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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 27-AUG-14 4W9R
TITLE CRYSTAL STRUCTURE OF UNCHARACTERISED PROTEIN COCH_1243 FROM
TITLE 2 CAPNOCYTOPHAGA OCHRACEA DSM 7271
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAPNOCYTOPHAGA OCHRACEA;
SOURCE 3 ORGANISM_TAXID: 521097;
SOURCE 4 STRAIN: ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845;
SOURCE 5 GENE: COCH_1243;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, UNKNOWN FUNCTION, GEBA
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,R.WU,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 1 10-SEP-14 4W9R 0
JRNL AUTH C.CHANG,R.WU,S.CLANCY,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF UNCHARACTERISED PROTEIN COCH_1243 FROM
JRNL TITL 2 CAPNOCYTOPHAGA OCHRACEA DSM 7271
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.3_1479)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 44135
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2221
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 43.3147 - 6.8032 1.00 2748 141 0.1639 0.1603
REMARK 3 2 6.8032 - 5.4032 1.00 2699 148 0.1609 0.2005
REMARK 3 3 5.4032 - 4.7212 1.00 2703 143 0.1291 0.1563
REMARK 3 4 4.7212 - 4.2899 1.00 2663 160 0.1250 0.1365
REMARK 3 5 4.2899 - 3.9827 1.00 2697 144 0.1410 0.1823
REMARK 3 6 3.9827 - 3.7480 0.99 2653 147 0.1669 0.1938
REMARK 3 7 3.7480 - 3.5604 1.00 2685 138 0.1826 0.2064
REMARK 3 8 3.5604 - 3.4055 0.99 2682 124 0.2156 0.2718
REMARK 3 9 3.4055 - 3.2744 1.00 2680 148 0.2225 0.2442
REMARK 3 10 3.2744 - 3.1615 1.00 2646 145 0.2309 0.2835
REMARK 3 11 3.1615 - 3.0626 1.00 2690 131 0.2422 0.2549
REMARK 3 12 3.0626 - 2.9751 0.99 2659 138 0.2500 0.3088
REMARK 3 13 2.9751 - 2.8968 0.98 2618 128 0.2572 0.3151
REMARK 3 14 2.8968 - 2.8261 0.96 2615 122 0.2698 0.3035
REMARK 3 15 2.8261 - 2.7619 0.91 2411 136 0.2583 0.3191
REMARK 3 16 2.7619 - 2.7031 0.78 2065 128 0.2559 0.2991
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.84
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 : 0.002 5953
REMARK 3 ANGLE : 0.692 8058
REMARK 3 CHIRALITY : 0.027 880
REMARK 3 PLANARITY : 0.004 1038
REMARK 3 DIHEDRAL : 10.592 2218
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 20 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2589 114.4292 11.5017
REMARK 3 T TENSOR
REMARK 3 T11: 0.6061 T22: -0.2102
REMARK 3 T33: 0.1396 T12: 0.1329
REMARK 3 T13: 0.1055 T23: 0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 0.0090 L22: 0.0114
REMARK 3 L33: 0.0170 L12: -0.0097
REMARK 3 L13: -0.0143 L23: 0.0040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0713 S12: -0.0121 S13: 0.0854
REMARK 3 S21: 0.1272 S22: 0.0241 S23: 0.0566
REMARK 3 S31: -0.3083 S32: -0.0932 S33: 0.1264
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7892 122.5515 11.0771
REMARK 3 T TENSOR
REMARK 3 T11: 0.6673 T22: 0.1099
REMARK 3 T33: 0.2522 T12: -0.2113
REMARK 3 T13: -0.0617 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.0124 L22: 0.0211
REMARK 3 L33: 0.0097 L12: 0.0146
REMARK 3 L13: -0.0048 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0768 S12: -0.0479 S13: 0.0438
REMARK 3 S21: 0.0815 S22: -0.0542 S23: -0.0706
REMARK 3 S31: -0.0142 S32: 0.0270 S33: 0.0057
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 309 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7842 94.5385 13.5173
REMARK 3 T TENSOR
REMARK 3 T11: 0.1917 T22: 0.1738
REMARK 3 T33: 0.2379 T12: 0.0127
REMARK 3 T13: -0.0417 T23: 0.0774
REMARK 3 L TENSOR
REMARK 3 L11: 0.0197 L22: 0.0382
REMARK 3 L33: 0.1366 L12: 0.0286
REMARK 3 L13: -0.0450 L23: -0.0644
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: -0.1600 S13: -0.0844
REMARK 3 S21: 0.0177 S22: -0.0816 S23: -0.0837
REMARK 3 S31: -0.1381 S32: 0.2273 S33: 0.0116
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 310 THROUGH 379 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6542 71.1815 21.3490
REMARK 3 T TENSOR
REMARK 3 T11: 0.2029 T22: 0.2219
REMARK 3 T33: 0.4153 T12: 0.1153
REMARK 3 T13: -0.0028 T23: 0.1781
REMARK 3 L TENSOR
REMARK 3 L11: 0.0354 L22: 0.0656
REMARK 3 L33: 0.0226 L12: -0.0057
REMARK 3 L13: -0.0104 L23: 0.0104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0336 S12: -0.0430 S13: -0.0692
REMARK 3 S21: 0.0722 S22: -0.0629 S23: 0.0010
REMARK 3 S31: 0.0471 S32: 0.0687 S33: -0.0701
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0177 100.0529 -17.0815
REMARK 3 T TENSOR
REMARK 3 T11: 0.3020 T22: 0.1284
REMARK 3 T33: 0.2384 T12: 0.0537
REMARK 3 T13: -0.0204 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0060 L22: 0.0056
REMARK 3 L33: 0.0058 L12: 0.0052
REMARK 3 L13: 0.0018 L23: -0.0021
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: 0.0585 S13: -0.0379
REMARK 3 S21: -0.0144 S22: -0.0433 S23: 0.0502
REMARK 3 S31: -0.0598 S32: -0.0560 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 62 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4106 99.4759 -18.5737
REMARK 3 T TENSOR
REMARK 3 T11: 0.2624 T22: 0.0917
REMARK 3 T33: 0.1494 T12: 0.0726
REMARK 3 T13: -0.0079 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.0563 L22: 0.0212
REMARK 3 L33: 0.0211 L12: 0.0211
REMARK 3 L13: 0.0155 L23: 0.0139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0698 S12: 0.0914 S13: -0.0150
REMARK 3 S21: -0.0114 S22: -0.0217 S23: 0.0240
REMARK 3 S31: -0.1381 S32: 0.0126 S33: 0.0175
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5780 102.7214 -16.0327
REMARK 3 T TENSOR
REMARK 3 T11: 0.2526 T22: 0.2182
REMARK 3 T33: 0.2632 T12: 0.0042
REMARK 3 T13: 0.0295 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.0156 L22: 0.0156
REMARK 3 L33: 0.0103 L12: 0.0110
REMARK 3 L13: -0.0022 L23: 0.0119
REMARK 3 S TENSOR
REMARK 3 S11: 0.1262 S12: 0.0400 S13: -0.0093
REMARK 3 S21: -0.0092 S22: -0.0275 S23: -0.1680
REMARK 3 S31: -0.1192 S32: 0.0732 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 233 THROUGH 344 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5481 131.8430 -22.1404
REMARK 3 T TENSOR
REMARK 3 T11: 0.3939 T22: -0.0822
REMARK 3 T33: 0.2362 T12: 0.0013
REMARK 3 T13: 0.0712 T23: 0.1796
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: 0.0134
REMARK 3 L33: 0.0341 L12: 0.0005
REMARK 3 L13: 0.0165 L23: -0.0202
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: 0.0488 S13: 0.1040
REMARK 3 S21: -0.0647 S22: -0.0318 S23: 0.0226
REMARK 3 S31: -0.0435 S32: 0.0337 S33: -0.0049
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 345 THROUGH 379 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9057 150.6329 -24.5712
REMARK 3 T TENSOR
REMARK 3 T11: 0.3268 T22: 0.1611
REMARK 3 T33: 0.5170 T12: -0.0136
REMARK 3 T13: 0.0219 T23: 0.1066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0051 L22: 0.0008
REMARK 3 L33: 0.0017 L12: -0.0021
REMARK 3 L13: 0.0028 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0309 S12: 0.0243 S13: 0.0253
REMARK 3 S21: -0.0006 S22: 0.0048 S23: 0.0409
REMARK 3 S31: -0.0408 S32: -0.0183 S33: -0.0000
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 4W9R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 1000
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SCALEPACK
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45202
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.1000
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) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.70
REMARK 200 R MERGE FOR SHELL (I) : 0.79500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M SODIUM ACETATE, 0.085M TRIS-CL,
REMARK 280 25.5% PEG4000, 15% GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.13033
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 92.26067
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.19550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 115.32583
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.06517
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 17
REMARK 465 ASN A 18
REMARK 465 ALA A 19
REMARK 465 LYS A 380
REMARK 465 ARG A 381
REMARK 465 LYS A 382
REMARK 465 SER A 383
REMARK 465 LYS A 384
REMARK 465 HIS A 385
REMARK 465 THR A 386
REMARK 465 LYS A 387
REMARK 465 VAL A 388
REMARK 465 ILE A 389
REMARK 465 GLU A 390
REMARK 465 PRO A 391
REMARK 465 ILE A 392
REMARK 465 GLU A 393
REMARK 465 PRO A 394
REMARK 465 THR A 395
REMARK 465 GLU A 396
REMARK 465 GLU A 397
REMARK 465 VAL A 398
REMARK 465 ALA A 399
REMARK 465 PRO A 400
REMARK 465 ALA A 401
REMARK 465 GLN A 402
REMARK 465 GLU A 403
REMARK 465 GLU A 404
REMARK 465 GLN A 405
REMARK 465 ASN A 406
REMARK 465 PRO A 407
REMARK 465 THR A 408
REMARK 465 ASP A 409
REMARK 465 GLU A 410
REMARK 465 SER A 411
REMARK 465 ASN A 412
REMARK 465 GLN A 413
REMARK 465 ASN A 414
REMARK 465 SER B 17
REMARK 465 ASN B 18
REMARK 465 LYS B 380
REMARK 465 ARG B 381
REMARK 465 LYS B 382
REMARK 465 SER B 383
REMARK 465 LYS B 384
REMARK 465 HIS B 385
REMARK 465 THR B 386
REMARK 465 LYS B 387
REMARK 465 VAL B 388
REMARK 465 ILE B 389
REMARK 465 GLU B 390
REMARK 465 PRO B 391
REMARK 465 ILE B 392
REMARK 465 GLU B 393
REMARK 465 PRO B 394
REMARK 465 THR B 395
REMARK 465 GLU B 396
REMARK 465 GLU B 397
REMARK 465 VAL B 398
REMARK 465 ALA B 399
REMARK 465 PRO B 400
REMARK 465 ALA B 401
REMARK 465 GLN B 402
REMARK 465 GLU B 403
REMARK 465 GLU B 404
REMARK 465 GLN B 405
REMARK 465 ASN B 406
REMARK 465 PRO B 407
REMARK 465 THR B 408
REMARK 465 ASP B 409
REMARK 465 GLU B 410
REMARK 465 SER B 411
REMARK 465 ASN B 412
REMARK 465 GLN B 413
REMARK 465 ASN B 414
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 20 CG CD OE1 NE2
REMARK 470 GLU A 100 CG CD OE1 OE2
REMARK 470 GLU A 152 CG CD OE1 OE2
REMARK 470 LYS A 153 CG CD CE NZ
REMARK 470 LYS A 229 CG CD CE NZ
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 ARG B 48 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 152 CG CD OE1 OE2
REMARK 470 LYS B 153 CG CD CE NZ
REMARK 470 GLU B 173 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 89 70.59 51.12
REMARK 500 VAL A 101 -66.88 -105.28
REMARK 500 ASN A 106 -119.65 57.13
REMARK 500 GLU A 118 -64.01 -128.86
REMARK 500 GLU A 139 -129.77 56.27
REMARK 500 LYS A 154 138.18 178.96
REMARK 500 ASN A 185 -75.71 -115.28
REMARK 500 GLU A 197 18.82 56.89
REMARK 500 THR A 262 -64.13 -99.46
REMARK 500 ASP A 362 -127.64 52.22
REMARK 500 THR B 61 -61.27 -109.30
REMARK 500 ASN B 106 -120.57 52.20
REMARK 500 GLU B 118 -64.70 -123.60
REMARK 500 GLU B 139 -129.66 56.70
REMARK 500 LYS B 154 138.85 -176.58
REMARK 500 ASN B 185 -76.41 -116.96
REMARK 500 GLU B 197 18.49 56.89
REMARK 500 THR B 262 -63.02 -99.56
REMARK 500 MSE B 264 -62.87 -109.02
REMARK 500 ASP B 362 -125.18 52.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC103154 RELATED DB: TARGETTRACK
DBREF 4W9R A 20 414 UNP C7M590 C7M590_CAPOD 20 414
DBREF 4W9R B 20 414 UNP C7M590 C7M590_CAPOD 20 414
SEQADV 4W9R SER A 17 UNP C7M590 EXPRESSION TAG
SEQADV 4W9R ASN A 18 UNP C7M590 EXPRESSION TAG
SEQADV 4W9R ALA A 19 UNP C7M590 EXPRESSION TAG
SEQADV 4W9R SER B 17 UNP C7M590 EXPRESSION TAG
SEQADV 4W9R ASN B 18 UNP C7M590 EXPRESSION TAG
SEQADV 4W9R ALA B 19 UNP C7M590 EXPRESSION TAG
SEQRES 1 A 398 SER ASN ALA GLN VAL ILE SER GLU THR PHE SER SER GLY
SEQRES 2 A 398 ARG LEU ASN ARG LYS GLN LYS ILE GLY ILE TYR LYS PRO
SEQRES 3 A 398 GLU LYS TYR THR ASP ARG GLN ALA TYR PRO LEU ILE VAL
SEQRES 4 A 398 VAL LEU ASN ALA GLU THR LEU MSE GLU PRO VAL VAL SER
SEQRES 5 A 398 MSE VAL ARG TYR TYR GLU GLN PHE GLY GLU MSE PRO LYS
SEQRES 6 A 398 CYS ILE VAL VAL GLY VAL TYR GLU PRO LYS GLN GLU ASP
SEQRES 7 A 398 VAL THR VAL VAL GLU GLU VAL GLY ARG PRO ILE ASN GLU
SEQRES 8 A 398 SER ALA ARG PHE PHE GLU PHE VAL SER ALA GLU LEU VAL
SEQRES 9 A 398 PRO TYR ILE GLN GLY LYS TYR PRO ILE ALA ASP LEU LYS
SEQRES 10 A 398 GLY VAL ILE ALA SER GLU GLU ALA GLY PHE LEU ALA ASN
SEQRES 11 A 398 TYR TYR MSE LEU ALA GLU LYS LYS PRO THR PHE ASN MSE
SEQRES 12 A 398 ILE VAL SER LEU ASN PRO VAL ALA LEU PRO ARG MSE GLY
SEQRES 13 A 398 GLU GLU PHE SER HIS ALA LEU ALA ALA GLY VAL PRO ASN
SEQRES 14 A 398 ARG LEU PHE TYR TYR MSE ALA THR ALA ASP VAL GLU ASN
SEQRES 15 A 398 LYS VAL VAL TYR ASP LYS ALA ILE GLN PHE GLU ARG ALA
SEQRES 16 A 398 MSE ARG SER ALA PRO VAL HIS GLU SER VAL GLU TYR HIS
SEQRES 17 A 398 PHE VAL ASP PHE LYS GLY SER SER VAL ASN ALA ALA LYS
SEQRES 18 A 398 LEU GLN GLY ILE ALA GLN ALA LEU ASP MSE CYS PHE ASP
SEQRES 19 A 398 ILE TYR LYS PRO ILE GLY GLY LYS GLU PHE LYS THR GLN
SEQRES 20 A 398 MSE GLU THR LEU GLU THR GLY ILE TYR GLU TYR LEU GLU
SEQRES 21 A 398 ASN LYS TYR ASN THR ILE TYR LYS GLN LEU GLY VAL LYS
SEQRES 22 A 398 LYS VAL PRO ILE LEU ASN ASP VAL MSE ALA THR TYR THR
SEQRES 23 A 398 ALA ILE ASN SER SER GLN ASP TRP GLU SER LEU LYS LYS
SEQRES 24 A 398 LEU ALA LYS TYR VAL GLU SER ASN GLY TYR LEU LYS THR
SEQRES 25 A 398 ALA MSE PRO ASN PHE PHE LEU ALA GLU TYR TYR GLU LYS
SEQRES 26 A 398 ILE GLY ASP ASP LYS LYS ALA LEU LYS THR TYR GLN LYS
SEQRES 27 A 398 ALA TYR THR GLU PRO ASN ILE ASP PHE ILE THR GLY ASP
SEQRES 28 A 398 LEU ILE ASN GLU ARG ILE THR HIS LEU GLN ALA THR LYS
SEQRES 29 A 398 ARG LYS SER LYS HIS THR LYS VAL ILE GLU PRO ILE GLU
SEQRES 30 A 398 PRO THR GLU GLU VAL ALA PRO ALA GLN GLU GLU GLN ASN
SEQRES 31 A 398 PRO THR ASP GLU SER ASN GLN ASN
SEQRES 1 B 398 SER ASN ALA GLN VAL ILE SER GLU THR PHE SER SER GLY
SEQRES 2 B 398 ARG LEU ASN ARG LYS GLN LYS ILE GLY ILE TYR LYS PRO
SEQRES 3 B 398 GLU LYS TYR THR ASP ARG GLN ALA TYR PRO LEU ILE VAL
SEQRES 4 B 398 VAL LEU ASN ALA GLU THR LEU MSE GLU PRO VAL VAL SER
SEQRES 5 B 398 MSE VAL ARG TYR TYR GLU GLN PHE GLY GLU MSE PRO LYS
SEQRES 6 B 398 CYS ILE VAL VAL GLY VAL TYR GLU PRO LYS GLN GLU ASP
SEQRES 7 B 398 VAL THR VAL VAL GLU GLU VAL GLY ARG PRO ILE ASN GLU
SEQRES 8 B 398 SER ALA ARG PHE PHE GLU PHE VAL SER ALA GLU LEU VAL
SEQRES 9 B 398 PRO TYR ILE GLN GLY LYS TYR PRO ILE ALA ASP LEU LYS
SEQRES 10 B 398 GLY VAL ILE ALA SER GLU GLU ALA GLY PHE LEU ALA ASN
SEQRES 11 B 398 TYR TYR MSE LEU ALA GLU LYS LYS PRO THR PHE ASN MSE
SEQRES 12 B 398 ILE VAL SER LEU ASN PRO VAL ALA LEU PRO ARG MSE GLY
SEQRES 13 B 398 GLU GLU PHE SER HIS ALA LEU ALA ALA GLY VAL PRO ASN
SEQRES 14 B 398 ARG LEU PHE TYR TYR MSE ALA THR ALA ASP VAL GLU ASN
SEQRES 15 B 398 LYS VAL VAL TYR ASP LYS ALA ILE GLN PHE GLU ARG ALA
SEQRES 16 B 398 MSE ARG SER ALA PRO VAL HIS GLU SER VAL GLU TYR HIS
SEQRES 17 B 398 PHE VAL ASP PHE LYS GLY SER SER VAL ASN ALA ALA LYS
SEQRES 18 B 398 LEU GLN GLY ILE ALA GLN ALA LEU ASP MSE CYS PHE ASP
SEQRES 19 B 398 ILE TYR LYS PRO ILE GLY GLY LYS GLU PHE LYS THR GLN
SEQRES 20 B 398 MSE GLU THR LEU GLU THR GLY ILE TYR GLU TYR LEU GLU
SEQRES 21 B 398 ASN LYS TYR ASN THR ILE TYR LYS GLN LEU GLY VAL LYS
SEQRES 22 B 398 LYS VAL PRO ILE LEU ASN ASP VAL MSE ALA THR TYR THR
SEQRES 23 B 398 ALA ILE ASN SER SER GLN ASP TRP GLU SER LEU LYS LYS
SEQRES 24 B 398 LEU ALA LYS TYR VAL GLU SER ASN GLY TYR LEU LYS THR
SEQRES 25 B 398 ALA MSE PRO ASN PHE PHE LEU ALA GLU TYR TYR GLU LYS
SEQRES 26 B 398 ILE GLY ASP ASP LYS LYS ALA LEU LYS THR TYR GLN LYS
SEQRES 27 B 398 ALA TYR THR GLU PRO ASN ILE ASP PHE ILE THR GLY ASP
SEQRES 28 B 398 LEU ILE ASN GLU ARG ILE THR HIS LEU GLN ALA THR LYS
SEQRES 29 B 398 ARG LYS SER LYS HIS THR LYS VAL ILE GLU PRO ILE GLU
SEQRES 30 B 398 PRO THR GLU GLU VAL ALA PRO ALA GLN GLU GLU GLN ASN
SEQRES 31 B 398 PRO THR ASP GLU SER ASN GLN ASN
MODRES 4W9R MSE A 63 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 69 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 79 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 149 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 159 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 171 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 191 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 212 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 247 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 264 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 298 MET MODIFIED RESIDUE
MODRES 4W9R MSE A 330 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 63 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 69 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 79 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 149 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 159 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 171 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 191 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 212 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 247 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 264 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 298 MET MODIFIED RESIDUE
MODRES 4W9R MSE B 330 MET MODIFIED RESIDUE
HET MSE A 63 8
HET MSE A 69 8
HET MSE A 79 8
HET MSE A 149 8
HET MSE A 159 8
HET MSE A 171 8
HET MSE A 191 8
HET MSE A 212 8
HET MSE A 247 8
HET MSE A 264 8
HET MSE A 298 8
HET MSE A 330 8
HET MSE B 63 8
HET MSE B 69 8
HET MSE B 79 8
HET MSE B 149 8
HET MSE B 159 8
HET MSE B 171 8
HET MSE B 191 8
HET MSE B 212 8
HET MSE B 247 8
HET MSE B 264 8
HET MSE B 298 8
HET MSE B 330 8
HET GOL A 501 6
HET GOL A 502 6
HET GOL A 503 6
HET ACT A 504 4
HET ACT A 505 4
HET GOL B 501 6
HET ACT B 502 4
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 24(C5 H11 N O2 SE)
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 6 ACT 3(C2 H3 O2 1-)
FORMUL 10 HOH *95(H2 O)
HELIX 1 AA1 ASN A 58 PHE A 76 1 19
HELIX 2 AA2 LYS A 91 THR A 96 1 6
HELIX 3 AA3 ASN A 106 GLU A 118 1 13
HELIX 4 AA4 GLU A 118 TYR A 127 1 10
HELIX 5 AA5 GLU A 139 ALA A 145 1 7
HELIX 6 AA6 ASN A 146 ALA A 151 5 6
HELIX 7 AA7 LEU A 168 ARG A 170 5 3
HELIX 8 AA8 MSE A 171 GLY A 182 1 12
HELIX 9 AA9 ASN A 198 ARG A 213 1 16
HELIX 10 AB1 VAL A 233 PHE A 249 1 17
HELIX 11 AB2 ASP A 250 LYS A 253 5 4
HELIX 12 AB3 GLY A 256 MSE A 264 1 9
HELIX 13 AB4 GLY A 270 GLY A 287 1 18
HELIX 14 AB5 ILE A 293 SER A 307 1 15
HELIX 15 AB6 ASP A 309 ASN A 323 1 15
HELIX 16 AB7 ALA A 329 GLY A 343 1 15
HELIX 17 AB8 ASP A 344 TYR A 356 1 13
HELIX 18 AB9 THR A 365 THR A 379 1 15
HELIX 19 AC1 ASN B 58 PHE B 76 1 19
HELIX 20 AC2 LYS B 91 THR B 96 1 6
HELIX 21 AC3 ASN B 106 GLU B 118 1 13
HELIX 22 AC4 GLU B 118 TYR B 127 1 10
HELIX 23 AC5 GLU B 139 ALA B 145 1 7
HELIX 24 AC6 ASN B 146 ALA B 151 5 6
HELIX 25 AC7 LEU B 168 ARG B 170 5 3
HELIX 26 AC8 MSE B 171 GLY B 182 1 12
HELIX 27 AC9 ASN B 198 ARG B 213 1 16
HELIX 28 AD1 VAL B 233 PHE B 249 1 17
HELIX 29 AD2 ASP B 250 LYS B 253 5 4
HELIX 30 AD3 GLY B 256 MSE B 264 1 9
HELIX 31 AD4 GLY B 270 GLY B 287 1 18
HELIX 32 AD5 ILE B 293 SER B 307 1 15
HELIX 33 AD6 ASP B 309 ASN B 323 1 15
HELIX 34 AD7 ALA B 329 ILE B 342 1 14
HELIX 35 AD8 ASP B 344 TYR B 356 1 13
HELIX 36 AD9 THR B 365 THR B 379 1 15
SHEET 1 AA1 8 VAL A 21 SER A 28 0
SHEET 2 AA1 8 ARG A 33 TYR A 40 -1 O GLN A 35 N PHE A 26
SHEET 3 AA1 8 ILE A 83 VAL A 87 -1 O VAL A 84 N TYR A 40
SHEET 4 AA1 8 TYR A 51 VAL A 56 1 N VAL A 56 O VAL A 85
SHEET 5 AA1 8 ILE A 129 SER A 138 1 O ILE A 136 N VAL A 55
SHEET 6 AA1 8 MSE A 159 PRO A 165 1 O LEU A 163 N ALA A 137
SHEET 7 AA1 8 LEU A 187 VAL A 196 1 O TYR A 190 N SER A 162
SHEET 8 AA1 8 VAL A 221 SER A 232 1 O GLU A 222 N LEU A 187
SHEET 1 AA2 8 VAL B 21 SER B 28 0
SHEET 2 AA2 8 ARG B 33 TYR B 40 -1 O GLN B 35 N PHE B 26
SHEET 3 AA2 8 ILE B 83 VAL B 87 -1 O VAL B 84 N TYR B 40
SHEET 4 AA2 8 TYR B 51 VAL B 56 1 N VAL B 56 O VAL B 87
SHEET 5 AA2 8 ILE B 129 SER B 138 1 O GLY B 134 N LEU B 53
SHEET 6 AA2 8 MSE B 159 PRO B 165 1 O VAL B 161 N VAL B 135
SHEET 7 AA2 8 LEU B 187 VAL B 196 1 O TYR B 190 N SER B 162
SHEET 8 AA2 8 VAL B 221 SER B 232 1 O GLU B 222 N LEU B 187
LINK C LEU A 62 N MSE A 63 1555 1555 1.33
LINK C MSE A 63 N GLU A 64 1555 1555 1.33
LINK C SER A 68 N MSE A 69 1555 1555 1.33
LINK C MSE A 69 N VAL A 70 1555 1555 1.33
LINK C GLU A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N PRO A 80 1555 1555 1.34
LINK C TYR A 148 N MSE A 149 1555 1555 1.33
LINK C MSE A 149 N LEU A 150 1555 1555 1.33
LINK C ASN A 158 N MSE A 159 1555 1555 1.33
LINK C MSE A 159 N ILE A 160 1555 1555 1.33
LINK C ARG A 170 N MSE A 171 1555 1555 1.33
LINK C MSE A 171 N GLY A 172 1555 1555 1.33
LINK C TYR A 190 N MSE A 191 1555 1555 1.33
LINK C MSE A 191 N ALA A 192 1555 1555 1.33
LINK C ALA A 211 N MSE A 212 1555 1555 1.33
LINK C MSE A 212 N ARG A 213 1555 1555 1.33
LINK C ASP A 246 N MSE A 247 1555 1555 1.33
LINK C MSE A 247 N CYS A 248 1555 1555 1.33
LINK C GLN A 263 N MSE A 264 1555 1555 1.33
LINK C MSE A 264 N GLU A 265 1555 1555 1.33
LINK C VAL A 297 N MSE A 298 1555 1555 1.33
LINK C MSE A 298 N ALA A 299 1555 1555 1.33
LINK C ALA A 329 N MSE A 330 1555 1555 1.33
LINK C MSE A 330 N PRO A 331 1555 1555 1.35
LINK C LEU B 62 N MSE B 63 1555 1555 1.33
LINK C MSE B 63 N GLU B 64 1555 1555 1.33
LINK C SER B 68 N MSE B 69 1555 1555 1.33
LINK C MSE B 69 N VAL B 70 1555 1555 1.33
LINK C GLU B 78 N MSE B 79 1555 1555 1.33
LINK C MSE B 79 N PRO B 80 1555 1555 1.34
LINK C TYR B 148 N MSE B 149 1555 1555 1.33
LINK C MSE B 149 N LEU B 150 1555 1555 1.33
LINK C ASN B 158 N MSE B 159 1555 1555 1.33
LINK C MSE B 159 N ILE B 160 1555 1555 1.33
LINK C ARG B 170 N MSE B 171 1555 1555 1.33
LINK C MSE B 171 N GLY B 172 1555 1555 1.33
LINK C TYR B 190 N MSE B 191 1555 1555 1.33
LINK C MSE B 191 N ALA B 192 1555 1555 1.33
LINK C ALA B 211 N MSE B 212 1555 1555 1.33
LINK C MSE B 212 N AARG B 213 1555 1555 1.33
LINK C MSE B 212 N BARG B 213 1555 1555 1.33
LINK C ASP B 246 N MSE B 247 1555 1555 1.33
LINK C MSE B 247 N CYS B 248 1555 1555 1.33
LINK C GLN B 263 N MSE B 264 1555 1555 1.33
LINK C MSE B 264 N GLU B 265 1555 1555 1.33
LINK C VAL B 297 N MSE B 298 1555 1555 1.33
LINK C MSE B 298 N ALA B 299 1555 1555 1.33
LINK C ALA B 329 N MSE B 330 1555 1555 1.33
LINK C MSE B 330 N PRO B 331 1555 1555 1.35
SITE 1 AC1 5 ASP A 246 MSE A 247 ASP A 250 GLY B 230
SITE 2 AC1 5 SER B 232
SITE 1 AC2 1 GLY A 324
SITE 1 AC3 4 GLY A 230 SER A 232 ASP B 246 ASP B 250
SITE 1 AC4 4 TYR A 301 GLU A 337 ARG A 372 ASP B 362
SITE 1 AC5 1 GLY B 324
SITE 1 AC6 4 ASP A 362 TYR B 301 GLU B 337 ARG B 372
CRYST1 145.229 145.229 138.391 90.00 90.00 120.00 P 61 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006886 0.003975 0.000000 0.00000
SCALE2 0.000000 0.007951 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007226 0.00000
TER 2898 THR A 379
TER 5792 THR B 379
MASTER 514 0 31 36 16 0 7 6 5874 2 277 62
END |