HEADER HYDROLASE ACTIVATOR, PROTEIN BINDING 29-JUN-06 2HIB
TITLE HUMAN FORMYLGLYCINE GENERATING ENZYME, C336S MUTANT, IODIDE CO-
TITLE 2 CRYSTALLIZATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SULFATASE-MODIFYING FACTOR 1;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: RESIDUES 86-371;
COMPND 5 SYNONYM: C-ALPHA-FORMYGLYCINE- GENERATING ENZYME 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL: FIBROSARCOMA CELLS
KEYWDS HYDROLASE ACTIVATOR, PROTEIN BINDING, FORMYLGLYCINE, POST-
KEYWDS 2 TRANSLATIONAL MODIFICATION, ENDOPLASMIC RETICULUM, SULFATASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.RUDOLPH,D.ROESER
REVDAT 6 25-OCT-23 2HIB 1 REMARK
REVDAT 5 10-NOV-21 2HIB 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 2HIB 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 2HIB 1 VERSN
REVDAT 2 24-FEB-09 2HIB 1 VERSN
REVDAT 1 01-MAY-07 2HIB 0
JRNL AUTH D.ROESER,B.SCHMIDT,A.PREUSSER-KUNZE,M.G.RUDOLPH
JRNL TITL PROBING THE OXYGEN-BINDING SITE OF THE HUMAN
JRNL TITL 2 FORMYLGLYCINE-GENERATING ENZYME USING HALIDE IONS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 621 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17452787
JRNL DOI 10.1107/S0907444907009961
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 19211
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 963
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1228
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.97000
REMARK 3 B33 (A**2) : -1.02000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.185
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.181
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2333 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1591 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3189 ; 1.264 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3837 ; 0.873 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 276 ; 6.719 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 117 ;34.179 ;23.675
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 341 ;13.445 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;16.002 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 319 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2617 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 497 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 484 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1708 ; 0.210 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1131 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1107 ; 0.093 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 198 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 8 ; 0.100 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 11 ; 0.139 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 22 ; 0.141 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.185 ; 0.200
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): 1392 ; 0.694 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 554 ; 0.144 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2230 ; 1.195 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1085 ; 1.604 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 958 ; 2.535 ; 4.500
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 : BABINET MODEL WITH 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 3 THE CLOSE CONTACTS ARE PARTIAL OCCUPANCY CONTACTS,
REMARK 3 WHERE THE OCCUPANCIES OF THE CLASHING ATOMS SUM UP TO ONE.
REMARK 4
REMARK 4 2HIB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5419
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72271
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
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 (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.41300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2AIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, CALCIUM IODIDE, TRIS, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+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 30.94500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.94500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.55500
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, 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 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 X1186 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER X 163
REMARK 465 GLU X 164
REMARK 465 GLN X 165
REMARK 465 VAL X 166
REMARK 465 LYS X 167
REMARK 465 THR X 168
REMARK 465 ASN X 169
REMARK 465 ILE X 170
REMARK 465 GLN X 171
REMARK 465 GLN X 172
REMARK 465 ALA X 173
REMARK 465 VAL X 174
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 O ALA X 87 O HOH X 1121 1.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP X 105 67.05 -116.80
REMARK 500 ILE X 260 -160.35 -125.55
REMARK 500 PHE X 284 163.62 71.09
REMARK 500 ASN X 297 -100.11 66.98
REMARK 500 TYR X 340 -41.38 -137.94
REMARK 500 TYR X 344 36.40 -86.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA X1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU X 130 OE2
REMARK 620 2 ASN X 293 O 91.7
REMARK 620 3 GLY X 296 O 95.3 89.5
REMARK 620 4 ALA X 298 O 84.7 174.0 86.1
REMARK 620 5 GLU X 300 OE2 89.9 81.0 169.3 103.7
REMARK 620 6 HOH X1045 O 161.2 107.2 85.4 76.5 92.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA X1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN X 259 OD1
REMARK 620 2 ILE X 260 O 101.8
REMARK 620 3 ASP X 273 OD1 95.6 125.3
REMARK 620 4 ASP X 273 OD2 88.7 76.9 52.0
REMARK 620 5 PHE X 275 O 90.1 151.7 78.0 129.6
REMARK 620 6 HOH X1022 O 174.0 82.3 85.3 96.5 84.3
REMARK 620 7 HOH X1080 O 90.3 74.2 157.4 150.2 80.2 86.6
REMARK 620 N 1 2 3 4 5 6
DBREF 2HIB X 86 371 UNP Q8NBK3 SUMF1_HUMAN 86 371
SEQADV 2HIB SER X 336 UNP Q8NBK3 CYS 336 ENGINEERED MUTATION
SEQRES 1 X 286 LEU ALA HIS SER LYS MET VAL PRO ILE PRO ALA GLY VAL
SEQRES 2 X 286 PHE THR MET GLY THR ASP ASP PRO GLN ILE LYS GLN ASP
SEQRES 3 X 286 GLY GLU ALA PRO ALA ARG ARG VAL THR ILE ASP ALA PHE
SEQRES 4 X 286 TYR MET ASP ALA TYR GLU VAL SER ASN THR GLU PHE GLU
SEQRES 5 X 286 LYS PHE VAL ASN SER THR GLY TYR LEU THR GLU ALA GLU
SEQRES 6 X 286 LYS PHE GLY ASP SER PHE VAL PHE GLU GLY MET LEU SER
SEQRES 7 X 286 GLU GLN VAL LYS THR ASN ILE GLN GLN ALA VAL ALA ALA
SEQRES 8 X 286 ALA PRO TRP TRP LEU PRO VAL LYS GLY ALA ASN TRP ARG
SEQRES 9 X 286 HIS PRO GLU GLY PRO ASP SER THR ILE LEU HIS ARG PRO
SEQRES 10 X 286 ASP HIS PRO VAL LEU HIS VAL SER TRP ASN ASP ALA VAL
SEQRES 11 X 286 ALA TYR CYS THR TRP ALA GLY LYS ARG LEU PRO THR GLU
SEQRES 12 X 286 ALA GLU TRP GLU TYR SER CYS ARG GLY GLY LEU HIS ASN
SEQRES 13 X 286 ARG LEU PHE PRO TRP GLY ASN LYS LEU GLN PRO LYS GLY
SEQRES 14 X 286 GLN HIS TYR ALA ASN ILE TRP GLN GLY GLU PHE PRO VAL
SEQRES 15 X 286 THR ASN THR GLY GLU ASP GLY PHE GLN GLY THR ALA PRO
SEQRES 16 X 286 VAL ASP ALA PHE PRO PRO ASN GLY TYR GLY LEU TYR ASN
SEQRES 17 X 286 ILE VAL GLY ASN ALA TRP GLU TRP THR SER ASP TRP TRP
SEQRES 18 X 286 THR VAL HIS HIS SER VAL GLU GLU THR LEU ASN PRO LYS
SEQRES 19 X 286 GLY PRO PRO SER GLY LYS ASP ARG VAL LYS LYS GLY GLY
SEQRES 20 X 286 SER TYR MET SER HIS ARG SER TYR CYS TYR ARG TYR ARG
SEQRES 21 X 286 CYS ALA ALA ARG SER GLN ASN THR PRO ASP SER SER ALA
SEQRES 22 X 286 SER ASN LEU GLY PHE ARG CYS ALA ALA ASP ARG LEU PRO
MODRES 2HIB ASN X 141 ASN GLYCOSYLATION SITE
HET NAG A 1 14
HET NAG A 2 14
HET CA X1001 1
HET CA X1002 1
HET IOD X1003 1
HET IOD X1004 1
HET IOD X1005 1
HET IOD X1006 1
HET IOD X1007 1
HET IOD X1008 1
HET IOD X1009 1
HET IOD X1010 1
HET IOD X1011 1
HET IOD X1012 1
HET IOD X1013 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM IOD IODIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 CA 2(CA 2+)
FORMUL 5 IOD 11(I 1-)
FORMUL 16 HOH *258(H2 O)
HELIX 1 1 ILE X 108 GLY X 112 5 5
HELIX 2 2 SER X 132 GLY X 144 1 13
HELIX 3 3 THR X 147 GLY X 153 1 7
HELIX 4 4 GLY X 160 LEU X 162 5 3
HELIX 5 5 SER X 210 ALA X 221 1 12
HELIX 6 6 THR X 227 GLY X 237 1 11
HELIX 7 7 GLN X 251 GLN X 255 5 5
SHEET 1 A 3 MET X 91 ILE X 94 0
SHEET 2 A 3 PHE X 124 ASP X 127 -1 O PHE X 124 N ILE X 94
SHEET 3 A 3 ALA X 366 ALA X 367 -1 O ALA X 367 N TYR X 125
SHEET 1 B 3 GLY X 97 MET X 101 0
SHEET 2 B 3 ARG X 117 ILE X 121 -1 O ARG X 117 N MET X 101
SHEET 3 B 3 THR X 315 LEU X 316 1 O THR X 315 N THR X 120
SHEET 1 C 2 ASP X 154 PHE X 158 0
SHEET 2 C 2 TRP X 180 LYS X 184 -1 O VAL X 183 N SER X 155
SHEET 1 D 4 SER X 350 ASN X 352 0
SHEET 2 D 4 ARG X 327 LYS X 330 -1 N ARG X 327 O ASN X 352
SHEET 3 D 4 TRP X 299 TRP X 305 -1 N GLU X 300 O LYS X 330
SHEET 4 D 4 LEU X 361 GLY X 362 1 O GLY X 362 N TRP X 299
SSBOND 1 CYS X 218 CYS X 365 1555 1555 2.04
SSBOND 2 CYS X 235 CYS X 346 1555 1555 2.07
LINK ND2 ASN X 141 C1 NAG A 1 1555 1555 1.46
LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.44
LINK OE2 GLU X 130 CA CA X1001 1555 1555 2.37
LINK OD1 ASN X 259 CA CA X1002 1555 1555 2.34
LINK O ILE X 260 CA CA X1002 1555 1555 2.30
LINK OD1 ASP X 273 CA CA X1002 1555 1555 2.46
LINK OD2 ASP X 273 CA CA X1002 1555 1555 2.53
LINK O PHE X 275 CA CA X1002 1555 1555 2.31
LINK O ASN X 293 CA CA X1001 1555 1555 2.36
LINK O GLY X 296 CA CA X1001 1555 1555 2.44
LINK O ALA X 298 CA CA X1001 1555 1555 2.40
LINK OE2 GLU X 300 CA CA X1001 1555 1555 2.44
LINK CA CA X1001 O HOH X1045 1555 1555 2.22
LINK CA CA X1002 O HOH X1022 1555 1555 2.39
LINK CA CA X1002 O HOH X1080 1555 1555 2.46
CISPEP 1 ALA X 114 PRO X 115 0 -3.14
CISPEP 2 PHE X 265 PRO X 266 0 -1.02
CRYST1 61.890 109.110 43.492 90.00 90.00 90.00 P 21 21 2 4
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 0.016158 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009165 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022993 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
