HEADER HYDROLASE/HYDROLASE INHIBITOR 06-APR-94 1GHB
TITLE A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF
TITLE 2 N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA-CHYMOTRYPSIN;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.21.1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: GAMMA-CHYMOTRYPSIN;
COMPND 7 CHAIN: F;
COMPND 8 EC: 3.4.21.1;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: GAMMA-CHYMOTRYPSIN;
COMPND 11 CHAIN: G;
COMPND 12 EC: 3.4.21.1;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: PRO-GLY-ALA;
COMPND 15 CHAIN: P;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_TAXID: 9913;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 6 ORGANISM_TAXID: 9913;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 9 ORGANISM_TAXID: 9913;
SOURCE 10 MOL_ID: 4
KEYWDS SERINE PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.YENNAWAR,N.H.YENNAWAR,G.K.FARBER
REVDAT 3 13-JUL-11 1GHB 1 VERSN
REVDAT 2 24-FEB-09 1GHB 1 VERSN
REVDAT 1 22-JUN-94 1GHB 0
JRNL AUTH H.P.YENNAWAR,N.H.YENNAWAR,G.K.FARBER
JRNL TITL A STRUCTURAL EXPLANATION FOR ENZYME MEMORY IN NONAQUEOUS
JRNL TITL 2 SOLVENTS.
JRNL REF J.AM.CHEM.SOC. V. 117 577 1995
JRNL REFN ISSN 0002-7863
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.H.YENNAWAR,H.P.YENNAWAR,G.K.FARBER
REMARK 1 TITL X-RAY CRYSTAL STRUCTURE OF GAMMA-CHYMOTRYPSIN IN HEXANE
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1754
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.61
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
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 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 34.80000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.75500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.80000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.80000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 48.75500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.80000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.75500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.80000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 48.75500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, P
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 69.60000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 139.20000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 139.20000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 208.80000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, P
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 104.40000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 34.80000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 146.26500
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 34.80000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 174.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 146.26500
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, P
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 GLY E 12
REMARK 465 LEU E 13
REMARK 465 ALA G 149
REMARK 465 ASN G 150
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER E 11 CA C O CB OG
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 PRO P 571 CA - N - CD ANGL. DEV. = -10.1 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 TRP F 27 69.67 -118.16
REMARK 500 PHE F 71 -56.08 -132.49
REMARK 500 SER F 115 -155.38 -141.82
REMARK 500 CYS F 136 -165.64 -124.92
REMARK 500 LEU F 143 133.22 -38.78
REMARK 500 ALA G 179 37.95 -92.96
REMARK 500 LEU G 209 109.72 -55.61
REMARK 500 SER G 214 -72.30 -110.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU F 49 23.0 L L OUTSIDE RANGE
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 E 658 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH E 665 DISTANCE = 7.30 ANGSTROMS
REMARK 525 HOH E 666 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH E 667 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH E 671 DISTANCE = 10.70 ANGSTROMS
REMARK 525 HOH E 672 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH E 673 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH E 674 DISTANCE = 9.72 ANGSTROMS
REMARK 525 HOH E 675 DISTANCE = 9.23 ANGSTROMS
REMARK 525 HOH E 676 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH E 677 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH E 678 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH F 771 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH F 783 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH F 790 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH F 797 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH F 798 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH F 799 DISTANCE = 8.60 ANGSTROMS
REMARK 525 HOH F 801 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH F 802 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH F 803 DISTANCE = 8.45 ANGSTROMS
REMARK 525 HOH F 804 DISTANCE = 10.08 ANGSTROMS
REMARK 525 HOH F 806 DISTANCE = 10.48 ANGSTROMS
REMARK 525 HOH F 809 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH F 810 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH F 812 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH F 814 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH F 817 DISTANCE = 12.94 ANGSTROMS
REMARK 525 HOH F 820 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH F 821 DISTANCE = 9.53 ANGSTROMS
REMARK 525 HOH F 822 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH F 823 DISTANCE = 10.65 ANGSTROMS
REMARK 525 HOH F 824 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH F 825 DISTANCE = 8.18 ANGSTROMS
REMARK 525 HOH F 829 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH F 833 DISTANCE = 12.20 ANGSTROMS
REMARK 525 HOH F 834 DISTANCE = 10.07 ANGSTROMS
REMARK 525 HOH F 836 DISTANCE = 10.04 ANGSTROMS
REMARK 525 HOH F 839 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH F 846 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH F 847 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH F 848 DISTANCE = 9.30 ANGSTROMS
REMARK 525 HOH F 849 DISTANCE = 10.10 ANGSTROMS
REMARK 525 HOH F 850 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH F 852 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH F 855 DISTANCE = 10.30 ANGSTROMS
REMARK 525 HOH F 856 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH F 857 DISTANCE = 12.92 ANGSTROMS
REMARK 525 HOH F 858 DISTANCE = 13.08 ANGSTROMS
REMARK 525 HOH F 859 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH F 861 DISTANCE = 11.24 ANGSTROMS
REMARK 525 HOH F 863 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH F 865 DISTANCE = 8.58 ANGSTROMS
REMARK 525 HOH F 866 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH F 875 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH G 720 DISTANCE = 8.38 ANGSTROMS
REMARK 525 HOH G 733 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH G 746 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH G 753 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH G 771 DISTANCE = 9.73 ANGSTROMS
REMARK 525 HOH G 772 DISTANCE = 10.06 ANGSTROMS
REMARK 525 HOH G 773 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH G 774 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH G 777 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH G 781 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH G 782 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH G 783 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH G 785 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH G 786 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH G 787 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH G 789 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH G 791 DISTANCE = 8.00 ANGSTROMS
REMARK 525 HOH G 792 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH G 794 DISTANCE = 13.58 ANGSTROMS
REMARK 525 HOH G 795 DISTANCE = 10.23 ANGSTROMS
REMARK 525 HOH G 796 DISTANCE = 10.96 ANGSTROMS
REMARK 525 HOH G 797 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH G 798 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH G 800 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH G 807 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH G 809 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH G 812 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH G 814 DISTANCE = 8.50 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX E 651
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX G 652
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX E 653
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX F 654
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEX F 655
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA G 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA G 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA F 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN P OF PRO-GLY-ALA
DBREF 1GHB E 1 13 UNP P00766 CTRA_BOVIN 1 13
DBREF 1GHB F 16 146 UNP P00766 CTRA_BOVIN 16 146
DBREF 1GHB G 149 245 UNP P00766 CTRA_BOVIN 149 245
DBREF 1GHB P 571 573 PDB 1GHB 1GHB 571 573
SEQRES 1 E 13 CYS GLY VAL PRO ALA ILE GLN PRO VAL LEU SER GLY LEU
SEQRES 1 F 131 ILE VAL ASN GLY GLU GLU ALA VAL PRO GLY SER TRP PRO
SEQRES 2 F 131 TRP GLN VAL SER LEU GLN ASP LYS THR GLY PHE HIS PHE
SEQRES 3 F 131 CYS GLY GLY SER LEU ILE ASN GLU ASN TRP VAL VAL THR
SEQRES 4 F 131 ALA ALA HIS CYS GLY VAL THR THR SER ASP VAL VAL VAL
SEQRES 5 F 131 ALA GLY GLU PHE ASP GLN GLY SER SER SER GLU LYS ILE
SEQRES 6 F 131 GLN LYS LEU LYS ILE ALA LYS VAL PHE LYS ASN SER LYS
SEQRES 7 F 131 TYR ASN SER LEU THR ILE ASN ASN ASP ILE THR LEU LEU
SEQRES 8 F 131 LYS LEU SER THR ALA ALA SER PHE SER GLN THR VAL SER
SEQRES 9 F 131 ALA VAL CYS LEU PRO SER ALA SER ASP ASP PHE ALA ALA
SEQRES 10 F 131 GLY THR THR CYS VAL THR THR GLY TRP GLY LEU THR ARG
SEQRES 11 F 131 TYR
SEQRES 1 G 97 ALA ASN THR PRO ASP ARG LEU GLN GLN ALA SER LEU PRO
SEQRES 2 G 97 LEU LEU SER ASN THR ASN CYS LYS LYS TYR TRP GLY THR
SEQRES 3 G 97 LYS ILE LYS ASP ALA MET ILE CYS ALA GLY ALA SER GLY
SEQRES 4 G 97 VAL SER SER CYS MET GLY ASP SER GLY GLY PRO LEU VAL
SEQRES 5 G 97 CYS LYS LYS ASN GLY ALA TRP THR LEU VAL GLY ILE VAL
SEQRES 6 G 97 SER TRP GLY SER SER THR CYS SER THR SER THR PRO GLY
SEQRES 7 G 97 VAL TYR ALA ARG VAL THR ALA LEU VAL ASN TRP VAL GLN
SEQRES 8 G 97 GLN THR LEU ALA ALA ASN
SEQRES 1 P 3 PRO GLY ALA
HET ACE E 600 3
HET TRP E 601 15
HET HEX E 651 6
HET HEX G 652 6
HET HEX E 653 6
HET HEX F 654 6
HET HEX F 655 6
HET IPA G 701 4
HET IPA G 702 4
HET IPA F 703 4
HETNAM ACE ACETYL GROUP
HETNAM TRP TRYPTOPHAN
HETNAM HEX HEXANE
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 5 ACE C2 H4 O
FORMUL 5 TRP C11 H12 N2 O2
FORMUL 6 HEX 5(C6 H14)
FORMUL 11 IPA 3(C3 H8 O)
FORMUL 14 HOH *309(H2 O)
HELIX 1 1 ALA F 55 GLY F 59 5 5
HELIX 2 2 SER G 164 GLY G 173 1 10
HELIX 3 3 THR G 174 ILE G 176 5 3
HELIX 4 4 VAL G 231 ASN G 245 1 15
SHEET 1 A 7 GLU F 20 GLU F 21 0
SHEET 2 A 7 GLN G 156 PRO G 161 -1 O GLN G 157 N GLU F 20
SHEET 3 A 7 THR F 135 GLY F 140 -1 N CYS F 136 O LEU G 160
SHEET 4 A 7 PRO G 198 LYS G 203 -1 O VAL G 200 N VAL F 137
SHEET 5 A 7 ALA G 206 TRP G 215 -1 O THR G 208 N CYS G 201
SHEET 6 A 7 PRO G 225 ARG G 230 -1 O VAL G 227 N TRP G 215
SHEET 7 A 7 MET G 180 GLY G 184 -1 N ILE G 181 O TYR G 228
SHEET 1 B 7 GLN F 30 GLN F 34 0
SHEET 2 B 7 HIS F 40 ASN F 48 -1 O CYS F 42 N LEU F 33
SHEET 3 B 7 TRP F 51 THR F 54 -1 O VAL F 53 N SER F 45
SHEET 4 B 7 THR F 104 LEU F 108 -1 O THR F 104 N THR F 54
SHEET 5 B 7 GLN F 81 LYS F 90 -1 N ALA F 86 O LYS F 107
SHEET 6 B 7 VAL F 65 ALA F 68 -1 N VAL F 66 O LEU F 83
SHEET 7 B 7 GLN F 30 GLN F 34 -1 N GLN F 34 O VAL F 65
SSBOND 1 CYS E 1 CYS F 122 1555 1555 2.03
SSBOND 2 CYS F 42 CYS F 58 1555 1555 2.02
SSBOND 3 CYS F 136 CYS G 201 1555 1555 2.02
SSBOND 4 CYS G 168 CYS G 182 1555 1555 2.03
SSBOND 5 CYS G 191 CYS G 220 1555 1555 2.03
LINK C ACE E 600 N TRP E 601 1555 1555 1.33
SITE 1 AC1 7 TRP E 601 SER G 189 SER G 190 GLY G 216
SITE 2 AC1 7 SER G 217 GLY G 226 HOH G 717
SITE 1 AC2 14 ACE E 600 SER G 190 MET G 192 SER G 195
SITE 2 AC2 14 VAL G 213 SER G 214 TRP G 215 GLY G 216
SITE 3 AC2 14 SER G 217 CYS G 220 GLY G 226 VAL G 227
SITE 4 AC2 14 TYR G 228 ALA P 573
SITE 1 AC3 5 ILE F 16 ASN F 18 GLY F 19 THR F 144
SITE 2 AC3 5 GLN G 156
SITE 1 AC4 5 HOH E 659 GLU F 20 SER G 159 SER G 186
SITE 2 AC4 5 GLY G 187
SITE 1 AC5 8 CYS E 1 VAL E 3 THR F 37 LYS F 93
SITE 2 AC5 8 SER F 119 ALA F 120 HOH F 709 HOH F 869
SITE 1 AC6 3 HOH E 676 GLU F 20 GLU F 21
SITE 1 AC7 1 GLU F 49
SITE 1 AC8 7 PHE F 41 SER F 96 LEU F 97 MET G 192
SITE 2 AC8 7 GLY G 193 SER G 195 ALA P 573
SITE 1 AC9 2 SER G 218 HOH G 769
SITE 1 BC1 7 ALA F 56 GLY F 59 VAL F 60 THR F 61
SITE 2 BC1 7 VAL F 88 LYS F 90 THR F 104
SITE 1 BC2 11 TRP E 601 HIS F 57 LEU F 97 ILE F 99
SITE 2 BC2 11 HOH F 737 SER G 195 SER G 214 TRP G 215
SITE 3 BC2 11 GLY G 216 IPA G 701 HOH P 574
CRYST1 69.600 69.600 97.510 90.00 90.00 90.00 P 42 21 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 0.014368 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010255 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
