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HEADER BIOSYNTHETIC PROTEIN 15-MAR-17 5XAV
TITLE STRUCTURE OF PHAC FROM CHROMOBACTERIUM SP. USM2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTRACELLULAR POLYHYDROXYALKANOATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 175-567;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHROMOBACTERIUM SP. USM2;
SOURCE 3 ORGANISM_TAXID: 611307;
SOURCE 4 GENE: PHAC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOPLASTIC SYNTHASE, PHAC, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.CHEK,S.Y.KIM,T.MORI,H.ARSAD,M.R.SAMIAN,K.SUDESH,T.HAKOSHIMA
REVDAT 1 26-JUL-17 5XAV 0
JRNL AUTH M.F.CHEK,S.Y.KIM,T.MORI,H.ARSAD,M.R.SAMIAN,K.SUDESH,
JRNL AUTH 2 T.HAKOSHIMA
JRNL TITL STRUCTURE OF POLYHYDROXYALKANOATE (PHA) SYNTHASE PHAC FROM
JRNL TITL 2 CHROMOBACTERIUM SP. USM2, PRODUCING BIODEGRADABLE PLASTICS
JRNL REF SCI REP V. 7 2017
JRNL REFN ESSN 2045-2322
JRNL DOI 10.1038/S41598-017-05509-4
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 137380
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.123
REMARK 3 R VALUE (WORKING SET) : 0.121
REMARK 3 FREE R VALUE : 0.157
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6908
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 36.1161 - 4.5917 0.95 4227 232 0.1439 0.1612
REMARK 3 2 4.5917 - 3.6456 1.00 4358 236 0.1179 0.1353
REMARK 3 3 3.6456 - 3.1851 1.00 4375 242 0.1249 0.1483
REMARK 3 4 3.1851 - 2.8940 1.00 4383 249 0.1286 0.1624
REMARK 3 5 2.8940 - 2.6867 1.00 4356 231 0.1250 0.1436
REMARK 3 6 2.6867 - 2.5283 1.00 4378 240 0.1210 0.1689
REMARK 3 7 2.5283 - 2.4017 1.00 4354 225 0.1201 0.1595
REMARK 3 8 2.4017 - 2.2972 1.00 4341 247 0.1162 0.1659
REMARK 3 9 2.2972 - 2.2088 1.00 4370 242 0.1094 0.1535
REMARK 3 10 2.2088 - 2.1326 1.00 4352 212 0.1050 0.1387
REMARK 3 11 2.1326 - 2.0659 1.00 4384 218 0.1040 0.1482
REMARK 3 12 2.0659 - 2.0069 1.00 4391 208 0.1071 0.1645
REMARK 3 13 2.0069 - 1.9540 1.00 4326 234 0.1042 0.1470
REMARK 3 14 1.9540 - 1.9064 1.00 4366 221 0.1049 0.1467
REMARK 3 15 1.9064 - 1.8630 1.00 4364 198 0.1082 0.1562
REMARK 3 16 1.8630 - 1.8234 1.00 4391 239 0.1105 0.1630
REMARK 3 17 1.8234 - 1.7869 1.00 4328 262 0.1134 0.1551
REMARK 3 18 1.7869 - 1.7532 1.00 4327 225 0.1076 0.1481
REMARK 3 19 1.7532 - 1.7219 1.00 4376 209 0.1093 0.1686
REMARK 3 20 1.7219 - 1.6927 1.00 4356 237 0.1124 0.1730
REMARK 3 21 1.6927 - 1.6654 1.00 4333 232 0.1106 0.1521
REMARK 3 22 1.6654 - 1.6398 1.00 4335 245 0.1180 0.1902
REMARK 3 23 1.6398 - 1.6156 1.00 4332 250 0.1182 0.1734
REMARK 3 24 1.6156 - 1.5929 1.00 4311 235 0.1233 0.1799
REMARK 3 25 1.5929 - 1.5714 1.00 4393 231 0.1283 0.1867
REMARK 3 26 1.5714 - 1.5509 1.00 4346 190 0.1376 0.1712
REMARK 3 27 1.5509 - 1.5316 1.00 4365 237 0.1468 0.2022
REMARK 3 28 1.5316 - 1.5131 1.00 4346 231 0.1600 0.2068
REMARK 3 29 1.5131 - 1.4955 1.00 4348 226 0.1687 0.2291
REMARK 3 30 1.4955 - 1.4787 0.98 4260 224 0.1738 0.2060
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.019 6098
REMARK 3 ANGLE : 1.603 8314
REMARK 3 CHIRALITY : 0.132 908
REMARK 3 PLANARITY : 0.012 1059
REMARK 3 DIHEDRAL : 13.888 2203
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5XAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1300003172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 137720
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.479
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 : 11.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 58.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.64400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BIS-TRIS PH5.5, 60 MM AMMONIUM
REMARK 280 SULFATE 5% PEG4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.30367
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 70.60733
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.95550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 88.25917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.65183
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: 2250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 GLY A 173
REMARK 465 ASN A 372
REMARK 465 TYR A 373
REMARK 465 VAL A 374
REMARK 465 VAL A 375
REMARK 465 ASN A 376
REMARK 465 ASN A 377
REMARK 465 TYR A 378
REMARK 465 LEU A 379
REMARK 465 LEU A 380
REMARK 465 GLY A 381
REMARK 465 LYS A 382
REMARK 465 THR A 383
REMARK 465 PRO A 384
REMARK 465 ALA A 563
REMARK 465 ALA A 564
REMARK 465 ALA A 565
REMARK 465 LEU A 566
REMARK 465 ASN A 567
REMARK 465 GLY B 173
REMARK 465 TYR B 373
REMARK 465 VAL B 374
REMARK 465 VAL B 375
REMARK 465 ASN B 376
REMARK 465 ASN B 377
REMARK 465 TYR B 378
REMARK 465 LEU B 379
REMARK 465 LEU B 380
REMARK 465 GLY B 381
REMARK 465 LYS B 382
REMARK 465 THR B 383
REMARK 465 ALA B 563
REMARK 465 ALA B 564
REMARK 465 ALA B 565
REMARK 465 LEU B 566
REMARK 465 ASN B 567
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 HOH B 991 O HOH B 1016 1.62
REMARK 500 O HOH B 972 O HOH B 988 1.63
REMARK 500 O HOH B 669 O HOH B 987 1.63
REMARK 500 O HOH A 650 O HOH A 967 1.67
REMARK 500 O HOH B 808 O HOH B 966 1.67
REMARK 500 O HOH B 838 O HOH B 988 1.71
REMARK 500 O HOH B 918 O HOH B 985 1.72
REMARK 500 O HOH A 824 O HOH A 1014 1.73
REMARK 500 O HOH A 1142 O HOH A 1144 1.74
REMARK 500 O HOH B 856 O HOH B 985 1.76
REMARK 500 O HOH B 912 O HOH B 987 1.79
REMARK 500 O HOH B 948 O HOH B 1072 1.84
REMARK 500 O HOH A 1013 O HOH A 1056 1.85
REMARK 500 O HOH A 998 O HOH A 1025 1.93
REMARK 500 O HOH B 607 O HOH B 816 1.94
REMARK 500 O HOH A 609 O HOH A 970 1.95
REMARK 500 O HOH B 840 O HOH B 948 1.96
REMARK 500 O HOH B 730 O HOH B 1007 1.97
REMARK 500 O HOH A 953 O HOH A 970 1.99
REMARK 500 O HOH A 888 O HOH A 1020 1.99
REMARK 500 O HOH B 607 O HOH B 1008 1.99
REMARK 500 O HOH B 653 O HOH B 1001 2.01
REMARK 500 O HOH B 769 O HOH B 1011 2.01
REMARK 500 O HOH A 801 O HOH A 1020 2.01
REMARK 500 O HOH A 938 O HOH A 985 2.02
REMARK 500 O HOH B 691 O HOH B 975 2.03
REMARK 500 O HOH B 943 O HOH B 1066 2.04
REMARK 500 NZ LYS B 489 O HOH B 601 2.04
REMARK 500 O HOH B 863 O HOH B 986 2.07
REMARK 500 O HOH B 877 O HOH B 1057 2.09
REMARK 500 O HOH A 1076 O HOH A 1122 2.09
REMARK 500 O HOH A 851 O HOH B 1004 2.12
REMARK 500 O HOH A 1014 O HOH A 1053 2.13
REMARK 500 O HOH A 1015 O HOH A 1025 2.14
REMARK 500 O HOH A 797 O HOH A 943 2.15
REMARK 500 O HOH A 670 O HOH A 1001 2.18
REMARK 500 O HOH B 943 O HOH B 1073 2.19
REMARK 500 SG CYS A 291 O HOH A 998 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 809 O HOH A 1013 5554 1.66
REMARK 500 O HOH B 1067 O HOH B 1089 6445 2.05
REMARK 500 O HOH B 696 O HOH B 966 6445 2.05
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 SER A 475 CB SER A 475 OG -0.078
REMARK 500 GLU A 542 CD GLU A 542 OE1 0.069
REMARK 500 GLU B 209 CD GLU B 209 OE2 0.066
REMARK 500 GLU B 255 CD GLU B 255 OE2 0.078
REMARK 500 GLU B 326 CD GLU B 326 OE1 0.074
REMARK 500 ASP B 388 CB ASP B 388 CG 0.156
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 ARG A 359 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU A 524 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
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 220 -178.75 57.30
REMARK 500 LEU A 227 -94.05 -80.59
REMARK 500 CYS A 291 -133.12 60.02
REMARK 500 LYS A 310 79.10 -101.08
REMARK 500 SER A 475 -171.93 79.94
REMARK 500 ARG A 490 -149.55 71.93
REMARK 500 ASN A 495 116.55 -165.75
REMARK 500 LEU B 227 -101.82 -86.64
REMARK 500 CYS B 291 -134.14 62.03
REMARK 500 SER B 475 -169.31 80.97
REMARK 500 ARG B 490 -150.10 68.87
REMARK 500 ASN B 495 115.19 -166.10
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 ALA A 385 PRO A 386 122.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1133 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A1134 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1135 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A1136 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A1137 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A1138 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1139 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A1140 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH A1141 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A1142 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A1143 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A1144 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH A1145 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH A1146 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH A1147 DISTANCE = 8.09 ANGSTROMS
REMARK 525 HOH A1148 DISTANCE = 9.24 ANGSTROMS
REMARK 525 HOH B1099 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1100 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH B1101 DISTANCE = 7.03 ANGSTROMS
DBREF 5XAV A 175 567 UNP E1APK1 E1APK1_9NEIS 175 567
DBREF 5XAV B 175 567 UNP E1APK1 E1APK1_9NEIS 175 567
SEQADV 5XAV GLY A 173 UNP E1APK1 EXPRESSION TAG
SEQADV 5XAV PRO A 174 UNP E1APK1 EXPRESSION TAG
SEQADV 5XAV GLY B 173 UNP E1APK1 EXPRESSION TAG
SEQADV 5XAV PRO B 174 UNP E1APK1 EXPRESSION TAG
SEQRES 1 A 395 GLY PRO PHE GLN ILE GLY LYS ASN LEU VAL VAL THR PRO
SEQRES 2 A 395 GLY GLU VAL VAL PHE ARG ASN GLU LEU ILE GLU LEU ILE
SEQRES 3 A 395 GLN TYR THR PRO THR THR GLU LYS VAL HIS GLU LYS PRO
SEQRES 4 A 395 LEU LEU PHE VAL PRO PRO CYS ILE ASN LYS TYR TYR LEU
SEQRES 5 A 395 MET ASP LEU GLN PRO ASP ASN SER MET VAL ARG HIS PHE
SEQRES 6 A 395 VAL GLY GLN GLY TYR ARG VAL PHE LEU VAL SER TRP ARG
SEQRES 7 A 395 SER ALA VAL PRO GLU MET LYS ASN PHE THR TRP GLU THR
SEQRES 8 A 395 TYR ILE GLU LYS GLY VAL PHE ALA ALA ALA GLU ALA VAL
SEQRES 9 A 395 GLN LYS ILE THR LYS GLN PRO THR MET ASN ALA LEU GLY
SEQRES 10 A 395 PHE CYS VAL GLY GLY VAL ILE LEU THR THR ALA LEU CYS
SEQRES 11 A 395 VAL ALA GLN ALA LYS GLY LEU LYS TYR PHE ASP SER ALA
SEQRES 12 A 395 THR PHE MET THR SER LEU ILE ASP HIS ALA GLU PRO GLY
SEQRES 13 A 395 GLU ILE SER PHE PHE ILE ASP GLU ALA LEU VAL ALA SER
SEQRES 14 A 395 ARG GLU ALA LYS MET ALA ALA GLY GLY ILE ILE SER GLY
SEQRES 15 A 395 LYS GLU ILE GLY ARG THR PHE ALA SER LEU ARG ALA ASN
SEQRES 16 A 395 ASP LEU VAL TRP ASN TYR VAL VAL ASN ASN TYR LEU LEU
SEQRES 17 A 395 GLY LYS THR PRO ALA PRO PHE ASP LEU LEU TYR TRP ASN
SEQRES 18 A 395 ASN ASP ALA VAL ASP LEU PRO LEU PRO MET HIS THR PHE
SEQRES 19 A 395 MET LEU ARG GLN PHE TYR ILE ASN ASN ALA LEU ILE THR
SEQRES 20 A 395 PRO GLY ALA ILE THR LEU CYS GLY VAL PRO ILE ASP ILE
SEQRES 21 A 395 SER LYS ILE ASP ILE PRO VAL TYR MET PHE ALA ALA ARG
SEQRES 22 A 395 GLU ASP HIS ILE VAL LEU TRP SER SER ALA TYR SER GLY
SEQRES 23 A 395 LEU LYS TYR LEU SER GLY THR PRO SER ARG ARG PHE VAL
SEQRES 24 A 395 LEU GLY ALA SER GLY HIS ILE ALA GLY SER ILE ASN PRO
SEQRES 25 A 395 VAL THR LYS ASP LYS ARG ASN TYR TRP THR ASN GLU GLN
SEQRES 26 A 395 LEU PRO VAL ASN PRO GLU GLU TRP LEU GLU GLY ALA GLN
SEQRES 27 A 395 SER HIS PRO GLY SER TRP TRP LYS ASP TRP ASP ALA TRP
SEQRES 28 A 395 LEU ALA PRO GLN SER GLY LYS GLN VAL PRO ALA PRO LYS
SEQRES 29 A 395 MET LEU GLY SER LYS GLU PHE PRO PRO LEU GLN PRO ALA
SEQRES 30 A 395 PRO GLY SER TYR VAL LEU ALA LYS ALA MET PRO PRO VAL
SEQRES 31 A 395 ALA ALA ALA LEU ASN
SEQRES 1 B 395 GLY PRO PHE GLN ILE GLY LYS ASN LEU VAL VAL THR PRO
SEQRES 2 B 395 GLY GLU VAL VAL PHE ARG ASN GLU LEU ILE GLU LEU ILE
SEQRES 3 B 395 GLN TYR THR PRO THR THR GLU LYS VAL HIS GLU LYS PRO
SEQRES 4 B 395 LEU LEU PHE VAL PRO PRO CYS ILE ASN LYS TYR TYR LEU
SEQRES 5 B 395 MET ASP LEU GLN PRO ASP ASN SER MET VAL ARG HIS PHE
SEQRES 6 B 395 VAL GLY GLN GLY TYR ARG VAL PHE LEU VAL SER TRP ARG
SEQRES 7 B 395 SER ALA VAL PRO GLU MET LYS ASN PHE THR TRP GLU THR
SEQRES 8 B 395 TYR ILE GLU LYS GLY VAL PHE ALA ALA ALA GLU ALA VAL
SEQRES 9 B 395 GLN LYS ILE THR LYS GLN PRO THR MET ASN ALA LEU GLY
SEQRES 10 B 395 PHE CYS VAL GLY GLY VAL ILE LEU THR THR ALA LEU CYS
SEQRES 11 B 395 VAL ALA GLN ALA LYS GLY LEU LYS TYR PHE ASP SER ALA
SEQRES 12 B 395 THR PHE MET THR SER LEU ILE ASP HIS ALA GLU PRO GLY
SEQRES 13 B 395 GLU ILE SER PHE PHE ILE ASP GLU ALA LEU VAL ALA SER
SEQRES 14 B 395 ARG GLU ALA LYS MET ALA ALA GLY GLY ILE ILE SER GLY
SEQRES 15 B 395 LYS GLU ILE GLY ARG THR PHE ALA SER LEU ARG ALA ASN
SEQRES 16 B 395 ASP LEU VAL TRP ASN TYR VAL VAL ASN ASN TYR LEU LEU
SEQRES 17 B 395 GLY LYS THR PRO ALA PRO PHE ASP LEU LEU TYR TRP ASN
SEQRES 18 B 395 ASN ASP ALA VAL ASP LEU PRO LEU PRO MET HIS THR PHE
SEQRES 19 B 395 MET LEU ARG GLN PHE TYR ILE ASN ASN ALA LEU ILE THR
SEQRES 20 B 395 PRO GLY ALA ILE THR LEU CYS GLY VAL PRO ILE ASP ILE
SEQRES 21 B 395 SER LYS ILE ASP ILE PRO VAL TYR MET PHE ALA ALA ARG
SEQRES 22 B 395 GLU ASP HIS ILE VAL LEU TRP SER SER ALA TYR SER GLY
SEQRES 23 B 395 LEU LYS TYR LEU SER GLY THR PRO SER ARG ARG PHE VAL
SEQRES 24 B 395 LEU GLY ALA SER GLY HIS ILE ALA GLY SER ILE ASN PRO
SEQRES 25 B 395 VAL THR LYS ASP LYS ARG ASN TYR TRP THR ASN GLU GLN
SEQRES 26 B 395 LEU PRO VAL ASN PRO GLU GLU TRP LEU GLU GLY ALA GLN
SEQRES 27 B 395 SER HIS PRO GLY SER TRP TRP LYS ASP TRP ASP ALA TRP
SEQRES 28 B 395 LEU ALA PRO GLN SER GLY LYS GLN VAL PRO ALA PRO LYS
SEQRES 29 B 395 MET LEU GLY SER LYS GLU PHE PRO PRO LEU GLN PRO ALA
SEQRES 30 B 395 PRO GLY SER TYR VAL LEU ALA LYS ALA MET PRO PRO VAL
SEQRES 31 B 395 ALA ALA ALA LEU ASN
FORMUL 3 HOH *1049(H2 O)
HELIX 1 AA1 LYS A 221 ASP A 226 5 6
HELIX 2 AA2 SER A 232 GLN A 240 1 9
HELIX 3 AA3 VAL A 253 LYS A 257 5 5
HELIX 4 AA4 THR A 260 LYS A 267 1 8
HELIX 5 AA5 GLY A 268 LYS A 281 1 14
HELIX 6 AA6 CYS A 291 GLY A 308 1 18
HELIX 7 AA7 GLY A 328 PHE A 333 5 6
HELIX 8 AA8 ASP A 335 LYS A 345 1 11
HELIX 9 AA9 MET A 346 GLY A 349 5 4
HELIX 10 AB1 SER A 353 ALA A 362 1 10
HELIX 11 AB2 ARG A 365 LEU A 369 5 5
HELIX 12 AB3 PRO A 386 ASP A 395 1 10
HELIX 13 AB4 LEU A 401 PHE A 411 1 11
HELIX 14 AB5 ASN A 415 THR A 419 5 5
HELIX 15 AB6 ASP A 431 ILE A 435 5 5
HELIX 16 AB7 LEU A 451 GLY A 458 1 8
HELIX 17 AB8 LEU A 459 LEU A 462 5 4
HELIX 18 AB9 GLY A 476 ILE A 482 1 7
HELIX 19 AC1 ASN A 501 GLY A 508 1 8
HELIX 20 AC2 TRP A 516 ALA A 525 1 10
HELIX 21 AC3 PRO A 526 SER A 528 5 3
HELIX 22 AC4 SER A 552 ALA A 556 5 5
HELIX 23 AC5 LYS B 221 ASP B 226 5 6
HELIX 24 AC6 GLN B 228 ASN B 231 5 4
HELIX 25 AC7 SER B 232 GLN B 240 1 9
HELIX 26 AC8 VAL B 253 LYS B 257 5 5
HELIX 27 AC9 THR B 260 LYS B 267 1 8
HELIX 28 AD1 GLY B 268 LYS B 281 1 14
HELIX 29 AD2 CYS B 291 GLY B 308 1 18
HELIX 30 AD3 PRO B 327 ILE B 334 5 8
HELIX 31 AD4 ASP B 335 LYS B 345 1 11
HELIX 32 AD5 MET B 346 GLY B 349 5 4
HELIX 33 AD6 SER B 353 PHE B 361 1 9
HELIX 34 AD7 ARG B 365 VAL B 370 5 6
HELIX 35 AD8 PRO B 386 ASP B 395 1 10
HELIX 36 AD9 LEU B 401 PHE B 411 1 11
HELIX 37 AE1 ASN B 415 THR B 419 5 5
HELIX 38 AE2 ASP B 431 ILE B 435 5 5
HELIX 39 AE3 LEU B 451 GLY B 458 1 8
HELIX 40 AE4 LEU B 459 LEU B 462 5 4
HELIX 41 AE5 GLY B 476 ILE B 482 1 7
HELIX 42 AE6 ASN B 501 GLY B 508 1 8
HELIX 43 AE7 TRP B 516 ALA B 525 1 10
HELIX 44 AE8 PRO B 526 SER B 528 5 3
HELIX 45 AE9 SER B 552 ALA B 556 5 5
SHEET 1 AA111 GLN A 510 PRO A 513 0
SHEET 2 AA111 ASN A 491 THR A 494 -1 N TYR A 492 O HIS A 512
SHEET 3 AA111 ARG A 468 GLY A 473 -1 N LEU A 472 O TRP A 493
SHEET 4 AA111 VAL A 439 ALA A 444 1 N ALA A 443 O GLY A 473
SHEET 5 AA111 PHE A 312 MET A 318 1 N PHE A 317 O PHE A 442
SHEET 6 AA111 MET A 285 PHE A 290 1 N GLY A 289 O THR A 316
SHEET 7 AA111 LEU A 212 VAL A 215 1 N VAL A 215 O LEU A 288
SHEET 8 AA111 VAL A 244 TRP A 249 1 O PHE A 245 N PHE A 214
SHEET 9 AA111 ILE A 195 TYR A 200 -1 N GLU A 196 O SER A 248
SHEET 10 AA111 GLY A 186 ARG A 191 -1 N GLU A 187 O GLN A 199
SHEET 11 AA111 GLN A 547 PRO A 548 -1 O GLN A 547 N VAL A 188
SHEET 1 AA2 2 LYS A 206 HIS A 208 0
SHEET 2 AA2 2 GLN A 531 PRO A 533 -1 O VAL A 532 N VAL A 207
SHEET 1 AA3 2 ILE A 351 ILE A 352 0
SHEET 2 AA3 2 LEU A 399 PRO A 400 -1 O LEU A 399 N ILE A 352
SHEET 1 AA4 2 THR A 424 LEU A 425 0
SHEET 2 AA4 2 VAL A 428 PRO A 429 -1 O VAL A 428 N LEU A 425
SHEET 1 AA511 GLN B 510 PRO B 513 0
SHEET 2 AA511 ASN B 491 THR B 494 -1 N TYR B 492 O HIS B 512
SHEET 3 AA511 ARG B 468 GLY B 473 -1 N LEU B 472 O TRP B 493
SHEET 4 AA511 VAL B 439 ALA B 444 1 N ALA B 443 O GLY B 473
SHEET 5 AA511 PHE B 312 MET B 318 1 N PHE B 317 O PHE B 442
SHEET 6 AA511 MET B 285 PHE B 290 1 N GLY B 289 O THR B 316
SHEET 7 AA511 LEU B 212 VAL B 215 1 N VAL B 215 O LEU B 288
SHEET 8 AA511 VAL B 244 TRP B 249 1 O PHE B 245 N PHE B 214
SHEET 9 AA511 ILE B 195 TYR B 200 -1 N GLU B 196 O SER B 248
SHEET 10 AA511 GLY B 186 ARG B 191 -1 N VAL B 189 O LEU B 197
SHEET 11 AA511 GLN B 547 PRO B 548 -1 O GLN B 547 N VAL B 188
SHEET 1 AA6 2 LYS B 206 HIS B 208 0
SHEET 2 AA6 2 GLN B 531 PRO B 533 -1 O VAL B 532 N VAL B 207
SHEET 1 AA7 2 ILE B 351 ILE B 352 0
SHEET 2 AA7 2 LEU B 399 PRO B 400 -1 O LEU B 399 N ILE B 352
SHEET 1 AA8 2 THR B 424 LEU B 425 0
SHEET 2 AA8 2 VAL B 428 PRO B 429 -1 O VAL B 428 N LEU B 425
CISPEP 1 VAL A 370 TRP A 371 0 0.09
CISPEP 2 ALA A 549 PRO A 550 0 12.95
CISPEP 3 ALA B 385 PRO B 386 0 1.91
CISPEP 4 ALA B 549 PRO B 550 0 12.90
CRYST1 117.332 117.332 105.911 90.00 90.00 120.00 P 61 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 0.008523 0.004921 0.000000 0.00000
SCALE2 0.000000 0.009841 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009442 0.00000
TER 2953 VAL A 562
TER 5921 VAL B 562
MASTER 457 0 0 45 34 0 0 6 6968 2 0 62
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