HEADER HYDROLASE 02-JUN-17 5O5R
TITLE X-RAY STRUCTURE OF HUMAN GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN
TITLE 2 COMPLEX WITH A UREA BASED INHIBITOR PSMA 1023
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE CARBOXYPEPTIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CELL GROWTH-INHIBITING GENE 27 PROTEIN,FOLATE HYDROLASE 1,
COMPND 5 FOLYLPOLY-GAMMA-GLUTAMATE CARBOXYPEPTIDASE,FGCP,GLUTAMATE
COMPND 6 CARBOXYPEPTIDASE II,GCPII,MEMBRANE GLUTAMATE CARBOXYPEPTIDASE,MGCP,N-
COMPND 7 ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE I,NAALADASE I,PROSTATE-
COMPND 8 SPECIFIC MEMBRANE ANTIGEN,PSMA,PTEROYLPOLY-GAMMA-GLUTAMATE
COMPND 9 CARBOXYPEPTIDASE;
COMPND 10 EC: 3.4.17.21;
COMPND 11 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: FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDERS S2 CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS GLUTAMATE CARBOXYPEPTIDASE II (GCPII); NAALADASE; PROSTATE-SPECIFIC
KEYWDS 2 MEMBRANE ANTIGEN; UREA BASED INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.MOTLOVA,Z.NOVAKOVA,C.BARINKA
REVDAT 3 17-JAN-24 5O5R 1 HETSYN LINK
REVDAT 2 29-JUL-20 5O5R 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 13-JUN-18 5O5R 0
JRNL AUTH L.MOTLOVA,Z.NOVAKOVA,C.BARINKA
JRNL TITL X-RAY STRUCTURE OF HUMAN GLUTAMATE CARBOXYPEPTIDASE II
JRNL TITL 2 (GCPII) IN COMPLEX WITH A UREA BASED INHIBITOR PSMA 1023
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 118929
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) : 0.126
REMARK 3 R VALUE (WORKING SET) : 0.124
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6313
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8645
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 460
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5546
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 304
REMARK 3 SOLVENT ATOMS : 624
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : -1.63000
REMARK 3 B33 (A**2) : 1.30000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.181
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6624 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5922 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9045 ; 1.563 ; 2.007
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13876 ; 2.090 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 808 ; 5.903 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 295 ;35.668 ;23.966
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1069 ;13.609 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;15.837 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 964 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7449 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1387 ; 0.008 ; 0.020
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): 3091 ; 2.405 ; 3.165
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3089 ; 2.335 ; 3.162
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3944 ; 2.742 ; 4.745
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3945 ; 2.742 ; 4.748
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3533 ; 3.416 ; 3.662
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3534 ; 3.415 ; 3.661
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5102 ; 3.812 ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7654 ; 3.827 ;38.857
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7511 ; 3.645 ;38.297
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 12542 ; 5.597 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 363 ;23.551 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 12564 ;12.516 ; 5.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 55 A 1525
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6870 49.8880 45.1190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0290 T22: 0.0029
REMARK 3 T33: 0.0148 T12: 0.0047
REMARK 3 T13: -0.0027 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.0910 L22: 0.2336
REMARK 3 L33: 0.0585 L12: -0.0530
REMARK 3 L13: 0.0040 L23: 0.0171
REMARK 3 S TENSOR
REMARK 3 S11: -0.0132 S12: 0.0028 S13: -0.0077
REMARK 3 S21: 0.0087 S22: 0.0157 S23: -0.0342
REMARK 3 S31: 0.0022 S32: 0.0071 S33: -0.0025
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5O5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1200005071.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JAN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : KMC-1
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 125247
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 49.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.95300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: 3BI1.PDB
REMARK 200
REMARK 200 REMARK: CLEAR BLOCK, 50 X 200 UM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34 % (V/V) PENTAERYTHRITOL PROPOXYLATE
REMARK 280 PO/OH 5/4, 2 % (W/V) PEG 3350, 100 MM TRIS-HCL, PH 8.0., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 50.75600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.10150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 79.58000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 50.75600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.10150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.58000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.75600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.10150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 79.58000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 50.75600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.10150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 79.58000
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: 14990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 94.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 130.20300
REMARK 350 BIOMT3 2 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 LYS A 44
REMARK 465 SER A 45
REMARK 465 SER A 46
REMARK 465 ASN A 47
REMARK 465 GLU A 48
REMARK 465 ALA A 49
REMARK 465 THR A 50
REMARK 465 ASN A 51
REMARK 465 ILE A 52
REMARK 465 THR A 53
REMARK 465 PRO A 54
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 OH TYR A 242 O HOH A 906 2.11
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 OE1 GLU A 276 O2 BMA E 3 2565 2.19
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 PHE A 164 5.95 84.24
REMARK 500 ASN A 178 -126.34 58.23
REMARK 500 LYS A 207 -41.54 71.62
REMARK 500 VAL A 382 -105.83 -129.03
REMARK 500 ALA A 452 59.61 -150.31
REMARK 500 ASP A 453 -154.85 -85.86
REMARK 500 SER A 517 -157.65 -148.76
REMARK 500 ASP A 567 65.88 -155.71
REMARK 500 PHE A 653 -121.00 -81.11
REMARK 500 ASP A 654 102.74 -50.57
REMARK 500 ASP A 654 136.81 77.21
REMARK 500 LYS A 655 6.15 -174.34
REMARK 500 ASP A 683 14.44 59.73
REMARK 500 ASN A 698 98.26 -167.46
REMARK 500 PHE A 705 57.16 37.35
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 A 819 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 269 O
REMARK 620 2 THR A 269 OG1 72.5
REMARK 620 3 TYR A 272 O 73.3 91.5
REMARK 620 4 GLU A 433 OE1 150.9 89.1 85.1
REMARK 620 5 GLU A 433 OE2 150.7 100.4 135.9 53.2
REMARK 620 6 GLU A 436 OE2 102.9 171.3 80.0 92.1 87.2
REMARK 620 7 HOH A1067 O 71.8 89.3 143.1 131.8 79.8 96.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 818 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 377 NE2
REMARK 620 2 ASP A 387 OD1 107.9
REMARK 620 3 ASP A 453 OD2 101.2 116.5
REMARK 620 4 HOH A1215 O 111.7 105.4 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 817 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 387 OD2
REMARK 620 2 GLU A 425 OE1 155.5
REMARK 620 3 GLU A 425 OE2 99.2 56.8
REMARK 620 4 HIS A 553 NE2 92.8 86.9 99.1
REMARK 620 5 9OQ A 801 OBA 106.0 98.4 153.8 86.7
REMARK 620 6 HOH A1215 O 94.6 92.4 94.3 163.5 77.1
REMARK 620 N 1 2 3 4 5
DBREF 5O5R A 44 750 UNP Q04609 FOLH1_HUMAN 44 750
SEQRES 1 A 707 LYS SER SER ASN GLU ALA THR ASN ILE THR PRO LYS HIS
SEQRES 2 A 707 ASN MET LYS ALA PHE LEU ASP GLU LEU LYS ALA GLU ASN
SEQRES 3 A 707 ILE LYS LYS PHE LEU TYR ASN PHE THR GLN ILE PRO HIS
SEQRES 4 A 707 LEU ALA GLY THR GLU GLN ASN PHE GLN LEU ALA LYS GLN
SEQRES 5 A 707 ILE GLN SER GLN TRP LYS GLU PHE GLY LEU ASP SER VAL
SEQRES 6 A 707 GLU LEU ALA HIS TYR ASP VAL LEU LEU SER TYR PRO ASN
SEQRES 7 A 707 LYS THR HIS PRO ASN TYR ILE SER ILE ILE ASN GLU ASP
SEQRES 8 A 707 GLY ASN GLU ILE PHE ASN THR SER LEU PHE GLU PRO PRO
SEQRES 9 A 707 PRO PRO GLY TYR GLU ASN VAL SER ASP ILE VAL PRO PRO
SEQRES 10 A 707 PHE SER ALA PHE SER PRO GLN GLY MET PRO GLU GLY ASP
SEQRES 11 A 707 LEU VAL TYR VAL ASN TYR ALA ARG THR GLU ASP PHE PHE
SEQRES 12 A 707 LYS LEU GLU ARG ASP MET LYS ILE ASN CYS SER GLY LYS
SEQRES 13 A 707 ILE VAL ILE ALA ARG TYR GLY LYS VAL PHE ARG GLY ASN
SEQRES 14 A 707 LYS VAL LYS ASN ALA GLN LEU ALA GLY ALA LYS GLY VAL
SEQRES 15 A 707 ILE LEU TYR SER ASP PRO ALA ASP TYR PHE ALA PRO GLY
SEQRES 16 A 707 VAL LYS SER TYR PRO ASP GLY TRP ASN LEU PRO GLY GLY
SEQRES 17 A 707 GLY VAL GLN ARG GLY ASN ILE LEU ASN LEU ASN GLY ALA
SEQRES 18 A 707 GLY ASP PRO LEU THR PRO GLY TYR PRO ALA ASN GLU TYR
SEQRES 19 A 707 ALA TYR ARG ARG GLY ILE ALA GLU ALA VAL GLY LEU PRO
SEQRES 20 A 707 SER ILE PRO VAL HIS PRO ILE GLY TYR TYR ASP ALA GLN
SEQRES 21 A 707 LYS LEU LEU GLU LYS MET GLY GLY SER ALA PRO PRO ASP
SEQRES 22 A 707 SER SER TRP ARG GLY SER LEU LYS VAL PRO TYR ASN VAL
SEQRES 23 A 707 GLY PRO GLY PHE THR GLY ASN PHE SER THR GLN LYS VAL
SEQRES 24 A 707 LYS MET HIS ILE HIS SER THR ASN GLU VAL THR ARG ILE
SEQRES 25 A 707 TYR ASN VAL ILE GLY THR LEU ARG GLY ALA VAL GLU PRO
SEQRES 26 A 707 ASP ARG TYR VAL ILE LEU GLY GLY HIS ARG ASP SER TRP
SEQRES 27 A 707 VAL PHE GLY GLY ILE ASP PRO GLN SER GLY ALA ALA VAL
SEQRES 28 A 707 VAL HIS GLU ILE VAL ARG SER PHE GLY THR LEU LYS LYS
SEQRES 29 A 707 GLU GLY TRP ARG PRO ARG ARG THR ILE LEU PHE ALA SER
SEQRES 30 A 707 TRP ASP ALA GLU GLU PHE GLY LEU LEU GLY SER THR GLU
SEQRES 31 A 707 TRP ALA GLU GLU ASN SER ARG LEU LEU GLN GLU ARG GLY
SEQRES 32 A 707 VAL ALA TYR ILE ASN ALA ASP SER SER ILE GLU GLY ASN
SEQRES 33 A 707 TYR THR LEU ARG VAL ASP CYS THR PRO LEU MET TYR SER
SEQRES 34 A 707 LEU VAL HIS ASN LEU THR LYS GLU LEU LYS SER PRO ASP
SEQRES 35 A 707 GLU GLY PHE GLU GLY LYS SER LEU TYR GLU SER TRP THR
SEQRES 36 A 707 LYS LYS SER PRO SER PRO GLU PHE SER GLY MET PRO ARG
SEQRES 37 A 707 ILE SER LYS LEU GLY SER GLY ASN ASP PHE GLU VAL PHE
SEQRES 38 A 707 PHE GLN ARG LEU GLY ILE ALA SER GLY ARG ALA ARG TYR
SEQRES 39 A 707 THR LYS ASN TRP GLU THR ASN LYS PHE SER GLY TYR PRO
SEQRES 40 A 707 LEU TYR HIS SER VAL TYR GLU THR TYR GLU LEU VAL GLU
SEQRES 41 A 707 LYS PHE TYR ASP PRO MET PHE LYS TYR HIS LEU THR VAL
SEQRES 42 A 707 ALA GLN VAL ARG GLY GLY MET VAL PHE GLU LEU ALA ASN
SEQRES 43 A 707 SER ILE VAL LEU PRO PHE ASP CYS ARG ASP TYR ALA VAL
SEQRES 44 A 707 VAL LEU ARG LYS TYR ALA ASP LYS ILE TYR SER ILE SER
SEQRES 45 A 707 MET LYS HIS PRO GLN GLU MET LYS THR TYR SER VAL SER
SEQRES 46 A 707 PHE ASP SER LEU PHE SER ALA VAL LYS ASN PHE THR GLU
SEQRES 47 A 707 ILE ALA SER LYS PHE SER GLU ARG LEU GLN ASP PHE ASP
SEQRES 48 A 707 LYS SER ASN PRO ILE VAL LEU ARG MET MET ASN ASP GLN
SEQRES 49 A 707 LEU MET PHE LEU GLU ARG ALA PHE ILE ASP PRO LEU GLY
SEQRES 50 A 707 LEU PRO ASP ARG PRO PHE TYR ARG HIS VAL ILE TYR ALA
SEQRES 51 A 707 PRO SER SER HIS ASN LYS TYR ALA GLY GLU SER PHE PRO
SEQRES 52 A 707 GLY ILE TYR ASP ALA LEU PHE ASP ILE GLU SER LYS VAL
SEQRES 53 A 707 ASP PRO SER LYS ALA TRP GLY GLU VAL LYS ARG GLN ILE
SEQRES 54 A 707 TYR VAL ALA ALA PHE THR VAL GLN ALA ALA ALA GLU THR
SEQRES 55 A 707 LEU SER GLU VAL ALA
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET MAN E 5 11
HET 9OQ A 801 74
HET NAG A 807 14
HET NAG A 816 14
HET ZN A 817 1
HET ZN A 818 1
HET CA A 819 1
HET CL A 820 1
HET PEG A 821 7
HET PEG A 822 7
HET EDO A 823 4
HET NAG A 824 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM 9OQ (2~{S})-2-[[(2~{S})-6-[[(2~{S})-2-[[4-[[[(2~{R})-2-
HETNAM 2 9OQ [[(2~{R})-2-[(6-FLUORANYLPYRIDIN-3-YL)CARBONYLAMINO]-
HETNAM 3 9OQ 5-OXIDANYL-5-OXIDANYLIDENE-PENTANOYL]AMINO]-5-
HETNAM 4 9OQ OXIDANYL-5-OXIDANYLIDENE-
HETNAM 5 9OQ PENTANOYL]AMINO]METHYL]PHENYL]CARBONYLAMINO]-3-
HETNAM 6 9OQ NAPHTHALEN-2-YL-PROPANOYL]AMINO]-1-OXIDANYL-1-
HETNAM 7 9OQ OXIDANYLIDENE-HEXAN-2-YL]CARBAMOYLAMINO]PENTANEDIOIC
HETNAM 8 9OQ ACID
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
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
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG 11(C8 H15 N O6)
FORMUL 3 FUC C6 H12 O5
FORMUL 4 BMA 2(C6 H12 O6)
FORMUL 5 MAN 2(C6 H12 O6)
FORMUL 6 9OQ C49 H55 F N8 O16
FORMUL 9 ZN 2(ZN 2+)
FORMUL 11 CA CA 2+
FORMUL 12 CL CL 1-
FORMUL 13 PEG 2(C4 H10 O3)
FORMUL 15 EDO C2 H6 O2
FORMUL 17 HOH *624(H2 O)
HELIX 1 AA1 ASN A 57 LEU A 65 1 9
HELIX 2 AA2 LYS A 66 THR A 78 1 13
HELIX 3 AA3 THR A 86 GLY A 104 1 19
HELIX 4 AA4 ARG A 181 ASP A 191 1 11
HELIX 5 AA5 PHE A 209 ALA A 220 1 12
HELIX 6 AA6 ASP A 230 PHE A 235 1 6
HELIX 7 AA7 GLY A 282 ALA A 286 5 5
HELIX 8 AA8 GLY A 298 GLU A 307 1 10
HELIX 9 AA9 ASP A 316 ARG A 320 5 5
HELIX 10 AB1 THR A 334 SER A 338 5 5
HELIX 11 AB2 PRO A 388 GLU A 408 1 21
HELIX 12 AB3 ALA A 423 GLY A 427 5 5
HELIX 13 AB4 LEU A 428 ARG A 445 1 18
HELIX 14 AB5 MET A 470 GLU A 480 1 11
HELIX 15 AB6 SER A 492 SER A 501 1 10
HELIX 16 AB7 ASP A 520 GLN A 526 1 7
HELIX 17 AB8 THR A 558 TYR A 566 1 9
HELIX 18 AB9 PHE A 570 SER A 590 1 21
HELIX 19 AC1 ASP A 596 MET A 616 1 21
HELIX 20 AC2 HIS A 618 SER A 626 1 9
HELIX 21 AC3 PHE A 629 PHE A 653 1 25
HELIX 22 AC4 ASN A 657 PHE A 675 1 19
HELIX 23 AC5 PHE A 705 PHE A 713 1 9
HELIX 24 AC6 ASP A 714 LYS A 718 5 5
HELIX 25 AC7 ASP A 720 THR A 745 1 26
SHEET 1 AA1 7 SER A 107 TYR A 119 0
SHEET 2 AA1 7 THR A 349 LEU A 362 -1 O ASN A 357 N ALA A 111
SHEET 3 AA1 7 ARG A 414 TRP A 421 -1 O PHE A 418 N GLY A 360
SHEET 4 AA1 7 GLU A 367 HIS A 377 1 N LEU A 374 O LEU A 417
SHEET 5 AA1 7 GLY A 446 ASN A 451 1 O ILE A 450 N ILE A 373
SHEET 6 AA1 7 ALA A 531 THR A 538 1 O GLY A 533 N ASN A 451
SHEET 7 AA1 7 THR A 461 CYS A 466 -1 N THR A 461 O THR A 538
SHEET 1 AA2 4 GLU A 137 ASN A 140 0
SHEET 2 AA2 4 TYR A 127 ILE A 131 -1 N ILE A 130 O PHE A 139
SHEET 3 AA2 4 LYS A 341 HIS A 345 -1 O LYS A 343 N SER A 129
SHEET 4 AA2 4 GLU A 171 GLY A 172 -1 N GLY A 172 O VAL A 342
SHEET 1 AA3 2 SER A 162 ALA A 163 0
SHEET 2 AA3 2 GLY A 256 ASN A 257 1 N GLY A 256 O ALA A 163
SHEET 1 AA4 4 LEU A 174 TYR A 176 0
SHEET 2 AA4 4 ILE A 200 ARG A 204 1 O ILE A 202 N VAL A 175
SHEET 3 AA4 4 GLY A 224 TYR A 228 1 O ILE A 226 N VAL A 201
SHEET 4 AA4 4 VAL A 294 ILE A 297 1 O ILE A 297 N LEU A 227
SHEET 1 AA5 2 TYR A 692 SER A 695 0
SHEET 2 AA5 2 ASN A 698 SER A 704 -1 O ALA A 701 N SER A 695
LINK ND2 ASN A 76 C1 NAG B 1 1555 1555 1.42
LINK ND2 ASN A 121 C1 NAG A 824 1555 1555 1.45
LINK ND2 ASN A 140 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 195 C1 NAG A 807 1555 1555 1.46
LINK ND2 ASN A 459 C1 NAG A 816 1555 1555 1.44
LINK ND2 ASN A 476 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 638 C1 NAG E 1 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.42
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.42
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45
LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.45
LINK O THR A 269 CA CA A 819 1555 1555 2.43
LINK OG1 THR A 269 CA CA A 819 1555 1555 2.44
LINK O TYR A 272 CA CA A 819 1555 1555 2.34
LINK NE2 HIS A 377 ZN ZN A 818 1555 1555 2.00
LINK OD2 ASP A 387 ZN ZN A 817 1555 1555 2.06
LINK OD1 ASP A 387 ZN ZN A 818 1555 1555 1.97
LINK OE1 GLU A 425 ZN ZN A 817 1555 1555 2.40
LINK OE2 GLU A 425 ZN ZN A 817 1555 1555 2.12
LINK OE1 GLU A 433 CA CA A 819 1555 1555 2.46
LINK OE2 GLU A 433 CA CA A 819 1555 1555 2.48
LINK OE2 GLU A 436 CA CA A 819 1555 1555 2.37
LINK OD2 ASP A 453 ZN ZN A 818 1555 1555 1.99
LINK NE2 HIS A 553 ZN ZN A 817 1555 1555 2.08
LINK OBA 9OQ A 801 ZN ZN A 817 1555 1555 2.50
LINK ZN ZN A 817 O HOH A1215 1555 1555 1.97
LINK ZN ZN A 818 O HOH A1215 1555 1555 1.93
LINK CA CA A 819 O HOH A1067 1555 1555 2.35
CISPEP 1 TYR A 242 PRO A 243 0 11.83
CISPEP 2 GLY A 330 PRO A 331 0 0.79
CISPEP 3 ASP A 387 PRO A 388 0 7.47
CRYST1 101.512 130.203 159.160 90.00 90.00 90.00 I 2 2 2 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 0.009851 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006283 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
