HEADER LYASE 27-JUL-12 4GBD
TITLE CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE FROM PSEUDOMONAS AERUGINOSA
TITLE 2 PAO1 WITH BOUND ZN AND METHYLTHIO-COFORMYCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: PA3170;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-CODONPLUS-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PJEXPRESS414
KEYWDS DEAMINASE, METHYLTIHOADENOSINE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HO,R.GUAN,S.C.ALMO,V.L.SCHRAMM
REVDAT 3 28-FEB-24 4GBD 1 REMARK SEQADV LINK
REVDAT 2 15-NOV-17 4GBD 1 REMARK
REVDAT 1 12-JUN-13 4GBD 0
JRNL AUTH R.GUAN,M.C.HO,R.F.FROHLICH,P.C.TYLER,S.C.ALMO,V.L.SCHRAMM
JRNL TITL METHYLTHIOADENOSINE DEAMINASE IN AN ALTERNATIVE QUORUM
JRNL TITL 2 SENSING PATHWAY IN PSEUDOMONAS AERUGINOSA.
JRNL REF BIOCHEMISTRY V. 51 9094 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 23050701
JRNL DOI 10.1021/BI301062Y
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 70236
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 + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3543
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4078
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 226
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6668
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 243
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : -0.18000
REMARK 3 B33 (A**2) : 0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.07000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.489
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6895 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9393 ; 1.655 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 881 ; 5.746 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 315 ;33.921 ;23.524
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1106 ;14.854 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;17.286 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1065 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5284 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4GBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000073972.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.975
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 11.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.65600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.26M SODIUM PHOSPHATE
REMARK 280 (MONOBASIC)/0.14M POTASSIUM PHOSPHATE (DIBASIC), PH 5.6, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Z
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 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 59.90700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.15500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.90700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 60.15500
REMARK 290 SMTRY3 4 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: 5290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 4
REMARK 465 ARG A 5
REMARK 465 SER A 441
REMARK 465 ASP A 442
REMARK 465 ARG A 443
REMARK 465 SER A 444
REMARK 465 MET B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ASN B 3
REMARK 465 VAL B 4
REMARK 465 ARG B 5
REMARK 465 ASN B 6
REMARK 465 SER B 441
REMARK 465 ASP B 442
REMARK 465 ARG B 443
REMARK 465 SER B 444
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 TRP A 92 CE2 TRP A 92 CD2 0.079
REMARK 500 HIS A 223 CG HIS A 223 CD2 0.060
REMARK 500 HIS A 279 CG HIS A 279 CD2 0.058
REMARK 500 HIS B 74 CG HIS B 74 CD2 0.060
REMARK 500 HIS B 223 CG HIS B 223 CD2 0.067
REMARK 500 TRP B 407 CE2 TRP B 407 CD2 0.074
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 MET A 233 CG - SD - CE ANGL. DEV. = 9.7 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 LEU A 13 75.18 -119.85
REMARK 500 VAL A 20 -43.30 77.60
REMARK 500 HIS A 96 -65.51 -134.81
REMARK 500 HIS A 258 -76.87 94.93
REMARK 500 ASP A 309 -164.40 69.13
REMARK 500 ASN A 314 -65.53 -141.20
REMARK 500 LEU A 317 48.40 -109.06
REMARK 500 LEU A 340 63.44 35.93
REMARK 500 THR A 350 -90.53 -128.18
REMARK 500 ALA A 397 17.62 -149.10
REMARK 500 VAL B 20 -44.01 77.48
REMARK 500 HIS B 96 -60.17 -135.94
REMARK 500 HIS B 258 -81.58 95.87
REMARK 500 ASP B 309 -163.37 65.92
REMARK 500 ASN B 314 -67.23 -136.43
REMARK 500 LEU B 317 47.77 -107.79
REMARK 500 LEU B 340 68.45 34.23
REMARK 500 THR B 350 -90.70 -127.25
REMARK 500 ALA B 397 19.19 -143.63
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 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 72 NE2
REMARK 620 2 HIS A 74 NE2 101.5
REMARK 620 3 HIS A 221 NE2 89.5 100.6
REMARK 620 4 ASP A 309 OD1 87.0 95.2 164.2
REMARK 620 5 MCF A 501 O8 126.8 131.2 87.4 82.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 282 OE1
REMARK 620 2 ASN A 314 OD1 86.4
REMARK 620 3 ASP A 316 OD1 174.2 88.0
REMARK 620 4 HOH A 724 O 83.6 79.2 93.7
REMARK 620 5 HOH A 725 O 91.2 173.5 94.5 106.5
REMARK 620 6 HOH A 726 O 100.2 94.9 82.0 172.9 79.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 72 NE2
REMARK 620 2 HIS B 74 NE2 98.6
REMARK 620 3 HIS B 221 NE2 94.1 105.6
REMARK 620 4 ASP B 309 OD1 83.7 88.8 165.5
REMARK 620 5 MCF B 501 O8 130.6 129.2 84.9 85.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 282 OE1
REMARK 620 2 ASN B 314 OD1 86.8
REMARK 620 3 ASP B 316 OD1 172.3 86.3
REMARK 620 4 HOH B 714 O 80.6 78.7 94.8
REMARK 620 5 HOH B 715 O 93.8 178.5 93.3 102.8
REMARK 620 6 HOH B 716 O 102.6 97.3 81.6 174.8 81.2
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 MCF A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MCF B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 504
DBREF 4GBD A 1 444 UNP Q9HZ64 Q9HZ64_PSEAE 1 444
DBREF 4GBD B 1 444 UNP Q9HZ64 Q9HZ64_PSEAE 1 444
SEQADV 4GBD MET A -13 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS A -12 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS A -11 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS A -10 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS A -9 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS A -8 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS A -7 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD GLU A -6 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD ASN A -5 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD LEU A -4 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD TYR A -3 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD PHE A -2 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD GLN A -1 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD GLY A 0 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD MET B -13 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS B -12 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS B -11 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS B -10 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS B -9 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS B -8 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD HIS B -7 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD GLU B -6 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD ASN B -5 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD LEU B -4 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD TYR B -3 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD PHE B -2 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD GLN B -1 UNP Q9HZ64 EXPRESSION TAG
SEQADV 4GBD GLY B 0 UNP Q9HZ64 EXPRESSION TAG
SEQRES 1 A 458 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 A 458 GLY MET PRO ASN VAL ARG ASN PRO PHE ASP LEU LEU LEU
SEQRES 3 A 458 LEU PRO THR TRP ILE VAL PRO VAL GLU PRO ALA GLY VAL
SEQRES 4 A 458 VAL LEU ARG ASP HIS ALA LEU GLY ILE ARG ASP GLY GLN
SEQRES 5 A 458 ILE ALA LEU VAL ALA PRO ARG GLU GLN ALA MET ARG HIS
SEQRES 6 A 458 GLY ALA THR GLU ILE ARG GLU LEU PRO GLY MET LEU LEU
SEQRES 7 A 458 ALA PRO GLY LEU VAL ASN ALA HIS GLY HIS SER ALA MET
SEQRES 8 A 458 SER LEU PHE ARG GLY LEU ALA ASP ASP LEU PRO LEU MET
SEQRES 9 A 458 THR TRP LEU GLN ASP HIS ILE TRP PRO ALA GLU GLY GLN
SEQRES 10 A 458 TRP VAL SER GLU ASP PHE ILE ARG ASP GLY THR GLU LEU
SEQRES 11 A 458 ALA ILE ALA GLU GLN VAL LYS GLY GLY ILE THR CYS PHE
SEQRES 12 A 458 SER ASP MET TYR PHE TYR PRO GLN ALA ILE CYS GLY VAL
SEQRES 13 A 458 VAL HIS ASP SER GLY VAL ARG ALA GLN VAL ALA ILE PRO
SEQRES 14 A 458 VAL LEU ASP PHE PRO ILE PRO GLY ALA ARG ASP SER ALA
SEQRES 15 A 458 GLU ALA ILE ARG GLN GLY MET ALA LEU PHE ASP ASP LEU
SEQRES 16 A 458 LYS HIS HIS PRO ARG ILE ARG ILE ALA PHE GLY PRO HIS
SEQRES 17 A 458 ALA PRO TYR THR VAL SER ASP ASP LYS LEU GLU GLN ILE
SEQRES 18 A 458 LEU VAL LEU THR GLU GLU LEU ASP ALA SER ILE GLN MET
SEQRES 19 A 458 HIS VAL HIS GLU THR ALA PHE GLU VAL GLU GLN ALA MET
SEQRES 20 A 458 GLU ARG ASN GLY GLU ARG PRO LEU ALA ARG LEU HIS ARG
SEQRES 21 A 458 LEU GLY LEU LEU GLY PRO ARG PHE GLN ALA VAL HIS MET
SEQRES 22 A 458 THR GLN VAL ASP ASN ASP ASP LEU ALA MET LEU VAL GLU
SEQRES 23 A 458 THR ASN SER SER VAL ILE HIS CYS PRO GLU SER ASN LEU
SEQRES 24 A 458 LYS LEU ALA SER GLY PHE CYS PRO VAL GLU LYS LEU TRP
SEQRES 25 A 458 GLN ALA GLY VAL ASN VAL ALA ILE GLY THR ASP GLY ALA
SEQRES 26 A 458 ALA SER ASN ASN ASP LEU ASP LEU LEU GLY GLU THR ARG
SEQRES 27 A 458 THR ALA ALA LEU LEU ALA LYS ALA VAL TYR GLY GLN ALA
SEQRES 28 A 458 THR ALA LEU ASP ALA HIS ARG ALA LEU ARG MET ALA THR
SEQRES 29 A 458 LEU ASN GLY ALA ARG ALA LEU GLY LEU GLU ARG LEU ILE
SEQRES 30 A 458 GLY SER LEU GLU ALA GLY LYS ALA ALA ASP LEU VAL ALA
SEQRES 31 A 458 PHE ASP LEU SER GLY LEU ALA GLN GLN PRO VAL TYR ASP
SEQRES 32 A 458 PRO VAL SER GLN LEU ILE TYR ALA SER GLY ARG ASP CYS
SEQRES 33 A 458 VAL ARG HIS VAL TRP VAL GLY GLY ARG GLN LEU LEU ASP
SEQRES 34 A 458 ASP GLY ARG LEU LEU ARG HIS ASP GLU GLN ARG LEU ILE
SEQRES 35 A 458 ALA ARG ALA ARG GLU TRP GLY ALA LYS ILE ALA ALA SER
SEQRES 36 A 458 ASP ARG SER
SEQRES 1 B 458 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 B 458 GLY MET PRO ASN VAL ARG ASN PRO PHE ASP LEU LEU LEU
SEQRES 3 B 458 LEU PRO THR TRP ILE VAL PRO VAL GLU PRO ALA GLY VAL
SEQRES 4 B 458 VAL LEU ARG ASP HIS ALA LEU GLY ILE ARG ASP GLY GLN
SEQRES 5 B 458 ILE ALA LEU VAL ALA PRO ARG GLU GLN ALA MET ARG HIS
SEQRES 6 B 458 GLY ALA THR GLU ILE ARG GLU LEU PRO GLY MET LEU LEU
SEQRES 7 B 458 ALA PRO GLY LEU VAL ASN ALA HIS GLY HIS SER ALA MET
SEQRES 8 B 458 SER LEU PHE ARG GLY LEU ALA ASP ASP LEU PRO LEU MET
SEQRES 9 B 458 THR TRP LEU GLN ASP HIS ILE TRP PRO ALA GLU GLY GLN
SEQRES 10 B 458 TRP VAL SER GLU ASP PHE ILE ARG ASP GLY THR GLU LEU
SEQRES 11 B 458 ALA ILE ALA GLU GLN VAL LYS GLY GLY ILE THR CYS PHE
SEQRES 12 B 458 SER ASP MET TYR PHE TYR PRO GLN ALA ILE CYS GLY VAL
SEQRES 13 B 458 VAL HIS ASP SER GLY VAL ARG ALA GLN VAL ALA ILE PRO
SEQRES 14 B 458 VAL LEU ASP PHE PRO ILE PRO GLY ALA ARG ASP SER ALA
SEQRES 15 B 458 GLU ALA ILE ARG GLN GLY MET ALA LEU PHE ASP ASP LEU
SEQRES 16 B 458 LYS HIS HIS PRO ARG ILE ARG ILE ALA PHE GLY PRO HIS
SEQRES 17 B 458 ALA PRO TYR THR VAL SER ASP ASP LYS LEU GLU GLN ILE
SEQRES 18 B 458 LEU VAL LEU THR GLU GLU LEU ASP ALA SER ILE GLN MET
SEQRES 19 B 458 HIS VAL HIS GLU THR ALA PHE GLU VAL GLU GLN ALA MET
SEQRES 20 B 458 GLU ARG ASN GLY GLU ARG PRO LEU ALA ARG LEU HIS ARG
SEQRES 21 B 458 LEU GLY LEU LEU GLY PRO ARG PHE GLN ALA VAL HIS MET
SEQRES 22 B 458 THR GLN VAL ASP ASN ASP ASP LEU ALA MET LEU VAL GLU
SEQRES 23 B 458 THR ASN SER SER VAL ILE HIS CYS PRO GLU SER ASN LEU
SEQRES 24 B 458 LYS LEU ALA SER GLY PHE CYS PRO VAL GLU LYS LEU TRP
SEQRES 25 B 458 GLN ALA GLY VAL ASN VAL ALA ILE GLY THR ASP GLY ALA
SEQRES 26 B 458 ALA SER ASN ASN ASP LEU ASP LEU LEU GLY GLU THR ARG
SEQRES 27 B 458 THR ALA ALA LEU LEU ALA LYS ALA VAL TYR GLY GLN ALA
SEQRES 28 B 458 THR ALA LEU ASP ALA HIS ARG ALA LEU ARG MET ALA THR
SEQRES 29 B 458 LEU ASN GLY ALA ARG ALA LEU GLY LEU GLU ARG LEU ILE
SEQRES 30 B 458 GLY SER LEU GLU ALA GLY LYS ALA ALA ASP LEU VAL ALA
SEQRES 31 B 458 PHE ASP LEU SER GLY LEU ALA GLN GLN PRO VAL TYR ASP
SEQRES 32 B 458 PRO VAL SER GLN LEU ILE TYR ALA SER GLY ARG ASP CYS
SEQRES 33 B 458 VAL ARG HIS VAL TRP VAL GLY GLY ARG GLN LEU LEU ASP
SEQRES 34 B 458 ASP GLY ARG LEU LEU ARG HIS ASP GLU GLN ARG LEU ILE
SEQRES 35 B 458 ALA ARG ALA ARG GLU TRP GLY ALA LYS ILE ALA ALA SER
SEQRES 36 B 458 ASP ARG SER
HET MCF A 501 21
HET ZN A 502 1
HET ZN A 503 1
HET PO4 A 504 5
HET MCF B 501 21
HET ZN B 502 1
HET ZN B 503 1
HET PO4 B 504 5
HETNAM MCF (8R)-3-(5-S-METHYL-5-THIO-BETA-D-RIBOFURANOSYL)-3,6,7,
HETNAM 2 MCF 8-TETRAHYDROIMIDAZO[4,5-D][1,3]DIAZEPIN-8-OL
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
FORMUL 3 MCF 2(C12 H18 N4 O4 S)
FORMUL 4 ZN 4(ZN 2+)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 11 HOH *243(H2 O)
HELIX 1 1 ARG A 45 GLY A 52 1 8
HELIX 2 2 HIS A 74 ARG A 81 5 8
HELIX 3 3 PRO A 88 HIS A 96 1 9
HELIX 4 4 HIS A 96 VAL A 105 1 10
HELIX 5 5 SER A 106 GLY A 124 1 19
HELIX 6 6 TYR A 135 GLY A 147 1 13
HELIX 7 7 ASP A 166 LEU A 181 1 16
HELIX 8 8 ALA A 195 VAL A 199 5 5
HELIX 9 9 SER A 200 ASP A 215 1 16
HELIX 10 10 THR A 225 GLY A 237 1 13
HELIX 11 11 ARG A 239 GLY A 248 1 10
HELIX 12 12 ASP A 263 ASN A 274 1 12
HELIX 13 13 CYS A 280 LEU A 287 1 8
HELIX 14 14 PRO A 293 ALA A 300 1 8
HELIX 15 15 ASP A 318 GLY A 335 1 18
HELIX 16 16 ASP A 341 THR A 350 1 10
HELIX 17 17 THR A 350 GLY A 358 1 9
HELIX 18 18 GLY A 381 GLN A 385 5 5
HELIX 19 19 ASP A 389 SER A 398 1 10
HELIX 20 20 GLY A 399 ASP A 401 5 3
HELIX 21 21 ASP A 423 ALA A 440 1 18
HELIX 22 22 ARG B 45 GLY B 52 1 8
HELIX 23 23 HIS B 74 ARG B 81 5 8
HELIX 24 24 PRO B 88 HIS B 96 1 9
HELIX 25 25 HIS B 96 VAL B 105 1 10
HELIX 26 26 SER B 106 GLY B 124 1 19
HELIX 27 27 TYR B 135 GLY B 147 1 13
HELIX 28 28 ASP B 166 LYS B 182 1 17
HELIX 29 29 ALA B 195 VAL B 199 5 5
HELIX 30 30 SER B 200 ASP B 215 1 16
HELIX 31 31 THR B 225 GLY B 237 1 13
HELIX 32 32 ARG B 239 LEU B 247 1 9
HELIX 33 33 ASP B 263 ASN B 274 1 12
HELIX 34 34 CYS B 280 LEU B 287 1 8
HELIX 35 35 PRO B 293 ALA B 300 1 8
HELIX 36 36 ASP B 318 GLY B 335 1 18
HELIX 37 37 ASP B 341 THR B 350 1 10
HELIX 38 38 THR B 350 LEU B 357 1 8
HELIX 39 39 GLY B 381 GLN B 385 5 5
HELIX 40 40 ASP B 389 SER B 398 1 10
HELIX 41 41 GLY B 399 ASP B 401 5 3
HELIX 42 42 ASP B 423 ALA B 440 1 18
SHEET 1 A 4 LEU A 27 ARG A 28 0
SHEET 2 A 4 PHE A 8 ILE A 17 -1 N ILE A 17 O LEU A 27
SHEET 3 A 4 HIS A 30 ARG A 35 -1 O ILE A 34 N LEU A 10
SHEET 4 A 4 GLN A 38 PRO A 44 -1 O GLN A 38 N ARG A 35
SHEET 1 B 7 LEU A 27 ARG A 28 0
SHEET 2 B 7 PHE A 8 ILE A 17 -1 N ILE A 17 O LEU A 27
SHEET 3 B 7 ALA A 53 PRO A 66 1 O ARG A 57 N LEU A 11
SHEET 4 B 7 LEU A 374 ASP A 378 -1 O PHE A 377 N LEU A 63
SHEET 5 B 7 VAL A 403 VAL A 408 -1 O ARG A 404 N ALA A 376
SHEET 6 B 7 ARG A 411 ASP A 415 -1 O LEU A 413 N VAL A 406
SHEET 7 B 7 ARG A 418 LEU A 419 -1 O ARG A 418 N ASP A 415
SHEET 1 C 4 LEU A 68 GLY A 73 0
SHEET 2 C 4 ILE A 126 MET A 132 1 O SER A 130 N ASN A 70
SHEET 3 C 4 ARG A 149 VAL A 156 1 O ALA A 153 N ASP A 131
SHEET 4 C 4 ILE A 187 PRO A 193 1 O GLY A 192 N ILE A 154
SHEET 1 D 4 ILE A 218 VAL A 222 0
SHEET 2 D 4 PHE A 254 HIS A 258 1 O VAL A 257 N MET A 220
SHEET 3 D 4 SER A 276 HIS A 279 1 O SER A 276 N ALA A 256
SHEET 4 D 4 ASN A 303 ILE A 306 1 O ALA A 305 N VAL A 277
SHEET 1 E 4 LEU B 27 ARG B 28 0
SHEET 2 E 4 PHE B 8 ILE B 17 -1 N ILE B 17 O LEU B 27
SHEET 3 E 4 HIS B 30 ARG B 35 -1 O ILE B 34 N LEU B 10
SHEET 4 E 4 GLN B 38 PRO B 44 -1 O LEU B 41 N GLY B 33
SHEET 1 F 7 LEU B 27 ARG B 28 0
SHEET 2 F 7 PHE B 8 ILE B 17 -1 N ILE B 17 O LEU B 27
SHEET 3 F 7 ALA B 53 PRO B 66 1 O LEU B 59 N LEU B 13
SHEET 4 F 7 LEU B 374 ASP B 378 -1 O PHE B 377 N LEU B 63
SHEET 5 F 7 VAL B 403 VAL B 408 -1 O TRP B 407 N LEU B 374
SHEET 6 F 7 ARG B 411 ASP B 415 -1 O ARG B 411 N VAL B 408
SHEET 7 F 7 ARG B 418 LEU B 419 -1 O ARG B 418 N ASP B 415
SHEET 1 G 4 LEU B 68 ASN B 70 0
SHEET 2 G 4 ILE B 126 MET B 132 1 O CYS B 128 N ASN B 70
SHEET 3 G 4 ARG B 149 VAL B 156 1 O ALA B 153 N ASP B 131
SHEET 4 G 4 ILE B 187 PRO B 193 1 O GLY B 192 N ILE B 154
SHEET 1 H 4 ILE B 218 VAL B 222 0
SHEET 2 H 4 PHE B 254 HIS B 258 1 O GLN B 255 N ILE B 218
SHEET 3 H 4 SER B 276 HIS B 279 1 O SER B 276 N ALA B 256
SHEET 4 H 4 ASN B 303 ILE B 306 1 O ALA B 305 N HIS B 279
LINK NE2 HIS A 72 ZN ZN A 502 1555 1555 1.82
LINK NE2 HIS A 74 ZN ZN A 502 1555 1555 2.08
LINK NE2 HIS A 221 ZN ZN A 502 1555 1555 2.13
LINK OE1 GLU A 282 ZN ZN A 503 1555 1555 2.12
LINK OD1 ASP A 309 ZN ZN A 502 1555 1555 2.27
LINK OD1 ASN A 314 ZN ZN A 503 1555 1555 2.26
LINK OD1 ASP A 316 ZN ZN A 503 1555 1555 2.20
LINK O8 MCF A 501 ZN ZN A 502 1555 1555 2.24
LINK ZN ZN A 503 O HOH A 724 1555 1555 2.01
LINK ZN ZN A 503 O HOH A 725 1555 1555 2.32
LINK ZN ZN A 503 O HOH A 726 1555 1555 1.99
LINK NE2 HIS B 72 ZN ZN B 502 1555 1555 2.12
LINK NE2 HIS B 74 ZN ZN B 502 1555 1555 2.06
LINK NE2 HIS B 221 ZN ZN B 502 1555 1555 2.23
LINK OE1 GLU B 282 ZN ZN B 503 1555 1555 2.08
LINK OD1 ASP B 309 ZN ZN B 502 1555 1555 2.27
LINK OD1 ASN B 314 ZN ZN B 503 1555 1555 2.15
LINK OD1 ASP B 316 ZN ZN B 503 1555 1555 2.16
LINK O8 MCF B 501 ZN ZN B 502 1555 1555 2.28
LINK ZN ZN B 503 O HOH B 714 1555 1555 2.31
LINK ZN ZN B 503 O HOH B 715 1555 1555 2.26
LINK ZN ZN B 503 O HOH B 716 1555 1555 2.27
CISPEP 1 GLU A 21 PRO A 22 0 -5.95
CISPEP 2 ASN A 314 ASN A 315 0 8.26
CISPEP 3 GLN A 385 PRO A 386 0 -10.22
CISPEP 4 GLU B 21 PRO B 22 0 -1.68
CISPEP 5 ASN B 314 ASN B 315 0 10.51
CISPEP 6 GLN B 385 PRO B 386 0 -7.32
SITE 1 AC1 18 HIS A 72 HIS A 74 MET A 77 LEU A 89
SITE 2 AC1 18 TRP A 92 ILE A 97 TRP A 98 GLU A 101
SITE 3 AC1 18 MET A 132 PHE A 134 GLY A 192 HIS A 194
SITE 4 AC1 18 HIS A 221 GLU A 224 HIS A 258 ASP A 309
SITE 5 AC1 18 ZN A 502 HOH A 614
SITE 1 AC2 5 HIS A 72 HIS A 74 HIS A 221 ASP A 309
SITE 2 AC2 5 MCF A 501
SITE 1 AC3 6 GLU A 282 ASN A 314 ASP A 316 HOH A 724
SITE 2 AC3 6 HOH A 725 HOH A 726
SITE 1 AC4 5 GLN A 384 GLY A 399 ASP A 401 CYS A 402
SITE 2 AC4 5 ARG B 400
SITE 1 AC5 16 HIS B 74 MET B 77 LEU B 89 TRP B 92
SITE 2 AC5 16 ILE B 97 TRP B 98 GLU B 101 MET B 132
SITE 3 AC5 16 PHE B 134 HIS B 194 HIS B 221 GLU B 224
SITE 4 AC5 16 HIS B 258 ASP B 309 ZN B 502 HOH B 610
SITE 1 AC6 5 HIS B 72 HIS B 74 HIS B 221 ASP B 309
SITE 2 AC6 5 MCF B 501
SITE 1 AC7 6 GLU B 282 ASN B 314 ASP B 316 HOH B 714
SITE 2 AC7 6 HOH B 715 HOH B 716
SITE 1 AC8 7 ARG A 400 HOH A 727 GLN B 384 GLY B 399
SITE 2 AC8 7 ASP B 401 CYS B 402 HOH B 711
CRYST1 119.814 120.310 77.298 90.00 108.00 90.00 C 1 2 1 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 0.008346 0.000000 0.002711 0.00000
SCALE2 0.000000 0.008312 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
