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HEADER HYDROLASE 06-JUL-20 7CI0
TITLE MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT S162A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;
SOURCE 3 ORGANISM_TAXID: 1044;
SOURCE 4 GENE: EH31_02760;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K-12
KEYWDS ESTERASE, MICROBIAL HORMONE-SENSITIVE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.YANG,Z.LI,X.XU,J.LI
REVDAT 1 14-JUL-21 7CI0 0
JRNL AUTH X.YANG
JRNL TITL MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT S162A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3247
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 : CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 221017
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 11063
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 47.3500 - 5.2900 1.00 7477 390 0.1683 0.1898
REMARK 3 2 5.2900 - 4.2000 1.00 7174 389 0.1316 0.1346
REMARK 3 3 4.2000 - 3.6700 1.00 7119 392 0.1435 0.1539
REMARK 3 4 3.6700 - 3.3300 1.00 7102 368 0.1574 0.1740
REMARK 3 5 3.3300 - 3.0900 1.00 7060 358 0.1732 0.1952
REMARK 3 6 3.0900 - 2.9100 1.00 7040 381 0.1773 0.1948
REMARK 3 7 2.9100 - 2.7600 1.00 7026 367 0.1733 0.1922
REMARK 3 8 2.7600 - 2.6400 1.00 7033 371 0.1687 0.1989
REMARK 3 9 2.6400 - 2.5400 1.00 6945 395 0.1730 0.1939
REMARK 3 10 2.5400 - 2.4500 1.00 6991 370 0.1730 0.2034
REMARK 3 11 2.4500 - 2.3800 1.00 6982 402 0.1707 0.1999
REMARK 3 12 2.3800 - 2.3100 1.00 6969 381 0.1708 0.2004
REMARK 3 13 2.3100 - 2.2500 1.00 6954 359 0.1761 0.2186
REMARK 3 14 2.2500 - 2.1900 1.00 6988 356 0.1815 0.2018
REMARK 3 15 2.1900 - 2.1400 1.00 6920 406 0.1866 0.2111
REMARK 3 16 2.1400 - 2.1000 1.00 6985 381 0.1897 0.2195
REMARK 3 17 2.1000 - 2.0600 1.00 6898 400 0.1906 0.2100
REMARK 3 18 2.0600 - 2.0200 1.00 6950 370 0.1945 0.2129
REMARK 3 19 2.0200 - 1.9800 1.00 6977 354 0.1907 0.2101
REMARK 3 20 1.9800 - 1.9500 1.00 6944 357 0.1938 0.2268
REMARK 3 21 1.9500 - 1.9200 1.00 6941 371 0.1962 0.2207
REMARK 3 22 1.9200 - 1.8900 1.00 6968 369 0.1998 0.2156
REMARK 3 23 1.8900 - 1.8600 1.00 6923 357 0.2056 0.2405
REMARK 3 24 1.8600 - 1.8300 1.00 6958 355 0.2144 0.2458
REMARK 3 25 1.8300 - 1.8100 1.00 6902 372 0.2274 0.2614
REMARK 3 26 1.8100 - 1.7900 1.00 6967 346 0.2344 0.2582
REMARK 3 27 1.7900 - 1.7600 1.00 6890 354 0.2467 0.2766
REMARK 3 28 1.7600 - 1.7400 1.00 7008 335 0.2478 0.2580
REMARK 3 29 1.7400 - 1.7200 1.00 6892 346 0.2622 0.2848
REMARK 3 30 1.7200 - 1.7000 0.97 6796 311 0.3302 0.3628
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) : 0.184
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.09
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.54
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 : 0.011 9678
REMARK 3 ANGLE : 1.001 13119
REMARK 3 CHIRALITY : 0.067 1478
REMARK 3 PLANARITY : 0.006 1715
REMARK 3 DIHEDRAL : 17.103 3453
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 7CI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1300017607.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 221017
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 48.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.01500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.490
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.5, PEG, AMMONIUM SULFATE,
REMARK 280 DIOXANE, PEG 1000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.19850
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.33050
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.19850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.33050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 C1 NPO D 812 LIES ON A SPECIAL POSITION.
REMARK 375 N1 NPO D 812 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2843 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B3092 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 THR A 2
REMARK 465 ASP A 3
REMARK 465 THR A 313
REMARK 465 ALA A 314
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASP B 3
REMARK 465 THR B 313
REMARK 465 ALA B 314
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ASP C 3
REMARK 465 THR C 313
REMARK 465 ALA C 314
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ASP D 3
REMARK 465 THR D 313
REMARK 465 ALA D 314
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 THR A 4 OG1 CG2
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 GLU B 204 CG CD OE1 OE2
REMARK 470 THR C 4 OG1 CG2
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 GLU C 204 CG CD OE1 OE2
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 O3 NPO D 801 HO1 EDO D 804 1.56
REMARK 500 O HOH C 699 O HOH C 765 1.74
REMARK 500 O HOH B 3010 O HOH B 3021 1.74
REMARK 500 O HOH A 675 O HOH A 723 1.96
REMARK 500 O HOH A 677 O HOH C 740 1.98
REMARK 500 O DMS D 806 O HOH D 901 1.99
REMARK 500 O1 DIO B 2714 O HOH B 2801 2.01
REMARK 500 O HOH D 1108 O HOH D 1182 2.04
REMARK 500 O HOH B 3016 O HOH B 3024 2.05
REMARK 500 O HOH A 676 O HOH A 840 2.07
REMARK 500 O HOH D 1062 O HOH D 1097 2.07
REMARK 500 OE2 GLU A 133 O HOH A 501 2.11
REMARK 500 O HOH A 838 O HOH A 842 2.11
REMARK 500 O HOH B 2877 O HOH B 3062 2.12
REMARK 500 NH1 ARG B 50 O HOH B 2802 2.13
REMARK 500 O DMS C 406 O HOH C 501 2.14
REMARK 500 OE1 GLU C 280 O HOH C 502 2.14
REMARK 500 OE1 GLU D 280 O HOH D 902 2.14
REMARK 500 OE2 GLU A 280 O HOH A 502 2.16
REMARK 500 O HOH D 1090 O HOH D 1177 2.16
REMARK 500 O GLU A 76 O2 GOL A 415 2.17
REMARK 500 O2 GOL A 414 O HOH A 503 2.17
REMARK 500 O2 EDO B 2703 O HOH B 2803 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2807 O HOH D 932 3554 1.97
REMARK 500 O HOH A 721 O HOH C 801 3544 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL D 211 C - N - CA ANGL. DEV. = 15.2 DEGREES
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 ALA A 22 -132.37 54.52
REMARK 500 ASP A 96 -164.53 -163.61
REMARK 500 PRO A 129 30.91 -99.83
REMARK 500 ALA A 162 -113.45 58.39
REMARK 500 LEU A 186 137.10 -173.94
REMARK 500 PHE A 191 57.88 36.17
REMARK 500 VAL A 211 -72.89 70.09
REMARK 500 HIS A 284 146.75 -39.66
REMARK 500 ASP B 96 -160.24 -163.00
REMARK 500 ALA B 162 -128.78 60.02
REMARK 500 PHE B 191 57.88 36.59
REMARK 500 VAL B 211 -71.85 70.24
REMARK 500 HIS B 284 150.68 -48.26
REMARK 500 ASP C 96 -160.29 -168.69
REMARK 500 PRO C 129 34.34 -99.32
REMARK 500 ALA C 162 -112.58 56.97
REMARK 500 PHE C 191 58.09 33.02
REMARK 500 VAL C 211 -72.57 70.19
REMARK 500 ASP D 96 -159.03 -165.77
REMARK 500 PRO D 129 34.75 -99.22
REMARK 500 ALA D 162 -113.68 55.09
REMARK 500 PHE D 191 57.23 34.90
REMARK 500 VAL D 211 -62.71 71.37
REMARK 500 SER D 285 12.60 80.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 864 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH C 865 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH C 866 DISTANCE = 5.91 ANGSTROMS
DBREF1 7CI0 A 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CI0 A A0A074MDU6 1 314
DBREF1 7CI0 B 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CI0 B A0A074MDU6 1 314
DBREF1 7CI0 C 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CI0 C A0A074MDU6 1 314
DBREF1 7CI0 D 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CI0 D A0A074MDU6 1 314
SEQADV 7CI0 ALA A 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQADV 7CI0 ALA B 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQADV 7CI0 ALA C 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQADV 7CI0 ALA D 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQRES 1 A 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 A 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 A 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 A 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 A 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 A 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 A 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 A 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 A 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 A 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 A 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 A 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 A 314 ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE
SEQRES 14 A 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 A 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 A 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 A 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 A 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 A 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 A 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 A 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 A 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 A 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 A 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 A 314 THR ALA
SEQRES 1 B 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 B 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 B 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 B 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 B 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 B 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 B 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 B 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 B 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 B 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 B 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 B 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 B 314 ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE
SEQRES 14 B 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 B 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 B 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 B 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 B 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 B 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 B 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 B 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 B 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 B 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 B 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 B 314 THR ALA
SEQRES 1 C 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 C 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 C 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 C 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 C 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 C 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 C 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 C 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 C 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 C 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 C 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 C 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 C 314 ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE
SEQRES 14 C 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 C 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 C 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 C 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 C 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 C 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 C 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 C 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 C 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 C 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 C 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 C 314 THR ALA
SEQRES 1 D 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 D 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 D 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 D 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 D 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 D 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 D 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 D 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 D 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 D 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 D 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 D 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 D 314 ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE
SEQRES 14 D 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 D 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 D 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 D 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 D 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 D 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 D 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 D 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 D 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 D 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 D 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 D 314 THR ALA
HET NPO A 401 15
HET NPO A 402 15
HET NPO A 403 15
HET 6NA A 404 19
HET PEG A 405 17
HET EDO A 406 10
HET DMS A 407 10
HET DMS A 408 10
HET DIO A 409 14
HET EDO A 410 10
HET DIO A 411 14
HET 6NA A 412 19
HET DIO A 413 14
HET GOL A 414 12
HET GOL A 415 13
HET GOL A 416 14
HET GOL A 417 14
HET SO4 A 418 5
HET PGE B2701 23
HET NPO B2702 15
HET EDO B2703 10
HET NPO B2704 15
HET 6NA B2705 19
HET DMS B2706 10
HET DMS B2707 10
HET EDO B2708 10
HET EDO B2709 10
HET DMS B2710 10
HET EDO B2711 10
HET EDO B2712 10
HET GOL B2713 12
HET DIO B2714 14
HET SO4 B2715 5
HET SO4 B2716 5
HET NA B2717 1
HET NPO C 401 15
HET NPO C 402 15
HET NPO C 403 15
HET EDO C 404 10
HET DMS C 405 8
HET DMS C 406 10
HET GOL C 407 13
HET DMS C 408 10
HET DIO C 409 14
HET GOL C 410 14
HET PGE C 411 22
HET GOL C 412 12
HET EDO C 413 10
HET DIO C 414 14
HET DMS C 415 10
HET SO4 C 416 5
HET NPO D 801 15
HET NPO D 802 15
HET PEG D 803 17
HET EDO D 804 10
HET DMS D 805 10
HET DMS D 806 10
HET MES D 807 24
HET DMS D 808 10
HET DMS D 809 10
HET DMS D 810 10
HET GOL D 811 14
HET NPO D 812 15
HET SO4 D 813 5
HETNAM NPO P-NITROPHENOL
HETNAM 6NA HEXANOIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NA SODIUM ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NPO 11(C6 H5 N O3)
FORMUL 8 6NA 3(C6 H12 O2)
FORMUL 9 PEG 2(C4 H10 O3)
FORMUL 10 EDO 10(C2 H6 O2)
FORMUL 11 DMS 14(C2 H6 O S)
FORMUL 13 DIO 6(C4 H8 O2)
FORMUL 18 GOL 9(C3 H8 O3)
FORMUL 22 SO4 5(O4 S 2-)
FORMUL 23 PGE 2(C6 H14 O4)
FORMUL 39 NA NA 1+
FORMUL 62 MES C6 H13 N O4 S
FORMUL 69 HOH *1361(H2 O)
HELIX 1 AA1 ARG A 8 ALA A 22 1 15
HELIX 2 AA2 THR A 30 ASP A 46 1 17
HELIX 3 AA3 HIS A 100 ASP A 112 1 13
HELIX 4 AA4 PRO A 129 SER A 144 1 16
HELIX 5 AA5 ALA A 162 LYS A 178 1 17
HELIX 6 AA6 SER A 200 PHE A 206 1 7
HELIX 7 AA7 THR A 213 LYS A 225 1 13
HELIX 8 AA8 PHE A 234 GLY A 238 5 5
HELIX 9 AA9 ILE A 256 ALA A 270 1 15
HELIX 10 AB1 SER A 285 ILE A 289 5 5
HELIX 11 AB2 SER A 295 GLY A 312 1 18
HELIX 12 AB3 ARG B 8 ALA B 22 1 15
HELIX 13 AB4 THR B 30 ASP B 46 1 17
HELIX 14 AB5 HIS B 100 ASP B 112 1 13
HELIX 15 AB6 PRO B 129 SER B 144 1 16
HELIX 16 AB7 SER B 145 GLY B 150 5 6
HELIX 17 AB8 ALA B 162 LYS B 178 1 17
HELIX 18 AB9 SER B 200 PHE B 206 1 7
HELIX 19 AC1 THR B 213 LYS B 225 1 13
HELIX 20 AC2 PHE B 234 GLY B 238 5 5
HELIX 21 AC3 ILE B 256 ALA B 270 1 15
HELIX 22 AC4 SER B 285 ILE B 289 5 5
HELIX 23 AC5 PRO B 294 GLY B 312 1 19
HELIX 24 AC6 ARG C 8 ALA C 22 1 15
HELIX 25 AC7 THR C 25 MET C 29 5 5
HELIX 26 AC8 THR C 30 ASP C 46 1 17
HELIX 27 AC9 HIS C 100 ASP C 112 1 13
HELIX 28 AD1 PRO C 129 SER C 144 1 16
HELIX 29 AD2 ALA C 162 LYS C 178 1 17
HELIX 30 AD3 SER C 200 PHE C 206 1 7
HELIX 31 AD4 THR C 213 LYS C 225 1 13
HELIX 32 AD5 PHE C 234 GLY C 238 5 5
HELIX 33 AD6 ILE C 256 ALA C 270 1 15
HELIX 34 AD7 SER C 285 ILE C 289 5 5
HELIX 35 AD8 SER C 295 GLY C 312 1 18
HELIX 36 AD9 ARG D 8 ALA D 22 1 15
HELIX 37 AE1 THR D 30 ASP D 46 1 17
HELIX 38 AE2 HIS D 100 ASP D 112 1 13
HELIX 39 AE3 PRO D 129 SER D 144 1 16
HELIX 40 AE4 SER D 145 GLY D 150 5 6
HELIX 41 AE5 ALA D 162 LYS D 178 1 17
HELIX 42 AE6 SER D 200 PHE D 206 1 7
HELIX 43 AE7 THR D 213 LYS D 225 1 13
HELIX 44 AE8 PHE D 234 GLY D 238 5 5
HELIX 45 AE9 ILE D 256 ALA D 270 1 15
HELIX 46 AF1 SER D 285 ILE D 289 5 5
HELIX 47 AF2 SER D 295 GLY D 312 1 18
SHEET 1 AA1 6 VAL A 54 GLY A 62 0
SHEET 2 AA1 6 GLY A 65 ASP A 73 -1 O LEU A 69 N LEU A 58
SHEET 3 AA1 6 VAL A 115 VAL A 118 -1 O VAL A 115 N TYR A 72
SHEET 4 AA1 6 GLY A 81 TYR A 87 1 N ILE A 84 O VAL A 116
SHEET 5 AA1 6 ALA A 153 ASP A 161 1 O ILE A 157 N VAL A 83
SHEET 6 AA1 6 VAL A 188 ILE A 190 1 O ILE A 190 N GLY A 160
SHEET 1 AA2 4 THR A 246 ALA A 251 0
SHEET 2 AA2 4 VAL A 274 MET A 279 1 O VAL A 275 N VAL A 248
SHEET 3 AA2 4 VAL B 274 MET B 279 -1 O VAL B 274 N TYR A 276
SHEET 4 AA2 4 THR B 246 ALA B 251 1 N VAL B 248 O VAL B 275
SHEET 1 AA3 6 VAL B 54 GLY B 62 0
SHEET 2 AA3 6 GLY B 65 ASP B 73 -1 O ILE B 67 N CYS B 60
SHEET 3 AA3 6 VAL B 115 VAL B 118 -1 O VAL B 115 N TYR B 72
SHEET 4 AA3 6 GLY B 81 TYR B 87 1 N ILE B 84 O VAL B 116
SHEET 5 AA3 6 ALA B 153 ASP B 161 1 O ILE B 159 N THR B 85
SHEET 6 AA3 6 VAL B 188 ILE B 190 1 O ILE B 190 N GLY B 160
SHEET 1 AA4 6 VAL C 54 PRO C 61 0
SHEET 2 AA4 6 ASP C 66 ASP C 73 -1 O ILE C 67 N CYS C 60
SHEET 3 AA4 6 VAL C 115 VAL C 118 -1 O VAL C 115 N TYR C 72
SHEET 4 AA4 6 GLY C 81 TYR C 87 1 N ILE C 84 O VAL C 116
SHEET 5 AA4 6 ALA C 153 ASP C 161 1 O ILE C 157 N VAL C 83
SHEET 6 AA4 6 VAL C 188 ILE C 190 1 O ILE C 190 N GLY C 160
SHEET 1 AA5 4 THR C 246 ALA C 251 0
SHEET 2 AA5 4 VAL C 274 MET C 279 1 O VAL C 275 N VAL C 248
SHEET 3 AA5 4 VAL D 274 MET D 279 -1 O TYR D 276 N VAL C 274
SHEET 4 AA5 4 THR D 246 ALA D 251 1 N VAL D 248 O VAL D 275
SHEET 1 AA6 6 VAL D 54 CYS D 60 0
SHEET 2 AA6 6 ILE D 67 ASP D 73 -1 O ILE D 67 N CYS D 60
SHEET 3 AA6 6 VAL D 115 VAL D 118 -1 O VAL D 115 N TYR D 72
SHEET 4 AA6 6 GLY D 81 TYR D 87 1 N ILE D 84 O VAL D 116
SHEET 5 AA6 6 ALA D 153 ASP D 161 1 O GLY D 155 N VAL D 83
SHEET 6 AA6 6 VAL D 188 ILE D 190 1 O ILE D 190 N GLY D 160
LINK NA NA B2717 O HOH B3043 1555 1555 2.71
CISPEP 1 ALA A 123 PRO A 124 0 0.02
CISPEP 2 PHE A 128 PRO A 129 0 2.54
CISPEP 3 ALA B 123 PRO B 124 0 2.84
CISPEP 4 PHE B 128 PRO B 129 0 4.02
CISPEP 5 ALA C 123 PRO C 124 0 1.66
CISPEP 6 PHE C 128 PRO C 129 0 0.88
CISPEP 7 ALA D 123 PRO D 124 0 3.13
CISPEP 8 PHE D 128 PRO D 129 0 3.69
CRYST1 70.397 129.771 220.661 90.00 90.00 90.00 P 21 2 21 16
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 0.014205 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004532 0.00000
TER 4534 GLY A 312
TER 9088 GLY B 312
TER 13635 GLY C 312
TER 18200 GLY D 312
MASTER 418 0 64 47 32 0 0 610881 4 792 100
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