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HEADER HYDROLASE 17-NOV-15 5ESR
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE (DCCA) FROM CAULOBACTER
TITLE 2 CRESCENTUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAULOBACTER CRESCENTUS (STRAIN ATCC 19089 /
SOURCE 3 CB15);
SOURCE 4 ORGANISM_TAXID: 190650;
SOURCE 5 STRAIN: ATCC 19089 / CB15;
SOURCE 6 GENE: DHMA, CC_1175;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PJ401EXPRESS
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,R.TORO,E.C.MUNDORFF,S.C.ALMO
REVDAT 1 01-JUN-16 5ESR 0
JRNL AUTH L.CARLUCCI,E.ZHOU,V.N.MALASHKEVICH,S.C.ALMO,E.C.MUNDORFF
JRNL TITL BIOCHEMICAL CHARACTERIZATION OF TWO HALOALKANE
JRNL TITL 2 DEHALOGENASES: DCCA FROM CAULOBACTER CRESCENTUS AND DSAA
JRNL TITL 3 FROM SACCHAROMONOSPORA AZUREA.
JRNL REF PROTEIN SCI. V. 25 877 2016
JRNL REFN ESSN 1469-896X
JRNL PMID 26833751
JRNL DOI 10.1002/PRO.2895
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 50696
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.127
REMARK 3 R VALUE (WORKING SET) : 0.126
REMARK 3 FREE R VALUE : 0.149
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2572
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 47.4074 - 4.5853 0.99 3090 131 0.1463 0.1352
REMARK 3 2 4.5853 - 3.6399 1.00 3111 153 0.1121 0.1363
REMARK 3 3 3.6399 - 3.1799 1.00 3091 166 0.1235 0.1399
REMARK 3 4 3.1799 - 2.8892 1.00 3084 176 0.1228 0.1669
REMARK 3 5 2.8892 - 2.6821 1.00 3051 165 0.1205 0.1472
REMARK 3 6 2.6821 - 2.5240 1.00 3119 172 0.1143 0.1479
REMARK 3 7 2.5240 - 2.3976 1.00 3099 141 0.1119 0.1386
REMARK 3 8 2.3976 - 2.2933 1.00 3071 175 0.1133 0.1359
REMARK 3 9 2.2933 - 2.2050 1.00 3102 130 0.1094 0.1339
REMARK 3 10 2.2050 - 2.1289 1.00 3119 140 0.1101 0.1179
REMARK 3 11 2.1289 - 2.0623 1.00 3110 174 0.1114 0.1378
REMARK 3 12 2.0623 - 2.0034 1.00 3078 156 0.1160 0.1484
REMARK 3 13 2.0034 - 1.9506 1.00 3121 142 0.1186 0.1437
REMARK 3 14 1.9506 - 1.9030 1.00 3045 202 0.1139 0.1452
REMARK 3 15 1.9030 - 1.8598 1.00 3094 163 0.1160 0.1418
REMARK 3 16 1.8598 - 1.8202 1.00 3043 175 0.1237 0.1457
REMARK 3 17 1.8202 - 1.7838 1.00 3107 187 0.1195 0.1815
REMARK 3 18 1.7838 - 1.7501 1.00 3019 173 0.1339 0.1565
REMARK 3 19 1.7501 - 1.7189 1.00 3131 150 0.1232 0.1293
REMARK 3 20 1.7189 - 1.6897 1.00 3087 173 0.1306 0.1532
REMARK 3 21 1.6897 - 1.6625 1.00 3059 196 0.1303 0.1485
REMARK 3 22 1.6625 - 1.6369 1.00 3053 179 0.1416 0.1618
REMARK 3 23 1.6369 - 1.6128 1.00 3067 185 0.1400 0.1765
REMARK 3 24 1.6128 - 1.5901 1.00 3119 165 0.1511 0.1628
REMARK 3 25 1.5901 - 1.5686 1.00 3041 179 0.1553 0.1745
REMARK 3 26 1.5686 - 1.5482 1.00 3098 138 0.1597 0.1908
REMARK 3 27 1.5482 - 1.5289 1.00 3071 161 0.1666 0.1998
REMARK 3 28 1.5289 - 1.5105 1.00 3103 175 0.1662 0.1880
REMARK 3 29 1.5105 - 1.4929 1.00 3110 173 0.1749 0.1690
REMARK 3 30 1.4929 - 1.4761 1.00 3060 163 0.1829 0.1712
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.66
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 : 0.008 2530
REMARK 3 ANGLE : 1.262 3461
REMARK 3 CHIRALITY : 0.072 372
REMARK 3 PLANARITY : 0.007 458
REMARK 3 DIHEDRAL : 12.305 919
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8632 21.3225 10.6223
REMARK 3 T TENSOR
REMARK 3 T11: 0.0477 T22: 0.0579
REMARK 3 T33: 0.0297 T12: -0.0068
REMARK 3 T13: 0.0003 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.3925 L22: 0.8987
REMARK 3 L33: 0.3777 L12: -0.3746
REMARK 3 L13: 0.0931 L23: -0.1682
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: -0.0244 S13: -0.0091
REMARK 3 S21: 0.0604 S22: 0.0035 S23: 0.0023
REMARK 3 S31: 0.0101 S32: 0.0099 S33: 0.0061
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 5ESR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215468.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50696
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.476
REMARK 200 RESOLUTION RANGE LOW (A) : 94.766
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11000
REMARK 200 FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.50
REMARK 200 R MERGE FOR SHELL (I) : 0.56300
REMARK 200 R SYM FOR SHELL (I) : 0.56300
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: 2XT0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.005 M COBALT CHLORIDE, 0.005
REMARK 280 MAGNESIUM CHLORIDE, 0.005 CADMIUM CHLORIDE, 0.005 NICKEL
REMARK 280 CHLORIDE, 0.1 M HEPES:NAOH, PH 7.5, 12% PEG 3350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 47.38300
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 47.38300
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 39.68850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.82150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.68850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.82150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 47.38300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.68850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.82150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 47.38300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.68850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.82150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: 3720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -181.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 79.64300
REMARK 350 BIOMT3 2 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 HOH A 745 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 773 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 905 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 937 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 943 LIES ON A SPECIAL POSITION.
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 OE2 GLU A 202 HZ2 LYS A 205 1.58
REMARK 500 O HOH A 766 O HOH A 813 1.91
REMARK 500 O HOH A 559 O HOH A 602 2.01
REMARK 500 O HOH A 783 O HOH A 813 2.08
REMARK 500 O HOH A 803 O HOH A 838 2.09
REMARK 500 O HOH A 674 O HOH A 813 2.11
REMARK 500 O HOH A 850 O HOH A 891 2.14
REMARK 500 O HOH A 535 O HOH A 789 2.17
REMARK 500 O HOH A 761 O HOH A 831 2.19
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 HE2 HIS A 308 CO CO A 401 4565 1.20
REMARK 500 HE2 HIS A 307 CO CO A 402 4565 1.29
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 PRO A 56 55.79 -105.53
REMARK 500 ASP A 123 -131.99 47.19
REMARK 500 SER A 223 -0.21 80.61
REMARK 500 HIS A 307 31.57 76.48
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 A 940 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 941 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 942 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 943 DISTANCE = 6.75 ANGSTROMS
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 CO A 407 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 22 CE1
REMARK 620 2 HIS A 22 NE2 28.4
REMARK 620 3 ASP A 40 O 104.2 109.4
REMARK 620 4 HOH A 674 O 76.4 104.7 75.6
REMARK 620 5 HOH A 766 O 71.1 86.1 138.2 62.8
REMARK 620 6 HOH A 768 O 161.8 149.7 92.3 101.0 91.5
REMARK 620 7 HOH A 542 O 100.8 74.5 80.0 153.8 141.6 89.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 403 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 25 CD
REMARK 620 2 GLU A 25 OE1 27.1
REMARK 620 3 GLU A 25 OE2 27.1 54.1
REMARK 620 4 HOH A 782 O 87.6 82.8 91.1
REMARK 620 5 HOH A 797 O 108.4 81.7 135.3 89.5
REMARK 620 6 HOH A 809 O 90.5 93.8 88.9 175.9 87.6
REMARK 620 7 GLU A 12 CD 73.0 99.1 47.8 114.3 156.2 68.6
REMARK 620 8 GLU A 12 OE1 73.9 100.0 48.8 114.8 155.7 68.1 1.0
REMARK 620 9 GLU A 12 OE2 74.7 101.1 49.2 113.0 157.5 69.9 2.4 2.1
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 406 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 123 OD1
REMARK 620 2 HOH A 803 O 89.4
REMARK 620 3 HOH A 747 O 80.4 167.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 180 O
REMARK 620 2 ASN A 180 OD1 83.5
REMARK 620 3 THR A 183 O 86.0 168.8
REMARK 620 4 THR A 183 OG1 81.0 96.0 78.6
REMARK 620 5 ARG A 185 O 166.7 94.6 94.8 86.2
REMARK 620 6 HOH A 613 O 109.0 98.2 88.8 163.5 84.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 238 CG
REMARK 620 2 ASP A 238 OD1 30.4
REMARK 620 3 ASP A 238 OD2 30.9 61.2
REMARK 620 4 HIS A 303 NE2 86.8 89.0 87.8
REMARK 620 5 HIS A 305 NE2 132.1 101.7 162.4 96.4
REMARK 620 6 HOH A 720 O 86.3 84.9 86.4 173.1 88.1
REMARK 620 7 HIS A 308 NE2 141.8 117.7 150.8 121.2 31.4 64.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 405 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 256 CD
REMARK 620 2 GLU A 256 OE1 30.4
REMARK 620 3 GLU A 256 OE2 30.5 60.8
REMARK 620 4 HOH A 562 O 88.0 96.1 84.6
REMARK 620 5 HOH A 630 O 124.3 95.1 154.0 88.8
REMARK 620 6 HOH A 537 O 92.0 81.6 97.7 175.4 87.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 408 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 293 OD1
REMARK 620 2 HOH A 701 O 88.3
REMARK 620 3 HOH A 859 O 171.8 91.9
REMARK 620 4 HOH A 737 O 94.5 98.2 93.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 402 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 304 NE2
REMARK 620 2 HIS A 306 NE2 95.0
REMARK 620 3 HOH A 742 O 173.2 87.4
REMARK 620 4 HOH A 753 O 89.3 91.7 84.2
REMARK 620 5 HOH A 775 O 91.3 173.6 86.4 89.3
REMARK 620 6 HIS A 307 NE2 123.7 33.2 60.7 106.6 140.7
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 CO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 409
DBREF 5ESR A 1 302 UNP Q9A919 DHMA_CAUCR 1 302
SEQADV 5ESR HIS A 303 UNP Q9A919 EXPRESSION TAG
SEQADV 5ESR HIS A 304 UNP Q9A919 EXPRESSION TAG
SEQADV 5ESR HIS A 305 UNP Q9A919 EXPRESSION TAG
SEQADV 5ESR HIS A 306 UNP Q9A919 EXPRESSION TAG
SEQADV 5ESR HIS A 307 UNP Q9A919 EXPRESSION TAG
SEQADV 5ESR HIS A 308 UNP Q9A919 EXPRESSION TAG
SEQRES 1 A 308 MET ASP VAL LEU ARG THR PRO ASP GLU ARG PHE GLU GLY
SEQRES 2 A 308 LEU ALA ASP TRP SER PHE ALA PRO HIS TYR THR GLU VAL
SEQRES 3 A 308 THR ASP ALA ASP GLY THR ALA LEU ARG ILE HIS HIS VAL
SEQRES 4 A 308 ASP GLU GLY PRO LYS ASP GLN ARG PRO ILE LEU LEU MET
SEQRES 5 A 308 HIS GLY GLU PRO SER TRP ALA TYR LEU TYR ARG LYS VAL
SEQRES 6 A 308 ILE ALA GLU LEU VAL ALA LYS GLY HIS ARG VAL VAL ALA
SEQRES 7 A 308 PRO ASP LEU VAL GLY PHE GLY ARG SER ASP LYS PRO ALA
SEQRES 8 A 308 LYS ARG THR ASP TYR THR TYR GLU ARG HIS VAL ALA TRP
SEQRES 9 A 308 MET SER ALA TRP LEU GLU GLN ASN ASP LEU LYS ASP ILE
SEQRES 10 A 308 VAL LEU PHE CYS GLN ASP TRP GLY GLY LEU ILE GLY LEU
SEQRES 11 A 308 ARG LEU VAL ALA ALA PHE PRO GLU ARG PHE SER ALA VAL
SEQRES 12 A 308 VAL VAL SER ASN THR GLY LEU PRO ILE GLY VAL GLY LYS
SEQRES 13 A 308 SER GLU GLY PHE GLU ALA TRP LEU ASN PHE SER GLN ASN
SEQRES 14 A 308 THR PRO GLU LEU PRO VAL GLY PHE ILE LEU ASN GLY GLY
SEQRES 15 A 308 THR ALA ARG ASP LEU SER ASP ALA GLU ARG SER ALA TYR
SEQRES 16 A 308 ASP ALA PRO PHE PRO ASP GLU SER TYR LYS GLU GLY ALA
SEQRES 17 A 308 ARG ILE PHE PRO ALA LEU VAL PRO ILE THR PRO GLU HIS
SEQRES 18 A 308 ALA SER VAL GLU GLU ASN LYS ALA ALA TRP ALA VAL LEU
SEQRES 19 A 308 GLU THR PHE ASP LYS PRO PHE VAL THR ALA PHE SER ASP
SEQRES 20 A 308 ALA ASP PRO ILE THR ARG GLY GLY GLU ALA MET PHE LEU
SEQRES 21 A 308 ALA ARG VAL PRO GLY THR LYS ASN VAL ALA HIS THR THR
SEQRES 22 A 308 LEU LYS GLY GLY HIS PHE VAL GLN GLU ASP SER PRO VAL
SEQRES 23 A 308 GLU ILE ALA ALA LEU LEU ASP GLY LEU VAL ALA GLY LEU
SEQRES 24 A 308 PRO GLN ALA HIS HIS HIS HIS HIS HIS
HET CO A 401 1
HET CO A 402 1
HET CO A 403 1
HET MG A 404 1
HET CO A 405 1
HET CO A 406 1
HET CO A 407 1
HET MG A 408 1
HET CL A 409 1
HETNAM CO COBALT (II) ION
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 CO 6(CO 2+)
FORMUL 5 MG 2(MG 2+)
FORMUL 10 CL CL 1-
FORMUL 11 HOH *443(H2 O)
HELIX 1 AA1 PRO A 7 GLU A 12 5 6
HELIX 2 AA2 TRP A 58 LEU A 61 5 4
HELIX 3 AA3 TYR A 62 LYS A 72 1 11
HELIX 4 AA4 LYS A 92 TYR A 96 5 5
HELIX 5 AA5 THR A 97 ASN A 112 1 16
HELIX 6 AA6 ASP A 123 PHE A 136 1 14
HELIX 7 AA7 SER A 157 THR A 170 1 14
HELIX 8 AA8 PRO A 174 GLY A 182 1 9
HELIX 9 AA9 SER A 188 ALA A 197 1 10
HELIX 10 AB1 ASP A 201 TYR A 204 5 4
HELIX 11 AB2 LYS A 205 VAL A 215 1 11
HELIX 12 AB3 SER A 223 GLU A 235 1 13
HELIX 13 AB4 THR A 252 GLY A 254 5 3
HELIX 14 AB5 GLY A 255 VAL A 263 1 9
HELIX 15 AB6 PRO A 264 LYS A 267 5 4
HELIX 16 AB7 PHE A 279 SER A 284 1 6
HELIX 17 AB8 SER A 284 LEU A 299 1 16
HELIX 18 AB9 PRO A 300 ALA A 302 5 3
SHEET 1 AA1 2 VAL A 3 LEU A 4 0
SHEET 2 AA1 2 LYS A 89 PRO A 90 -1 O LYS A 89 N LEU A 4
SHEET 1 AA2 7 HIS A 22 THR A 27 0
SHEET 2 AA2 7 ALA A 33 GLU A 41 -1 O LEU A 34 N VAL A 26
SHEET 3 AA2 7 ARG A 75 PRO A 79 -1 O VAL A 76 N GLU A 41
SHEET 4 AA2 7 PRO A 48 MET A 52 1 N ILE A 49 O VAL A 77
SHEET 5 AA2 7 ILE A 117 GLN A 122 1 O PHE A 120 N LEU A 50
SHEET 6 AA2 7 PHE A 140 SER A 146 1 O SER A 141 N ILE A 117
SHEET 7 AA2 7 PHE A 241 THR A 243 1 O VAL A 242 N VAL A 143
LINK CE1 HIS A 22 CO CO A 407 1555 1555 2.72
LINK NE2 HIS A 22 CO CO A 407 1555 1555 2.17
LINK CD GLU A 25 CO CO A 403 1555 1555 2.75
LINK OE1 GLU A 25 CO CO A 403 1555 1555 2.44
LINK OE2 GLU A 25 CO CO A 403 1555 1555 2.39
LINK O ASP A 40 CO CO A 407 1555 1555 2.29
LINK OD1 ASP A 123 CO CO A 406 1555 1555 2.10
LINK O ASN A 180 MG MG A 404 1555 1555 2.36
LINK OD1 ASN A 180 MG MG A 404 1555 1555 2.43
LINK O THR A 183 MG MG A 404 1555 1555 2.40
LINK OG1 THR A 183 MG MG A 404 1555 1555 2.46
LINK O ARG A 185 MG MG A 404 1555 1555 2.30
LINK CG ASP A 238 CO CO A 401 1555 1555 2.46
LINK OD1 ASP A 238 CO CO A 401 1555 1555 2.14
LINK OD2 ASP A 238 CO CO A 401 1555 1555 2.19
LINK CD GLU A 256 CO CO A 405 1555 1555 2.47
LINK OE1 GLU A 256 CO CO A 405 1555 1555 2.22
LINK OE2 GLU A 256 CO CO A 405 1555 1555 2.14
LINK OD1 ASP A 293 MG MG A 408 1555 1555 2.01
LINK NE2 HIS A 303 CO CO A 401 1555 1555 2.09
LINK NE2 HIS A 304 CO CO A 402 1555 1555 2.08
LINK NE2 HIS A 305 CO CO A 401 1555 1555 2.07
LINK NE2 HIS A 306 CO CO A 402 1555 1555 2.07
LINK CO CO A 401 O HOH A 720 1555 1555 2.16
LINK CO CO A 402 O HOH A 742 1555 1555 2.19
LINK CO CO A 402 O HOH A 753 1555 1555 2.14
LINK CO CO A 402 O HOH A 775 1555 1555 2.15
LINK CO CO A 403 O HOH A 782 1555 1555 2.19
LINK CO CO A 403 O HOH A 797 1555 1555 2.36
LINK CO CO A 403 O HOH A 809 1555 1555 2.33
LINK MG MG A 404 O HOH A 613 1555 1555 2.33
LINK CO CO A 405 O HOH A 562 1555 1555 2.30
LINK CO CO A 405 O HOH A 630 1555 1555 1.98
LINK CO CO A 405 O HOH A 537 1555 1555 1.79
LINK CO CO A 406 O HOH A 803 1555 1555 2.39
LINK CO CO A 406 O HOH A 747 1555 1555 2.46
LINK CO CO A 407 O HOH A 674 1555 1555 2.33
LINK CO CO A 407 O HOH A 766 1555 1555 2.22
LINK CO CO A 407 O HOH A 768 1555 1555 1.85
LINK CO CO A 407 O HOH A 542 1555 1555 2.70
LINK MG MG A 408 O HOH A 701 1555 1555 2.35
LINK MG MG A 408 O HOH A 859 1555 1555 1.94
LINK MG MG A 408 O HOH A 737 1555 1555 1.99
LINK CD GLU A 12 CO CO A 403 1555 4555 2.72
LINK OE1 GLU A 12 CO CO A 403 1555 4555 2.36
LINK OE2 GLU A 12 CO CO A 403 1555 4555 2.41
LINK NE2 HIS A 307 CO CO A 402 1555 4565 2.12
LINK NE2 HIS A 308 CO CO A 401 1555 4565 2.06
CISPEP 1 GLU A 55 PRO A 56 0 -15.13
SITE 1 AC1 5 ASP A 238 HIS A 303 HIS A 305 HIS A 308
SITE 2 AC1 5 HOH A 720
SITE 1 AC2 6 HIS A 304 HIS A 306 HIS A 307 HOH A 742
SITE 2 AC2 6 HOH A 753 HOH A 775
SITE 1 AC3 5 GLU A 12 GLU A 25 HOH A 782 HOH A 797
SITE 2 AC3 5 HOH A 809
SITE 1 AC4 4 ASN A 180 THR A 183 ARG A 185 HOH A 613
SITE 1 AC5 5 GLU A 256 HOH A 537 HOH A 562 HOH A 630
SITE 2 AC5 5 HOH A 851
SITE 1 AC6 4 ASP A 123 CL A 409 HOH A 747 HOH A 803
SITE 1 AC7 6 HIS A 22 ASP A 40 HOH A 542 HOH A 674
SITE 2 AC7 6 HOH A 766 HOH A 768
SITE 1 AC8 5 HIS A 74 ASP A 293 HOH A 701 HOH A 737
SITE 2 AC8 5 HOH A 859
SITE 1 AC9 5 GLU A 55 TRP A 124 TRP A 163 PRO A 212
SITE 2 AC9 5 CO A 406
CRYST1 79.377 79.643 94.766 90.00 90.00 90.00 C 2 2 21 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 0.012598 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012556 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010552 0.00000
TER 4841 HIS A 308
MASTER 473 0 9 18 9 0 16 6 2859 1 57 24
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