HEADER HYDROLASE,TRANSFERASE 10-APR-15 4Z9O
TITLE CRYSTAL STRUCTURE OF HUMAN GGT1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LARGE SUBUNIT (UNP RESIDUES 28-380);
COMPND 5 SYNONYM: GGT 1,GAMMA-GLUTAMYLTRANSFERASE 1,GLUTATHIONE HYDROLASE 1,
COMPND 6 LEUKOTRIENE-C4 HYDROLASE;
COMPND 7 EC: 2.3.2.2,3.4.19.13,3.4.19.14;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE 1;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: SMALL SUBUNIT (UNP RESIDUES 381-569);
COMPND 13 SYNONYM: GGT 1,GAMMA-GLUTAMYLTRANSFERASE 1,GLUTATHIONE HYDROLASE 1,
COMPND 14 LEUKOTRIENE-C4 HYDROLASE;
COMPND 15 EC: 2.3.2.2,3.4.19.13,3.4.19.14;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GGT1, GGT;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4919;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X-33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZAA;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: GGT1, GGT;
SOURCE 16 EXPRESSION_SYSTEM: PICHIA;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 4919;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: X-33;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAZMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PPICZAA
KEYWDS NTN-HYDROLASE FAMILY, GLYCOPROTEIN, N- GLYCOSYLATION, CELL SURFACE,
KEYWDS 2 HYDROLASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.S.TERZYAN,M.H.HANIGAN
REVDAT 6 29-JUL-20 4Z9O 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE
REVDAT 5 25-DEC-19 4Z9O 1 REMARK
REVDAT 4 27-SEP-17 4Z9O 1 SOURCE JRNL REMARK
REVDAT 3 22-JUL-15 4Z9O 1 JRNL
REVDAT 2 10-JUN-15 4Z9O 1 JRNL
REVDAT 1 03-JUN-15 4Z9O 0
JRNL AUTH S.S.TERZYAN,A.W.BURGETT,A.HEROUX,C.A.SMITH,B.H.MOOERS,
JRNL AUTH 2 M.H.HANIGAN
JRNL TITL HUMAN GAMMA-GLUTAMYL TRANSPEPTIDASE 1: STRUCTURES OF THE
JRNL TITL 2 FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES,
JRNL TITL 3 AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE
JRNL TITL 4 ACTIVE SITE DURING CATALYSIS.
JRNL REF J.BIOL.CHEM. V. 290 17576 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 26013825
JRNL DOI 10.1074/JBC.M115.659680
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.B.WEST,Y.CHEN,S.WICKHAM,A.HEROUX,K.CAHILL,M.H.HANIGAN,
REMARK 1 AUTH 2 B.H.MOOERS
REMARK 1 TITL NOVEL INSIGHTS INTO EUKARYOTIC GAMMA-GLUTAMYLTRANSPEPTIDASE
REMARK 1 TITL 2 1 FROM THE CRYSTAL STRUCTURE OF THE GLUTAMATE-BOUND HUMAN
REMARK 1 TITL 3 ENZYME.
REMARK 1 REF J.BIOL.CHEM. V. 288 31902 2013
REMARK 1 REFN ESSN 1083-351X
REMARK 1 PMID 24047895
REMARK 1 DOI 10.1074/JBC.M113.498139
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 27405
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1461
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1289
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 59.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 371
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : 0.02000
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): 0.258
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.718
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4294 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5845 ; 1.448 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 542 ; 6.060 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;37.145 ;23.495
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 675 ;14.594 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;18.432 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 674 ; 0.240 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3259 ; 0.006 ; 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): 2141 ; 2.308 ; 3.701
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2677 ; 3.561 ; 5.539
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2151 ; 3.651 ; 4.246
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: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4Z9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208772.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28718
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
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: REFMAC 5.8.0073
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, NH4CL, PH 6.3, VAPOR
REMARK 280 DIFFUSION, HANGING 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 51.99400
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 51.99400
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 52.79150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.64400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 52.79150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.64400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 51.99400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 52.79150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 62.64400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 51.99400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 52.79150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 62.64400
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: 12120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 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 858 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 907 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 A 28
REMARK 465 ALA A 29
REMARK 465 SER A 30
REMARK 465 LYS A 31
REMARK 465 GLU A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 376
REMARK 465 ASP A 377
REMARK 465 ASP A 378
REMARK 465 GLY A 379
REMARK 465 GLY A 380
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 HOH A 889 O HOH A 911 1.94
REMARK 500 ND2 ASN A 95 C2 NAG A 601 2.16
REMARK 500 ND2 ASN A 230 C2 NAG A 605 2.17
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 OD1 ASN A 35 OD1 ASN A 35 3554 2.18
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 ASN A 230 52.58 -161.31
REMARK 500 ASN B 401 -111.36 79.52
REMARK 500 PHE B 404 19.18 59.09
REMARK 500 ASN B 419 50.16 -116.50
REMARK 500 CYS B 454 57.78 -154.06
REMARK 500 CYS B 454 66.26 -158.38
REMARK 500 LEU B 508 -60.96 80.65
REMARK 500 THR B 539 -92.89 -112.24
REMARK 500 ALA B 542 177.57 64.14
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 929 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 930 DISTANCE = 5.92 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 NA B1104 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 882 O
REMARK 620 2 ALA B 556 O 130.2
REMARK 620 3 HOH B1251 O 125.1 104.4
REMARK 620 N 1 2
DBREF 4Z9O A 28 380 UNP P19440 GGT1_HUMAN 28 380
DBREF 4Z9O B 381 569 UNP P19440 GGT1_HUMAN 381 569
SEQADV 4Z9O ALA A 272 UNP P19440 VAL 272 VARIANT
SEQRES 1 A 353 SER ALA SER LYS GLU PRO ASP ASN HIS VAL TYR THR ARG
SEQRES 2 A 353 ALA ALA VAL ALA ALA ASP ALA LYS GLN CYS SER LYS ILE
SEQRES 3 A 353 GLY ARG ASP ALA LEU ARG ASP GLY GLY SER ALA VAL ASP
SEQRES 4 A 353 ALA ALA ILE ALA ALA LEU LEU CYS VAL GLY LEU MET ASN
SEQRES 5 A 353 ALA HIS SER MET GLY ILE GLY GLY GLY LEU PHE LEU THR
SEQRES 6 A 353 ILE TYR ASN SER THR THR ARG LYS ALA GLU VAL ILE ASN
SEQRES 7 A 353 ALA ARG GLU VAL ALA PRO ARG LEU ALA PHE ALA THR MET
SEQRES 8 A 353 PHE ASN SER SER GLU GLN SER GLN LYS GLY GLY LEU SER
SEQRES 9 A 353 VAL ALA VAL PRO GLY GLU ILE ARG GLY TYR GLU LEU ALA
SEQRES 10 A 353 HIS GLN ARG HIS GLY ARG LEU PRO TRP ALA ARG LEU PHE
SEQRES 11 A 353 GLN PRO SER ILE GLN LEU ALA ARG GLN GLY PHE PRO VAL
SEQRES 12 A 353 GLY LYS GLY LEU ALA ALA ALA LEU GLU ASN LYS ARG THR
SEQRES 13 A 353 VAL ILE GLU GLN GLN PRO VAL LEU CYS GLU VAL PHE CYS
SEQRES 14 A 353 ARG ASP ARG LYS VAL LEU ARG GLU GLY GLU ARG LEU THR
SEQRES 15 A 353 LEU PRO GLN LEU ALA ASP THR TYR GLU THR LEU ALA ILE
SEQRES 16 A 353 GLU GLY ALA GLN ALA PHE TYR ASN GLY SER LEU THR ALA
SEQRES 17 A 353 GLN ILE VAL LYS ASP ILE GLN ALA ALA GLY GLY ILE VAL
SEQRES 18 A 353 THR ALA GLU ASP LEU ASN ASN TYR ARG ALA GLU LEU ILE
SEQRES 19 A 353 GLU HIS PRO LEU ASN ILE SER LEU GLY ASP ALA VAL LEU
SEQRES 20 A 353 TYR MET PRO SER ALA PRO LEU SER GLY PRO VAL LEU ALA
SEQRES 21 A 353 LEU ILE LEU ASN ILE LEU LYS GLY TYR ASN PHE SER ARG
SEQRES 22 A 353 GLU SER VAL GLU SER PRO GLU GLN LYS GLY LEU THR TYR
SEQRES 23 A 353 HIS ARG ILE VAL GLU ALA PHE ARG PHE ALA TYR ALA LYS
SEQRES 24 A 353 ARG THR LEU LEU GLY ASP PRO LYS PHE VAL ASP VAL THR
SEQRES 25 A 353 GLU VAL VAL ARG ASN MET THR SER GLU PHE PHE ALA ALA
SEQRES 26 A 353 GLN LEU ARG ALA GLN ILE SER ASP ASP THR THR HIS PRO
SEQRES 27 A 353 ILE SER TYR TYR LYS PRO GLU PHE TYR THR PRO ASP ASP
SEQRES 28 A 353 GLY GLY
SEQRES 1 B 189 THR ALA HIS LEU SER VAL VAL ALA GLU ASP GLY SER ALA
SEQRES 2 B 189 VAL SER ALA THR SER THR ILE ASN LEU TYR PHE GLY SER
SEQRES 3 B 189 LYS VAL ARG SER PRO VAL SER GLY ILE LEU PHE ASN ASN
SEQRES 4 B 189 GLU MET ASP ASP PHE SER SER PRO SER ILE THR ASN GLU
SEQRES 5 B 189 PHE GLY VAL PRO PRO SER PRO ALA ASN PHE ILE GLN PRO
SEQRES 6 B 189 GLY LYS GLN PRO LEU SER SER MET CYS PRO THR ILE MET
SEQRES 7 B 189 VAL GLY GLN ASP GLY GLN VAL ARG MET VAL VAL GLY ALA
SEQRES 8 B 189 ALA GLY GLY THR GLN ILE THR THR ALA THR ALA LEU ALA
SEQRES 9 B 189 ILE ILE TYR ASN LEU TRP PHE GLY TYR ASP VAL LYS ARG
SEQRES 10 B 189 ALA VAL GLU GLU PRO ARG LEU HIS ASN GLN LEU LEU PRO
SEQRES 11 B 189 ASN VAL THR THR VAL GLU ARG ASN ILE ASP GLN ALA VAL
SEQRES 12 B 189 THR ALA ALA LEU GLU THR ARG HIS HIS HIS THR GLN ILE
SEQRES 13 B 189 ALA SER THR PHE ILE ALA VAL VAL GLN ALA ILE VAL ARG
SEQRES 14 B 189 THR ALA GLY GLY TRP ALA ALA ALA SER ASP SER ARG LYS
SEQRES 15 B 189 GLY GLY GLU PRO ALA GLY TYR
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET MES A 606 12
HET CL A 607 1
HET NAG B1101 14
HET MES B1102 12
HET CL B1103 1
HET NA B1104 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 8 MES 2(C6 H13 N O4 S)
FORMUL 9 CL 2(CL 1-)
FORMUL 13 NA NA 1+
FORMUL 14 HOH *371(H2 O)
HELIX 1 AA1 ALA A 47 ASP A 60 1 14
HELIX 2 AA2 SER A 63 ASN A 79 1 17
HELIX 3 AA3 SER A 121 LYS A 127 1 7
HELIX 4 AA4 GLY A 128 VAL A 132 5 5
HELIX 5 AA5 GLY A 136 GLY A 149 1 14
HELIX 6 AA6 PRO A 152 GLY A 167 1 16
HELIX 7 AA7 GLY A 171 LYS A 181 1 11
HELIX 8 AA8 LYS A 181 GLN A 188 1 8
HELIX 9 AA9 GLN A 188 PHE A 195 1 8
HELIX 10 AB1 LEU A 210 GLY A 224 1 15
HELIX 11 AB2 ALA A 225 ASN A 230 1 6
HELIX 12 AB3 LEU A 233 ALA A 244 1 12
HELIX 13 AB4 THR A 249 TYR A 256 1 8
HELIX 14 AB5 SER A 282 GLY A 295 1 14
HELIX 15 AB6 SER A 299 GLU A 304 5 6
HELIX 16 AB7 SER A 305 THR A 328 1 24
HELIX 17 AB8 VAL A 338 THR A 346 1 9
HELIX 18 AB9 SER A 347 ALA A 356 1 10
HELIX 19 AC1 PRO A 365 LYS A 370 5 6
HELIX 20 AC2 ASN B 419 PHE B 424 5 6
HELIX 21 AC3 SER B 438 PHE B 442 5 5
HELIX 22 AC4 GLY B 473 THR B 475 5 3
HELIX 23 AC5 GLN B 476 TRP B 490 1 15
HELIX 24 AC6 ASP B 494 GLU B 501 1 8
HELIX 25 AC7 ASP B 520 ARG B 530 1 11
SHEET 1 AA1 7 VAL A 37 TYR A 38 0
SHEET 2 AA1 7 GLY B 553 ALA B 557 -1 O TRP B 554 N TYR A 38
SHEET 3 AA1 7 VAL B 543 THR B 550 -1 N THR B 550 O GLY B 553
SHEET 4 AA1 7 VAL B 465 ALA B 472 -1 N VAL B 468 O ILE B 547
SHEET 5 AA1 7 THR B 456 GLY B 460 -1 N MET B 458 O ARG B 466
SHEET 6 AA1 7 ALA A 272 MET A 276 -1 N TYR A 275 O ILE B 457
SHEET 7 AA1 7 LEU A 265 LEU A 269 -1 N LEU A 269 O ALA A 272
SHEET 1 AA2 7 GLU A 259 ILE A 261 0
SHEET 2 AA2 7 LYS A 100 ALA A 106 -1 N ASN A 105 O GLU A 259
SHEET 3 AA2 7 GLY A 88 ASN A 95 -1 N LEU A 91 O ILE A 104
SHEET 4 AA2 7 ALA B 393 THR B 399 -1 O SER B 395 N THR A 92
SHEET 5 AA2 7 ALA B 382 VAL B 387 -1 N ALA B 382 O SER B 398
SHEET 6 AA2 7 ALA A 42 ALA A 44 -1 N ALA A 44 O SER B 385
SHEET 7 AA2 7 ALA B 567 GLY B 568 -1 O ALA B 567 N VAL A 43
SHEET 1 AA3 2 PHE A 168 PRO A 169 0
SHEET 2 AA3 2 ARG A 207 LEU A 208 -1 O LEU A 208 N PHE A 168
SHEET 1 AA4 2 CYS A 196 ARG A 197 0
SHEET 2 AA4 2 LYS A 200 VAL A 201 -1 O LYS A 200 N ARG A 197
SHEET 1 AA5 2 VAL B 408 ARG B 409 0
SHEET 2 AA5 2 LEU B 416 PHE B 417 -1 O PHE B 417 N VAL B 408
SHEET 1 AA6 3 LEU B 504 HIS B 505 0
SHEET 2 AA6 3 THR B 513 VAL B 515 -1 O THR B 514 N HIS B 505
SHEET 3 AA6 3 THR B 534 ILE B 536 1 O GLN B 535 N VAL B 515
SSBOND 1 CYS A 50 CYS A 74 1555 1555 2.13
SSBOND 2 CYS A 192 CYS A 196 1555 1555 2.11
LINK ND2 ASN A 95 C1 NAG A 601 1555 1555 1.49
LINK ND2 ASN A 120 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 230 C1 NAG A 605 1555 1555 1.44
LINK ND2 ASN A 266 C1 NAG A 604 1555 1555 1.43
LINK ND2 ASN A 344 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN B 511 C1 NAG B1101 1555 1555 1.43
LINK O HOH A 882 NA NA B1104 1555 1555 2.79
LINK O ALA B 556 NA NA B1104 1555 1555 2.82
LINK NA NA B1104 O HOH B1251 1555 1555 2.79
CISPEP 1 ALA A 279 PRO A 280 0 18.61
CISPEP 2 LEU B 509 PRO B 510 0 -0.36
CRYST1 105.583 125.288 103.988 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 0.009471 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007982 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009616 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
