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HEADER BIOSYNTHETIC PROTEIN 19-NOV-24 9KNJ
TITLE CRYSTAL STRUCTURE OF GLYCEROL-BOUND FULL-LENGTH PHA SYNTHASE (PHAC)
TITLE 2 FROM AEROMONAS CAVIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHA SYNTHASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROMONAS CAVIAE;
SOURCE 3 ORGANISM_TAXID: 648;
SOURCE 4 GENE: PHAC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHA SYNTHASE, FULL-LENGTH PHAC STRUCTURE, DIMER, TUNNEL, CATALYTIC
KEYWDS 2 TRIAD, GLYCEROL, POLYHYDROXYALKANOATE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.CHEK,S.Y.KIM,T.MORI,T.HAKOSHIMA
REVDAT 1 21-MAY-25 9KNJ 0
JRNL AUTH M.F.CHEK,S.Y.KIM,T.MORI,K.MATSUMOTO,S.SATO,T.HAKOSHIMA
JRNL TITL STRUCTURES OF POLYHYDROXYALKANOATE SYNTHASE PHAC FROM
JRNL TITL 2 AEROMONAS CAVIAE, PRODUCING BIODEGRADABLE PLASTICS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 04626 2025
JRNL REFN ESSN 1521-3773
JRNL PMID 40276819
JRNL DOI 10.1002/ANIE.202504626
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 58604
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.370
REMARK 3 FREE R VALUE TEST SET COUNT : 3808
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 8.0900 - 6.4200 0.99 4061 144 0.1888 0.2697
REMARK 3 2 6.4200 - 5.6100 0.97 3997 153 0.2096 0.1873
REMARK 3 3 5.6100 - 5.1000 0.99 4035 122 0.1864 0.2173
REMARK 3 4 5.1000 - 4.7400 0.99 4121 136 0.1721 0.2299
REMARK 3 5 4.7400 - 4.4600 0.99 4045 158 0.1653 0.1747
REMARK 3 6 4.4600 - 4.2300 0.99 4044 153 0.1786 0.2284
REMARK 3 7 4.2300 - 4.0500 0.98 4054 161 0.1868 0.2697
REMARK 3 8 4.0500 - 3.8900 0.96 3932 145 0.2057 0.2404
REMARK 3 9 3.8900 - 3.7600 0.97 4014 121 0.2217 0.2752
REMARK 3 10 3.7600 - 3.6400 0.98 4013 134 0.2212 0.2370
REMARK 3 11 3.6400 - 3.5400 0.98 4001 144 0.2246 0.2637
REMARK 3 12 3.5400 - 3.4400 0.97 4050 124 0.2343 0.2675
REMARK 3 13 3.4400 - 3.3600 0.97 3997 162 0.2313 0.2807
REMARK 3 14 3.3600 - 3.2800 0.98 3955 128 0.2479 0.3291
REMARK 3 15 3.2800 - 3.2100 0.98 4075 152 0.2754 0.3895
REMARK 3 16 3.2100 - 3.1500 0.98 4044 132 0.2897 0.3526
REMARK 3 17 3.1500 - 3.0900 0.98 4058 145 0.2856 0.3191
REMARK 3 18 3.0900 - 3.0400 0.99 4034 151 0.2795 0.3252
REMARK 3 19 3.0400 - 2.9800 0.99 4046 130 0.2773 0.3396
REMARK 3 20 2.9800 - 2.9400 0.99 4101 154 0.2855 0.3223
REMARK 3 21 2.9400 - 2.8900 0.99 4100 120 0.2849 0.3141
REMARK 3 22 2.8900 - 2.8500 0.99 4076 155 0.2838 0.3666
REMARK 3 23 2.8500 - 2.8100 0.99 4028 130 0.3039 0.3416
REMARK 3 24 2.8100 - 2.7700 0.99 4102 148 0.3372 0.3932
REMARK 3 25 2.7700 - 2.7300 0.99 4035 133 0.3442 0.3847
REMARK 3 26 2.7300 - 2.7000 0.98 4028 146 0.3666 0.3866
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.878
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 13127
REMARK 3 ANGLE : 0.761 17820
REMARK 3 CHIRALITY : 0.051 1963
REMARK 3 PLANARITY : 0.005 2298
REMARK 3 DIHEDRAL : 16.548 4791
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 5 through 40 or
REMARK 3 resid 53 through 77 or resid 105 through
REMARK 3 166 or resid 171 through 194 or resid 203
REMARK 3 through 553 or resid 558 through 583 or
REMARK 3 resid 603))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 5 through 77 or
REMARK 3 resid 105 through 166 or resid 171
REMARK 3 through 194 or resid 203 through 553 or
REMARK 3 resid 558 through 583 or resid 603))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and (resid 5 through 40 or
REMARK 3 resid 53 through 77 or resid 105 through
REMARK 3 194 or resid 203 through 601))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9KNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1300053598.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999994
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59959
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.680
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.57400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, GLYCEROL, PEG6000,
REMARK 280 OCTYL BETA-D-GLUCOPYRANOSIDE, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 78.51600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.03550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.51600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.03550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 GLY A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 PRO A 4
REMARK 465 GLY A 44
REMARK 465 GLN A 45
REMARK 465 VAL A 46
REMARK 465 LEU A 47
REMARK 465 GLU A 48
REMARK 465 GLN A 49
REMARK 465 GLY A 50
REMARK 465 GLY A 81
REMARK 465 GLN A 82
REMARK 465 PRO A 83
REMARK 465 SER A 84
REMARK 465 GLU A 85
REMARK 465 PRO A 86
REMARK 465 VAL A 87
REMARK 465 ILE A 88
REMARK 465 THR A 89
REMARK 465 PRO A 90
REMARK 465 GLU A 91
REMARK 465 ARG A 92
REMARK 465 SER A 93
REMARK 465 ASP A 94
REMARK 465 ARG A 95
REMARK 465 ARG A 96
REMARK 465 PHE A 97
REMARK 465 LYS A 98
REMARK 465 ALA A 99
REMARK 465 GLU A 100
REMARK 465 ALA A 101
REMARK 465 TRP A 102
REMARK 465 SER A 103
REMARK 465 GLU A 104
REMARK 465 ILE A 195
REMARK 465 ARG A 196
REMARK 465 LEU A 197
REMARK 465 GLU A 555
REMARK 465 ALA A 586
REMARK 465 CYS A 587
REMARK 465 PRO A 588
REMARK 465 THR A 589
REMARK 465 GLU A 590
REMARK 465 GLU A 591
REMARK 465 ASP A 592
REMARK 465 ALA A 593
REMARK 465 ALA A 594
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 PRO B 4
REMARK 465 ASP B 41
REMARK 465 ASP B 42
REMARK 465 LEU B 43
REMARK 465 GLY B 44
REMARK 465 GLN B 45
REMARK 465 VAL B 46
REMARK 465 LEU B 47
REMARK 465 GLU B 48
REMARK 465 GLN B 49
REMARK 465 GLY B 50
REMARK 465 SER B 51
REMARK 465 GLN B 52
REMARK 465 LYS B 78
REMARK 465 SER B 79
REMARK 465 ALA B 80
REMARK 465 GLY B 81
REMARK 465 GLN B 82
REMARK 465 PRO B 83
REMARK 465 SER B 84
REMARK 465 GLU B 85
REMARK 465 PRO B 86
REMARK 465 VAL B 87
REMARK 465 ILE B 88
REMARK 465 THR B 89
REMARK 465 PRO B 90
REMARK 465 GLU B 91
REMARK 465 ARG B 92
REMARK 465 SER B 93
REMARK 465 ASP B 94
REMARK 465 ARG B 95
REMARK 465 ARG B 96
REMARK 465 PHE B 97
REMARK 465 LYS B 98
REMARK 465 ALA B 99
REMARK 465 GLU B 100
REMARK 465 ALA B 101
REMARK 465 TRP B 102
REMARK 465 GLU B 169
REMARK 465 SER B 170
REMARK 465 ARG B 196
REMARK 465 LEU B 197
REMARK 465 GLU B 555
REMARK 465 GLY B 556
REMARK 465 ALA B 586
REMARK 465 CYS B 587
REMARK 465 PRO B 588
REMARK 465 THR B 589
REMARK 465 GLU B 590
REMARK 465 GLU B 591
REMARK 465 ASP B 592
REMARK 465 ALA B 593
REMARK 465 ALA B 594
REMARK 465 GLY C -1
REMARK 465 PRO C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 3
REMARK 465 PRO C 4
REMARK 465 GLN C 45
REMARK 465 VAL C 46
REMARK 465 LEU C 47
REMARK 465 GLU C 48
REMARK 465 GLN C 49
REMARK 465 GLY C 50
REMARK 465 SER C 79
REMARK 465 ALA C 80
REMARK 465 GLY C 81
REMARK 465 GLN C 82
REMARK 465 PRO C 83
REMARK 465 SER C 84
REMARK 465 GLU C 85
REMARK 465 PRO C 86
REMARK 465 VAL C 87
REMARK 465 ILE C 88
REMARK 465 THR C 89
REMARK 465 PRO C 90
REMARK 465 GLU C 91
REMARK 465 ARG C 92
REMARK 465 SER C 93
REMARK 465 ASP C 94
REMARK 465 ARG C 95
REMARK 465 ARG C 96
REMARK 465 PHE C 97
REMARK 465 LYS C 98
REMARK 465 ALA C 99
REMARK 465 GLU C 100
REMARK 465 ALA C 101
REMARK 465 TRP C 102
REMARK 465 SER C 103
REMARK 465 THR C 167
REMARK 465 LEU C 168
REMARK 465 GLU C 169
REMARK 465 SER C 170
REMARK 465 ARG C 196
REMARK 465 LEU C 197
REMARK 465 THR C 198
REMARK 465 ASP C 199
REMARK 465 GLU C 200
REMARK 465 SER C 201
REMARK 465 ALA C 202
REMARK 465 ASP C 554
REMARK 465 GLU C 555
REMARK 465 GLY C 556
REMARK 465 SER C 557
REMARK 465 VAL C 584
REMARK 465 PHE C 585
REMARK 465 ALA C 586
REMARK 465 CYS C 587
REMARK 465 PRO C 588
REMARK 465 THR C 589
REMARK 465 GLU C 590
REMARK 465 GLU C 591
REMARK 465 ASP C 592
REMARK 465 ALA C 593
REMARK 465 ALA C 594
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE1 TRP A 519 OE2 GLU A 567 4446 2.14
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 GLU A 169 56.42 38.77
REMARK 500 ASN A 248 167.55 80.25
REMARK 500 MET A 255 -67.06 -92.81
REMARK 500 CYS A 319 -129.30 54.88
REMARK 500 SER A 501 -162.41 74.47
REMARK 500 TYR A 516 -163.82 -129.85
REMARK 500 THR B 231 -9.39 70.75
REMARK 500 ASN B 248 167.64 73.68
REMARK 500 TYR B 251 -7.06 -55.29
REMARK 500 MET B 255 -70.16 -63.85
REMARK 500 CYS B 319 -131.53 57.77
REMARK 500 TYR B 516 -166.36 -127.09
REMARK 500 MET C 255 -63.92 -97.25
REMARK 500 CYS C 319 -117.66 54.37
REMARK 500 SER C 501 -166.50 -123.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 553 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9KNJ A 1 594 UNP O32471 O32471_AERCA 1 594
DBREF 9KNJ B 1 594 UNP O32471 O32471_AERCA 1 594
DBREF 9KNJ C 1 594 UNP O32471 O32471_AERCA 1 594
SEQADV 9KNJ GLY A -1 UNP O32471 EXPRESSION TAG
SEQADV 9KNJ PRO A 0 UNP O32471 EXPRESSION TAG
SEQADV 9KNJ GLY B -1 UNP O32471 EXPRESSION TAG
SEQADV 9KNJ PRO B 0 UNP O32471 EXPRESSION TAG
SEQADV 9KNJ GLY C -1 UNP O32471 EXPRESSION TAG
SEQADV 9KNJ PRO C 0 UNP O32471 EXPRESSION TAG
SEQRES 1 A 596 GLY PRO MET SER GLN PRO SER TYR GLY PRO LEU PHE GLU
SEQRES 2 A 596 ALA LEU ALA HIS TYR ASN ASP LYS LEU LEU ALA MET ALA
SEQRES 3 A 596 LYS ALA GLN THR GLU ARG THR ALA GLN ALA LEU LEU GLN
SEQRES 4 A 596 THR ASN LEU ASP ASP LEU GLY GLN VAL LEU GLU GLN GLY
SEQRES 5 A 596 SER GLN GLN PRO TRP GLN LEU ILE GLN ALA GLN MET ASN
SEQRES 6 A 596 TRP TRP GLN ASP GLN LEU LYS LEU MET GLN HIS THR LEU
SEQRES 7 A 596 LEU LYS SER ALA GLY GLN PRO SER GLU PRO VAL ILE THR
SEQRES 8 A 596 PRO GLU ARG SER ASP ARG ARG PHE LYS ALA GLU ALA TRP
SEQRES 9 A 596 SER GLU GLN PRO ILE TYR ASP TYR LEU LYS GLN SER TYR
SEQRES 10 A 596 LEU LEU THR ALA ARG HIS LEU LEU ALA SER VAL ASP ALA
SEQRES 11 A 596 LEU GLU GLY VAL PRO GLN LYS SER ARG GLU ARG LEU ARG
SEQRES 12 A 596 PHE PHE THR ARG GLN TYR VAL ASN ALA MET ALA PRO SER
SEQRES 13 A 596 ASN PHE LEU ALA THR ASN PRO GLU LEU LEU LYS LEU THR
SEQRES 14 A 596 LEU GLU SER ASP GLY GLN ASN LEU VAL ARG GLY LEU ALA
SEQRES 15 A 596 LEU LEU ALA GLU ASP LEU GLU ARG SER ALA ASP GLN LEU
SEQRES 16 A 596 ASN ILE ARG LEU THR ASP GLU SER ALA PHE GLU LEU GLY
SEQRES 17 A 596 ARG ASP LEU ALA LEU THR PRO GLY ARG VAL VAL GLN ARG
SEQRES 18 A 596 THR GLU LEU TYR GLU LEU ILE GLN TYR SER PRO THR THR
SEQRES 19 A 596 GLU THR VAL GLY LYS THR PRO VAL LEU ILE VAL PRO PRO
SEQRES 20 A 596 PHE ILE ASN LYS TYR TYR ILE MET ASP MET ARG PRO GLN
SEQRES 21 A 596 ASN SER LEU VAL ALA TRP LEU VAL ALA GLN GLY GLN THR
SEQRES 22 A 596 VAL PHE MET ILE SER TRP ARG ASN PRO GLY VAL ALA GLN
SEQRES 23 A 596 ALA GLN ILE ASP LEU ASP ASP TYR VAL VAL ASP GLY VAL
SEQRES 24 A 596 ILE ALA ALA LEU ASP GLY VAL GLU ALA ALA THR GLY GLU
SEQRES 25 A 596 ARG GLU VAL HIS GLY ILE GLY TYR CYS ILE GLY GLY THR
SEQRES 26 A 596 ALA LEU SER LEU ALA MET GLY TRP LEU ALA ALA ARG ARG
SEQRES 27 A 596 GLN LYS GLN ARG VAL ARG THR ALA THR LEU PHE THR THR
SEQRES 28 A 596 LEU LEU ASP PHE SER GLN PRO GLY GLU LEU GLY ILE PHE
SEQRES 29 A 596 ILE HIS GLU PRO ILE ILE ALA ALA LEU GLU ALA GLN ASN
SEQRES 30 A 596 GLU ALA LYS GLY ILE MET ASP GLY ARG GLN LEU ALA VAL
SEQRES 31 A 596 SER PHE SER LEU LEU ARG GLU ASN SER LEU TYR TRP ASN
SEQRES 32 A 596 TYR TYR ILE ASP SER TYR LEU LYS GLY GLN SER PRO VAL
SEQRES 33 A 596 ALA PHE ASP LEU LEU HIS TRP ASN SER ASP SER THR ASN
SEQRES 34 A 596 VAL ALA GLY LYS THR HIS ASN SER LEU LEU ARG ARG LEU
SEQRES 35 A 596 TYR LEU GLU ASN GLN LEU VAL LYS GLY GLU LEU LYS ILE
SEQRES 36 A 596 ARG ASN THR ARG ILE ASP LEU GLY LYS VAL LYS THR PRO
SEQRES 37 A 596 VAL LEU LEU VAL SER ALA VAL ASP ASP HIS ILE ALA LEU
SEQRES 38 A 596 TRP GLN GLY THR TRP GLN GLY MET LYS LEU PHE GLY GLY
SEQRES 39 A 596 GLU GLN ARG PHE LEU LEU ALA GLU SER GLY HIS ILE ALA
SEQRES 40 A 596 GLY ILE ILE ASN PRO PRO ALA ALA ASN LYS TYR GLY PHE
SEQRES 41 A 596 TRP HIS ASN GLY ALA GLU ALA GLU SER PRO GLU SER TRP
SEQRES 42 A 596 LEU ALA GLY ALA THR HIS GLN GLY GLY SER TRP TRP PRO
SEQRES 43 A 596 GLU MET MET GLY PHE ILE GLN ASN ARG ASP GLU GLY SER
SEQRES 44 A 596 GLU PRO VAL PRO ALA ARG VAL PRO GLU GLU GLY LEU ALA
SEQRES 45 A 596 PRO ALA PRO GLY HIS TYR VAL LYS VAL ARG LEU ASN PRO
SEQRES 46 A 596 VAL PHE ALA CYS PRO THR GLU GLU ASP ALA ALA
SEQRES 1 B 596 GLY PRO MET SER GLN PRO SER TYR GLY PRO LEU PHE GLU
SEQRES 2 B 596 ALA LEU ALA HIS TYR ASN ASP LYS LEU LEU ALA MET ALA
SEQRES 3 B 596 LYS ALA GLN THR GLU ARG THR ALA GLN ALA LEU LEU GLN
SEQRES 4 B 596 THR ASN LEU ASP ASP LEU GLY GLN VAL LEU GLU GLN GLY
SEQRES 5 B 596 SER GLN GLN PRO TRP GLN LEU ILE GLN ALA GLN MET ASN
SEQRES 6 B 596 TRP TRP GLN ASP GLN LEU LYS LEU MET GLN HIS THR LEU
SEQRES 7 B 596 LEU LYS SER ALA GLY GLN PRO SER GLU PRO VAL ILE THR
SEQRES 8 B 596 PRO GLU ARG SER ASP ARG ARG PHE LYS ALA GLU ALA TRP
SEQRES 9 B 596 SER GLU GLN PRO ILE TYR ASP TYR LEU LYS GLN SER TYR
SEQRES 10 B 596 LEU LEU THR ALA ARG HIS LEU LEU ALA SER VAL ASP ALA
SEQRES 11 B 596 LEU GLU GLY VAL PRO GLN LYS SER ARG GLU ARG LEU ARG
SEQRES 12 B 596 PHE PHE THR ARG GLN TYR VAL ASN ALA MET ALA PRO SER
SEQRES 13 B 596 ASN PHE LEU ALA THR ASN PRO GLU LEU LEU LYS LEU THR
SEQRES 14 B 596 LEU GLU SER ASP GLY GLN ASN LEU VAL ARG GLY LEU ALA
SEQRES 15 B 596 LEU LEU ALA GLU ASP LEU GLU ARG SER ALA ASP GLN LEU
SEQRES 16 B 596 ASN ILE ARG LEU THR ASP GLU SER ALA PHE GLU LEU GLY
SEQRES 17 B 596 ARG ASP LEU ALA LEU THR PRO GLY ARG VAL VAL GLN ARG
SEQRES 18 B 596 THR GLU LEU TYR GLU LEU ILE GLN TYR SER PRO THR THR
SEQRES 19 B 596 GLU THR VAL GLY LYS THR PRO VAL LEU ILE VAL PRO PRO
SEQRES 20 B 596 PHE ILE ASN LYS TYR TYR ILE MET ASP MET ARG PRO GLN
SEQRES 21 B 596 ASN SER LEU VAL ALA TRP LEU VAL ALA GLN GLY GLN THR
SEQRES 22 B 596 VAL PHE MET ILE SER TRP ARG ASN PRO GLY VAL ALA GLN
SEQRES 23 B 596 ALA GLN ILE ASP LEU ASP ASP TYR VAL VAL ASP GLY VAL
SEQRES 24 B 596 ILE ALA ALA LEU ASP GLY VAL GLU ALA ALA THR GLY GLU
SEQRES 25 B 596 ARG GLU VAL HIS GLY ILE GLY TYR CYS ILE GLY GLY THR
SEQRES 26 B 596 ALA LEU SER LEU ALA MET GLY TRP LEU ALA ALA ARG ARG
SEQRES 27 B 596 GLN LYS GLN ARG VAL ARG THR ALA THR LEU PHE THR THR
SEQRES 28 B 596 LEU LEU ASP PHE SER GLN PRO GLY GLU LEU GLY ILE PHE
SEQRES 29 B 596 ILE HIS GLU PRO ILE ILE ALA ALA LEU GLU ALA GLN ASN
SEQRES 30 B 596 GLU ALA LYS GLY ILE MET ASP GLY ARG GLN LEU ALA VAL
SEQRES 31 B 596 SER PHE SER LEU LEU ARG GLU ASN SER LEU TYR TRP ASN
SEQRES 32 B 596 TYR TYR ILE ASP SER TYR LEU LYS GLY GLN SER PRO VAL
SEQRES 33 B 596 ALA PHE ASP LEU LEU HIS TRP ASN SER ASP SER THR ASN
SEQRES 34 B 596 VAL ALA GLY LYS THR HIS ASN SER LEU LEU ARG ARG LEU
SEQRES 35 B 596 TYR LEU GLU ASN GLN LEU VAL LYS GLY GLU LEU LYS ILE
SEQRES 36 B 596 ARG ASN THR ARG ILE ASP LEU GLY LYS VAL LYS THR PRO
SEQRES 37 B 596 VAL LEU LEU VAL SER ALA VAL ASP ASP HIS ILE ALA LEU
SEQRES 38 B 596 TRP GLN GLY THR TRP GLN GLY MET LYS LEU PHE GLY GLY
SEQRES 39 B 596 GLU GLN ARG PHE LEU LEU ALA GLU SER GLY HIS ILE ALA
SEQRES 40 B 596 GLY ILE ILE ASN PRO PRO ALA ALA ASN LYS TYR GLY PHE
SEQRES 41 B 596 TRP HIS ASN GLY ALA GLU ALA GLU SER PRO GLU SER TRP
SEQRES 42 B 596 LEU ALA GLY ALA THR HIS GLN GLY GLY SER TRP TRP PRO
SEQRES 43 B 596 GLU MET MET GLY PHE ILE GLN ASN ARG ASP GLU GLY SER
SEQRES 44 B 596 GLU PRO VAL PRO ALA ARG VAL PRO GLU GLU GLY LEU ALA
SEQRES 45 B 596 PRO ALA PRO GLY HIS TYR VAL LYS VAL ARG LEU ASN PRO
SEQRES 46 B 596 VAL PHE ALA CYS PRO THR GLU GLU ASP ALA ALA
SEQRES 1 C 596 GLY PRO MET SER GLN PRO SER TYR GLY PRO LEU PHE GLU
SEQRES 2 C 596 ALA LEU ALA HIS TYR ASN ASP LYS LEU LEU ALA MET ALA
SEQRES 3 C 596 LYS ALA GLN THR GLU ARG THR ALA GLN ALA LEU LEU GLN
SEQRES 4 C 596 THR ASN LEU ASP ASP LEU GLY GLN VAL LEU GLU GLN GLY
SEQRES 5 C 596 SER GLN GLN PRO TRP GLN LEU ILE GLN ALA GLN MET ASN
SEQRES 6 C 596 TRP TRP GLN ASP GLN LEU LYS LEU MET GLN HIS THR LEU
SEQRES 7 C 596 LEU LYS SER ALA GLY GLN PRO SER GLU PRO VAL ILE THR
SEQRES 8 C 596 PRO GLU ARG SER ASP ARG ARG PHE LYS ALA GLU ALA TRP
SEQRES 9 C 596 SER GLU GLN PRO ILE TYR ASP TYR LEU LYS GLN SER TYR
SEQRES 10 C 596 LEU LEU THR ALA ARG HIS LEU LEU ALA SER VAL ASP ALA
SEQRES 11 C 596 LEU GLU GLY VAL PRO GLN LYS SER ARG GLU ARG LEU ARG
SEQRES 12 C 596 PHE PHE THR ARG GLN TYR VAL ASN ALA MET ALA PRO SER
SEQRES 13 C 596 ASN PHE LEU ALA THR ASN PRO GLU LEU LEU LYS LEU THR
SEQRES 14 C 596 LEU GLU SER ASP GLY GLN ASN LEU VAL ARG GLY LEU ALA
SEQRES 15 C 596 LEU LEU ALA GLU ASP LEU GLU ARG SER ALA ASP GLN LEU
SEQRES 16 C 596 ASN ILE ARG LEU THR ASP GLU SER ALA PHE GLU LEU GLY
SEQRES 17 C 596 ARG ASP LEU ALA LEU THR PRO GLY ARG VAL VAL GLN ARG
SEQRES 18 C 596 THR GLU LEU TYR GLU LEU ILE GLN TYR SER PRO THR THR
SEQRES 19 C 596 GLU THR VAL GLY LYS THR PRO VAL LEU ILE VAL PRO PRO
SEQRES 20 C 596 PHE ILE ASN LYS TYR TYR ILE MET ASP MET ARG PRO GLN
SEQRES 21 C 596 ASN SER LEU VAL ALA TRP LEU VAL ALA GLN GLY GLN THR
SEQRES 22 C 596 VAL PHE MET ILE SER TRP ARG ASN PRO GLY VAL ALA GLN
SEQRES 23 C 596 ALA GLN ILE ASP LEU ASP ASP TYR VAL VAL ASP GLY VAL
SEQRES 24 C 596 ILE ALA ALA LEU ASP GLY VAL GLU ALA ALA THR GLY GLU
SEQRES 25 C 596 ARG GLU VAL HIS GLY ILE GLY TYR CYS ILE GLY GLY THR
SEQRES 26 C 596 ALA LEU SER LEU ALA MET GLY TRP LEU ALA ALA ARG ARG
SEQRES 27 C 596 GLN LYS GLN ARG VAL ARG THR ALA THR LEU PHE THR THR
SEQRES 28 C 596 LEU LEU ASP PHE SER GLN PRO GLY GLU LEU GLY ILE PHE
SEQRES 29 C 596 ILE HIS GLU PRO ILE ILE ALA ALA LEU GLU ALA GLN ASN
SEQRES 30 C 596 GLU ALA LYS GLY ILE MET ASP GLY ARG GLN LEU ALA VAL
SEQRES 31 C 596 SER PHE SER LEU LEU ARG GLU ASN SER LEU TYR TRP ASN
SEQRES 32 C 596 TYR TYR ILE ASP SER TYR LEU LYS GLY GLN SER PRO VAL
SEQRES 33 C 596 ALA PHE ASP LEU LEU HIS TRP ASN SER ASP SER THR ASN
SEQRES 34 C 596 VAL ALA GLY LYS THR HIS ASN SER LEU LEU ARG ARG LEU
SEQRES 35 C 596 TYR LEU GLU ASN GLN LEU VAL LYS GLY GLU LEU LYS ILE
SEQRES 36 C 596 ARG ASN THR ARG ILE ASP LEU GLY LYS VAL LYS THR PRO
SEQRES 37 C 596 VAL LEU LEU VAL SER ALA VAL ASP ASP HIS ILE ALA LEU
SEQRES 38 C 596 TRP GLN GLY THR TRP GLN GLY MET LYS LEU PHE GLY GLY
SEQRES 39 C 596 GLU GLN ARG PHE LEU LEU ALA GLU SER GLY HIS ILE ALA
SEQRES 40 C 596 GLY ILE ILE ASN PRO PRO ALA ALA ASN LYS TYR GLY PHE
SEQRES 41 C 596 TRP HIS ASN GLY ALA GLU ALA GLU SER PRO GLU SER TRP
SEQRES 42 C 596 LEU ALA GLY ALA THR HIS GLN GLY GLY SER TRP TRP PRO
SEQRES 43 C 596 GLU MET MET GLY PHE ILE GLN ASN ARG ASP GLU GLY SER
SEQRES 44 C 596 GLU PRO VAL PRO ALA ARG VAL PRO GLU GLU GLY LEU ALA
SEQRES 45 C 596 PRO ALA PRO GLY HIS TYR VAL LYS VAL ARG LEU ASN PRO
SEQRES 46 C 596 VAL PHE ALA CYS PRO THR GLU GLU ASP ALA ALA
HET GOL A 601 6
HET GOL A 602 6
HET GOL A 603 6
HET GOL A 604 6
HET GOL A 605 6
HET GOL B 601 6
HET GOL B 602 6
HET GOL B 603 6
HET GOL B 604 6
HET GOL C 601 6
HET GOL C 602 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GOL 11(C3 H8 O3)
FORMUL 15 HOH *27(H2 O)
HELIX 1 AA1 TYR A 6 GLN A 37 1 32
HELIX 2 AA2 PRO A 54 LYS A 78 1 25
HELIX 3 AA3 PRO A 106 LEU A 129 1 24
HELIX 4 AA4 PRO A 133 MET A 151 1 19
HELIX 5 AA5 ALA A 152 THR A 159 5 8
HELIX 6 AA6 ASN A 160 LEU A 168 1 9
HELIX 7 AA7 GLN A 173 ASN A 194 1 22
HELIX 8 AA8 LYS A 249 ASP A 254 5 6
HELIX 9 AA9 SER A 260 GLN A 268 1 9
HELIX 10 AB1 GLY A 281 ALA A 285 5 5
HELIX 11 AB2 ASP A 288 ASP A 295 1 8
HELIX 12 AB3 GLY A 296 GLY A 309 1 14
HELIX 13 AB4 CYS A 319 ARG A 335 1 17
HELIX 14 AB5 PRO A 356 ILE A 363 5 8
HELIX 15 AB6 HIS A 364 GLY A 379 1 16
HELIX 16 AB7 ASP A 382 PHE A 390 1 9
HELIX 17 AB8 SER A 397 TYR A 403 1 7
HELIX 18 AB9 TYR A 403 LYS A 409 1 7
HELIX 19 AC1 PRO A 413 ASP A 424 1 12
HELIX 20 AC2 GLY A 430 ARG A 439 1 10
HELIX 21 AC3 ASP A 459 VAL A 463 5 5
HELIX 22 AC4 LEU A 479 LYS A 488 1 10
HELIX 23 AC5 PRO A 510 ASN A 514 5 5
HELIX 24 AC6 SER A 527 GLY A 534 1 8
HELIX 25 AC7 TRP A 542 ASP A 554 1 13
HELIX 26 AC8 HIS A 575 VAL A 579 5 5
HELIX 27 AC9 TYR B 6 ALA B 34 1 29
HELIX 28 AD1 PRO B 54 LEU B 77 1 24
HELIX 29 AD2 GLU B 104 LEU B 129 1 26
HELIX 30 AD3 PRO B 133 MET B 151 1 19
HELIX 31 AD4 ALA B 152 PHE B 156 5 5
HELIX 32 AD5 ASN B 160 LEU B 168 1 9
HELIX 33 AD6 GLY B 172 ILE B 195 1 24
HELIX 34 AD7 TYR B 250 ASP B 254 5 5
HELIX 35 AD8 SER B 260 GLN B 268 1 9
HELIX 36 AD9 GLY B 281 ALA B 285 5 5
HELIX 37 AE1 ASP B 288 ASP B 295 1 8
HELIX 38 AE2 GLY B 296 GLY B 309 1 14
HELIX 39 AE3 CYS B 319 ARG B 335 1 17
HELIX 40 AE4 PRO B 356 PHE B 362 5 7
HELIX 41 AE5 HIS B 364 GLY B 379 1 16
HELIX 42 AE6 ASP B 382 VAL B 388 1 7
HELIX 43 AE7 SER B 397 TYR B 403 1 7
HELIX 44 AE8 TYR B 403 LYS B 409 1 7
HELIX 45 AE9 PRO B 413 SER B 423 1 11
HELIX 46 AF1 GLY B 430 ARG B 439 1 10
HELIX 47 AF2 ASP B 459 VAL B 463 5 5
HELIX 48 AF3 LEU B 479 LYS B 488 1 10
HELIX 49 AF4 SER B 527 GLY B 534 1 8
HELIX 50 AF5 TRP B 542 ASN B 552 1 11
HELIX 51 AF6 HIS B 575 VAL B 579 5 5
HELIX 52 AF7 TYR C 6 LEU C 35 1 30
HELIX 53 AF8 PRO C 54 LEU C 76 1 23
HELIX 54 AF9 GLN C 105 LEU C 129 1 25
HELIX 55 AG1 PRO C 133 MET C 151 1 19
HELIX 56 AG2 ALA C 152 THR C 159 5 8
HELIX 57 AG3 ASN C 160 LYS C 165 1 6
HELIX 58 AG4 GLY C 172 ILE C 195 1 24
HELIX 59 AG5 LYS C 249 ASP C 254 5 6
HELIX 60 AG6 SER C 260 GLN C 268 1 9
HELIX 61 AG7 GLY C 281 ALA C 285 5 5
HELIX 62 AG8 ASP C 288 ASP C 295 1 8
HELIX 63 AG9 VAL C 297 GLY C 309 1 13
HELIX 64 AH1 CYS C 319 ARG C 335 1 17
HELIX 65 AH2 PRO C 356 ILE C 361 5 6
HELIX 66 AH3 HIS C 364 GLY C 379 1 16
HELIX 67 AH4 ASP C 382 PHE C 390 1 9
HELIX 68 AH5 SER C 397 TYR C 402 1 6
HELIX 69 AH6 TYR C 403 LYS C 409 1 7
HELIX 70 AH7 PRO C 413 ASP C 424 1 12
HELIX 71 AH8 GLY C 430 LEU C 440 1 11
HELIX 72 AH9 ASP C 459 VAL C 463 5 5
HELIX 73 AI1 LEU C 479 LYS C 488 1 10
HELIX 74 AI2 SER C 527 GLY C 534 1 8
HELIX 75 AI3 TRP C 542 ARG C 553 1 12
HELIX 76 AI4 HIS C 575 VAL C 579 5 5
SHEET 1 AA111 THR A 536 GLY A 539 0
SHEET 2 AA111 GLY A 517 HIS A 520 -1 N HIS A 520 O THR A 536
SHEET 3 AA111 GLN A 494 ALA A 499 -1 N LEU A 498 O TRP A 519
SHEET 4 AA111 VAL A 467 ALA A 472 1 N SER A 471 O ALA A 499
SHEET 5 AA111 VAL A 341 PHE A 347 1 N LEU A 346 O LEU A 468
SHEET 6 AA111 VAL A 313 TYR A 318 1 N GLY A 317 O PHE A 347
SHEET 7 AA111 VAL A 240 VAL A 243 1 N VAL A 243 O ILE A 316
SHEET 8 AA111 VAL A 272 TRP A 277 1 O PHE A 273 N VAL A 240
SHEET 9 AA111 TYR A 223 TYR A 228 -1 N ILE A 226 O MET A 274
SHEET 10 AA111 GLY A 214 ARG A 219 -1 N ARG A 215 O GLN A 227
SHEET 11 AA111 ALA A 570 PRO A 571 -1 O ALA A 570 N VAL A 216
SHEET 1 AA2 2 THR A 234 VAL A 235 0
SHEET 2 AA2 2 VAL A 560 PRO A 561 -1 O VAL A 560 N VAL A 235
SHEET 1 AA3 2 ILE A 380 MET A 381 0
SHEET 2 AA3 2 VAL A 428 ALA A 429 -1 O VAL A 428 N MET A 381
SHEET 1 AA4 2 LYS A 452 ILE A 453 0
SHEET 2 AA4 2 THR A 456 ARG A 457 -1 O THR A 456 N ILE A 453
SHEET 1 AA511 THR B 536 GLY B 539 0
SHEET 2 AA511 GLY B 517 HIS B 520 -1 N HIS B 520 O THR B 536
SHEET 3 AA511 GLN B 494 ALA B 499 -1 N LEU B 498 O TRP B 519
SHEET 4 AA511 VAL B 467 ALA B 472 1 N SER B 471 O ALA B 499
SHEET 5 AA511 VAL B 341 PHE B 347 1 N LEU B 346 O LEU B 468
SHEET 6 AA511 VAL B 313 TYR B 318 1 N GLY B 315 O THR B 343
SHEET 7 AA511 VAL B 240 VAL B 243 1 N VAL B 243 O ILE B 316
SHEET 8 AA511 VAL B 272 TRP B 277 1 O PHE B 273 N VAL B 240
SHEET 9 AA511 TYR B 223 TYR B 228 -1 N GLU B 224 O SER B 276
SHEET 10 AA511 GLY B 214 ARG B 219 -1 N ARG B 215 O GLN B 227
SHEET 11 AA511 ALA B 570 PRO B 571 -1 O ALA B 570 N VAL B 216
SHEET 1 AA6 2 THR B 234 VAL B 235 0
SHEET 2 AA6 2 VAL B 560 PRO B 561 -1 O VAL B 560 N VAL B 235
SHEET 1 AA7 2 ILE B 380 MET B 381 0
SHEET 2 AA7 2 VAL B 428 ALA B 429 -1 O VAL B 428 N MET B 381
SHEET 1 AA811 THR C 536 HIS C 537 0
SHEET 2 AA811 PHE C 518 HIS C 520 -1 N HIS C 520 O THR C 536
SHEET 3 AA811 GLN C 494 ALA C 499 -1 N LEU C 498 O TRP C 519
SHEET 4 AA811 VAL C 467 ALA C 472 1 N SER C 471 O ALA C 499
SHEET 5 AA811 VAL C 341 PHE C 347 1 N LEU C 346 O LEU C 468
SHEET 6 AA811 VAL C 313 TYR C 318 1 N GLY C 317 O PHE C 347
SHEET 7 AA811 VAL C 240 VAL C 243 1 N VAL C 243 O ILE C 316
SHEET 8 AA811 VAL C 272 TRP C 277 1 O PHE C 273 N VAL C 240
SHEET 9 AA811 TYR C 223 TYR C 228 -1 N ILE C 226 O MET C 274
SHEET 10 AA811 GLY C 214 ARG C 219 -1 N ARG C 215 O GLN C 227
SHEET 11 AA811 ALA C 570 PRO C 571 -1 O ALA C 570 N VAL C 216
SHEET 1 AA9 2 THR C 234 GLY C 236 0
SHEET 2 AA9 2 PRO C 559 PRO C 561 -1 O VAL C 560 N VAL C 235
SHEET 1 AB1 2 ILE C 380 MET C 381 0
SHEET 2 AB1 2 VAL C 428 ALA C 429 -1 O VAL C 428 N MET C 381
CISPEP 1 ALA A 572 PRO A 573 0 -3.75
CISPEP 2 ALA B 572 PRO B 573 0 -3.94
CISPEP 3 ALA C 572 PRO C 573 0 2.31
CRYST1 157.032 96.071 143.296 90.00 90.42 90.00 C 1 2 1 12
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 0.006368 0.000000 0.000047 0.00000
SCALE2 0.000000 0.010409 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006979 0.00000
MTRIX1 1 0.456425 -0.889246 -0.030291 5.95316 1
MTRIX2 1 -0.887349 -0.452418 -0.089053 -76.40602 1
MTRIX3 1 0.065485 0.067524 -0.995566 101.28855 1
MTRIX1 2 -0.446619 -0.893309 0.050307 -72.00071 1
MTRIX2 2 0.893788 -0.442874 0.070752 52.43705 1
MTRIX3 2 -0.040923 0.076563 0.996225 -49.38580 1
TER 4310 PHE A 585
TER 8565 PHE B 585
TER 12784 PRO C 583
MASTER 485 0 11 76 47 0 0 1212874 3 66 138
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