HEADER HYDROLASE/HYDROLASE INHIBITOR 06-FEB-15 4Y10
TITLE TRYPSIN IN COMPLEX WITH WITH BPTI MUTANT (2S)-2-AMINO-4,4-
TITLE 2 DIFLUOROBUTANOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: BETA-TRYPSIN, TRYPSIN;
COMPND 5 EC: 3.4.21.4;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;
COMPND 8 CHAIN: I;
COMPND 9 FRAGMENT: UNP RESIDUES 36-93;
COMPND 10 SYNONYM: APROTININ,BASIC PROTEASE INHIBITOR,BPTI;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: NON-CANONICAL AMINO ACID INCORPORATED (OBF)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: CATTLE;
SOURCE 9 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE INHIBITORS, DIGESTION, METAL-BINDING, PROTEASE, SECRETED,
KEYWDS 2 SERINE PROTEASE, ZYMOGEN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.LOLL,S.YE,A.A.BERGER,U.MUELOW,C.ALINGS,M.C.WAHL,B.KOKSCH
REVDAT 4 15-NOV-23 4Y10 1 LINK ATOM
REVDAT 3 18-APR-18 4Y10 1 JRNL REMARK LINK SITE
REVDAT 3 2 1 ATOM
REVDAT 2 26-AUG-15 4Y10 1 JRNL
REVDAT 1 24-JUN-15 4Y10 0
JRNL AUTH S.YE,B.LOLL,A.A.BERGER,U.MULOW,C.ALINGS,M.C.WAHL,B.KOKSCH
JRNL TITL FLUORINE TEAMS UP WITH WATER TO RESTORE INHIBITOR ACTIVITY
JRNL TITL 2 TO MUTANT BPTI.
JRNL REF CHEM SCI V. 6 5246 2015
JRNL REFN ISSN 2041-6520
JRNL PMID 29449928
JRNL DOI 10.1039/C4SC03227F
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 79833
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.139
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3992
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 34.1344 - 4.1971 0.99 2788 148 0.1541 0.1849
REMARK 3 2 4.1971 - 3.3323 1.00 2690 141 0.1229 0.1254
REMARK 3 3 3.3323 - 2.9113 1.00 2672 141 0.1385 0.1803
REMARK 3 4 2.9113 - 2.6452 1.00 2652 139 0.1436 0.1726
REMARK 3 5 2.6452 - 2.4557 1.00 2642 139 0.1322 0.1379
REMARK 3 6 2.4557 - 2.3109 1.00 2626 139 0.1292 0.1479
REMARK 3 7 2.3109 - 2.1952 1.00 2626 138 0.1236 0.1418
REMARK 3 8 2.1952 - 2.0997 1.00 2625 138 0.1222 0.1633
REMARK 3 9 2.0997 - 2.0189 1.00 2611 137 0.1242 0.1626
REMARK 3 10 2.0189 - 1.9492 1.00 2611 138 0.1244 0.1600
REMARK 3 11 1.9492 - 1.8883 1.00 2629 138 0.1262 0.1445
REMARK 3 12 1.8883 - 1.8343 0.99 2613 138 0.1251 0.1617
REMARK 3 13 1.8343 - 1.7860 1.00 2600 137 0.1235 0.1768
REMARK 3 14 1.7860 - 1.7424 1.00 2603 136 0.1262 0.1432
REMARK 3 15 1.7424 - 1.7028 1.00 2613 138 0.1251 0.1537
REMARK 3 16 1.7028 - 1.6666 1.00 2603 137 0.1238 0.1517
REMARK 3 17 1.6666 - 1.6332 1.00 2592 136 0.1279 0.1688
REMARK 3 18 1.6332 - 1.6024 1.00 2623 139 0.1342 0.1750
REMARK 3 19 1.6024 - 1.5738 1.00 2615 137 0.1367 0.1528
REMARK 3 20 1.5738 - 1.5471 1.00 2579 136 0.1496 0.2038
REMARK 3 21 1.5471 - 1.5222 1.00 2615 137 0.1516 0.1723
REMARK 3 22 1.5222 - 1.4988 1.00 2594 137 0.1522 0.1839
REMARK 3 23 1.4988 - 1.4767 1.00 2590 136 0.1618 0.1884
REMARK 3 24 1.4767 - 1.4559 1.00 2578 136 0.1716 0.2244
REMARK 3 25 1.4559 - 1.4362 1.00 2612 138 0.1782 0.2521
REMARK 3 26 1.4362 - 1.4176 1.00 2620 137 0.2010 0.2631
REMARK 3 27 1.4176 - 1.3999 1.00 2594 137 0.2144 0.2656
REMARK 3 28 1.3999 - 1.3830 1.00 2554 134 0.2245 0.2556
REMARK 3 29 1.3830 - 1.3669 0.94 2471 130 0.2514 0.2658
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.070
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 : 0.019 2330
REMARK 3 ANGLE : 1.691 3177
REMARK 3 CHIRALITY : 0.100 343
REMARK 3 PLANARITY : 0.011 408
REMARK 3 DIHEDRAL : 11.950 864
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 4Y10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206597.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79871
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.94000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 TO 2.2 M AMMONIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 37.34700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.92700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 61.80600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.34700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.92700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.80600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.34700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.92700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.80600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.34700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.92700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 61.80600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
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 ARG I 1
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 HZ1 LYS E 107 O4 SO4 E 303 1.54
REMARK 500 O HOH I 204 O HOH I 223 2.07
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 HH TYR I 21 HH TYR I 21 4559 1.28
REMARK 500 HD22 ASN E 221 HZ2 LYS E 237 8459 1.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL E 75 C VAL E 75 O -0.200
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 E 75 CA - C - N ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG E 117 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP E 191 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG I 53 NE - CZ - NH2 ANGL. DEV. = -3.7 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 ASP E 71 -75.71 -122.28
REMARK 500 SER E 212 -71.15 -122.45
REMARK 500 ASN I 44 109.86 -160.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL E 75 -13.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 308 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 70 OE2
REMARK 620 2 ASN E 72 O 89.7
REMARK 620 3 VAL E 75 O 166.2 83.4
REMARK 620 4 GLU E 80 OE2 101.3 164.0 88.0
REMARK 620 5 HOH E 408 O 82.8 88.8 109.0 81.2
REMARK 620 6 HOH E 476 O 79.1 101.7 90.5 91.9 158.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Y0Y RELATED DB: PDB
REMARK 900 RELATED ID: 4Y0Z RELATED DB: PDB
REMARK 900 RELATED ID: 4Y11 RELATED DB: PDB
DBREF 4Y10 E 16 243 UNP P00760 TRY1_BOVIN 24 246
DBREF 4Y10 I 1 58 UNP P00974 BPT1_BOVIN 36 93
SEQADV 4Y10 OBF I 15 UNP P00974 LYS 50 ENGINEERED MUTATION
SEQRES 1 E 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 E 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 E 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 E 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 E 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 E 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 E 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 E 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 E 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 E 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 E 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 E 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 E 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 E 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 E 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 E 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 E 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 E 223 SER ASN
SEQRES 1 I 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO
SEQRES 2 I 58 CYS OBF ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 3 I 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG
SEQRES 4 I 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET
SEQRES 5 I 58 ARG THR CYS GLY GLY ALA
HET OBF I 15 13
HET SO4 E 301 5
HET SO4 E 302 5
HET SO4 E 303 5
HET SO4 E 304 5
HET SO4 E 305 5
HET SO4 E 306 5
HET GOL E 307 14
HET CA E 308 1
HET SO4 I 101 5
HET SO4 I 102 5
HET SO4 I 103 5
HETNAM OBF (2S)-2-AMINO-4,4-DIFLUOROBUTANOIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 OBF C4 H7 F2 N O2
FORMUL 3 SO4 9(O4 S 2-)
FORMUL 9 GOL C3 H8 O3
FORMUL 10 CA CA 2+
FORMUL 14 HOH *346(H2 O)
HELIX 1 AA1 ALA E 55 TYR E 59 5 5
HELIX 2 AA2 SER E 164 TYR E 172 1 9
HELIX 3 AA3 TYR E 232 SER E 242 1 11
HELIX 4 AA4 ASP I 3 GLU I 7 5 5
HELIX 5 AA5 SER I 47 GLY I 56 1 10
SHEET 1 AA1 7 TYR E 20 THR E 21 0
SHEET 2 AA1 7 LYS E 156 PRO E 161 -1 O CYS E 157 N TYR E 20
SHEET 3 AA1 7 GLN E 135 GLY E 140 -1 N ILE E 138 O LEU E 158
SHEET 4 AA1 7 PRO E 200 CYS E 203 -1 O VAL E 202 N LEU E 137
SHEET 5 AA1 7 LYS E 206 TRP E 213 -1 O LYS E 206 N CYS E 203
SHEET 6 AA1 7 GLY E 224 LYS E 228 -1 O VAL E 225 N TRP E 213
SHEET 7 AA1 7 MET E 180 ALA E 183 -1 N PHE E 181 O TYR E 226
SHEET 1 AA2 7 GLN E 30 ASN E 34 0
SHEET 2 AA2 7 HIS E 40 ASN E 48 -1 O CYS E 42 N LEU E 33
SHEET 3 AA2 7 TRP E 51 SER E 54 -1 O TRP E 51 N ILE E 47
SHEET 4 AA2 7 MET E 104 LEU E 108 -1 O ILE E 106 N VAL E 52
SHEET 5 AA2 7 GLN E 81 VAL E 90 -1 N ILE E 89 O LEU E 105
SHEET 6 AA2 7 GLN E 64 LEU E 67 -1 N LEU E 67 O GLN E 81
SHEET 7 AA2 7 GLN E 30 ASN E 34 -1 N SER E 32 O ARG E 66
SHEET 1 AA3 2 ILE I 18 ASN I 24 0
SHEET 2 AA3 2 LEU I 29 TYR I 35 -1 O TYR I 35 N ILE I 18
SSBOND 1 CYS E 22 CYS E 157 1555 1555 2.09
SSBOND 2 CYS E 42 CYS E 58 1555 1555 2.05
SSBOND 3 CYS E 128 CYS E 230 1555 1555 2.01
SSBOND 4 CYS E 136 CYS E 203 1555 1555 2.03
SSBOND 5 CYS E 168 CYS E 182 1555 1555 2.04
SSBOND 6 CYS E 193 CYS E 217 1555 1555 2.07
SSBOND 7 CYS I 5 CYS I 55 1555 1555 2.04
SSBOND 8 CYS I 14 CYS I 38 1555 1555 2.09
SSBOND 9 CYS I 30 CYS I 51 1555 1555 2.13
LINK C CYS I 14 N OBF I 15 1555 1555 1.33
LINK C OBF I 15 N ALA I 16 1555 1555 1.33
LINK OE2 GLU E 70 CA CA E 308 1555 1555 2.33
LINK O ASN E 72 CA CA E 308 1555 1555 2.33
LINK O VAL E 75 CA CA E 308 1555 1555 2.21
LINK OE2 GLU E 80 CA CA E 308 1555 1555 2.35
LINK CA CA E 308 O HOH E 408 1555 1555 2.40
LINK CA CA E 308 O HOH E 476 1555 1555 2.37
SITE 1 AC1 6 LYS E 169 PRO E 173 GLY E 174 HOH E 473
SITE 2 AC1 6 HOH E 481 HOH E 510
SITE 1 AC2 9 TYR E 59 LYS E 60 SER E 61 HOH E 409
SITE 2 AC2 9 HOH E 434 HOH E 515 HOH E 566 HOH E 412
SITE 3 AC2 9 LYS I 46
SITE 1 AC3 3 LYS E 87 LYS E 107 HOH E 446
SITE 1 AC4 4 ASN E 95 THR E 98 ASN E 100 HOH E 417
SITE 1 AC5 5 THR E 177 SER E 178 SO4 E 306 HOH E 490
SITE 2 AC5 5 HOH E 595
SITE 1 AC6 5 ASN E 100 ASN E 179 SO4 E 305 HOH E 401
SITE 2 AC6 5 HOH E 423
SITE 1 AC7 4 TYR E 20 CYS E 22 THR E 26 VAL E 27
SITE 1 AC8 6 GLU E 70 ASN E 72 VAL E 75 GLU E 80
SITE 2 AC8 6 HOH E 476 HOH E 408
SITE 1 AC9 7 GLU I 7 ARG I 42 HOH I 209 HOH I 236
SITE 2 AC9 7 HOH I 202 HOH I 224 HOH I 255
SITE 1 AD1 7 PRO I 9 TYR I 10 THR I 11 GLY I 12
SITE 2 AD1 7 HOH I 263 HOH I 241 HOH I 253
SITE 1 AD2 7 ARG I 20 TYR I 35 HOH I 205 HOH I 234
SITE 2 AD2 7 HOH I 246 HOH I 207 HOH I 264
CRYST1 74.694 81.854 123.612 90.00 90.00 90.00 I 2 2 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 0.013388 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008090 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
