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HEADER BIOSYNTHETIC PROTEIN 20-MAY-15 4ZXH
TITLE CRYSTAL STRUCTURE OF HOLO-AB3403 A FOUR DOMAIN NONRIBOSOMAL PEPTIDE
TITLE 2 SYNTHETASE FROM ACINETOBACTER BAUMANII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABBFA_003403;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER BAUMANNII (STRAIN AB307-0294);
SOURCE 3 ORGANISM_TAXID: 557600;
SOURCE 4 STRAIN: AB307-0294;
SOURCE 5 GENE: ABBFA_003403;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS NONRIBOSOMAL PEPTIDE SYNTHETASE, NRPS, CONDENSATION, ADENYLATION,
KEYWDS 2 PCP, THIOESTERASE, PHOSPHOPANTETHEINE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.J.DRAKE,B.R.MILLER,C.L.ALLEN,A.M.GULICK
REVDAT 2 27-JAN-16 4ZXH 1 JRNL
REVDAT 1 30-DEC-15 4ZXH 0
JRNL AUTH E.J.DRAKE,B.R.MILLER,C.SHI,J.T.TARRASCH,J.A.SUNDLOV,
JRNL AUTH 2 C.L.ALLEN,G.SKINIOTIS,C.C.ALDRICH,A.M.GULICK
JRNL TITL STRUCTURES OF TWO DISTINCT CONFORMATIONS OF
JRNL TITL 2 HOLO-NON-RIBOSOMAL PEPTIDE SYNTHETASES.
JRNL REF NATURE V. 529 235 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 26762461
JRNL DOI 10.1038/NATURE16163
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 66540
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 49.8034 - 6.5030 0.99 4953 154 0.1609 0.1960
REMARK 3 2 6.5030 - 5.1633 1.00 4744 147 0.1618 0.2348
REMARK 3 3 5.1633 - 4.5111 1.00 4663 144 0.1300 0.1569
REMARK 3 4 4.5111 - 4.0989 1.00 4626 143 0.1388 0.1941
REMARK 3 5 4.0989 - 3.8052 1.00 4625 144 0.1496 0.2104
REMARK 3 6 3.8052 - 3.5809 1.00 4565 142 0.1685 0.2343
REMARK 3 7 3.5809 - 3.4016 1.00 4581 141 0.1890 0.2322
REMARK 3 8 3.4016 - 3.2536 1.00 4593 142 0.2155 0.2664
REMARK 3 9 3.2536 - 3.1284 1.00 4530 141 0.2206 0.2816
REMARK 3 10 3.1284 - 3.0204 1.00 4551 141 0.2237 0.2932
REMARK 3 11 3.0204 - 2.9260 1.00 4539 140 0.2335 0.2764
REMARK 3 12 2.9260 - 2.8424 1.00 4543 141 0.2503 0.3768
REMARK 3 13 2.8424 - 2.7675 1.00 4503 140 0.2527 0.3420
REMARK 3 14 2.7675 - 2.7000 1.00 4525 139 0.2479 0.3136
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.01
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 : 0.009 10495
REMARK 3 ANGLE : 1.178 14293
REMARK 3 CHIRALITY : 0.045 1638
REMARK 3 PLANARITY : 0.006 1852
REMARK 3 DIHEDRAL : 13.461 3838
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 191:445))
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2921 60.6443 163.2479
REMARK 3 T TENSOR
REMARK 3 T11: 0.1691 T22: 0.3835
REMARK 3 T33: 0.2388 T12: -0.0245
REMARK 3 T13: 0.0748 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 2.6099 L22: 1.4559
REMARK 3 L33: 1.5443 L12: -0.2563
REMARK 3 L13: 0.3169 L23: -0.1001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0937 S12: -0.1751 S13: 0.2547
REMARK 3 S21: 0.1976 S22: 0.1552 S23: 0.1531
REMARK 3 S31: -0.2038 S32: -0.1752 S33: 0.0003
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 446:480))
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2490 23.3821 131.2673
REMARK 3 T TENSOR
REMARK 3 T11: 0.3659 T22: 0.7526
REMARK 3 T33: 0.7707 T12: -0.0188
REMARK 3 T13: -0.0404 T23: -0.4397
REMARK 3 L TENSOR
REMARK 3 L11: 1.3588 L22: 1.0678
REMARK 3 L33: 4.9480 L12: -0.4603
REMARK 3 L13: -2.3078 L23: -0.2017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: 0.8336 S13: -0.5635
REMARK 3 S21: 0.0266 S22: 0.0101 S23: 0.6682
REMARK 3 S31: 0.4603 S32: -0.9633 S33: 0.9250
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 481:862))
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6686 31.2616 122.5092
REMARK 3 T TENSOR
REMARK 3 T11: 0.2297 T22: 0.3437
REMARK 3 T33: 0.2517 T12: 0.0472
REMARK 3 T13: -0.0339 T23: -0.1027
REMARK 3 L TENSOR
REMARK 3 L11: 1.8936 L22: 2.0099
REMARK 3 L33: 2.3969 L12: -0.3842
REMARK 3 L13: -1.1341 L23: 1.2165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0246 S12: 0.1153 S13: 0.1872
REMARK 3 S21: -0.2350 S22: -0.1018 S23: 0.1271
REMARK 3 S31: -0.2588 S32: -0.1640 S33: -0.0108
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 863:959))
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7266 43.1514 150.2990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1395 T22: 0.3489
REMARK 3 T33: 0.2921 T12: -0.0564
REMARK 3 T13: -0.0176 T23: -0.0875
REMARK 3 L TENSOR
REMARK 3 L11: 4.5830 L22: 1.3161
REMARK 3 L33: 3.7152 L12: -1.2783
REMARK 3 L13: -1.3035 L23: 0.9510
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: 0.0866 S13: 0.1411
REMARK 3 S21: -0.0123 S22: 0.0259 S23: 0.0646
REMARK 3 S31: 0.1234 S32: -0.1201 S33: -0.0627
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 960:973))
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2859 48.1308 168.3005
REMARK 3 T TENSOR
REMARK 3 T11: 0.1659 T22: 0.3471
REMARK 3 T33: 0.4805 T12: -0.1365
REMARK 3 T13: 0.0054 T23: -0.1257
REMARK 3 L TENSOR
REMARK 3 L11: 0.0918 L22: 1.3732
REMARK 3 L33: 3.2143 L12: -0.3596
REMARK 3 L13: -0.5442 L23: 2.0955
REMARK 3 S TENSOR
REMARK 3 S11: -0.2889 S12: 0.2325 S13: -0.0733
REMARK 3 S21: 0.1668 S22: -0.1562 S23: 0.2338
REMARK 3 S31: 0.4959 S32: -0.3659 S33: 0.2005
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 974:1044))
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7026 59.7317 172.8109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1371 T22: 0.2255
REMARK 3 T33: 0.2202 T12: 0.0479
REMARK 3 T13: -0.0029 T23: -0.0598
REMARK 3 L TENSOR
REMARK 3 L11: 4.8308 L22: 2.1636
REMARK 3 L33: 2.6722 L12: 2.6291
REMARK 3 L13: 0.3352 L23: -0.5738
REMARK 3 S TENSOR
REMARK 3 S11: -0.0765 S12: 0.1002 S13: 0.1751
REMARK 3 S21: -0.0263 S22: 0.0250 S23: -0.0583
REMARK 3 S31: -0.1177 S32: -0.2022 S33: 0.0075
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 1045:1053))
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7845 74.8607 174.0367
REMARK 3 T TENSOR
REMARK 3 T11: 0.5546 T22: 0.4902
REMARK 3 T33: 0.5730 T12: 0.0010
REMARK 3 T13: -0.1840 T23: 0.0642
REMARK 3 L TENSOR
REMARK 3 L11: 0.1575 L22: 0.2726
REMARK 3 L33: 1.9895 L12: 0.0787
REMARK 3 L13: -0.5367 L23: -0.0636
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: 0.4900 S13: -0.1997
REMARK 3 S21: -0.8479 S22: 0.0639 S23: 0.2840
REMARK 3 S31: -0.0963 S32: -1.5781 S33: -0.1044
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 1054:1318))
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0173 72.1765 188.6479
REMARK 3 T TENSOR
REMARK 3 T11: 0.2706 T22: 0.1014
REMARK 3 T33: 0.2260 T12: -0.0184
REMARK 3 T13: 0.0192 T23: -0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 2.3253 L22: 2.1141
REMARK 3 L33: 2.1561 L12: 0.7166
REMARK 3 L13: 0.3741 L23: 0.1487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0773 S12: -0.0994 S13: 0.2678
REMARK 3 S21: 0.2893 S22: -0.0482 S23: 0.0730
REMARK 3 S31: -0.2764 S32: -0.0955 S33: 0.0081
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 191:445))
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3963 37.6331 158.0315
REMARK 3 T TENSOR
REMARK 3 T11: 0.1705 T22: 0.4336
REMARK 3 T33: 0.4185 T12: -0.0824
REMARK 3 T13: 0.0345 T23: -0.0673
REMARK 3 L TENSOR
REMARK 3 L11: 2.3571 L22: 1.0471
REMARK 3 L33: 0.8381 L12: -0.6285
REMARK 3 L13: 0.4630 L23: -0.2740
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: 0.2265 S13: -0.7385
REMARK 3 S21: 0.1647 S22: 0.0273 S23: 0.2373
REMARK 3 S31: 0.3120 S32: -0.0886 S33: -0.1442
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 4ZXH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 113.15
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66559
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 49.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.31800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.490
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 69.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.75-0.95 M POTASSIUM CITRATE, 0.01
REMARK 280 -0.025 M GLYCINE, 0.05 M BTP, PH 8, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 287.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 174.30350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.09350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.09350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 261.45525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.09350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.09350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 87.15175
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.09350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.09350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 261.45525
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.09350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.09350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 87.15175
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 174.30350
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 ASN A 501
REMARK 465 ASP A 502
REMARK 465 GLY A 627
REMARK 465 SER A 628
REMARK 465 THR A 629
REMARK 465 GLY A 630
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 GLN A 78 CG CD OE1 NE2
REMARK 470 GLU A 101 CD OE1 OE2
REMARK 470 LYS A 184 CE NZ
REMARK 470 ASP A 191 CG OD1 OD2
REMARK 470 GLU A 195 CG CD OE1 OE2
REMARK 470 LYS A 205 CG CD CE NZ
REMARK 470 LYS A 247 CG CD CE NZ
REMARK 470 ASP A 248 CG OD1 OD2
REMARK 470 GLU A 250 CG CD OE1 OE2
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 ARG A 286 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 360 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 442 CG CD OE1 OE2
REMARK 470 LYS A 461 CG CD CE NZ
REMARK 470 LYS A 472 CE NZ
REMARK 470 LYS A 487 CD CE NZ
REMARK 470 GLU A 566 CG CD OE1 OE2
REMARK 470 LEU A 590 CG CD1 CD2
REMARK 470 ASN A 591 CG OD1 ND2
REMARK 470 GLU A 608 CG CD OE1 OE2
REMARK 470 VAL A 610 O
REMARK 470 GLU A 612 CG CD OE1 OE2
REMARK 470 SER A 626 CB OG
REMARK 470 LYS A 631 CG CD CE NZ
REMARK 470 LYS A 707 CG CD CE NZ
REMARK 470 ASP A 724 CG OD1 OD2
REMARK 470 GLU A 726 CG CD OE1 OE2
REMARK 470 LYS A 779 CG CD CE NZ
REMARK 470 GLU A 826 CG CD OE1 OE2
REMARK 470 GLN A 868 CG CD OE1 NE2
REMARK 470 LYS A 870 CG CD CE NZ
REMARK 470 ASP A 889 CG OD1 OD2
REMARK 470 ASP A 903 CG OD1 OD2
REMARK 470 ASN A 904 CG OD1 ND2
REMARK 470 GLN A 915 CG CD OE1 NE2
REMARK 470 GLU A 916 CG CD OE1 OE2
REMARK 470 LYS A 956 CG CD CE NZ
REMARK 470 GLN A 965 CG CD OE1 NE2
REMARK 470 LYS A1018 CE NZ
REMARK 470 GLU A1023 CG CD OE1 OE2
REMARK 470 LYS A1046 CG CD CE NZ
REMARK 470 GLU A1047 CG CD OE1 OE2
REMARK 470 LYS A1049 CG CD CE NZ
REMARK 470 GLU A1062 CG CD OE1 OE2
REMARK 470 LYS A1217 CE NZ
REMARK 470 LYS A1283 CG CD CE NZ
REMARK 470 ASP A1284 CG OD1 OD2
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 N HIS A 0 NI NI A 1404 1.70
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 MET A 1 46.54 -177.72
REMARK 500 ASN A 3 37.28 -61.47
REMARK 500 LEU A 4 -56.64 -128.55
REMARK 500 ALA A 5 132.52 62.07
REMARK 500 LEU A 124 33.61 -99.85
REMARK 500 ILE A 190 73.36 50.97
REMARK 500 ASP A 192 -8.71 -55.15
REMARK 500 ARG A 283 72.02 -115.30
REMARK 500 LEU A 351 -41.88 68.42
REMARK 500 LYS A 461 -73.85 -65.33
REMARK 500 ASP A 462 47.09 -92.80
REMARK 500 LYS A 472 129.08 -37.72
REMARK 500 THR A 767 91.79 75.59
REMARK 500 VAL A 768 -87.94 59.91
REMARK 500 ASP A 820 -178.71 -171.29
REMARK 500 HIS A 862 32.03 -144.18
REMARK 500 ARG A 864 90.56 80.03
REMARK 500 ILE A 871 -128.08 -102.95
REMARK 500 ASP A 903 -145.84 -77.53
REMARK 500 LYS A 951 49.12 77.76
REMARK 500 TYR A1032 78.15 -112.43
REMARK 500 PRO A1070 -167.11 -79.12
REMARK 500 CYS A1135 -127.99 54.14
REMARK 500 GLU A1173 158.41 -44.14
REMARK 500 LYS A1283 -64.35 -102.67
REMARK 500 ASP A1294 -166.82 -106.93
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 862 GLY A 863 -134.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A1404 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 0 ND1
REMARK 620 2 HIS A 524 NE2 59.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 369 O
REMARK 620 2 LEU A 370 O 77.8
REMARK 620 3 LEU A 372 O 107.1 87.8
REMARK 620 4 ILE A 374 O 103.3 172.4 84.7
REMARK 620 5 SER A 389 OG 82.0 90.7 170.2 96.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PNS A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 A 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 1404
DBREF 4ZXH A 1 1318 UNP B7H2D0 B7H2D0_ACIB3 1 1318
SEQADV 4ZXH GLY A -1 UNP B7H2D0 EXPRESSION TAG
SEQADV 4ZXH HIS A 0 UNP B7H2D0 EXPRESSION TAG
SEQRES 1 A 1320 GLY HIS MET ASN ASN LEU ALA ARG LEU GLU PRO GLU VAL
SEQRES 2 A 1320 LEU SER ARG HIS ALA ILE SER SER GLU GLN LEU GLY ILE
SEQRES 3 A 1320 TRP TYR ILE GLN ARG LEU GLU PRO THR CYS SER ALA TYR
SEQRES 4 A 1320 ASN MET VAL VAL ALA PHE ASP VAL LYS VAL ASN GLN SER
SEQRES 5 A 1320 LEU GLY ASN LYS PRO ILE GLU ILE LEU GLU ALA VAL MET
SEQRES 6 A 1320 HIS ASP TYR PRO LEU LEU ARG VAL SER MET PRO ALA ASN
SEQRES 7 A 1320 ASP GLN GLY ILE GLU GLN LEU ILE TRP ASP ARG VAL TYR
SEQRES 8 A 1320 PRO ASN ILE ILE PHE SER ASP ALA ARG HIS ILE GLU ALA
SEQRES 9 A 1320 SER ASP LEU THR GLN LEU VAL GLU GLN ASP THR LYS GLN
SEQRES 10 A 1320 PRO PHE ASP LEU THR GLN PRO PRO LEU TRP ARG ILE HIS
SEQRES 11 A 1320 CYS TYR GLU CYS GLY GLN ASN HIS TYR VAL ILE ALA PHE
SEQRES 12 A 1320 VAL ILE HIS HIS ALA LEU MET ASP PHE TRP SER ILE GLY
SEQRES 13 A 1320 LEU LEU LEU ARG ASP VAL SER LYS ARG PHE GLY LEU VAL
SEQRES 14 A 1320 ALA GLU SER ASP ALA VAL ASN GLY ILE GLU PHE VAL GLN
SEQRES 15 A 1320 TYR ALA ASP LYS GLN GLN SER SER VAL ILE ASP ASP THR
SEQRES 16 A 1320 ASP GLU SER LEU ILE PHE TRP LYS ASN ALA LEU LYS HIS
SEQRES 17 A 1320 ALA PRO HIS VAL HIS SER ILE PRO LEU ASP TYR PRO ARG
SEQRES 18 A 1320 PRO ALA VAL GLN GLN HIS LYS GLY SER SER LEU VAL PHE
SEQRES 19 A 1320 ARG VAL SER GLU SER VAL SER SER GLY LEU VAL ASN LEU
SEQRES 20 A 1320 ALA LYS ASP TYR GLU ILE THR LEU PHE GLY LEU VAL LEU
SEQRES 21 A 1320 SER GLY PHE TYR VAL LEU LEU HIS LYS LEU SER ASN GLU
SEQRES 22 A 1320 ASN ASN LEU VAL ILE ALA THR PRO VAL ALA GLY ARG LEU
SEQRES 23 A 1320 GLU ARG SER LEU ARG ASN ALA LEU GLY GLN PHE VAL ASN
SEQRES 24 A 1320 THR ILE ALA ILE HIS MET ASP ILE ASP ALA ASP GLN THR
SEQRES 25 A 1320 LEU ARG GLN PHE THR GLN GLN VAL GLN GLU GLN LEU ARG
SEQRES 26 A 1320 GLN SER LEU LYS HIS GLN LYS ILE ALA PHE SER ARG VAL
SEQRES 27 A 1320 VAL GLU ALA VAL SER PRO LYS ARG ASP GLY SER ILE ASN
SEQRES 28 A 1320 PRO LEU ALA GLN ILE GLY MET PHE TRP GLU ARG LEU GLY
SEQRES 29 A 1320 GLY MET ASP GLU PHE LYS GLU LEU LEU LEU PRO ILE GLN
SEQRES 30 A 1320 THR PRO ALA THR LEU VAL GLY GLN ASP LEU THR LEU GLY
SEQRES 31 A 1320 SER PHE PRO VAL ARG GLN GLN GLU GLY GLN LEU ASP ILE
SEQRES 32 A 1320 THR LEU GLU MET GLY GLY GLU TYR GLN GLY GLU LEU VAL
SEQRES 33 A 1320 GLY VAL LEU LYS TYR ASN THR ASP LEU PHE SER ALA GLN
SEQRES 34 A 1320 SER ALA GLU ASN MET VAL GLN LEU LEU GLN ALA VAL LEU
SEQRES 35 A 1320 SER GLU MET VAL ALA HIS PRO GLU ARG LYS ILE VAL GLU
SEQRES 36 A 1320 LEU ASP ILE ALA PRO ASP TYR LYS ASP GLY ILE GLN PHE
SEQRES 37 A 1320 GLU ALA LEU ARG GLY LYS ALA THR ASP TYR ALA GLN HIS
SEQRES 38 A 1320 ASP LEU PHE ALA MET ILE LEU LYS GLN ILE ASP GLU ARG
SEQRES 39 A 1320 GLY ASP ASN HIS ALA LEU THR SER ASN ASP HIS THR VAL
SEQRES 40 A 1320 SER TYR ARG GLU LEU GLY GLN HIS ILE ALA GLY ILE ALA
SEQRES 41 A 1320 GLU TYR LEU ARG ALA HIS GLY ILE THR GLN GLY ASP ARG
SEQRES 42 A 1320 VAL GLY LEU MET LEU ASP ARG THR ALA LEU LEU PRO ALA
SEQRES 43 A 1320 ALA ILE LEU GLY ILE TRP ALA ALA GLY ALA ALA TYR VAL
SEQRES 44 A 1320 PRO LEU ASP PRO ASN PHE PRO THR GLU ARG LEU GLN ASN
SEQRES 45 A 1320 ILE ILE GLU ASP ALA GLU PRO LYS VAL ILE LEU THR GLN
SEQRES 46 A 1320 THR GLU LEU MET ASP GLY LEU ASN VAL SER VAL PRO ARG
SEQRES 47 A 1320 LEU ASP ILE ASN GLN ALA GLY VAL VAL ALA LEU GLU GLN
SEQRES 48 A 1320 VAL ARG GLU THR LEU ALA PHE GLY ASP ILE ALA TYR VAL
SEQRES 49 A 1320 MET TYR THR SER GLY SER THR GLY LYS PRO LYS GLY VAL
SEQRES 50 A 1320 ARG ILE GLY HIS PRO SER ILE ILE ASN PHE LEU LEU SER
SEQRES 51 A 1320 MET ASN ASP ARG LEU GLN VAL THR THR GLU THR GLN LEU
SEQRES 52 A 1320 LEU ALA ILE THR THR TYR ALA PHE ASP ILE SER ILE LEU
SEQRES 53 A 1320 GLU LEU LEU ILE PRO LEU MET TYR GLY GLY VAL VAL HIS
SEQRES 54 A 1320 VAL CYS PRO ARG GLU VAL SER GLN ASP GLY ILE GLN LEU
SEQRES 55 A 1320 VAL ASP TYR LEU ASN ALA LYS SER ILE ASN VAL LEU GLN
SEQRES 56 A 1320 ALA THR PRO ALA THR TRP LYS MET LEU LEU ASP SER GLU
SEQRES 57 A 1320 TRP SER GLY ASN ALA GLY LEU THR ALA LEU CYS GLY GLY
SEQRES 58 A 1320 GLU ALA LEU ASP THR ILE LEU ALA GLU LYS LEU LEU GLY
SEQRES 59 A 1320 LYS VAL GLY CYS LEU TRP ASN VAL TYR GLY PRO THR GLU
SEQRES 60 A 1320 THR THR VAL TRP SER SER ALA ALA ARG ILE THR ASP ALA
SEQRES 61 A 1320 LYS TYR ILE ASP LEU GLY GLU PRO LEU ALA ASN THR GLN
SEQRES 62 A 1320 LEU TYR VAL LEU ASP GLU GLN GLN ARG LEU VAL PRO PRO
SEQRES 63 A 1320 GLY VAL MET GLY GLU LEU TRP ILE GLY GLY ASP GLY LEU
SEQRES 64 A 1320 ALA VAL ASP TYR TRP GLN ARG PRO GLU LEU THR ASP ALA
SEQRES 65 A 1320 GLN PHE ARG THR LEU PRO SER LEU PRO ASN ALA GLY ARG
SEQRES 66 A 1320 LEU TYR ARG THR GLY ASP LYS VAL CYS LEU ARG THR ASP
SEQRES 67 A 1320 GLY ARG LEU THR HIS HIS GLY ARG LEU ASP PHE GLN VAL
SEQRES 68 A 1320 LYS ILE ARG GLY PHE ARG ILE GLU LEU GLY GLU ILE GLU
SEQRES 69 A 1320 ASN VAL LEU LYS GLN ILE ASP GLY ILE THR ASP ALA VAL
SEQRES 70 A 1320 VAL LEU VAL LYS THR THR GLY ASP ASN ASP GLN LYS LEU
SEQRES 71 A 1320 VAL ALA TYR VAL THR GLY GLN GLU LEU ASP ILE ALA GLY
SEQRES 72 A 1320 LEU LYS LYS ASN LEU GLN ILE HIS LEU PRO ALA TYR MET
SEQRES 73 A 1320 VAL PRO SER ALA PHE ILE ARG LEU ASP GLU PHE PRO MET
SEQRES 74 A 1320 THR ALA ASN LYS LYS LEU ASP ARG LYS ALA PHE PRO GLU
SEQRES 75 A 1320 PRO ILE PHE GLU GLN SER ASN ASP TYR VAL ALA PRO ARG
SEQRES 76 A 1320 ASP PRO ILE GLU ILE GLU LEU CYS THR THR PHE GLU GLN
SEQRES 77 A 1320 ILE LEU SER VAL LYS ARG VAL GLY ILE HIS ASP ASP PHE
SEQRES 78 A 1320 PHE GLU LEU GLY GLY HIS SER LEU LEU ALA VAL LYS LEU
SEQRES 79 A 1320 VAL ASN HIS LEU LYS LYS ALA PHE GLY THR GLU LEU SER
SEQRES 80 A 1320 VAL ALA LEU LEU ALA GLN TYR SER THR VAL GLU ARG LEU
SEQRES 81 A 1320 GLY GLU ILE ILE ARG GLU ASN LYS GLU ILE LYS PRO SER
SEQRES 82 A 1320 ILE VAL ILE GLU LEU ARG ARG GLY THR TYR GLU GLN PRO
SEQRES 83 A 1320 LEU TRP LEU PHE HIS PRO ILE GLY GLY SER THR PHE CYS
SEQRES 84 A 1320 TYR MET GLU LEU SER ARG HIS LEU ASN PRO ASN ARG THR
SEQRES 85 A 1320 LEU ARG ALA ILE GLN SER PRO GLY LEU ILE GLU ALA ASP
SEQRES 86 A 1320 ALA ALA GLU VAL ALA ILE GLU GLU MET ALA THR LEU TYR
SEQRES 87 A 1320 ILE ALA GLU MET GLN LYS MET GLN PRO GLN GLY PRO TYR
SEQRES 88 A 1320 PHE LEU GLY GLY TRP CYS PHE GLY GLY ALA ILE ALA TYR
SEQRES 89 A 1320 GLU ILE SER ARG GLN LEU ARG GLN MET GLY GLN GLN VAL
SEQRES 90 A 1320 THR GLY ILE VAL MET ILE ASP THR ARG ALA PRO ILE PRO
SEQRES 91 A 1320 GLU ASN VAL PRO GLU ASP ALA ASP ASP ALA MET LEU LEU
SEQRES 92 A 1320 SER TRP PHE ALA ARG ASP LEU ALA ALA PRO TYR GLY LYS
SEQRES 93 A 1320 LYS LEU THR ILE PRO ALA GLN TYR LEU ARG GLU LEU SER
SEQRES 94 A 1320 PRO ASP GLN MET PHE ASP HIS VAL LEU LYS GLU ALA LYS
SEQRES 95 A 1320 ALA ILE ASN VAL LEU PRO LEU ASP ALA ASP PRO SER ASP
SEQRES 96 A 1320 PHE ARG LEU TYR PHE ASP THR TYR LEU ALA ASN GLY ILE
SEQRES 97 A 1320 ALA LEU GLN THR TYR PHE PRO GLU PRO GLU ASP PHE PRO
SEQRES 98 A 1320 ILE LEU LEU VAL LYS ALA LYS ASP GLU GLN GLU ASP PHE
SEQRES 99 A 1320 GLY GLU SER LEU GLY TRP ASP GLN LEU VAL LYS ASP THR
SEQRES 100 A 1320 LEU THR GLN VAL ASP LEU PRO GLY ASP HIS SER SER ILE
SEQRES 101 A 1320 MET TYR ALA GLU ASN VAL VAL ALA VAL ALA GLN THR ILE
SEQRES 102 A 1320 ASP GLN MET TYR PRO ILE PRO
HET PNS A1401 27
HET PX4 A1402 46
HET K A1403 1
HET NI A1404 1
HETNAM PNS 4'-PHOSPHOPANTETHEINE
HETNAM PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
HETNAM K POTASSIUM ION
HETNAM NI NICKEL (II) ION
FORMUL 2 PNS C11 H23 N2 O7 P S
FORMUL 3 PX4 C36 H73 N O8 P 1+
FORMUL 4 K K 1+
FORMUL 5 NI NI 2+
FORMUL 6 HOH *25(H2 O)
HELIX 1 AA1 SER A 18 GLU A 31 1 14
HELIX 2 AA2 GLN A 49 GLY A 52 5 4
HELIX 3 AA3 ASN A 53 TYR A 66 1 14
HELIX 4 AA4 PRO A 67 LEU A 69 5 3
HELIX 5 AA5 GLU A 101 LYS A 114 1 14
HELIX 6 AA6 ASP A 149 PHE A 164 1 16
HELIX 7 AA7 ILE A 176 GLN A 186 1 11
HELIX 8 AA8 ASP A 194 LEU A 204 1 11
HELIX 9 AA9 SER A 235 ASP A 248 1 14
HELIX 10 AB1 THR A 252 ASN A 270 1 19
HELIX 11 AB2 GLU A 285 ARG A 289 5 5
HELIX 12 AB3 THR A 310 HIS A 328 1 19
HELIX 13 AB4 ALA A 332 SER A 341 1 10
HELIX 14 AB5 MET A 364 LEU A 372 5 9
HELIX 15 AB6 SER A 425 HIS A 446 1 22
HELIX 16 AB7 PHE A 466 ARG A 470 5 5
HELIX 17 AB8 ASP A 475 HIS A 479 5 5
HELIX 18 AB9 ASP A 480 GLY A 493 1 14
HELIX 19 AC1 TYR A 507 HIS A 524 1 18
HELIX 20 AC2 ALA A 540 ALA A 552 1 13
HELIX 21 AC3 PRO A 564 GLU A 576 1 13
HELIX 22 AC4 THR A 584 MET A 587 5 4
HELIX 23 AC5 ASN A 600 ALA A 602 5 3
HELIX 24 AC6 ALA A 606 VAL A 610 5 5
HELIX 25 AC7 HIS A 639 GLN A 654 1 16
HELIX 26 AC8 ILE A 671 ILE A 678 1 8
HELIX 27 AC9 PRO A 690 GLN A 695 1 6
HELIX 28 AD1 ASP A 696 SER A 708 1 13
HELIX 29 AD2 THR A 715 ASP A 724 1 10
HELIX 30 AD3 ASP A 743 GLY A 752 1 10
HELIX 31 AD4 PRO A 763 THR A 767 5 5
HELIX 32 AD5 ARG A 824 GLN A 831 1 8
HELIX 33 AD6 GLU A 877 GLN A 887 1 11
HELIX 34 AD7 ASP A 918 LEU A 930 1 13
HELIX 35 AD8 PRO A 931 VAL A 935 5 5
HELIX 36 AD9 ASP A 954 PHE A 958 5 5
HELIX 37 AE1 ASP A 974 SER A 989 1 16
HELIX 38 AE2 HIS A 1005 GLY A 1021 1 17
HELIX 39 AE3 SER A 1025 TYR A 1032 1 8
HELIX 40 AE4 THR A 1034 ASN A 1045 1 12
HELIX 41 AE5 THR A 1075 CYS A 1077 5 3
HELIX 42 AE6 TYR A 1078 LEU A 1085 1 8
HELIX 43 AE7 SER A 1096 ILE A 1100 5 5
HELIX 44 AE8 ALA A 1108 GLN A 1124 1 17
HELIX 45 AE9 CYS A 1135 MET A 1151 1 17
HELIX 46 AF1 ILE A 1167 VAL A 1171 5 5
HELIX 47 AF2 ASP A 1176 ALA A 1190 1 15
HELIX 48 AF3 PRO A 1191 GLY A 1193 5 3
HELIX 49 AF4 PRO A 1199 GLU A 1205 1 7
HELIX 50 AF5 SER A 1207 ILE A 1222 1 16
HELIX 51 AF6 ASP A 1230 THR A 1250 1 21
HELIX 52 AF7 GLY A 1277 LEU A 1281 5 5
HELIX 53 AF8 SER A 1296 MET A 1299 5 4
HELIX 54 AF9 TYR A 1300 TYR A 1315 1 16
SHEET 1 AA1 3 VAL A 11 ALA A 16 0
SHEET 2 AA1 3 GLY A 79 TRP A 85 -1 O GLN A 82 N HIS A 15
SHEET 3 AA1 3 VAL A 71 SER A 72 -1 N SER A 72 O LEU A 83
SHEET 1 AA2 3 VAL A 11 ALA A 16 0
SHEET 2 AA2 3 GLY A 79 TRP A 85 -1 O GLN A 82 N HIS A 15
SHEET 3 AA2 3 ALA A 75 ASN A 76 -1 N ASN A 76 O GLY A 79
SHEET 1 AA3 6 ILE A 92 ASP A 96 0
SHEET 2 AA3 6 TRP A 125 GLY A 133 1 O CYS A 129 N ILE A 93
SHEET 3 AA3 6 HIS A 136 HIS A 144 -1 O HIS A 136 N CYS A 132
SHEET 4 AA3 6 ASN A 38 VAL A 47 -1 N VAL A 45 O TYR A 137
SHEET 5 AA3 6 LEU A 385 SER A 389 -1 O GLY A 388 N ASP A 44
SHEET 6 AA3 6 LEU A 380 VAL A 381 -1 N LEU A 380 O LEU A 387
SHEET 1 AA4 4 GLY A 227 ARG A 233 0
SHEET 2 AA4 4 GLU A 412 ASN A 420 -1 O GLY A 415 N PHE A 232
SHEET 3 AA4 4 ILE A 401 TYR A 409 -1 N THR A 402 O LYS A 418
SHEET 4 AA4 4 ILE A 354 TRP A 358 1 N GLY A 355 O LEU A 403
SHEET 1 AA5 2 ASN A 273 ALA A 277 0
SHEET 2 AA5 2 ALA A 300 ASP A 304 -1 O ILE A 301 N ILE A 276
SHEET 1 AA6 9 VAL A 505 SER A 506 0
SHEET 2 AA6 9 HIS A 496 THR A 499 -1 N LEU A 498 O VAL A 505
SHEET 3 AA6 9 VAL A 685 VAL A 688 1 O VAL A 686 N ALA A 497
SHEET 4 AA6 9 GLN A 660 ALA A 663 1 N LEU A 661 O HIS A 687
SHEET 5 AA6 9 VAL A 711 ALA A 714 1 O VAL A 711 N LEU A 662
SHEET 6 AA6 9 ASN A 730 GLY A 738 1 O THR A 734 N LEU A 712
SHEET 7 AA6 9 VAL A 754 TYR A 761 1 O CYS A 756 N ALA A 735
SHEET 8 AA6 9 SER A 771 ILE A 775 -1 O ALA A 773 N ASN A 759
SHEET 9 AA6 9 GLU A 785 PRO A 786 -1 O GLU A 785 N ALA A 772
SHEET 1 AA7 4 ALA A 555 PRO A 558 0
SHEET 2 AA7 4 ARG A 531 MET A 535 1 N VAL A 532 O ALA A 555
SHEET 3 AA7 4 VAL A 579 THR A 582 1 O LEU A 581 N GLY A 533
SHEET 4 AA7 4 ARG A 596 ASP A 598 1 O LEU A 597 N THR A 582
SHEET 1 AA8 3 ILE A 619 THR A 625 0
SHEET 2 AA8 3 LYS A 633 GLY A 638 -1 O ILE A 637 N ALA A 620
SHEET 3 AA8 3 ASP A 820 TYR A 821 -1 O ASP A 820 N ARG A 636
SHEET 1 AA9 4 THR A 790 LEU A 795 0
SHEET 2 AA9 4 MET A 807 GLY A 814 -1 O GLU A 809 N LEU A 795
SHEET 3 AA9 4 LEU A 844 LEU A 853 -1 O TYR A 845 N ILE A 812
SHEET 4 AA9 4 PHE A 832 ARG A 833 -1 N ARG A 833 O LEU A 844
SHEET 1 AB1 4 THR A 790 LEU A 795 0
SHEET 2 AB1 4 MET A 807 GLY A 814 -1 O GLU A 809 N LEU A 795
SHEET 3 AB1 4 LEU A 844 LEU A 853 -1 O TYR A 845 N ILE A 812
SHEET 4 AB1 4 LEU A 859 HIS A 861 -1 O THR A 860 N CYS A 852
SHEET 1 AB2 3 ILE A 891 THR A 901 0
SHEET 2 AB2 3 ASP A 905 GLY A 914 -1 O TYR A 911 N VAL A 895
SHEET 3 AB2 3 ALA A 938 ARG A 941 1 O ALA A 938 N ALA A 910
SHEET 1 AB3 7 VAL A1053 ARG A1057 0
SHEET 2 AB3 7 LEU A1091 ILE A1094 -1 O ALA A1093 N ILE A1054
SHEET 3 AB3 7 LEU A1065 PHE A1068 1 N LEU A1067 O ARG A1092
SHEET 4 AB3 7 TYR A1129 TRP A1134 1 O PHE A1130 N TRP A1066
SHEET 5 AB3 7 VAL A1155 ILE A1161 1 O THR A1156 N TYR A1129
SHEET 6 AB3 7 ILE A1260 ALA A1265 1 O LEU A1261 N MET A1160
SHEET 7 AB3 7 LEU A1286 LEU A1291 1 O THR A1287 N LEU A1262
LINK ND1 HIS A 0 NI NI A1404 1555 1555 2.09
LINK O GLU A 369 K K A1403 1555 1555 2.91
LINK O LEU A 370 K K A1403 1555 1555 2.97
LINK O LEU A 372 K K A1403 1555 1555 2.93
LINK O ILE A 374 K K A1403 1555 1555 2.75
LINK OG SER A 389 K K A1403 1555 1555 2.95
LINK OG SER A1006 P24 PNS A1401 1555 1555 1.61
LINK NE2 HIS A 524 NI NI A1404 1555 5545 2.11
CISPEP 1 PRO A 122 PRO A 123 0 1.80
CISPEP 2 GLY A 1127 PRO A 1128 0 4.03
SITE 1 AC1 13 GLY A 23 TYR A 37 THR A 298 PHE A 333
SITE 2 AC1 13 SER A 334 ARG A 344 ASN A 349 PHE A 357
SITE 3 AC1 13 GLN A 398 LEU A 399 HIS A1005 SER A1006
SITE 4 AC1 13 HOH A1515
SITE 1 AC2 8 PRO A 55 LEU A 59 TRP A 125 TYR A 137
SITE 2 AC2 8 PHE A 141 LEU A 157 VAL A 160 PHE A 164
SITE 1 AC3 5 GLU A 369 LEU A 370 LEU A 372 ILE A 374
SITE 2 AC3 5 SER A 389
SITE 1 AC4 3 GLY A -1 HIS A 0 HIS A 524
CRYST1 116.187 116.187 348.607 90.00 90.00 90.00 P 43 21 2 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 0.008607 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008607 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002869 0.00000
TER 10202 PRO A1318
MASTER 526 0 4 54 52 0 9 610283 1 83 102
END |