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HEADER SIGNALING PROTEIN 31-JUL-20 6ZYF
TITLE NOTUM_GHRELIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HNOTUM;
COMPND 5 EC: 3.1.1.98;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOTUM, OK/SW-CL.30;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS NOTUM GHRELIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONES
REVDAT 1 10-MAR-21 6ZYF 0
JRNL AUTH Y.ZHAO,L.N.SCHUHMACHER,M.ROBERTS,S.KAKUGAWA,G.BINEVA-TODD,
JRNL AUTH 2 S.HOWELL,N.O'REILLY,C.PERRET,A.P.SNIJDERS,J.P.VINCENT,
JRNL AUTH 3 E.Y.JONES
JRNL TITL NOTUM DEACYLATES OCTANOYLATED GHRELIN
JRNL REF MOLECULAR METABOLISM 2021
JRNL DOI 10.1016/J.MOLMET.2021.101201
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 44663
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2257
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 92.0400 - 5.5200 1.00 2891 159 0.1827 0.1905
REMARK 3 2 5.5200 - 4.3800 1.00 2748 146 0.1656 0.1903
REMARK 3 3 4.3800 - 3.8300 1.00 2710 150 0.1885 0.2460
REMARK 3 4 3.8300 - 3.4800 1.00 2684 147 0.2151 0.2268
REMARK 3 5 3.4800 - 3.2300 1.00 2692 146 0.2335 0.2527
REMARK 3 6 3.2300 - 3.0400 1.00 2682 117 0.2546 0.2753
REMARK 3 7 3.0400 - 2.8800 0.99 2671 132 0.2672 0.3016
REMARK 3 8 2.8800 - 2.7600 0.99 2643 156 0.2679 0.2531
REMARK 3 9 2.7600 - 2.6500 0.99 2606 145 0.2771 0.3060
REMARK 3 10 2.6500 - 2.5600 0.99 2622 122 0.2843 0.3077
REMARK 3 11 2.5600 - 2.4800 0.99 2626 140 0.3011 0.3456
REMARK 3 12 2.4800 - 2.4100 0.98 2594 133 0.3088 0.3003
REMARK 3 13 2.4100 - 2.3500 0.98 2599 146 0.3373 0.3594
REMARK 3 14 2.3500 - 2.2900 0.98 2577 117 0.3587 0.3587
REMARK 3 15 2.2900 - 2.2400 0.97 2564 157 0.3632 0.4001
REMARK 3 16 2.2400 - 2.1900 0.95 2497 144 0.3828 0.3705
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.53
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 86 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.5398 29.4557 -19.9132
REMARK 3 T TENSOR
REMARK 3 T11: 0.4847 T22: 0.2339
REMARK 3 T33: -0.1849 T12: -0.6144
REMARK 3 T13: -0.1244 T23: -0.8531
REMARK 3 L TENSOR
REMARK 3 L11: 0.0567 L22: 0.0826
REMARK 3 L33: 0.0373 L12: -0.0155
REMARK 3 L13: 0.0183 L23: 0.0398
REMARK 3 S TENSOR
REMARK 3 S11: -0.1751 S12: -0.2209 S13: 0.5212
REMARK 3 S21: 0.1289 S22: -0.0643 S23: -0.3105
REMARK 3 S31: -0.0846 S32: 0.0277 S33: -0.1377
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.4575 21.0980 -22.9363
REMARK 3 T TENSOR
REMARK 3 T11: 0.2005 T22: 0.3707
REMARK 3 T33: 0.0909 T12: -0.6057
REMARK 3 T13: -0.2624 T23: -0.3100
REMARK 3 L TENSOR
REMARK 3 L11: 0.3584 L22: 0.3544
REMARK 3 L33: 0.2151 L12: -0.1119
REMARK 3 L13: 0.2686 L23: 0.3057
REMARK 3 S TENSOR
REMARK 3 S11: 0.5241 S12: -0.1645 S13: 0.5835
REMARK 3 S21: -0.1135 S22: -0.0759 S23: -0.4647
REMARK 3 S31: -0.2936 S32: -0.4007 S33: 0.3539
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.4824 12.5313 -34.2413
REMARK 3 T TENSOR
REMARK 3 T11: 0.3638 T22: 0.3459
REMARK 3 T33: 0.2319 T12: -0.1924
REMARK 3 T13: 0.0127 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.3571 L22: 1.2422
REMARK 3 L33: 0.6150 L12: 0.5204
REMARK 3 L13: 0.2182 L23: -0.2493
REMARK 3 S TENSOR
REMARK 3 S11: 0.0370 S12: 0.0379 S13: 0.0436
REMARK 3 S21: -0.1238 S22: -0.0049 S23: 0.0205
REMARK 3 S31: 0.1374 S32: -0.0960 S33: 0.0267
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 86 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2070 31.2850 -12.8616
REMARK 3 T TENSOR
REMARK 3 T11: 0.3544 T22: 0.4315
REMARK 3 T33: 0.1584 T12: -0.2291
REMARK 3 T13: 0.0447 T23: -0.1104
REMARK 3 L TENSOR
REMARK 3 L11: 0.4812 L22: 0.5160
REMARK 3 L33: 0.0320 L12: 0.4557
REMARK 3 L13: 0.2222 L23: 0.2505
REMARK 3 S TENSOR
REMARK 3 S11: -0.4491 S12: 0.4788 S13: -0.0806
REMARK 3 S21: -0.2465 S22: 0.4860 S23: 0.1038
REMARK 3 S31: 0.2061 S32: -0.4403 S33: -0.0020
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 185 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3678 28.6198 -3.6876
REMARK 3 T TENSOR
REMARK 3 T11: 0.3463 T22: 0.3911
REMARK 3 T33: 0.2909 T12: -0.1780
REMARK 3 T13: 0.0521 T23: -0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 0.1974 L22: 0.1135
REMARK 3 L33: 0.0857 L12: 0.0295
REMARK 3 L13: 0.1440 L23: 0.0056
REMARK 3 S TENSOR
REMARK 3 S11: -0.1265 S12: 0.1349 S13: -0.0472
REMARK 3 S21: -0.1214 S22: 0.1930 S23: 0.0485
REMARK 3 S31: 0.2979 S32: -0.2095 S33: 0.0057
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 186 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9203 40.4688 -11.3976
REMARK 3 T TENSOR
REMARK 3 T11: 0.3656 T22: 0.3719
REMARK 3 T33: 0.3568 T12: -0.1722
REMARK 3 T13: 0.0316 T23: 0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 0.4116 L22: 0.2320
REMARK 3 L33: 0.1165 L12: -0.0611
REMARK 3 L13: 0.1534 L23: -0.0640
REMARK 3 S TENSOR
REMARK 3 S11: -0.4539 S12: 0.4570 S13: 0.4345
REMARK 3 S21: -0.2121 S22: 0.3798 S23: 0.0891
REMARK 3 S31: -0.0163 S32: -0.0444 S33: -0.0537
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 225 THROUGH 286 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9213 32.3196 -3.1246
REMARK 3 T TENSOR
REMARK 3 T11: 0.2383 T22: 0.1962
REMARK 3 T33: 0.3657 T12: -0.0089
REMARK 3 T13: 0.0264 T23: -0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 0.4896 L22: 0.1511
REMARK 3 L33: -0.1161 L12: 0.3839
REMARK 3 L13: 0.0354 L23: 0.0294
REMARK 3 S TENSOR
REMARK 3 S11: -0.1781 S12: 0.1479 S13: 0.0778
REMARK 3 S21: 0.0627 S22: 0.2205 S23: -0.3567
REMARK 3 S31: 0.0659 S32: 0.0955 S33: -0.0147
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 287 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7955 25.5621 -0.5157
REMARK 3 T TENSOR
REMARK 3 T11: 0.2435 T22: 0.2704
REMARK 3 T33: 0.5812 T12: 0.0164
REMARK 3 T13: 0.0560 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.4978 L22: 0.3284
REMARK 3 L33: 0.3193 L12: 0.3432
REMARK 3 L13: 0.1066 L23: -0.1168
REMARK 3 S TENSOR
REMARK 3 S11: -0.1832 S12: 0.0118 S13: -0.3953
REMARK 3 S21: 0.0681 S22: 0.1498 S23: -0.5834
REMARK 3 S31: 0.0114 S32: 0.1548 S33: 0.0040
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 395 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6022 21.8094 13.2791
REMARK 3 T TENSOR
REMARK 3 T11: 0.5353 T22: 0.4092
REMARK 3 T33: 0.5452 T12: -0.0557
REMARK 3 T13: -0.1022 T23: 0.2197
REMARK 3 L TENSOR
REMARK 3 L11: 0.2226 L22: 0.0304
REMARK 3 L33: 0.1517 L12: 0.1158
REMARK 3 L13: 0.1245 L23: -0.0068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0418 S12: -1.2924 S13: -0.5673
REMARK 3 S21: 0.6392 S22: -0.1159 S23: 0.0703
REMARK 3 S31: 0.2987 S32: -0.0046 S33: -0.0240
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 86 THROUGH 194 OR
REMARK 3 RESID 199 THROUGH 418 OR RESID 432
REMARK 3 THROUGH 451 OR RESID 501))
REMARK 3 SELECTION : (CHAIN B AND (RESID 86 THROUGH 143 OR
REMARK 3 (RESID 144 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB OR NAME CG OR NAME
REMARK 3 CD )) OR RESID 145 THROUGH 451 OR RESID
REMARK 3 501))
REMARK 3 ATOM PAIRS NUMBER : 3269
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ZYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1292110524.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92819
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45353
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 92.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4UZQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0 0.1 M KCL 15% PEG
REMARK 280 MME 5000, EVAPORATION, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 37.70900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 92.03600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.70900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 92.03600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 78
REMARK 465 THR A 79
REMARK 465 GLY A 80
REMARK 465 SER A 81
REMARK 465 ALA A 82
REMARK 465 GLN A 83
REMARK 465 GLN A 84
REMARK 465 LEU A 85
REMARK 465 LYS A 197
REMARK 465 ASN A 198
REMARK 465 ASP A 420
REMARK 465 SER A 421
REMARK 465 HIS A 422
REMARK 465 LYS A 423
REMARK 465 ALA A 424
REMARK 465 SER A 425
REMARK 465 LYS A 426
REMARK 465 THR A 427
REMARK 465 PRO A 428
REMARK 465 LEU A 429
REMARK 465 LYS A 430
REMARK 465 GLY A 431
REMARK 465 GLY A 452
REMARK 465 THR A 453
REMARK 465 LYS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
REMARK 465 GLU B 78
REMARK 465 THR B 79
REMARK 465 GLY B 80
REMARK 465 SER B 81
REMARK 465 ALA B 82
REMARK 465 GLN B 83
REMARK 465 GLN B 84
REMARK 465 LEU B 85
REMARK 465 SER B 195
REMARK 465 GLU B 196
REMARK 465 LYS B 197
REMARK 465 ASN B 198
REMARK 465 HIS B 419
REMARK 465 ASP B 420
REMARK 465 SER B 421
REMARK 465 HIS B 422
REMARK 465 LYS B 423
REMARK 465 ALA B 424
REMARK 465 SER B 425
REMARK 465 LYS B 426
REMARK 465 THR B 427
REMARK 465 PRO B 428
REMARK 465 LEU B 429
REMARK 465 LYS B 430
REMARK 465 GLY B 431
REMARK 465 GLY B 452
REMARK 465 THR B 453
REMARK 465 LYS B 454
REMARK 465 HIS B 455
REMARK 465 HIS B 456
REMARK 465 HIS B 457
REMARK 465 HIS B 458
REMARK 465 HIS B 459
REMARK 465 HIS B 460
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 ARG A 144 NE CZ NH1 NH2
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 NZ LYS A 194 O GLU A 196 2.13
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 TRP A 128 -140.15 59.10
REMARK 500 SER A 192 168.33 65.07
REMARK 500 SER A 195 -97.25 -84.61
REMARK 500 ALA A 232 -121.74 60.29
REMARK 500 PHE A 339 76.09 -119.84
REMARK 500 GLU A 390 154.08 71.37
REMARK 500 ILE A 391 -31.86 -164.71
REMARK 500 TRP B 128 -140.53 60.00
REMARK 500 SER B 193 78.81 -105.75
REMARK 500 ALA B 232 -122.15 60.52
REMARK 500 ILE B 283 -13.10 50.70
REMARK 500 THR B 352 37.64 -97.82
REMARK 500 GLU B 390 154.80 71.30
REMARK 500 ILE B 391 -138.00 -165.05
REMARK 500 ILE B 392 -22.76 38.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 K4Q B 502
DBREF 6ZYF A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
DBREF 6ZYF B 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6ZYF GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF ALA A 232 UNP Q6P988 SER 232 CONFLICT
SEQADV 6ZYF SER A 330 UNP Q6P988 CYS 330 CONFLICT
SEQADV 6ZYF GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF GLU B 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF THR B 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF GLY B 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF ALA B 232 UNP Q6P988 SER 232 CONFLICT
SEQADV 6ZYF SER B 330 UNP Q6P988 CYS 330 CONFLICT
SEQADV 6ZYF GLY B 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF THR B 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF LYS B 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS B 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS B 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS B 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS B 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS B 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZYF HIS B 460 UNP Q6P988 EXPRESSION TAG
SEQRES 1 A 383 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 A 383 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 A 383 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 A 383 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 A 383 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 A 383 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 A 383 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 A 383 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 A 383 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 A 383 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 A 383 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 A 383 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER ALA ALA
SEQRES 13 A 383 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 A 383 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 A 383 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 A 383 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 A 383 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 A 383 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 A 383 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 A 383 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 A 383 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 A 383 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 A 383 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 A 383 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 A 383 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 A 383 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 A 383 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 A 383 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 A 383 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS
SEQRES 30 A 383 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 383 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 B 383 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 B 383 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 B 383 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 B 383 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 B 383 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 B 383 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 B 383 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 B 383 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 B 383 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 B 383 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 B 383 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER ALA ALA
SEQRES 13 B 383 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 B 383 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 B 383 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 B 383 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 B 383 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 B 383 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 B 383 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 B 383 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 B 383 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 B 383 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 B 383 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 B 383 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 B 383 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 B 383 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 B 383 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 B 383 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 B 383 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS
SEQRES 30 B 383 HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET K4Q A 502 15
HET NAG B 501 14
HET K4Q B 502 10
HET EDO B 503 4
HET EDO B 504 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM K4Q [(2~{S})-2-AZANYL-3-OXIDANYLIDENE-PROPYL] OCTANOATE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 K4Q 2(C11 H21 N O3)
FORMUL 7 EDO 2(C2 H6 O2)
FORMUL 9 HOH *56(H2 O)
HELIX 1 AA1 ASN A 132 MET A 143 1 12
HELIX 2 AA2 ARG A 144 SER A 148 5 5
HELIX 3 AA3 THR A 159 SER A 163 5 5
HELIX 4 AA4 MET A 203 GLY A 217 1 15
HELIX 5 AA5 ARG A 218 ALA A 223 5 6
HELIX 6 AA6 ALA A 232 LEU A 252 1 21
HELIX 7 AA7 ALA A 286 ASN A 299 1 14
HELIX 8 AA8 PRO A 303 ARG A 308 1 6
HELIX 9 AA9 GLU A 314 PHE A 319 5 6
HELIX 10 AB1 PHE A 320 TYR A 325 1 6
HELIX 11 AB2 PRO A 326 LEU A 328 5 3
HELIX 12 AB3 ASP A 340 ASP A 347 1 8
HELIX 13 AB4 GLY A 359 LEU A 375 1 17
HELIX 14 AB5 ARG A 394 ASP A 399 5 6
HELIX 15 AB6 LEU A 407 LEU A 418 1 12
HELIX 16 AB7 ASN B 132 MET B 143 1 12
HELIX 17 AB8 ARG B 144 SER B 148 5 5
HELIX 18 AB9 THR B 159 SER B 163 5 5
HELIX 19 AC1 MET B 203 GLY B 217 1 15
HELIX 20 AC2 ARG B 218 ALA B 223 5 6
HELIX 21 AC3 ALA B 232 LEU B 252 1 21
HELIX 22 AC4 ALA B 286 ASN B 299 1 14
HELIX 23 AC5 PRO B 303 PHE B 310 1 8
HELIX 24 AC6 GLU B 314 PHE B 319 5 6
HELIX 25 AC7 PHE B 320 TYR B 325 1 6
HELIX 26 AC8 PRO B 326 LEU B 328 5 3
HELIX 27 AC9 GLU B 341 ASP B 347 1 7
HELIX 28 AD1 GLN B 357 LYS B 376 1 20
HELIX 29 AD2 ARG B 394 ASP B 399 5 6
HELIX 30 AD3 LEU B 407 LEU B 418 1 12
SHEET 1 AA110 THR A 155 ARG A 156 0
SHEET 2 AA110 LEU A 89 LEU A 93 -1 N LEU A 89 O ARG A 156
SHEET 3 AA110 GLY A 108 LYS A 112 -1 O TYR A 109 N HIS A 92
SHEET 4 AA110 ASN A 176 ILE A 180 -1 O PHE A 179 N TYR A 110
SHEET 5 AA110 ARG A 119 LEU A 124 1 N LEU A 121 O ASN A 176
SHEET 6 AA110 VAL A 225 SER A 231 1 O ALA A 229 N LEU A 122
SHEET 7 AA110 GLN A 258 ASP A 264 1 O ARG A 260 N LEU A 228
SHEET 8 AA110 VAL A 332 VAL A 335 1 O VAL A 335 N ALA A 263
SHEET 9 AA110 SER A 381 ALA A 383 1 O PHE A 382 N VAL A 334
SHEET 10 AA110 HIS A 435 VAL A 437 1 O LEU A 436 N ALA A 383
SHEET 1 AA2 2 GLN A 401 VAL A 402 0
SHEET 2 AA2 2 THR A 405 SER A 406 -1 O THR A 405 N VAL A 402
SHEET 1 AA310 THR B 155 ARG B 156 0
SHEET 2 AA310 LEU B 89 LEU B 93 -1 N LEU B 89 O ARG B 156
SHEET 3 AA310 GLY B 108 LYS B 112 -1 O TYR B 109 N HIS B 92
SHEET 4 AA310 ASN B 176 ILE B 180 -1 O PHE B 179 N TYR B 110
SHEET 5 AA310 ARG B 119 LEU B 124 1 N PHE B 123 O ILE B 180
SHEET 6 AA310 VAL B 225 SER B 231 1 O ALA B 229 N LEU B 122
SHEET 7 AA310 GLN B 258 ASP B 264 1 O ARG B 260 N LEU B 228
SHEET 8 AA310 VAL B 332 VAL B 335 1 O VAL B 335 N ALA B 263
SHEET 9 AA310 SER B 381 ALA B 383 1 O PHE B 382 N VAL B 334
SHEET 10 AA310 HIS B 435 VAL B 437 1 O LEU B 436 N ALA B 383
SHEET 1 AA4 2 PHE B 339 ASP B 340 0
SHEET 2 AA4 2 LEU B 387 SER B 388 1 O SER B 388 N PHE B 339
SHEET 1 AA5 2 GLN B 401 VAL B 402 0
SHEET 2 AA5 2 THR B 405 SER B 406 -1 O THR B 405 N VAL B 402
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.03
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.03
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.03
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.03
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.03
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.03
SSBOND 8 CYS B 101 CYS B 183 1555 1555 2.03
SSBOND 9 CYS B 130 CYS B 136 1555 1555 2.03
SSBOND 10 CYS B 279 CYS B 285 1555 1555 2.03
SSBOND 11 CYS B 306 CYS B 318 1555 1555 2.03
SSBOND 12 CYS B 386 CYS B 449 1555 1555 2.03
SSBOND 13 CYS B 413 CYS B 432 1555 1555 2.03
SSBOND 14 CYS B 440 CYS B 445 1555 1555 2.03
LINK ND2 ASN A 96 C1 NAG A 501 1555 1555 1.44
LINK ND2 ASN B 96 C1 NAG B 501 1555 1555 1.44
CRYST1 75.418 184.072 61.811 90.00 90.00 90.00 P 21 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 0.013259 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016178 0.00000
TER 2818 THR A 451
TER 5615 THR B 451
MASTER 484 0 6 30 26 0 0 6 5730 2 91 60
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