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HEADER BIOSYNTHETIC PROTEIN 20-MAY-15 4ZXI
TITLE CRYSTAL STRUCTURE OF HOLO-AB3403 A FOUR DOMAIN NONRIBOSOMAL PEPTIDE
TITLE 2 SYNTHETASE BOUND TO AMP AND GLYCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROCIDINE SYNTHETASE 3;
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 4ZXI 1 JRNL
REVDAT 1 30-DEC-15 4ZXI 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. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 52895
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2971
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 45.0399 - 7.9867 1.00 4565 145 0.1704 0.2157
REMARK 3 2 7.9867 - 6.3450 1.00 4546 150 0.1774 0.2268
REMARK 3 3 6.3450 - 5.5446 1.00 4576 140 0.1694 0.2455
REMARK 3 4 5.5446 - 5.0383 1.00 4565 136 0.1428 0.1955
REMARK 3 5 5.0383 - 4.6776 1.00 4580 142 0.1229 0.1495
REMARK 3 6 4.6776 - 4.4021 1.00 4561 149 0.1181 0.1702
REMARK 3 7 4.4021 - 4.1818 1.00 4580 142 0.1203 0.1672
REMARK 3 8 4.1818 - 3.9999 1.00 4551 134 0.1308 0.1862
REMARK 3 9 3.9999 - 3.8460 1.00 4603 145 0.1387 0.2027
REMARK 3 10 3.8460 - 3.7133 1.00 4563 139 0.1520 0.2158
REMARK 3 11 3.7133 - 3.5973 1.00 4578 140 0.1688 0.2192
REMARK 3 12 3.5973 - 3.4945 1.00 4548 143 0.1752 0.2464
REMARK 3 13 3.4945 - 3.4025 1.00 4572 135 0.1906 0.2204
REMARK 3 14 3.4025 - 3.3195 1.00 4556 159 0.2061 0.2895
REMARK 3 15 3.3195 - 3.2441 1.00 4594 134 0.2269 0.2564
REMARK 3 16 3.2441 - 3.1751 1.00 4578 142 0.2428 0.3094
REMARK 3 17 3.1751 - 3.1116 1.00 4546 144 0.2608 0.2806
REMARK 3 18 3.1116 - 3.0529 1.00 4564 118 0.2703 0.2914
REMARK 3 19 3.0529 - 2.9984 1.00 4619 142 0.2818 0.3110
REMARK 3 20 2.9984 - 2.9475 1.00 4578 151 0.2953 0.3427
REMARK 3 21 2.9475 - 2.9000 1.00 4550 141 0.3195 0.3962
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.65
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 10400
REMARK 3 ANGLE : 1.181 14180
REMARK 3 CHIRALITY : 0.045 1641
REMARK 3 PLANARITY : 0.006 1828
REMARK 3 DIHEDRAL : 13.630 3759
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 1054:1318))
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6603 -59.6363 -10.7392
REMARK 3 T TENSOR
REMARK 3 T11: 0.2254 T22: 0.4476
REMARK 3 T33: 0.2848 T12: -0.0259
REMARK 3 T13: -0.0941 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 2.7684 L22: 1.7849
REMARK 3 L33: 2.5065 L12: -0.1869
REMARK 3 L13: -0.6567 L23: 0.1272
REMARK 3 S TENSOR
REMARK 3 S11: -0.0473 S12: -0.1855 S13: -0.2878
REMARK 3 S21: 0.1457 S22: 0.1717 S23: -0.1031
REMARK 3 S31: 0.0880 S32: 0.1130 S33: -0.1200
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 191:445))
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1633 -37.0298 -16.1697
REMARK 3 T TENSOR
REMARK 3 T11: 0.2712 T22: 0.5120
REMARK 3 T33: 0.4623 T12: -0.0759
REMARK 3 T13: -0.0593 T23: 0.1103
REMARK 3 L TENSOR
REMARK 3 L11: 2.0271 L22: 1.2675
REMARK 3 L33: 0.9390 L12: -0.5042
REMARK 3 L13: -0.4884 L23: 0.1182
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: 0.3173 S13: 0.6328
REMARK 3 S21: 0.0804 S22: 0.0382 S23: -0.2263
REMARK 3 S31: -0.2456 S32: 0.1295 S33: -0.0243
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 446:480))
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5815 -22.7319 -43.0715
REMARK 3 T TENSOR
REMARK 3 T11: 0.4994 T22: 0.8751
REMARK 3 T33: 1.1102 T12: 0.0575
REMARK 3 T13: 0.0189 T23: 0.3998
REMARK 3 L TENSOR
REMARK 3 L11: 1.3998 L22: 0.3074
REMARK 3 L33: 4.3288 L12: 0.0172
REMARK 3 L13: 2.4304 L23: 0.2835
REMARK 3 S TENSOR
REMARK 3 S11: -0.1462 S12: 0.5602 S13: 0.3510
REMARK 3 S21: 0.0213 S22: 0.0033 S23: -0.6226
REMARK 3 S31: -0.6001 S32: 0.5152 S33: 0.1556
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 481:862))
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7546 -30.4039 -51.1487
REMARK 3 T TENSOR
REMARK 3 T11: 0.2727 T22: 0.3908
REMARK 3 T33: 0.3699 T12: 0.0492
REMARK 3 T13: 0.0356 T23: 0.1394
REMARK 3 L TENSOR
REMARK 3 L11: 2.2627 L22: 2.4829
REMARK 3 L33: 2.4777 L12: -0.3542
REMARK 3 L13: 1.1138 L23: -1.0393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0155 S12: -0.0097 S13: -0.2539
REMARK 3 S21: -0.1439 S22: -0.0653 S23: -0.1761
REMARK 3 S31: 0.1535 S32: 0.1207 S33: 0.0678
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 863:959))
REMARK 3 ORIGIN FOR THE GROUP (A): -39.5770 -42.8419 -23.9892
REMARK 3 T TENSOR
REMARK 3 T11: 0.2123 T22: 0.4402
REMARK 3 T33: 0.4051 T12: -0.0128
REMARK 3 T13: 0.0322 T23: 0.1025
REMARK 3 L TENSOR
REMARK 3 L11: 4.1369 L22: 2.2248
REMARK 3 L33: 3.6535 L12: -1.3529
REMARK 3 L13: 0.8330 L23: -1.1238
REMARK 3 S TENSOR
REMARK 3 S11: -0.0168 S12: -0.0574 S13: -0.0543
REMARK 3 S21: 0.0417 S22: 0.0645 S23: -0.0433
REMARK 3 S31: -0.2210 S32: 0.1489 S33: -0.0636
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 960:973))
REMARK 3 ORIGIN FOR THE GROUP (A): -44.0175 -47.8393 -6.0158
REMARK 3 T TENSOR
REMARK 3 T11: 0.3442 T22: 0.3837
REMARK 3 T33: 0.5645 T12: -0.0739
REMARK 3 T13: -0.0782 T23: 0.0933
REMARK 3 L TENSOR
REMARK 3 L11: 1.0143 L22: 2.1268
REMARK 3 L33: 8.1364 L12: -1.4737
REMARK 3 L13: 2.8795 L23: -4.1711
REMARK 3 S TENSOR
REMARK 3 S11: -0.5532 S12: 0.1317 S13: 0.4585
REMARK 3 S21: 0.4969 S22: -0.5621 S23: -0.8862
REMARK 3 S31: -1.0757 S32: 0.5469 S33: 1.1021
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 974:1044))
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3077 -58.9779 -1.2317
REMARK 3 T TENSOR
REMARK 3 T11: 0.2236 T22: 0.2717
REMARK 3 T33: 0.3557 T12: 0.0364
REMARK 3 T13: 0.0017 T23: 0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 4.1043 L22: 1.2748
REMARK 3 L33: 2.8649 L12: 2.2349
REMARK 3 L13: -0.7251 L23: 0.0548
REMARK 3 S TENSOR
REMARK 3 S11: 0.0465 S12: 0.0121 S13: -0.2578
REMARK 3 S21: 0.0108 S22: -0.0545 S23: -0.2706
REMARK 3 S31: 0.1520 S32: 0.2918 S33: -0.0390
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 1045:1053))
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8739 -73.6830 -0.9092
REMARK 3 T TENSOR
REMARK 3 T11: 0.6911 T22: 0.5095
REMARK 3 T33: 0.6594 T12: 0.0703
REMARK 3 T13: 0.0831 T23: -0.1671
REMARK 3 L TENSOR
REMARK 3 L11: 0.5707 L22: 0.8631
REMARK 3 L33: 5.2041 L12: 0.6153
REMARK 3 L13: -1.5888 L23: -2.1082
REMARK 3 S TENSOR
REMARK 3 S11: 0.2600 S12: 0.4876 S13: -0.1940
REMARK 3 S21: -1.1479 S22: -0.2834 S23: -0.1727
REMARK 3 S31: 0.2030 S32: 0.4992 S33: 0.0278
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 1054:1318))
REMARK 3 ORIGIN FOR THE GROUP (A): -45.6059 -71.5901 13.8926
REMARK 3 T TENSOR
REMARK 3 T11: 0.3136 T22: 0.1590
REMARK 3 T33: 0.2284 T12: -0.0211
REMARK 3 T13: -0.0179 T23: 0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 2.7637 L22: 2.4934
REMARK 3 L33: 2.4403 L12: 0.5202
REMARK 3 L13: -0.0294 L23: -0.0740
REMARK 3 S TENSOR
REMARK 3 S11: 0.1252 S12: -0.1086 S13: -0.1722
REMARK 3 S21: 0.2665 S22: -0.0835 S23: -0.1296
REMARK 3 S31: 0.2729 S32: 0.0719 S33: -0.0314
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 4ZXI 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_1000210023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-15
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) : 1.0332
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 : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52900
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 45.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.33600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.250
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 (%): 68.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
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 171.01000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.05000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.05000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 256.51500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.05000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.05000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.50500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.05000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.05000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 256.51500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.05000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.05000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 85.50500
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 171.01000
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: 3230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 ASN A 2 CG OD1 ND2
REMARK 470 GLU A 8 CG CD OE1 OE2
REMARK 470 GLN A 49 CD OE1 NE2
REMARK 470 LYS A 54 CE NZ
REMARK 470 GLN A 78 CG CD OE1 NE2
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 101 CD OE1 OE2
REMARK 470 GLN A 180 CG CD OE1 NE2
REMARK 470 LYS A 184 CG CD CE NZ
REMARK 470 VAL A 189 CG1 CG2
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 HIS A 206 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 236 CG CD OE1 OE2
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 GLN A 313 CG CD OE1 NE2
REMARK 470 LEU A 361 CG CD1 CD2
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 GLN A 427 CG CD OE1 NE2
REMARK 470 GLU A 442 CG CD OE1 OE2
REMARK 470 LYS A 450 CG CD CE NZ
REMARK 470 ASP A 459 CG OD1 OD2
REMARK 470 LYS A 461 CG CD CE NZ
REMARK 470 LYS A 487 CD CE NZ
REMARK 470 HIS A 503 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 566 CG CD OE1 OE2
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 LYS A 631 CG CD CE NZ
REMARK 470 GLU A 658 CG CD OE1 OE2
REMARK 470 GLU A 692 CG CD OE1 OE2
REMARK 470 ASN A 705 CG OD1 ND2
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 ASP A 866 CG OD1 OD2
REMARK 470 PHE A 867 CG CD1 CD2 CE1 CE2 CZ
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 ASP A 918 CG OD1 OD2
REMARK 470 LYS A 924 CG CD CE NZ
REMARK 470 LYS A 956 CG CD CE NZ
REMARK 470 GLU A 964 CG CD OE1 OE2
REMARK 470 GLN A 965 CG CD OE1 NE2
REMARK 470 SER A 966 OG
REMARK 470 ASN A 967 CG OD1 ND2
REMARK 470 ASP A 968 CG OD1 OD2
REMARK 470 ASN A1014 CG OD1 ND2
REMARK 470 LYS A1018 CD 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 ARG A1058 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1062 CG CD OE1 OE2
REMARK 470 GLN A1150 CG CD OE1 NE2
REMARK 470 GLN A1154 CD OE1 NE2
REMARK 470 GLU A1173 CG CD OE1 OE2
REMARK 470 LYS A1217 CE NZ
REMARK 470 GLU A1254 CG CD OE1 OE2
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: 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 3 52.29 -108.69
REMARK 500 ALA A 5 130.31 68.37
REMARK 500 ASN A 76 -150.28 -121.44
REMARK 500 HIS A 206 30.05 -91.48
REMARK 500 HIS A 225 53.19 34.19
REMARK 500 TYR A 249 -148.31 -102.43
REMARK 500 LEU A 351 -28.31 61.65
REMARK 500 LEU A 361 87.78 54.68
REMARK 500 MET A 364 42.19 -99.83
REMARK 500 PRO A 377 -5.36 -59.07
REMARK 500 ASP A 459 84.60 -60.97
REMARK 500 LYS A 472 127.03 -35.72
REMARK 500 ALA A 497 -56.79 -124.63
REMARK 500 SER A 593 59.55 -90.35
REMARK 500 ALA A 706 -85.31 -66.45
REMARK 500 LYS A 707 3.83 -61.71
REMARK 500 THR A 767 96.07 76.12
REMARK 500 VAL A 768 -90.77 53.26
REMARK 500 THR A 855 37.28 -69.00
REMARK 500 ASP A 856 -28.58 -151.94
REMARK 500 HIS A 862 14.52 -141.04
REMARK 500 ARG A 864 174.88 68.25
REMARK 500 GLN A 965 -81.55 -65.41
REMARK 500 PRO A1070 -166.15 -78.38
REMARK 500 GLN A1126 -143.87 -136.35
REMARK 500 CYS A1135 -131.83 51.40
REMARK 500 ASN A1223 34.63 73.20
REMARK 500 LYS A1283 -66.36 -96.56
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 A1405 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 0 N
REMARK 620 2 HIS A 0 ND1 97.2
REMARK 620 3 HIS A 524 NE2 156.6 61.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1406 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 764 OG1
REMARK 620 2 GLY A1402 O 83.6
REMARK 620 3 AMP A1403 O5' 162.8 113.5
REMARK 620 N 1 2
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 GLY A 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue XP4 A 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1406
DBREF 4ZXI A 1 1318 UNP B7H2D0 B7H2D0_ACIB3 1 1318
SEQADV 4ZXI GLY A -1 UNP B7H2D0 EXPRESSION TAG
SEQADV 4ZXI 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 21
HET GLY A1402 5
HET AMP A1403 23
HET XP4 A1404 40
HET NI A1405 1
HET MG A1406 1
HETNAM PNS 4'-PHOSPHOPANTETHEINE
HETNAM GLY GLYCINE
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM XP4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHATE
HETNAM NI NICKEL (II) ION
HETNAM MG MAGNESIUM ION
FORMUL 2 PNS C11 H23 N2 O7 P S
FORMUL 3 GLY C2 H5 N O2
FORMUL 4 AMP C10 H14 N5 O7 P
FORMUL 5 XP4 C31 H60 O8 P 1-
FORMUL 6 NI NI 2+
FORMUL 7 MG MG 2+
FORMUL 8 HOH *16(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 LYS A 205 1 12
HELIX 9 AA9 SER A 235 TYR A 249 1 15
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 LEU A 326 1 17
HELIX 13 AB4 LYS A 327 GLN A 329 5 3
HELIX 14 AB5 ALA A 332 SER A 341 1 10
HELIX 15 AB6 LYS A 368 LEU A 372 5 5
HELIX 16 AB7 SER A 425 HIS A 446 1 22
HELIX 17 AB8 LYS A 450 LEU A 454 5 5
HELIX 18 AB9 ASP A 475 HIS A 479 5 5
HELIX 19 AC1 ASP A 480 GLY A 493 1 14
HELIX 20 AC2 TYR A 507 HIS A 524 1 18
HELIX 21 AC3 ALA A 540 ALA A 552 1 13
HELIX 22 AC4 PRO A 564 GLU A 576 1 13
HELIX 23 AC5 THR A 584 MET A 587 5 4
HELIX 24 AC6 ASN A 600 ALA A 602 5 3
HELIX 25 AC7 ALA A 606 VAL A 610 5 5
HELIX 26 AC8 HIS A 639 GLN A 654 1 16
HELIX 27 AC9 ILE A 671 ILE A 678 1 8
HELIX 28 AD1 PRO A 690 GLN A 695 1 6
HELIX 29 AD2 ASP A 696 SER A 708 1 13
HELIX 30 AD3 THR A 715 SER A 725 1 11
HELIX 31 AD4 ASP A 743 GLY A 752 1 10
HELIX 32 AD5 PRO A 763 THR A 767 5 5
HELIX 33 AD6 ARG A 824 GLN A 831 1 8
HELIX 34 AD7 GLU A 877 GLN A 887 1 11
HELIX 35 AD8 ASP A 918 LEU A 930 1 13
HELIX 36 AD9 PRO A 931 VAL A 935 5 5
HELIX 37 AE1 ASP A 954 PHE A 958 5 5
HELIX 38 AE2 ASP A 974 SER A 989 1 16
HELIX 39 AE3 HIS A 1005 PHE A 1020 1 16
HELIX 40 AE4 SER A 1025 TYR A 1032 1 8
HELIX 41 AE5 THR A 1034 ASN A 1045 1 12
HELIX 42 AE6 CYS A 1077 LEU A 1085 1 9
HELIX 43 AE7 SER A 1096 ILE A 1100 5 5
HELIX 44 AE8 ALA A 1108 LYS A 1122 1 15
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 ALA A 1221 1 15
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 THR A 379 VAL A 381 -1 N LEU A 380 O LEU A 387
SHEET 1 AA4 6 GLY A 227 VAL A 234 0
SHEET 2 AA4 6 GLU A 412 ASN A 420 -1 O LEU A 417 N LEU A 230
SHEET 3 AA4 6 ILE A 401 TYR A 409 -1 N THR A 402 O LYS A 418
SHEET 4 AA4 6 ILE A 354 TRP A 358 1 N PHE A 357 O MET A 405
SHEET 5 AA4 6 ASN A 273 VAL A 280 1 N ALA A 277 O ILE A 354
SHEET 6 AA4 6 ASN A 297 ASP A 304 -1 O ILE A 299 N THR A 278
SHEET 1 AA5 2 HIS A 496 LEU A 498 0
SHEET 2 AA5 2 VAL A 505 SER A 506 -1 O VAL A 505 N ALA A 497
SHEET 1 AA6 4 ALA A 555 PRO A 558 0
SHEET 2 AA6 4 ARG A 531 MET A 535 1 N VAL A 532 O ALA A 555
SHEET 3 AA6 4 VAL A 579 THR A 582 1 O LEU A 581 N GLY A 533
SHEET 4 AA6 4 ARG A 596 ASP A 598 1 O LEU A 597 N ILE A 580
SHEET 1 AA7 3 ILE A 619 THR A 625 0
SHEET 2 AA7 3 LYS A 633 GLY A 638 -1 O ILE A 637 N ALA A 620
SHEET 3 AA7 3 ASP A 820 TYR A 821 -1 O ASP A 820 N ARG A 636
SHEET 1 AA8 7 VAL A 685 VAL A 688 0
SHEET 2 AA8 7 GLN A 660 ALA A 663 1 N LEU A 661 O HIS A 687
SHEET 3 AA8 7 VAL A 711 ALA A 714 1 O VAL A 711 N LEU A 662
SHEET 4 AA8 7 ASN A 730 GLY A 738 1 O THR A 734 N LEU A 712
SHEET 5 AA8 7 VAL A 754 TYR A 761 1 O CYS A 756 N ALA A 735
SHEET 6 AA8 7 SER A 771 ILE A 775 -1 O ALA A 773 N ASN A 759
SHEET 7 AA8 7 GLU A 785 PRO A 786 -1 O GLU A 785 N ALA A 772
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 PHE A 939 ARG A 941 1 O ILE A 940 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 ILE A1158
SHEET 7 AB3 7 LEU A1286 LEU A1291 1 O THR A1287 N LEU A1262
LINK N HIS A 0 NI NI A1405 1555 1555 1.95
LINK ND1 HIS A 0 NI NI A1405 1555 1555 2.02
LINK OG1 THR A 764 MG MG A1406 1555 1555 2.96
LINK OG SER A1006 P24 PNS A1401 1555 1555 1.64
LINK O GLY A1402 MG MG A1406 1555 1555 1.97
LINK O5' AMP A1403 MG MG A1406 1555 1555 2.67
LINK NE2 HIS A 524 NI NI A1405 1555 5454 1.94
CISPEP 1 PRO A 122 PRO A 123 0 -0.27
SITE 1 AC1 9 GLY A 23 ILE A 27 TYR A 37 THR A 298
SITE 2 AC1 9 SER A 334 VAL A 337 ARG A 344 ASN A 349
SITE 3 AC1 9 SER A1006
SITE 1 AC2 10 PHE A 669 ASP A 670 GLY A 739 GLY A 762
SITE 2 AC2 10 PRO A 763 THR A 764 VAL A 768 LYS A 952
SITE 3 AC2 10 AMP A1403 MG A1406
SITE 1 AC3 14 THR A 625 SER A 626 GLY A 739 GLU A 740
SITE 2 AC3 14 ASN A 759 VAL A 760 TYR A 761 PRO A 763
SITE 3 AC3 14 ASP A 849 HIS A 861 ARG A 864 LYS A 952
SITE 4 AC3 14 GLY A1402 MG A1406
SITE 1 AC4 5 ILE A 56 LEU A 59 TYR A 137 LEU A 157
SITE 2 AC4 5 VAL A 160
SITE 1 AC5 3 GLY A -1 HIS A 0 HIS A 524
SITE 1 AC6 3 THR A 764 GLY A1402 AMP A1403
CRYST1 116.100 116.100 342.020 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 0.008613 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008613 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002924 0.00000
TER 10092 PRO A1318
MASTER 549 0 6 54 52 0 14 610184 1 91 102
END |