HEADER HYDROLASE 26-NOV-03 1RLT
TITLE TRANSITION STATE ANALOGUE OF YBIV FROM E. COLI K12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.3.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: YBIV, B0822;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 (PACYC);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS HAD FAMILY, TRANSITION-STATE ANALOGUE, ALUMINUM FLUORIDE,
KEYWDS 2 PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROBERTS,S.Y.LEE,E.MCCULLAGH,R.E.SILVERSMITH,D.E.WEMMER
REVDAT 7 23-AUG-23 1RLT 1 REMARK
REVDAT 6 27-OCT-21 1RLT 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 1RLT 1 VERSN
REVDAT 4 24-FEB-09 1RLT 1 VERSN
REVDAT 3 22-MAR-05 1RLT 1 JRNL
REVDAT 2 01-MAR-05 1RLT 1 JRNL
REVDAT 1 07-DEC-04 1RLT 0
JRNL AUTH A.ROBERTS,S.Y.LEE,E.MCCULLAGH,R.E.SILVERSMITH,D.E.WEMMER
JRNL TITL YBIV FROM ESCHERICHIA COLI K12 IS A HAD PHOSPHATASE.
JRNL REF PROTEINS V. 58 790 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15657928
JRNL DOI 10.1002/PROT.20267
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 181307.640
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 59839
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6051
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8330
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 922
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 397
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.02000
REMARK 3 B22 (A**2) : -6.63000
REMARK 3 B33 (A**2) : 16.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.220
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.070 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.550 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.420 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.320 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 42.18
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ALFNEW.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CRY.TOP
REMARK 3 TOPOLOGY FILE 3 : ALFNEW.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RLT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61606
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: PDB ID 1RLM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, ALUMINUM
REMARK 280 CHLORIDE, SODIUM FLUORIDE, CACODYLIC ACID, MAGNESIUM CHLORIDE,
REMARK 280 PH 5.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 35.88050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.92500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.58300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.92500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.88050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.58300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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 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 ALA A 2
REMARK 465 SER A 271
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 271
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 271
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 SER D 271
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 C TYR B 267 CD PRO B 268 1.58
REMARK 500 C TYR D 267 CD PRO D 268 1.66
REMARK 500 O TYR B 267 CD PRO B 268 1.74
REMARK 500 O GLY C 195 O HOH C 880 1.88
REMARK 500 OG1 THR A 266 O HOH A 920 2.08
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 PRO B 268 CD PRO B 268 N -0.098
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 PRO A 268 C - N - CA ANGL. DEV. = 26.5 DEGREES
REMARK 500 PRO A 268 C - N - CD ANGL. DEV. = -24.6 DEGREES
REMARK 500 PRO B 159 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 PRO B 268 C - N - CA ANGL. DEV. = 56.2 DEGREES
REMARK 500 PRO B 268 C - N - CD ANGL. DEV. = -57.4 DEGREES
REMARK 500 PRO C 154 CA - N - CD ANGL. DEV. = -21.8 DEGREES
REMARK 500 PRO C 268 C - N - CA ANGL. DEV. = 33.2 DEGREES
REMARK 500 PRO C 268 C - N - CD ANGL. DEV. = -29.6 DEGREES
REMARK 500 PRO D 268 C - N - CA ANGL. DEV. = 57.5 DEGREES
REMARK 500 PRO D 268 C - N - CD ANGL. DEV. = -57.7 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 THR A 13 -94.81 -127.55
REMARK 500 ASN A 68 17.57 57.55
REMARK 500 GLU A 83 143.68 -175.62
REMARK 500 LYS A 100 16.67 -64.62
REMARK 500 PHE A 182 -168.30 -117.90
REMARK 500 LEU A 190 53.43 -92.39
REMARK 500 ASP A 215 -14.85 -147.23
REMARK 500 MET B 10 -69.99 -108.61
REMARK 500 THR B 13 -83.04 -126.41
REMARK 500 ASN B 68 19.17 55.65
REMARK 500 GLN B 101 39.15 -96.51
REMARK 500 GLU B 116 4.02 -66.39
REMARK 500 GLU B 141 42.96 -90.61
REMARK 500 LEU B 160 5.18 -61.41
REMARK 500 VAL B 161 10.69 -151.79
REMARK 500 VAL B 176 154.83 179.37
REMARK 500 PHE B 180 39.30 -149.14
REMARK 500 ASP B 215 -19.13 -142.79
REMARK 500 ASN B 218 4.18 -65.46
REMARK 500 TYR B 267 130.85 -31.23
REMARK 500 PRO B 268 -21.87 97.12
REMARK 500 PHE B 269 37.74 -97.48
REMARK 500 MET C 10 -69.88 -103.73
REMARK 500 THR C 13 -88.33 -126.34
REMARK 500 ASN C 68 10.77 57.78
REMARK 500 LEU C 153 130.73 -21.18
REMARK 500 PRO C 159 -72.22 -51.86
REMARK 500 ILE C 172 -52.41 -129.77
REMARK 500 LEU C 190 49.57 -90.44
REMARK 500 ASN C 218 11.76 -62.50
REMARK 500 ALA C 236 -172.49 -66.46
REMARK 500 ASP C 248 171.56 -59.73
REMARK 500 PHE C 269 67.13 -106.44
REMARK 500 MET D 10 -71.99 -98.70
REMARK 500 THR D 13 -76.54 -131.78
REMARK 500 GLU D 83 114.24 -170.48
REMARK 500 ILE D 172 -52.24 -128.91
REMARK 500 PRO D 207 -7.89 -48.57
REMARK 500 ASN D 218 4.92 -69.49
REMARK 500 PRO D 268 -20.69 101.48
REMARK 500 PHE D 269 44.05 -103.01
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 AF3 A 801 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 9 OD2
REMARK 620 2 AF3 A 801 F1 117.3
REMARK 620 3 AF3 A 801 F2 96.3 120.4
REMARK 620 4 AF3 A 801 F3 53.2 120.4 119.2
REMARK 620 5 ASP A 9 OD1 38.9 80.1 107.8 80.7
REMARK 620 6 ASP A 11 N 65.9 161.9 42.9 76.5 97.6
REMARK 620 7 SER A 44 OG 136.8 64.2 58.0 167.8 111.5 100.7
REMARK 620 8 MG A 805 MG 33.6 128.8 106.8 20.9 67.1 64.7 164.3
REMARK 620 9 HOH A 911 O 142.5 86.8 94.8 90.4 157.3 100.5 78.4 109.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 805 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 9 OD2
REMARK 620 2 ASP A 11 O 94.0
REMARK 620 3 ASP A 215 OD1 80.3 89.0
REMARK 620 4 AF3 A 801 F3 87.8 114.0 154.9
REMARK 620 5 HOH A 807 O 82.8 165.2 76.3 80.4
REMARK 620 6 HOH A 892 O 162.7 92.3 83.7 104.3 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 B 802 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 9 OD2
REMARK 620 2 AF3 B 802 F1 104.9
REMARK 620 3 AF3 B 802 F2 102.8 119.8
REMARK 620 4 AF3 B 802 F3 59.6 120.4 119.7
REMARK 620 5 ASP B 9 OD1 39.7 70.1 104.1 93.9
REMARK 620 6 MET B 10 N 59.4 114.8 45.9 104.3 61.5
REMARK 620 7 ASP B 11 N 73.7 164.3 47.3 72.9 102.3 50.6
REMARK 620 8 SER B 44 OG 139.9 74.5 50.8 155.3 110.3 84.0 96.4
REMARK 620 9 MG B 806 MG 36.9 118.2 116.1 22.7 72.9 86.6 70.4 166.7
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 806 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 9 OD2
REMARK 620 2 ASP B 11 O 96.1
REMARK 620 3 ASP B 215 OD1 76.1 81.1
REMARK 620 4 AF3 B 802 F3 94.9 102.6 170.7
REMARK 620 5 HOH B 816 O 80.9 169.7 88.6 87.6
REMARK 620 6 HOH B 889 O 162.8 86.0 87.4 101.3 94.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 C 803 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 9 OD1
REMARK 620 2 AF3 C 803 F1 97.2
REMARK 620 3 AF3 C 803 F2 90.6 120.5
REMARK 620 4 AF3 C 803 F3 80.4 119.4 120.1
REMARK 620 5 ASP C 9 OD2 38.9 98.2 121.5 46.1
REMARK 620 6 SER C 44 OG 105.2 45.5 75.5 163.8 131.8
REMARK 620 7 MG C 807 MG 71.6 111.8 126.4 11.7 35.2 157.2
REMARK 620 8 HOH C 811 O 166.2 94.9 89.1 87.8 132.3 88.1 97.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 807 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 9 OD2
REMARK 620 2 ASP C 11 O 84.7
REMARK 620 3 ASP C 215 OD2 119.5 82.8
REMARK 620 4 ASP C 215 OD1 75.0 94.4 47.6
REMARK 620 5 AF3 C 803 F3 81.8 110.6 156.6 144.1
REMARK 620 6 HOH C 839 O 168.8 102.1 53.6 95.4 103.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 D 804 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 9 OD1
REMARK 620 2 AF3 D 804 F1 76.6
REMARK 620 3 AF3 D 804 F2 105.3 120.4
REMARK 620 4 AF3 D 804 F3 85.7 119.6 120.0
REMARK 620 5 ASP D 9 OD2 40.4 111.8 102.5 51.4
REMARK 620 6 ASP D 11 N 100.4 169.6 50.4 69.6 69.4
REMARK 620 7 MG D 808 MG 71.4 116.7 120.1 14.6 37.2 70.9
REMARK 620 8 HOH D 889 O 154.6 82.1 97.4 93.0 144.3 103.0 107.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 808 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 9 OD2
REMARK 620 2 ASP D 11 O 80.8
REMARK 620 3 ASP D 215 OD1 78.5 86.7
REMARK 620 4 AF3 D 804 F3 79.8 95.2 157.6
REMARK 620 5 HOH D 897 O 169.2 91.6 93.5 108.7
REMARK 620 6 HOH D 899 O 84.2 162.4 81.2 91.2 101.9
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 MG A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 758
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 759
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RLM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NATIVE YBIV
REMARK 900 RELATED ID: 1RLO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BERYLLOFLUORIDE-BOUND YBIV
DBREF 1RLT A 1 271 UNP P75792 YBIV_ECOLI 1 271
DBREF 1RLT B 1 271 UNP P75792 YBIV_ECOLI 1 271
DBREF 1RLT C 1 271 UNP P75792 YBIV_ECOLI 1 271
DBREF 1RLT D 1 271 UNP P75792 YBIV_ECOLI 1 271
SEQADV 1RLT ALA A 2 UNP P75792 SER 2 ENGINEERED MUTATION
SEQADV 1RLT TYR A 267 UNP P75792 SER 267 ENGINEERED MUTATION
SEQADV 1RLT ALA B 2 UNP P75792 SER 2 ENGINEERED MUTATION
SEQADV 1RLT TYR B 267 UNP P75792 SER 267 ENGINEERED MUTATION
SEQADV 1RLT ALA C 2 UNP P75792 SER 2 ENGINEERED MUTATION
SEQADV 1RLT TYR C 267 UNP P75792 SER 267 ENGINEERED MUTATION
SEQADV 1RLT ALA D 2 UNP P75792 SER 2 ENGINEERED MUTATION
SEQADV 1RLT TYR D 267 UNP P75792 SER 267 ENGINEERED MUTATION
SEQRES 1 A 271 MET ALA VAL LYS VAL ILE VAL THR ASP MET ASP GLY THR
SEQRES 2 A 271 PHE LEU ASN ASP ALA LYS THR TYR ASN GLN PRO ARG PHE
SEQRES 3 A 271 MET ALA GLN TYR GLN GLU LEU LYS LYS ARG GLY ILE LYS
SEQRES 4 A 271 PHE VAL VAL ALA SER GLY ASN GLN TYR TYR GLN LEU ILE
SEQRES 5 A 271 SER PHE PHE PRO GLU LEU LYS ASP GLU ILE SER PHE VAL
SEQRES 6 A 271 ALA GLU ASN GLY ALA LEU VAL TYR GLU HIS GLY LYS GLN
SEQRES 7 A 271 LEU PHE HIS GLY GLU LEU THR ARG HIS GLU SER ARG ILE
SEQRES 8 A 271 VAL ILE GLY GLU LEU LEU LYS ASP LYS GLN LEU ASN PHE
SEQRES 9 A 271 VAL ALA CYS GLY LEU GLN SER ALA TYR VAL SER GLU ASN
SEQRES 10 A 271 ALA PRO GLU ALA PHE VAL ALA LEU MET ALA LYS HIS TYR
SEQRES 11 A 271 HIS ARG LEU LYS PRO VAL LYS ASP TYR GLN GLU ILE ASP
SEQRES 12 A 271 ASP VAL LEU PHE LYS PHE SER LEU ASN LEU PRO ASP GLU
SEQRES 13 A 271 GLN ILE PRO LEU VAL ILE ASP LYS LEU HIS VAL ALA LEU
SEQRES 14 A 271 ASP GLY ILE MET LYS PRO VAL THR SER GLY PHE GLY PHE
SEQRES 15 A 271 ILE ASP LEU ILE ILE PRO GLY LEU HIS LYS ALA ASN GLY
SEQRES 16 A 271 ILE SER ARG LEU LEU LYS ARG TRP ASP LEU SER PRO GLN
SEQRES 17 A 271 ASN VAL VAL ALA ILE GLY ASP SER GLY ASN ASP ALA GLU
SEQRES 18 A 271 MET LEU LYS MET ALA ARG TYR SER PHE ALA MET GLY ASN
SEQRES 19 A 271 ALA ALA GLU ASN ILE LYS GLN ILE ALA ARG TYR ALA THR
SEQRES 20 A 271 ASP ASP ASN ASN HIS GLU GLY ALA LEU ASN VAL ILE GLN
SEQRES 21 A 271 ALA VAL LEU ASP ASN THR TYR PRO PHE ASN SER
SEQRES 1 B 271 MET ALA VAL LYS VAL ILE VAL THR ASP MET ASP GLY THR
SEQRES 2 B 271 PHE LEU ASN ASP ALA LYS THR TYR ASN GLN PRO ARG PHE
SEQRES 3 B 271 MET ALA GLN TYR GLN GLU LEU LYS LYS ARG GLY ILE LYS
SEQRES 4 B 271 PHE VAL VAL ALA SER GLY ASN GLN TYR TYR GLN LEU ILE
SEQRES 5 B 271 SER PHE PHE PRO GLU LEU LYS ASP GLU ILE SER PHE VAL
SEQRES 6 B 271 ALA GLU ASN GLY ALA LEU VAL TYR GLU HIS GLY LYS GLN
SEQRES 7 B 271 LEU PHE HIS GLY GLU LEU THR ARG HIS GLU SER ARG ILE
SEQRES 8 B 271 VAL ILE GLY GLU LEU LEU LYS ASP LYS GLN LEU ASN PHE
SEQRES 9 B 271 VAL ALA CYS GLY LEU GLN SER ALA TYR VAL SER GLU ASN
SEQRES 10 B 271 ALA PRO GLU ALA PHE VAL ALA LEU MET ALA LYS HIS TYR
SEQRES 11 B 271 HIS ARG LEU LYS PRO VAL LYS ASP TYR GLN GLU ILE ASP
SEQRES 12 B 271 ASP VAL LEU PHE LYS PHE SER LEU ASN LEU PRO ASP GLU
SEQRES 13 B 271 GLN ILE PRO LEU VAL ILE ASP LYS LEU HIS VAL ALA LEU
SEQRES 14 B 271 ASP GLY ILE MET LYS PRO VAL THR SER GLY PHE GLY PHE
SEQRES 15 B 271 ILE ASP LEU ILE ILE PRO GLY LEU HIS LYS ALA ASN GLY
SEQRES 16 B 271 ILE SER ARG LEU LEU LYS ARG TRP ASP LEU SER PRO GLN
SEQRES 17 B 271 ASN VAL VAL ALA ILE GLY ASP SER GLY ASN ASP ALA GLU
SEQRES 18 B 271 MET LEU LYS MET ALA ARG TYR SER PHE ALA MET GLY ASN
SEQRES 19 B 271 ALA ALA GLU ASN ILE LYS GLN ILE ALA ARG TYR ALA THR
SEQRES 20 B 271 ASP ASP ASN ASN HIS GLU GLY ALA LEU ASN VAL ILE GLN
SEQRES 21 B 271 ALA VAL LEU ASP ASN THR TYR PRO PHE ASN SER
SEQRES 1 C 271 MET ALA VAL LYS VAL ILE VAL THR ASP MET ASP GLY THR
SEQRES 2 C 271 PHE LEU ASN ASP ALA LYS THR TYR ASN GLN PRO ARG PHE
SEQRES 3 C 271 MET ALA GLN TYR GLN GLU LEU LYS LYS ARG GLY ILE LYS
SEQRES 4 C 271 PHE VAL VAL ALA SER GLY ASN GLN TYR TYR GLN LEU ILE
SEQRES 5 C 271 SER PHE PHE PRO GLU LEU LYS ASP GLU ILE SER PHE VAL
SEQRES 6 C 271 ALA GLU ASN GLY ALA LEU VAL TYR GLU HIS GLY LYS GLN
SEQRES 7 C 271 LEU PHE HIS GLY GLU LEU THR ARG HIS GLU SER ARG ILE
SEQRES 8 C 271 VAL ILE GLY GLU LEU LEU LYS ASP LYS GLN LEU ASN PHE
SEQRES 9 C 271 VAL ALA CYS GLY LEU GLN SER ALA TYR VAL SER GLU ASN
SEQRES 10 C 271 ALA PRO GLU ALA PHE VAL ALA LEU MET ALA LYS HIS TYR
SEQRES 11 C 271 HIS ARG LEU LYS PRO VAL LYS ASP TYR GLN GLU ILE ASP
SEQRES 12 C 271 ASP VAL LEU PHE LYS PHE SER LEU ASN LEU PRO ASP GLU
SEQRES 13 C 271 GLN ILE PRO LEU VAL ILE ASP LYS LEU HIS VAL ALA LEU
SEQRES 14 C 271 ASP GLY ILE MET LYS PRO VAL THR SER GLY PHE GLY PHE
SEQRES 15 C 271 ILE ASP LEU ILE ILE PRO GLY LEU HIS LYS ALA ASN GLY
SEQRES 16 C 271 ILE SER ARG LEU LEU LYS ARG TRP ASP LEU SER PRO GLN
SEQRES 17 C 271 ASN VAL VAL ALA ILE GLY ASP SER GLY ASN ASP ALA GLU
SEQRES 18 C 271 MET LEU LYS MET ALA ARG TYR SER PHE ALA MET GLY ASN
SEQRES 19 C 271 ALA ALA GLU ASN ILE LYS GLN ILE ALA ARG TYR ALA THR
SEQRES 20 C 271 ASP ASP ASN ASN HIS GLU GLY ALA LEU ASN VAL ILE GLN
SEQRES 21 C 271 ALA VAL LEU ASP ASN THR TYR PRO PHE ASN SER
SEQRES 1 D 271 MET ALA VAL LYS VAL ILE VAL THR ASP MET ASP GLY THR
SEQRES 2 D 271 PHE LEU ASN ASP ALA LYS THR TYR ASN GLN PRO ARG PHE
SEQRES 3 D 271 MET ALA GLN TYR GLN GLU LEU LYS LYS ARG GLY ILE LYS
SEQRES 4 D 271 PHE VAL VAL ALA SER GLY ASN GLN TYR TYR GLN LEU ILE
SEQRES 5 D 271 SER PHE PHE PRO GLU LEU LYS ASP GLU ILE SER PHE VAL
SEQRES 6 D 271 ALA GLU ASN GLY ALA LEU VAL TYR GLU HIS GLY LYS GLN
SEQRES 7 D 271 LEU PHE HIS GLY GLU LEU THR ARG HIS GLU SER ARG ILE
SEQRES 8 D 271 VAL ILE GLY GLU LEU LEU LYS ASP LYS GLN LEU ASN PHE
SEQRES 9 D 271 VAL ALA CYS GLY LEU GLN SER ALA TYR VAL SER GLU ASN
SEQRES 10 D 271 ALA PRO GLU ALA PHE VAL ALA LEU MET ALA LYS HIS TYR
SEQRES 11 D 271 HIS ARG LEU LYS PRO VAL LYS ASP TYR GLN GLU ILE ASP
SEQRES 12 D 271 ASP VAL LEU PHE LYS PHE SER LEU ASN LEU PRO ASP GLU
SEQRES 13 D 271 GLN ILE PRO LEU VAL ILE ASP LYS LEU HIS VAL ALA LEU
SEQRES 14 D 271 ASP GLY ILE MET LYS PRO VAL THR SER GLY PHE GLY PHE
SEQRES 15 D 271 ILE ASP LEU ILE ILE PRO GLY LEU HIS LYS ALA ASN GLY
SEQRES 16 D 271 ILE SER ARG LEU LEU LYS ARG TRP ASP LEU SER PRO GLN
SEQRES 17 D 271 ASN VAL VAL ALA ILE GLY ASP SER GLY ASN ASP ALA GLU
SEQRES 18 D 271 MET LEU LYS MET ALA ARG TYR SER PHE ALA MET GLY ASN
SEQRES 19 D 271 ALA ALA GLU ASN ILE LYS GLN ILE ALA ARG TYR ALA THR
SEQRES 20 D 271 ASP ASP ASN ASN HIS GLU GLY ALA LEU ASN VAL ILE GLN
SEQRES 21 D 271 ALA VAL LEU ASP ASN THR TYR PRO PHE ASN SER
HET MG A 805 1
HET ACT A 800 4
HET AF3 A 801 4
HET MG B 806 1
HET AF3 B 802 4
HET MG C 807 1
HET AF3 C 803 4
HET GOL C 759 6
HET MG D 808 1
HET AF3 D 804 4
HET GOL D 758 6
HETNAM MG MAGNESIUM ION
HETNAM ACT ACETATE ION
HETNAM AF3 ALUMINUM FLUORIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 MG 4(MG 2+)
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 7 AF3 4(AL F3)
FORMUL 12 GOL 2(C3 H8 O3)
FORMUL 16 HOH *397(H2 O)
HELIX 1 1 ASN A 22 ARG A 36 1 15
HELIX 2 2 GLN A 47 ILE A 52 1 6
HELIX 3 3 SER A 53 PHE A 55 5 3
HELIX 4 4 GLU A 67 GLY A 69 5 3
HELIX 5 5 THR A 85 LEU A 97 1 13
HELIX 6 6 PRO A 119 LYS A 128 1 10
HELIX 7 7 ASP A 138 ILE A 142 5 5
HELIX 8 8 GLN A 157 LEU A 169 1 13
HELIX 9 9 HIS A 191 ASP A 204 1 14
HELIX 10 10 SER A 206 GLN A 208 5 3
HELIX 11 11 SER A 216 ASN A 218 5 3
HELIX 12 12 ASP A 219 ALA A 226 1 8
HELIX 13 13 ALA A 236 ALA A 243 1 8
HELIX 14 14 ASP A 249 HIS A 252 5 4
HELIX 15 15 GLU A 253 ASN A 265 1 13
HELIX 16 16 ASN B 22 GLY B 37 1 16
HELIX 17 17 GLN B 47 ILE B 52 1 6
HELIX 18 18 SER B 53 PHE B 55 5 3
HELIX 19 19 GLU B 67 GLY B 69 5 3
HELIX 20 20 THR B 85 LEU B 97 1 13
HELIX 21 21 PRO B 119 ALA B 127 1 9
HELIX 22 22 PRO B 154 LEU B 160 5 7
HELIX 23 23 VAL B 161 LEU B 169 1 9
HELIX 24 24 HIS B 191 ASP B 204 1 14
HELIX 25 25 SER B 206 GLN B 208 5 3
HELIX 26 26 SER B 216 ASN B 218 5 3
HELIX 27 27 ASP B 219 ALA B 226 1 8
HELIX 28 28 ALA B 236 ALA B 243 1 8
HELIX 29 29 GLU B 253 ASP B 264 1 12
HELIX 30 30 ASN C 22 ARG C 36 1 15
HELIX 31 31 GLN C 47 ILE C 52 1 6
HELIX 32 32 SER C 53 PHE C 55 5 3
HELIX 33 33 GLU C 67 GLY C 69 5 3
HELIX 34 34 THR C 85 LYS C 98 1 14
HELIX 35 35 PRO C 119 ALA C 127 1 9
HELIX 36 36 ASP C 138 ILE C 142 5 5
HELIX 37 37 PRO C 159 LEU C 169 1 11
HELIX 38 38 HIS C 191 TRP C 203 1 13
HELIX 39 39 SER C 206 GLN C 208 5 3
HELIX 40 40 SER C 216 ASN C 218 5 3
HELIX 41 41 ASP C 219 ALA C 226 1 8
HELIX 42 42 ALA C 236 ALA C 243 1 8
HELIX 43 43 ASP C 249 HIS C 252 5 4
HELIX 44 44 GLU C 253 ASN C 265 1 13
HELIX 45 45 ASN D 22 ARG D 36 1 15
HELIX 46 46 GLN D 47 ILE D 52 1 6
HELIX 47 47 SER D 53 PHE D 55 5 3
HELIX 48 48 GLU D 67 GLY D 69 5 3
HELIX 49 49 THR D 85 LEU D 97 1 13
HELIX 50 50 PRO D 119 LYS D 128 1 10
HELIX 51 51 ASP D 138 ILE D 142 5 5
HELIX 52 52 PRO D 154 GLU D 156 5 3
HELIX 53 53 GLN D 157 LEU D 169 1 13
HELIX 54 54 HIS D 191 ASP D 204 1 14
HELIX 55 55 SER D 206 GLN D 208 5 3
HELIX 56 56 SER D 216 ASN D 218 5 3
HELIX 57 57 ASP D 219 ALA D 226 1 8
HELIX 58 58 ALA D 236 ALA D 243 1 8
HELIX 59 59 ASP D 249 HIS D 252 5 4
HELIX 60 60 GLU D 253 ASN D 265 1 13
SHEET 1 A 8 LYS A 77 HIS A 81 0
SHEET 2 A 8 LEU A 71 GLU A 74 -1 N VAL A 72 O LEU A 79
SHEET 3 A 8 SER A 63 ALA A 66 -1 N ALA A 66 O LEU A 71
SHEET 4 A 8 LYS A 39 ALA A 43 1 N VAL A 42 O VAL A 65
SHEET 5 A 8 VAL A 5 THR A 8 1 N THR A 8 O VAL A 41
SHEET 6 A 8 VAL A 210 GLY A 214 1 O VAL A 211 N VAL A 7
SHEET 7 A 8 TYR A 228 ALA A 231 1 O PHE A 230 N ALA A 212
SHEET 8 A 8 TYR A 245 ALA A 246 1 O TYR A 245 N ALA A 231
SHEET 1 B 6 LEU A 133 VAL A 136 0
SHEET 2 B 6 ALA A 112 SER A 115 1 N ALA A 112 O LYS A 134
SHEET 3 B 6 PHE A 104 GLY A 108 -1 N ALA A 106 O TYR A 113
SHEET 4 B 6 LEU A 146 PRO A 154 -1 O LYS A 148 N CYS A 107
SHEET 5 B 6 PHE A 182 ILE A 186 -1 O ILE A 183 N LEU A 151
SHEET 6 B 6 LYS A 174 THR A 177 -1 N VAL A 176 O ASP A 184
SHEET 1 C 8 LYS B 77 HIS B 81 0
SHEET 2 C 8 LEU B 71 GLU B 74 -1 N VAL B 72 O LEU B 79
SHEET 3 C 8 SER B 63 ALA B 66 -1 N ALA B 66 O LEU B 71
SHEET 4 C 8 LYS B 39 ALA B 43 1 N VAL B 42 O VAL B 65
SHEET 5 C 8 VAL B 5 THR B 8 1 N THR B 8 O VAL B 41
SHEET 6 C 8 VAL B 210 GLY B 214 1 O VAL B 211 N VAL B 7
SHEET 7 C 8 TYR B 228 ALA B 231 1 O PHE B 230 N ALA B 212
SHEET 8 C 8 TYR B 245 ALA B 246 1 O TYR B 245 N ALA B 231
SHEET 1 D 6 LEU B 133 VAL B 136 0
SHEET 2 D 6 ALA B 112 SER B 115 1 N ALA B 112 O LYS B 134
SHEET 3 D 6 PHE B 104 GLY B 108 -1 N ALA B 106 O TYR B 113
SHEET 4 D 6 LEU B 146 LEU B 151 -1 O LYS B 148 N CYS B 107
SHEET 5 D 6 ILE B 183 ILE B 186 -1 O ILE B 183 N LEU B 151
SHEET 6 D 6 LYS B 174 THR B 177 -1 N VAL B 176 O ASP B 184
SHEET 1 E 8 LYS C 77 HIS C 81 0
SHEET 2 E 8 LEU C 71 GLU C 74 -1 N VAL C 72 O PHE C 80
SHEET 3 E 8 SER C 63 ALA C 66 -1 N PHE C 64 O TYR C 73
SHEET 4 E 8 LYS C 39 ALA C 43 1 N VAL C 42 O VAL C 65
SHEET 5 E 8 VAL C 5 THR C 8 1 N THR C 8 O VAL C 41
SHEET 6 E 8 VAL C 210 GLY C 214 1 O VAL C 211 N VAL C 7
SHEET 7 E 8 TYR C 228 MET C 232 1 O MET C 232 N GLY C 214
SHEET 8 E 8 TYR C 245 THR C 247 1 O TYR C 245 N ALA C 231
SHEET 1 F 6 LEU C 133 VAL C 136 0
SHEET 2 F 6 ALA C 112 SER C 115 1 N VAL C 114 O VAL C 136
SHEET 3 F 6 PHE C 104 GLY C 108 -1 N ALA C 106 O TYR C 113
SHEET 4 F 6 LEU C 146 LEU C 151 -1 O LYS C 148 N CYS C 107
SHEET 5 F 6 ILE C 183 ILE C 186 -1 O ILE C 183 N LEU C 151
SHEET 6 F 6 LYS C 174 THR C 177 -1 N LYS C 174 O ILE C 186
SHEET 1 G 8 LYS D 77 HIS D 81 0
SHEET 2 G 8 LEU D 71 GLU D 74 -1 N VAL D 72 O PHE D 80
SHEET 3 G 8 SER D 63 ALA D 66 -1 N ALA D 66 O LEU D 71
SHEET 4 G 8 LYS D 39 ALA D 43 1 N VAL D 42 O VAL D 65
SHEET 5 G 8 VAL D 5 THR D 8 1 N ILE D 6 O VAL D 41
SHEET 6 G 8 VAL D 210 GLY D 214 1 O VAL D 211 N VAL D 7
SHEET 7 G 8 TYR D 228 ALA D 231 1 O PHE D 230 N ALA D 212
SHEET 8 G 8 TYR D 245 ALA D 246 1 O TYR D 245 N ALA D 231
SHEET 1 H 6 LEU D 133 VAL D 136 0
SHEET 2 H 6 ALA D 112 SER D 115 1 N VAL D 114 O VAL D 136
SHEET 3 H 6 ASN D 103 GLY D 108 -1 N ALA D 106 O TYR D 113
SHEET 4 H 6 LEU D 146 ASN D 152 -1 O LYS D 148 N CYS D 107
SHEET 5 H 6 PHE D 182 ILE D 186 -1 O ILE D 183 N LEU D 151
SHEET 6 H 6 LYS D 174 THR D 177 -1 N LYS D 174 O ILE D 186
LINK OG SER C 178 O3 GOL C 759 1555 1555 2.05
LINK OD2 ASP A 9 AL AF3 A 801 1555 1555 3.49
LINK OD1 ASP A 9 AL AF3 A 801 1555 1555 2.75
LINK OD2 ASP A 9 MG MG A 805 1555 1555 2.03
LINK N ASP A 11 AL AF3 A 801 1555 1555 3.72
LINK O ASP A 11 MG MG A 805 1555 1555 1.91
LINK OG SER A 44 AL AF3 A 801 1555 1555 3.53
LINK OD1 ASP A 215 MG MG A 805 1555 1555 2.21
LINK F3 AF3 A 801 MG MG A 805 1555 1555 2.05
LINK AL AF3 A 801 MG MG A 805 1555 1555 3.52
LINK AL AF3 A 801 O HOH A 911 1555 1555 3.13
LINK MG MG A 805 O HOH A 807 1555 1555 2.27
LINK MG MG A 805 O HOH A 892 1555 1555 2.05
LINK OD2 ASP B 9 AL AF3 B 802 1555 1555 3.43
LINK OD1 ASP B 9 AL AF3 B 802 1555 1555 2.78
LINK OD2 ASP B 9 MG MG B 806 1555 1555 2.14
LINK N MET B 10 AL AF3 B 802 1555 1555 3.71
LINK N ASP B 11 AL AF3 B 802 1555 1555 3.57
LINK O ASP B 11 MG MG B 806 1555 1555 2.09
LINK OG SER B 44 AL AF3 B 802 1555 1555 3.64
LINK OD1 ASP B 215 MG MG B 806 1555 1555 2.18
LINK F3 AF3 B 802 MG MG B 806 1555 1555 1.88
LINK AL AF3 B 802 MG MG B 806 1555 1555 3.31
LINK AL AF3 B 802 O HOH B 857 1555 1555 3.14
LINK MG MG B 806 O HOH B 816 1555 1555 2.16
LINK MG MG B 806 O HOH B 889 1555 1555 2.13
LINK OD1 ASP C 9 AL AF3 C 803 1555 1555 2.71
LINK OD2 ASP C 9 AL AF3 C 803 1555 1555 3.50
LINK OD2 ASP C 9 MG MG C 807 1555 1555 2.12
LINK O ASP C 11 MG MG C 807 1555 1555 2.03
LINK OG SER C 44 AL AF3 C 803 1555 1555 3.62
LINK OD2 ASP C 215 MG MG C 807 1555 1555 2.95
LINK OD1 ASP C 215 MG MG C 807 1555 1555 1.81
LINK F3 AF3 C 803 MG MG C 807 1555 1555 1.89
LINK AL AF3 C 803 MG MG C 807 1555 1555 3.51
LINK AL AF3 C 803 O HOH C 811 1555 1555 3.17
LINK MG MG C 807 O HOH C 839 1555 1555 2.23
LINK OD1 ASP D 9 AL AF3 D 804 1555 1555 2.83
LINK OD2 ASP D 9 AL AF3 D 804 1555 1555 3.35
LINK OD2 ASP D 9 MG MG D 808 1555 1555 2.19
LINK N ASP D 11 AL AF3 D 804 1555 1555 3.61
LINK O ASP D 11 MG MG D 808 1555 1555 1.95
LINK OD1 ASP D 215 MG MG D 808 1555 1555 2.11
LINK AL AF3 D 804 MG MG D 808 1555 1555 3.51
LINK F3 AF3 D 804 MG MG D 808 1555 1555 1.92
LINK AL AF3 D 804 O HOH D 889 1555 1555 3.15
LINK MG MG D 808 O HOH D 897 1555 1555 2.10
LINK MG MG D 808 O HOH D 899 1555 1555 2.05
CISPEP 1 TYR A 267 PRO A 268 0 -2.44
CISPEP 2 TYR C 267 PRO C 268 0 1.52
SITE 1 AC1 6 ASP A 9 ASP A 11 ASP A 215 AF3 A 801
SITE 2 AC1 6 HOH A 807 HOH A 892
SITE 1 AC2 6 ASP B 9 ASP B 11 ASP B 215 AF3 B 802
SITE 2 AC2 6 HOH B 816 HOH B 889
SITE 1 AC3 5 ASP C 9 ASP C 11 ASP C 215 AF3 C 803
SITE 2 AC3 5 HOH C 839
SITE 1 AC4 6 ASP D 9 ASP D 11 ASP D 215 AF3 D 804
SITE 2 AC4 6 HOH D 897 HOH D 899
SITE 1 AC5 4 LYS A 19 LYS A 128 HIS A 129 HOH A 834
SITE 1 AC6 10 ASP A 9 MET A 10 ASP A 11 SER A 44
SITE 2 AC6 10 GLY A 45 ASN A 46 GLY A 179 LYS A 192
SITE 3 AC6 10 MG A 805 HOH A 807
SITE 1 AC7 10 ASP B 9 MET B 10 ASP B 11 SER B 44
SITE 2 AC7 10 GLY B 45 GLY B 179 LYS B 192 ASN B 218
SITE 3 AC7 10 MG B 806 HOH B 816
SITE 1 AC8 9 ASP C 9 MET C 10 ASP C 11 SER C 44
SITE 2 AC8 9 GLY C 45 LYS C 192 ASP C 215 ASN C 218
SITE 3 AC8 9 MG C 807
SITE 1 AC9 9 ASP D 9 MET D 10 ASP D 11 SER D 44
SITE 2 AC9 9 GLY D 45 LYS D 192 ASN D 218 MG D 808
SITE 3 AC9 9 HOH D 899
SITE 1 BC1 6 GLY D 45 TYR D 130 SER D 150 SER D 178
SITE 2 BC1 6 PHE D 182 ASP D 184
SITE 1 BC2 7 MET C 126 TYR C 130 SER C 150 SER C 178
SITE 2 BC2 7 PHE C 182 ASP C 184 HOH C 811
CRYST1 71.761 91.166 183.850 90.00 90.00 90.00 P 21 21 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 0.013935 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010969 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005439 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
