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HEADER HYDROLASE 13-MAR-15 4YPV
TITLE HIGH-RESOLUTION STRUCTURE OF A METAGENOME-DERIVED ESTERASE EST8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EST8;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARVIBACULUM;
SOURCE 3 ORGANISM_TAXID: 256616;
SOURCE 4 GENE: EST8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ESTERASE, EST8, METAGENOME, MICROBIAL CONSORTIUM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.PEREIRA,C.T.MAESTER,E.MACEDO LEMOS,M.HYVONEN,A.BALAN
REVDAT 1 18-MAY-16 4YPV 0
JRNL AUTH M.R.PEREIRA,C.T.MAESTER,E.MACEDO LEMOS,M.HYVONEN,A.BALAN
JRNL TITL HIGH-RESOLUTION OF AN ESTERASE EST8 METAGENOME-DERIVED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 35626
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1780
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 27.9883 - 4.3450 0.99 2776 129 0.1252 0.1494
REMARK 3 2 4.3450 - 3.4508 0.99 2699 116 0.1309 0.1609
REMARK 3 3 3.4508 - 3.0152 0.99 2599 164 0.1578 0.1992
REMARK 3 4 3.0152 - 2.7397 0.99 2628 135 0.1666 0.2085
REMARK 3 5 2.7397 - 2.5435 0.99 2611 141 0.1692 0.1799
REMARK 3 6 2.5435 - 2.3936 0.98 2587 118 0.1660 0.1882
REMARK 3 7 2.3936 - 2.2738 0.99 2596 153 0.1579 0.1783
REMARK 3 8 2.2738 - 2.1749 0.99 2557 140 0.1540 0.1726
REMARK 3 9 2.1749 - 2.0912 0.99 2573 137 0.1647 0.2100
REMARK 3 10 2.0912 - 2.0190 0.98 2557 151 0.1775 0.2234
REMARK 3 11 2.0190 - 1.9559 0.98 2544 137 0.1847 0.2269
REMARK 3 12 1.9559 - 1.9000 0.98 2535 128 0.1944 0.1992
REMARK 3 13 1.9000 - 1.8500 0.98 2584 131 0.2122 0.2372
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 2396
REMARK 3 ANGLE : 0.986 3265
REMARK 3 CHIRALITY : 0.042 363
REMARK 3 PLANARITY : 0.005 436
REMARK 3 DIHEDRAL : 11.992 859
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7101 20.9501 20.2426
REMARK 3 T TENSOR
REMARK 3 T11: 0.4583 T22: 0.6237
REMARK 3 T33: 0.6372 T12: 0.0399
REMARK 3 T13: 0.0498 T23: -0.2491
REMARK 3 L TENSOR
REMARK 3 L11: 2.8085 L22: 1.7875
REMARK 3 L33: 2.8853 L12: 0.4600
REMARK 3 L13: 1.6156 L23: 1.1274
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: 0.6835 S13: -0.7130
REMARK 3 S21: -0.0391 S22: -0.1016 S23: -0.2541
REMARK 3 S31: 0.4568 S32: 0.3392 S33: -0.0364
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8697 40.3208 22.7377
REMARK 3 T TENSOR
REMARK 3 T11: 0.2519 T22: 0.4942
REMARK 3 T33: 0.3595 T12: -0.0181
REMARK 3 T13: 0.0329 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 2.8583 L22: 2.3366
REMARK 3 L33: 2.4649 L12: -1.2206
REMARK 3 L13: 0.0465 L23: -0.0210
REMARK 3 S TENSOR
REMARK 3 S11: 0.2388 S12: 0.7407 S13: 0.0584
REMARK 3 S21: -0.2300 S22: -0.2893 S23: -0.3484
REMARK 3 S31: -0.0734 S32: 0.3538 S33: -0.0323
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4497 43.0557 33.3564
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: 0.2141
REMARK 3 T33: 0.1732 T12: -0.0263
REMARK 3 T13: -0.0100 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 2.5141 L22: 2.7692
REMARK 3 L33: 2.5968 L12: -1.1265
REMARK 3 L13: -0.1459 L23: 0.1069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0500 S12: 0.1784 S13: 0.0851
REMARK 3 S21: 0.1757 S22: -0.0315 S23: -0.0804
REMARK 3 S31: -0.1753 S32: -0.0236 S33: 0.0205
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 176 THROUGH 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0798 25.0309 34.6773
REMARK 3 T TENSOR
REMARK 3 T11: 0.3408 T22: 0.2493
REMARK 3 T33: 0.4230 T12: -0.0375
REMARK 3 T13: 0.0523 T23: -0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 2.3732 L22: 3.0898
REMARK 3 L33: 2.7199 L12: -0.8685
REMARK 3 L13: -0.3089 L23: 0.4505
REMARK 3 S TENSOR
REMARK 3 S11: -0.1724 S12: 0.1605 S13: -0.8417
REMARK 3 S21: 0.4265 S22: -0.0476 S23: 0.3081
REMARK 3 S31: 0.6419 S32: -0.1168 S33: 0.1331
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 210 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4960 26.3301 42.3257
REMARK 3 T TENSOR
REMARK 3 T11: 0.5045 T22: 0.2912
REMARK 3 T33: 0.3739 T12: 0.0817
REMARK 3 T13: -0.0425 T23: 0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 4.2062 L22: 2.8422
REMARK 3 L33: 3.0599 L12: -2.1937
REMARK 3 L13: -1.8439 L23: 0.4825
REMARK 3 S TENSOR
REMARK 3 S11: -0.4193 S12: -0.5167 S13: -0.6511
REMARK 3 S21: 0.9529 S22: 0.2245 S23: -0.0107
REMARK 3 S31: 0.6775 S32: 0.4757 S33: 0.0682
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1894 27.8302 29.3816
REMARK 3 T TENSOR
REMARK 3 T11: 0.2819 T22: 0.3967
REMARK 3 T33: 0.4950 T12: -0.1174
REMARK 3 T13: 0.0395 T23: -0.1406
REMARK 3 L TENSOR
REMARK 3 L11: 2.1135 L22: 1.9398
REMARK 3 L33: 1.6811 L12: -0.7002
REMARK 3 L13: -0.2505 L23: 0.3166
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.4871 S13: -0.7623
REMARK 3 S21: 0.0402 S22: -0.1314 S23: 0.5411
REMARK 3 S31: 0.4138 S32: -0.4597 S33: 0.1273
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 4YPV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207905.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.919
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35630
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 27.985
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.470
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.53
REMARK 200 R MERGE FOR SHELL (I) : 0.57100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1EVQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1% PEG 8000, 1.4 M TRIAMMONIUM
REMARK 280 CITRATE, PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 32.88833
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 65.77667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.77667
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 32.88833
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 MET A -36
REMARK 465 GLY A -35
REMARK 465 SER A -34
REMARK 465 SER A -33
REMARK 465 HIS A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 SER A -26
REMARK 465 SER A -25
REMARK 465 GLY A -24
REMARK 465 LEU A -23
REMARK 465 VAL A -22
REMARK 465 PRO A -21
REMARK 465 ARG A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 MET A -16
REMARK 465 ALA A -15
REMARK 465 SER A -14
REMARK 465 MET A -13
REMARK 465 THR A -12
REMARK 465 GLY A -11
REMARK 465 GLY A -10
REMARK 465 GLN A -9
REMARK 465 GLN A -8
REMARK 465 MET A -7
REMARK 465 GLY A -6
REMARK 465 ARG A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 GLU A -2
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 PHE A -1 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 0 OG1 CG2
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 OD2 ASP A 297 O HOH A 401 1.85
REMARK 500 OD1 ASP A 297 O HOH A 402 1.91
REMARK 500 NH1 ARG A 260 O HOH A 403 1.93
REMARK 500 O ALA A 19 O HOH A 404 1.94
REMARK 500 O HOH A 566 O HOH A 576 1.99
REMARK 500 O HOH A 441 O HOH A 457 2.07
REMARK 500 O HOH A 482 O HOH A 577 2.10
REMARK 500 N GLY A 74 O HOH A 405 2.10
REMARK 500 OXT ALA A 311 O HOH A 406 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 ASP A 93 -161.27 -165.12
REMARK 500 PHE A 125 136.38 -39.98
REMARK 500 SER A 159 -123.19 63.29
REMARK 500 TYR A 187 65.59 25.84
REMARK 500 PHE A 207 -67.96 76.16
REMARK 500 ASN A 222 54.69 -98.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4YPV A -36 311 PDB 4YPV 4YPV -36 311
SEQRES 1 A 348 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 348 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 348 GLY GLN GLN MET GLY ARG GLY SER GLU PHE THR MET ALA
SEQRES 4 A 348 LEU ASP PRO GLN ALA LYS GLY LEU LEU ASP ALA MET ALA
SEQRES 5 A 348 ALA ASN PRO ALA PRO ARG ILE ILE ASP LEU PRO VAL LYS
SEQRES 6 A 348 GLU ALA ARG GLU MET TYR ARG GLY ILE ALA ALA GLN LEU
SEQRES 7 A 348 ASP LEU GLN ASP LEU PRO ILE GLY LYS THR GLU ASP ARG
SEQRES 8 A 348 LYS ILE PRO GLY PRO ALA GLY ASP ILE PRO VAL ARG ILE
SEQRES 9 A 348 TYR THR PRO VAL ALA ALA GLY GLY ALA ALA LEU PRO VAL
SEQRES 10 A 348 LEU VAL TYR PHE HIS GLY GLY GLY TRP VAL ILE GLY ASP
SEQRES 11 A 348 LEU GLU THR HIS ASP ALA LEU CYS ARG SER PHE ALA ASN
SEQRES 12 A 348 GLU ALA GLY CYS LYS VAL VAL ALA VAL ASP TYR ARG LEU
SEQRES 13 A 348 ALA PRO GLU HIS ARG PHE PRO ALA ALA ALA GLU ASP CYS
SEQRES 14 A 348 LEU ALA ALA VAL LYS TRP VAL GLU THR ASN ALA SER GLU
SEQRES 15 A 348 ILE GLY VAL ASP ALA ASN ARG ILE ALA VAL ALA GLY ASP
SEQRES 16 A 348 SER ALA GLY GLY ASN LEU ALA ALA VAL VAL SER GLN LEU
SEQRES 17 A 348 ALA LEU ALA ALA LYS GLY PRO ARG ILE ALA PHE GLN LEU
SEQRES 18 A 348 LEU ILE TYR PRO VAL THR ASP THR ASN VAL ASP THR ALA
SEQRES 19 A 348 SER TYR ARG GLU ASN ALA SER GLY TYR PHE LEU GLU ARG
SEQRES 20 A 348 ASP GLY MET ILE TRP PHE PHE ASP HIS TYR LEU ASN GLY
SEQRES 21 A 348 ALA ASP ARG THR ASP PRO ARG VAL ALA PRO LEU ARG ALA
SEQRES 22 A 348 ALA SER LEU ALA GLY LEU PRO ARG ALA TYR VAL ILE THR
SEQRES 23 A 348 ALA GLY PHE ASP PRO LEU LYS ASP GLU GLY ARG ALA TYR
SEQRES 24 A 348 ALA GLU ALA LEU LYS ALA ALA GLY VAL PRO THR GLU TYR
SEQRES 25 A 348 VAL ASN TYR GLU GLY MET ILE HIS GLY PHE PHE ASN LEU
SEQRES 26 A 348 GLN ALA ALA PHE ASP VAL SER ARG ASP ALA VAL LYS ALA
SEQRES 27 A 348 ALA ALA LYS ALA LEU LYS GLU ALA LEU ALA
FORMUL 2 HOH *197(H2 O)
HELIX 1 AA1 ASP A 4 ALA A 16 1 13
HELIX 2 AA2 ARG A 21 LEU A 25 5 5
HELIX 3 AA3 PRO A 26 ASP A 42 1 17
HELIX 4 AA4 HIS A 97 GLY A 109 1 13
HELIX 5 AA5 PRO A 126 ASN A 142 1 17
HELIX 6 AA6 ASN A 142 GLY A 147 1 6
HELIX 7 AA7 SER A 159 LYS A 176 1 18
HELIX 8 AA8 THR A 196 ASN A 202 1 7
HELIX 9 AA9 GLU A 209 LEU A 221 1 13
HELIX 10 AB1 ALA A 232 ALA A 236 5 5
HELIX 11 AB2 LEU A 255 ALA A 269 1 15
HELIX 12 AB3 GLY A 284 LEU A 288 5 5
HELIX 13 AB4 PHE A 292 LEU A 310 1 19
SHEET 1 AA1 8 LYS A 50 ILE A 56 0
SHEET 2 AA1 8 ILE A 63 THR A 69 -1 O VAL A 65 N ARG A 54
SHEET 3 AA1 8 LYS A 111 VAL A 115 -1 O ALA A 114 N ARG A 66
SHEET 4 AA1 8 LEU A 78 PHE A 84 1 N LEU A 81 O VAL A 113
SHEET 5 AA1 8 VAL A 148 ASP A 158 1 O ALA A 154 N VAL A 82
SHEET 6 AA1 8 PHE A 182 ILE A 186 1 O LEU A 184 N VAL A 155
SHEET 7 AA1 8 ALA A 245 ALA A 250 1 O TYR A 246 N LEU A 185
SHEET 8 AA1 8 THR A 273 TYR A 278 1 O GLU A 274 N VAL A 247
CISPEP 1 ALA A 120 PRO A 121 0 -0.79
CISPEP 2 PHE A 125 PRO A 126 0 3.85
CISPEP 3 GLY A 177 PRO A 178 0 -0.80
CRYST1 85.496 85.496 98.665 90.00 90.00 120.00 P 31 2 1 6
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 0.011696 0.006753 0.000000 0.00000
SCALE2 0.000000 0.013506 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010135 0.00000
TER 2345 ALA A 311
MASTER 393 0 0 13 8 0 0 6 2541 1 0 27
END |