GLU F 626 N MET F 586
SHEET 3 AA9 4 LYS F 658 ILE F 661 1 O PHE F 660 N LEU F 627
SHEET 4 AA9 4 ASP F 681 LEU F 684 1 O ASP F 681 N LEU F 659
LINK OG SER A 97 C5 6OM A 301 1555 1555 1.55
LINK NE2 HIS A 247 C3 6OM A 301 1555 1555 1.53
CISPEP 1 ASP A 131 TYR A 132 0 8.70
CISPEP 2 VAL A 156 HIS A 157 0 23.42
CISPEP 3 GLU B 22 PRO B 23 0 -13.00
CISPEP 4 LEU B 32 THR B 33 0 -12.64
CISPEP 5 ALA B 41 ALA B 42 0 28.01
CISPEP 6 SER B 91 PRO B 92 0 -4.79
CISPEP 7 GLU B 310 ALA B 311 0 1.05
CISPEP 8 SER B 371 TRP B 372 0 21.42
CISPEP 9 GLU B 557 GLY B 558 0 4.23
CISPEP 10 TYR B 689 PRO B 690 0 -3.32
CISPEP 11 GLU B 693 ASN B 694 0 -6.47
CISPEP 12 GLU C 71 ALA C 72 0 -9.17
CISPEP 13 ALA C 76 ALA C 77 0 -2.58
CISPEP 14 ALA C 96 THR C 97 0 -0.96
CISPEP 15 THR C 97 LEU C 98 0 -2.11
CISPEP 16 ASP E 131 TYR E 132 0 22.14
CISPEP 17 LEU F 32 THR F 33 0 -9.33
CISPEP 18 SER F 91 PRO F 92 0 -6.94
CISPEP 19 GLU F 310 ALA F 311 0 0.12
CISPEP 20 GLN F 604 MET F 605 0 -1.09
CISPEP 21 TYR F 689 PRO F 690 0 4.37
CISPEP 22 ASN F 694 ASP F 695 0 -21.45
CISPEP 23 GLU G 71 ALA G 72 0 -4.85
CISPEP 24 ALA G 76 ALA G 77 0 -15.24
CISPEP 25 ALA G 96 THR G 97 0 6.45
CISPEP 26 THR G 97 LEU G 98 0 -6.49
SITE 1 AC1 4 PHE A 28 SER A 97 VAL A 98 HIS A 247
SITE 1 AC2 5 PHE E 28 HIS E 96 SER E 97 VAL E 98
SITE 2 AC2 5 HIS E 247
CRYST1 106.397 172.979 186.845 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009399 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005781 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005352 0.00000
TER 2002 PRO A 266
TER 6794 ASP B 719
TER 7819 GLU C 160
TER 9821 PRO E 266
TER 14604 ASP F 719
TER 15644 GLU G 160
MASTER 872 0 2 87 65 0 3 615676 6 16 182
END |