HEADER HYDROLASE/HYDROLASE INHIBITOR 09-APR-14 4Q2K
TITLE BOVINE ALPHA CHYMOTRYPSIN BOUND TO A CYCLIC PEPTIDE INHIBITOR, 5B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHYMOTRYPSINOGEN A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CHYMOTRYPSIN A CHAIN A, CHYMOTRYPSIN A CHAIN B, CHYMOTRYPSIN
COMPND 5 A CHAIN C;
COMPND 6 EC: 3.4.21.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS CHYMOTRYPSIN, PROTEASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.Y.CHAN,J.B.BRUNING,A.D.ABELL
REVDAT 3 08-NOV-23 4Q2K 1 REMARK
REVDAT 2 24-AUG-22 4Q2K 1 JRNL REMARK LINK
REVDAT 1 23-JUL-14 4Q2K 0
JRNL AUTH K.C.CHUA,M.PIETSCH,X.ZHANG,S.HAUTMANN,H.Y.CHAN,J.B.BRUNING,
JRNL AUTH 2 M.GUTSCHOW,A.D.ABELL
JRNL TITL MACROCYCLIC PROTEASE INHIBITORS WITH REDUCED PEPTIDE
JRNL TITL 2 CHARACTER.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 53 7828 2014
JRNL REFN ESSN 1521-3773
JRNL PMID 24903745
JRNL DOI 10.1002/ANIE.201404301
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 42860
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.570
REMARK 3 FREE R VALUE TEST SET COUNT : 1958
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.9888 - 5.2967 1.00 3084 142 0.1837 0.2219
REMARK 3 2 5.2967 - 4.2064 1.00 3006 143 0.1629 0.2065
REMARK 3 3 4.2064 - 3.6753 0.99 3018 155 0.1860 0.2183
REMARK 3 4 3.6753 - 3.3396 0.99 3000 140 0.1936 0.2723
REMARK 3 5 3.3396 - 3.1004 0.99 2966 146 0.2111 0.2730
REMARK 3 6 3.1004 - 2.9177 0.98 2961 137 0.2247 0.3105
REMARK 3 7 2.9177 - 2.7716 0.97 2920 149 0.2241 0.2419
REMARK 3 8 2.7716 - 2.6510 0.97 2931 132 0.2297 0.3179
REMARK 3 9 2.6510 - 2.5490 0.97 2878 137 0.2315 0.3079
REMARK 3 10 2.5490 - 2.4611 0.96 2886 143 0.2440 0.3147
REMARK 3 11 2.4611 - 2.3841 0.96 2872 133 0.2299 0.3085
REMARK 3 12 2.3841 - 2.3160 0.94 2844 141 0.2367 0.3151
REMARK 3 13 2.3160 - 2.2550 0.92 2770 130 0.2451 0.4039
REMARK 3 14 2.2550 - 2.2000 0.93 2766 130 0.2501 0.3473
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.01
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 7142
REMARK 3 ANGLE : 1.384 9699
REMARK 3 CHIRALITY : 0.071 1136
REMARK 3 PLANARITY : 0.005 1212
REMARK 3 DIHEDRAL : 15.102 2441
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Q2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085523.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : RIGAKU VARIMAX HF MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 0.1.26
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43580
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 34.984
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.29300
REMARK 200 R SYM FOR SHELL (I) : 0.29300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: 1YPH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 2M AMMONIUM SULFATE, PH
REMARK 280 7.0, VAPOR DIFFUSION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 54.67000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: A, D
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 SER A 11
REMARK 465 GLY A 12
REMARK 465 LEU A 13
REMARK 465 SER A 14
REMARK 465 ARG A 15
REMARK 465 TYR A 94
REMARK 465 ASN A 95
REMARK 465 SER A 96
REMARK 465 LEU A 97
REMARK 465 THR A 98
REMARK 465 ILE A 99
REMARK 465 ASN A 100
REMARK 465 THR A 147
REMARK 465 ASN A 148
REMARK 465 GLY B 12
REMARK 465 LEU B 13
REMARK 465 SER B 14
REMARK 465 ARG B 15
REMARK 465 LYS B 93
REMARK 465 TYR B 94
REMARK 465 ASN B 95
REMARK 465 SER B 96
REMARK 465 LEU B 97
REMARK 465 THR B 98
REMARK 465 THR B 147
REMARK 465 ASN B 148
REMARK 465 ALA B 149
REMARK 465 ASN B 150
REMARK 465 SER C 11
REMARK 465 GLY C 12
REMARK 465 LEU C 13
REMARK 465 SER C 14
REMARK 465 ARG C 15
REMARK 465 SER C 96
REMARK 465 LEU C 97
REMARK 465 THR C 98
REMARK 465 ILE C 99
REMARK 465 THR C 147
REMARK 465 ASN C 148
REMARK 465 SER D 11
REMARK 465 GLY D 12
REMARK 465 LEU D 13
REMARK 465 SER D 14
REMARK 465 ARG D 15
REMARK 465 TYR D 94
REMARK 465 ASN D 95
REMARK 465 SER D 96
REMARK 465 LEU D 97
REMARK 465 THR D 98
REMARK 465 THR D 147
REMARK 465 ASN D 148
REMARK 465 ALA D 149
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 HIS A 57 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 11 OG
REMARK 470 SER B 77 OG
REMARK 470 GLU B 78 CG CD OE1 OE2
REMARK 470 LYS B 79 CG CD CE NZ
REMARK 470 ILE B 99 CG1 CG2 CD1
REMARK 470 ASN B 100 CG OD1 ND2
REMARK 470 LYS C 36 CG CD CE NZ
REMARK 470 THR C 37 OG1 CG2
REMARK 470 SER C 77 OG
REMARK 470 LYS C 93 CG CD CE NZ
REMARK 470 ARG C 154 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 203 CG CD CE NZ
REMARK 470 ASN C 204 CG OD1 ND2
REMARK 470 SER D 76 OG
REMARK 470 ILE D 99 CG1 CG2 CD1
REMARK 470 ASN D 100 CG OD1 ND2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 36 CD CE NZ
REMARK 480 GLU A 49 CD
REMARK 480 LYS A 84 CD CE NZ
REMARK 480 SER A 189 OG
REMARK 480 LYS B 36 CD CE NZ
REMARK 480 LYS B 84 CD CE NZ
REMARK 480 SER B 189 OG
REMARK 480 GLU C 20 CD
REMARK 480 LYS C 84 CD CE NZ
REMARK 480 SER C 189 OG
REMARK 480 LYS D 36 CD CE NZ
REMARK 480 LYS D 84 CD CE NZ
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 D 470 O HOH D 476 1.91
REMARK 500 O HOH D 455 O HOH D 475 1.95
REMARK 500 O HOH D 419 O HOH D 429 2.02
REMARK 500 OE2 GLU C 21 O HOH C 464 2.08
REMARK 500 ND2 ASN C 245 O HOH C 460 2.08
REMARK 500 O HOH B 487 O HOH B 497 2.08
REMARK 500 NZ LYS B 82 O HOH B 527 2.08
REMARK 500 N ILE D 176 O HOH D 420 2.11
REMARK 500 O HOH C 482 O HOH D 515 2.13
REMARK 500 SG CYS C 58 O HOH C 451 2.13
REMARK 500 O HOH D 451 O HOH D 489 2.15
REMARK 500 O HOH B 478 O HOH B 479 2.15
REMARK 500 O HOH A 464 O HOH A 482 2.15
REMARK 500 O GLY B 133 O HOH B 472 2.15
REMARK 500 O ASN C 245 O HOH C 426 2.17
REMARK 500 O HOH C 450 O HOH C 499 2.17
REMARK 500 O HOH B 455 O HOH B 456 2.18
REMARK 500 O HOH B 412 O HOH B 446 2.18
REMARK 500 O HOH B 486 O HOH B 501 2.18
REMARK 500 O HOH A 453 O HOH A 477 2.19
REMARK 500 O HOH D 469 O HOH D 471 2.19
REMARK 500 O GLU B 70 O HOH B 410 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS B 84 CB LYS B 84 CG -0.163
REMARK 500 LYS B 84 CE LYS B 84 NZ -0.210
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS B 84 CD - CE - NZ ANGL. DEV. = -15.2 DEGREES
REMARK 500 LYS B 170 CG - CD - CE ANGL. DEV. = -22.0 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 SER A 115 -163.24 -161.50
REMARK 500 ASN A 150 35.53 -97.68
REMARK 500 SER A 186 22.78 -140.36
REMARK 500 SER A 214 -65.83 -125.85
REMARK 500 LEU B 10 -93.28 -114.27
REMARK 500 ASN B 101 96.46 56.62
REMARK 500 SER B 214 -71.64 -109.67
REMARK 500 LYS C 36 7.14 -67.05
REMARK 500 ASN C 48 -165.24 -167.93
REMARK 500 PHE C 71 -63.13 -142.50
REMARK 500 SER C 92 -74.12 -50.13
REMARK 500 LYS C 93 33.49 -91.00
REMARK 500 ASN C 101 71.91 -112.18
REMARK 500 ASN C 204 48.70 85.67
REMARK 500 SER C 214 -74.04 -123.25
REMARK 500 ASP D 35 -176.54 -69.37
REMARK 500 ASN D 48 -170.15 -177.81
REMARK 500 PHE D 71 -54.60 -122.71
REMARK 500 LYS D 79 69.00 -68.44
REMARK 500 ASN D 101 95.94 55.65
REMARK 500 ARG D 145 117.86 -167.31
REMARK 500 SER D 214 -68.25 -120.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5BF A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5BF B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5BF C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5BF D 301
DBREF 4Q2K A 1 245 UNP P00766 CTRA_BOVIN 1 245
DBREF 4Q2K B 1 245 UNP P00766 CTRA_BOVIN 1 245
DBREF 4Q2K C 1 245 UNP P00766 CTRA_BOVIN 1 245
DBREF 4Q2K D 1 245 UNP P00766 CTRA_BOVIN 1 245
SEQRES 1 A 245 CYS GLY VAL PRO ALA ILE GLN PRO VAL LEU SER GLY LEU
SEQRES 2 A 245 SER ARG ILE VAL ASN GLY GLU GLU ALA VAL PRO GLY SER
SEQRES 3 A 245 TRP PRO TRP GLN VAL SER LEU GLN ASP LYS THR GLY PHE
SEQRES 4 A 245 HIS PHE CYS GLY GLY SER LEU ILE ASN GLU ASN TRP VAL
SEQRES 5 A 245 VAL THR ALA ALA HIS CYS GLY VAL THR THR SER ASP VAL
SEQRES 6 A 245 VAL VAL ALA GLY GLU PHE ASP GLN GLY SER SER SER GLU
SEQRES 7 A 245 LYS ILE GLN LYS LEU LYS ILE ALA LYS VAL PHE LYS ASN
SEQRES 8 A 245 SER LYS TYR ASN SER LEU THR ILE ASN ASN ASP ILE THR
SEQRES 9 A 245 LEU LEU LYS LEU SER THR ALA ALA SER PHE SER GLN THR
SEQRES 10 A 245 VAL SER ALA VAL CYS LEU PRO SER ALA SER ASP ASP PHE
SEQRES 11 A 245 ALA ALA GLY THR THR CYS VAL THR THR GLY TRP GLY LEU
SEQRES 12 A 245 THR ARG TYR THR ASN ALA ASN THR PRO ASP ARG LEU GLN
SEQRES 13 A 245 GLN ALA SER LEU PRO LEU LEU SER ASN THR ASN CYS LYS
SEQRES 14 A 245 LYS TYR TRP GLY THR LYS ILE LYS ASP ALA MET ILE CYS
SEQRES 15 A 245 ALA GLY ALA SER GLY VAL SER SER CYS MET GLY ASP SER
SEQRES 16 A 245 GLY GLY PRO LEU VAL CYS LYS LYS ASN GLY ALA TRP THR
SEQRES 17 A 245 LEU VAL GLY ILE VAL SER TRP GLY SER SER THR CYS SER
SEQRES 18 A 245 THR SER THR PRO GLY VAL TYR ALA ARG VAL THR ALA LEU
SEQRES 19 A 245 VAL ASN TRP VAL GLN GLN THR LEU ALA ALA ASN
SEQRES 1 B 245 CYS GLY VAL PRO ALA ILE GLN PRO VAL LEU SER GLY LEU
SEQRES 2 B 245 SER ARG ILE VAL ASN GLY GLU GLU ALA VAL PRO GLY SER
SEQRES 3 B 245 TRP PRO TRP GLN VAL SER LEU GLN ASP LYS THR GLY PHE
SEQRES 4 B 245 HIS PHE CYS GLY GLY SER LEU ILE ASN GLU ASN TRP VAL
SEQRES 5 B 245 VAL THR ALA ALA HIS CYS GLY VAL THR THR SER ASP VAL
SEQRES 6 B 245 VAL VAL ALA GLY GLU PHE ASP GLN GLY SER SER SER GLU
SEQRES 7 B 245 LYS ILE GLN LYS LEU LYS ILE ALA LYS VAL PHE LYS ASN
SEQRES 8 B 245 SER LYS TYR ASN SER LEU THR ILE ASN ASN ASP ILE THR
SEQRES 9 B 245 LEU LEU LYS LEU SER THR ALA ALA SER PHE SER GLN THR
SEQRES 10 B 245 VAL SER ALA VAL CYS LEU PRO SER ALA SER ASP ASP PHE
SEQRES 11 B 245 ALA ALA GLY THR THR CYS VAL THR THR GLY TRP GLY LEU
SEQRES 12 B 245 THR ARG TYR THR ASN ALA ASN THR PRO ASP ARG LEU GLN
SEQRES 13 B 245 GLN ALA SER LEU PRO LEU LEU SER ASN THR ASN CYS LYS
SEQRES 14 B 245 LYS TYR TRP GLY THR LYS ILE LYS ASP ALA MET ILE CYS
SEQRES 15 B 245 ALA GLY ALA SER GLY VAL SER SER CYS MET GLY ASP SER
SEQRES 16 B 245 GLY GLY PRO LEU VAL CYS LYS LYS ASN GLY ALA TRP THR
SEQRES 17 B 245 LEU VAL GLY ILE VAL SER TRP GLY SER SER THR CYS SER
SEQRES 18 B 245 THR SER THR PRO GLY VAL TYR ALA ARG VAL THR ALA LEU
SEQRES 19 B 245 VAL ASN TRP VAL GLN GLN THR LEU ALA ALA ASN
SEQRES 1 C 245 CYS GLY VAL PRO ALA ILE GLN PRO VAL LEU SER GLY LEU
SEQRES 2 C 245 SER ARG ILE VAL ASN GLY GLU GLU ALA VAL PRO GLY SER
SEQRES 3 C 245 TRP PRO TRP GLN VAL SER LEU GLN ASP LYS THR GLY PHE
SEQRES 4 C 245 HIS PHE CYS GLY GLY SER LEU ILE ASN GLU ASN TRP VAL
SEQRES 5 C 245 VAL THR ALA ALA HIS CYS GLY VAL THR THR SER ASP VAL
SEQRES 6 C 245 VAL VAL ALA GLY GLU PHE ASP GLN GLY SER SER SER GLU
SEQRES 7 C 245 LYS ILE GLN LYS LEU LYS ILE ALA LYS VAL PHE LYS ASN
SEQRES 8 C 245 SER LYS TYR ASN SER LEU THR ILE ASN ASN ASP ILE THR
SEQRES 9 C 245 LEU LEU LYS LEU SER THR ALA ALA SER PHE SER GLN THR
SEQRES 10 C 245 VAL SER ALA VAL CYS LEU PRO SER ALA SER ASP ASP PHE
SEQRES 11 C 245 ALA ALA GLY THR THR CYS VAL THR THR GLY TRP GLY LEU
SEQRES 12 C 245 THR ARG TYR THR ASN ALA ASN THR PRO ASP ARG LEU GLN
SEQRES 13 C 245 GLN ALA SER LEU PRO LEU LEU SER ASN THR ASN CYS LYS
SEQRES 14 C 245 LYS TYR TRP GLY THR LYS ILE LYS ASP ALA MET ILE CYS
SEQRES 15 C 245 ALA GLY ALA SER GLY VAL SER SER CYS MET GLY ASP SER
SEQRES 16 C 245 GLY GLY PRO LEU VAL CYS LYS LYS ASN GLY ALA TRP THR
SEQRES 17 C 245 LEU VAL GLY ILE VAL SER TRP GLY SER SER THR CYS SER
SEQRES 18 C 245 THR SER THR PRO GLY VAL TYR ALA ARG VAL THR ALA LEU
SEQRES 19 C 245 VAL ASN TRP VAL GLN GLN THR LEU ALA ALA ASN
SEQRES 1 D 245 CYS GLY VAL PRO ALA ILE GLN PRO VAL LEU SER GLY LEU
SEQRES 2 D 245 SER ARG ILE VAL ASN GLY GLU GLU ALA VAL PRO GLY SER
SEQRES 3 D 245 TRP PRO TRP GLN VAL SER LEU GLN ASP LYS THR GLY PHE
SEQRES 4 D 245 HIS PHE CYS GLY GLY SER LEU ILE ASN GLU ASN TRP VAL
SEQRES 5 D 245 VAL THR ALA ALA HIS CYS GLY VAL THR THR SER ASP VAL
SEQRES 6 D 245 VAL VAL ALA GLY GLU PHE ASP GLN GLY SER SER SER GLU
SEQRES 7 D 245 LYS ILE GLN LYS LEU LYS ILE ALA LYS VAL PHE LYS ASN
SEQRES 8 D 245 SER LYS TYR ASN SER LEU THR ILE ASN ASN ASP ILE THR
SEQRES 9 D 245 LEU LEU LYS LEU SER THR ALA ALA SER PHE SER GLN THR
SEQRES 10 D 245 VAL SER ALA VAL CYS LEU PRO SER ALA SER ASP ASP PHE
SEQRES 11 D 245 ALA ALA GLY THR THR CYS VAL THR THR GLY TRP GLY LEU
SEQRES 12 D 245 THR ARG TYR THR ASN ALA ASN THR PRO ASP ARG LEU GLN
SEQRES 13 D 245 GLN ALA SER LEU PRO LEU LEU SER ASN THR ASN CYS LYS
SEQRES 14 D 245 LYS TYR TRP GLY THR LYS ILE LYS ASP ALA MET ILE CYS
SEQRES 15 D 245 ALA GLY ALA SER GLY VAL SER SER CYS MET GLY ASP SER
SEQRES 16 D 245 GLY GLY PRO LEU VAL CYS LYS LYS ASN GLY ALA TRP THR
SEQRES 17 D 245 LEU VAL GLY ILE VAL SER TRP GLY SER SER THR CYS SER
SEQRES 18 D 245 THR SER THR PRO GLY VAL TYR ALA ARG VAL THR ALA LEU
SEQRES 19 D 245 VAL ASN TRP VAL GLN GLN THR LEU ALA ALA ASN
HET 5BF A 301 45
HET 5BF B 301 45
HET 5BF C 301 45
HET 5BF D 301 45
HETNAM 5BF (11S)-4,9-DIOXO-N-[(2S)-1-OXO-3-PHENYLPROPAN-2-YL]-17,
HETNAM 2 5BF 22-DIOXA-10,30-DIAZATETRACYCLO[21.2.2.2~13,16~.1~5,
HETNAM 3 5BF 8~]TRIACONTA-1(25),5,7,13,15,23,26,28-OCTAENE-11-
HETNAM 4 5BF CARBOXAMIDE
FORMUL 5 5BF 4(C36 H37 N3 O6)
FORMUL 9 HOH *505(H2 O)
HELIX 1 1 ALA A 55 GLY A 59 5 5
HELIX 2 2 SER A 164 GLY A 173 1 10
HELIX 3 3 THR A 174 ILE A 176 5 3
HELIX 4 4 LEU A 234 ASN A 245 1 12
HELIX 5 5 ALA B 55 GLY B 59 5 5
HELIX 6 6 SER B 164 GLY B 173 1 10
HELIX 7 7 THR B 174 ILE B 176 5 3
HELIX 8 8 VAL B 231 ALA B 244 1 14
HELIX 9 9 ALA C 55 GLY C 59 5 5
HELIX 10 10 SER C 164 GLY C 173 1 10
HELIX 11 11 THR C 174 ILE C 176 5 3
HELIX 12 12 LEU C 234 ASN C 245 1 12
HELIX 13 13 ALA D 55 GLY D 59 5 5
HELIX 14 14 SER D 164 GLY D 173 1 10
HELIX 15 15 THR D 174 ILE D 176 5 3
HELIX 16 16 VAL D 231 ALA D 244 1 14
SHEET 1 A 7 GLU A 20 GLU A 21 0
SHEET 2 A 7 GLN A 156 PRO A 161 -1 O GLN A 157 N GLU A 20
SHEET 3 A 7 THR A 135 GLY A 140 -1 N CYS A 136 O LEU A 160
SHEET 4 A 7 PRO A 198 LYS A 203 -1 O VAL A 200 N VAL A 137
SHEET 5 A 7 ALA A 206 TRP A 215 -1 O GLY A 211 N LEU A 199
SHEET 6 A 7 PRO A 225 ARG A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 A 7 MET A 180 GLY A 184 -1 N ILE A 181 O TYR A 228
SHEET 1 B 7 GLN A 30 GLN A 34 0
SHEET 2 B 7 HIS A 40 LEU A 46 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TRP A 51 THR A 54 -1 O VAL A 53 N SER A 45
SHEET 4 B 7 THR A 104 LEU A 108 -1 O LEU A 106 N VAL A 52
SHEET 5 B 7 GLN A 81 LYS A 90 -1 N PHE A 89 O LEU A 105
SHEET 6 B 7 VAL A 65 ALA A 68 -1 N VAL A 66 O LEU A 83
SHEET 7 B 7 GLN A 30 GLN A 34 -1 N SER A 32 O VAL A 67
SHEET 1 C 7 GLU B 20 GLU B 21 0
SHEET 2 C 7 GLN B 156 PRO B 161 -1 O GLN B 157 N GLU B 20
SHEET 3 C 7 THR B 135 GLY B 140 -1 N CYS B 136 O LEU B 160
SHEET 4 C 7 PRO B 198 LYS B 203 -1 O VAL B 200 N VAL B 137
SHEET 5 C 7 ALA B 206 TRP B 215 -1 O THR B 208 N CYS B 201
SHEET 6 C 7 PRO B 225 ARG B 230 -1 O VAL B 227 N TRP B 215
SHEET 7 C 7 MET B 180 GLY B 184 -1 N ALA B 183 O GLY B 226
SHEET 1 D 7 GLN B 30 GLN B 34 0
SHEET 2 D 7 HIS B 40 ASN B 48 -1 O CYS B 42 N LEU B 33
SHEET 3 D 7 TRP B 51 THR B 54 -1 O VAL B 53 N SER B 45
SHEET 4 D 7 THR B 104 LEU B 108 -1 O LEU B 106 N VAL B 52
SHEET 5 D 7 GLN B 81 LYS B 90 -1 N PHE B 89 O LEU B 105
SHEET 6 D 7 VAL B 65 ALA B 68 -1 N VAL B 66 O LEU B 83
SHEET 7 D 7 GLN B 30 GLN B 34 -1 N GLN B 34 O VAL B 65
SHEET 1 E 7 GLU C 20 GLU C 21 0
SHEET 2 E 7 GLN C 156 PRO C 161 -1 O GLN C 157 N GLU C 20
SHEET 3 E 7 THR C 135 GLY C 140 -1 N CYS C 136 O LEU C 160
SHEET 4 E 7 PRO C 198 LYS C 202 -1 O VAL C 200 N VAL C 137
SHEET 5 E 7 TRP C 207 TRP C 215 -1 O THR C 208 N CYS C 201
SHEET 6 E 7 PRO C 225 ARG C 230 -1 O VAL C 227 N TRP C 215
SHEET 7 E 7 MET C 180 GLY C 184 -1 N ILE C 181 O TYR C 228
SHEET 1 F 7 GLN C 30 GLN C 34 0
SHEET 2 F 7 HIS C 40 LEU C 46 -1 O CYS C 42 N LEU C 33
SHEET 3 F 7 TRP C 51 THR C 54 -1 O VAL C 53 N SER C 45
SHEET 4 F 7 THR C 104 LEU C 108 -1 O LEU C 106 N VAL C 52
SHEET 5 F 7 GLN C 81 LYS C 90 -1 N PHE C 89 O LEU C 105
SHEET 6 F 7 VAL C 65 ALA C 68 -1 N VAL C 66 O LEU C 83
SHEET 7 F 7 GLN C 30 GLN C 34 -1 N GLN C 34 O VAL C 65
SHEET 1 G 7 GLU D 20 GLU D 21 0
SHEET 2 G 7 GLN D 156 PRO D 161 -1 O GLN D 157 N GLU D 20
SHEET 3 G 7 THR D 135 GLY D 140 -1 N CYS D 136 O LEU D 160
SHEET 4 G 7 PRO D 198 LYS D 203 -1 O VAL D 200 N VAL D 137
SHEET 5 G 7 ALA D 206 TRP D 215 -1 O GLY D 211 N LEU D 199
SHEET 6 G 7 PRO D 225 ARG D 230 -1 O VAL D 227 N TRP D 215
SHEET 7 G 7 MET D 180 GLY D 184 -1 N ILE D 181 O TYR D 228
SHEET 1 H 7 GLN D 30 GLN D 34 0
SHEET 2 H 7 HIS D 40 ASN D 48 -1 O CYS D 42 N LEU D 33
SHEET 3 H 7 TRP D 51 THR D 54 -1 O VAL D 53 N SER D 45
SHEET 4 H 7 THR D 104 LEU D 108 -1 O LEU D 106 N VAL D 52
SHEET 5 H 7 GLN D 81 LYS D 90 -1 N PHE D 89 O LEU D 105
SHEET 6 H 7 VAL D 65 ALA D 68 -1 N VAL D 66 O LEU D 83
SHEET 7 H 7 GLN D 30 GLN D 34 -1 N SER D 32 O VAL D 67
SSBOND 1 CYS A 1 CYS A 122 1555 1555 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 3 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.03
SSBOND 6 CYS B 1 CYS B 122 1555 1555 2.02
SSBOND 7 CYS B 42 CYS B 58 1555 1555 2.03
SSBOND 8 CYS B 136 CYS B 201 1555 1555 2.03
SSBOND 9 CYS B 168 CYS B 182 1555 1555 2.05
SSBOND 10 CYS B 191 CYS B 220 1555 1555 2.02
SSBOND 11 CYS C 1 CYS C 122 1555 1555 2.03
SSBOND 12 CYS C 42 CYS C 58 1555 1555 2.02
SSBOND 13 CYS C 136 CYS C 201 1555 1555 2.03
SSBOND 14 CYS C 168 CYS C 182 1555 1555 2.02
SSBOND 15 CYS C 191 CYS C 220 1555 1555 2.04
SSBOND 16 CYS D 1 CYS D 122 1555 1555 2.04
SSBOND 17 CYS D 42 CYS D 58 1555 1555 2.03
SSBOND 18 CYS D 136 CYS D 201 1555 1555 2.02
SSBOND 19 CYS D 168 CYS D 182 1555 1555 2.02
SSBOND 20 CYS D 191 CYS D 220 1555 1555 2.04
LINK OG SER A 195 C37 5BF A 301 1555 1555 1.60
LINK OG SER B 195 C37 5BF B 301 1555 1555 1.54
LINK OG SER C 195 C37 5BF C 301 1555 1555 1.56
LINK OG SER D 195 C37 5BF D 301 1555 1555 1.62
CISPEP 1 ILE D 99 ASN D 100 0 16.54
SITE 1 AC1 12 CYS A 191 MET A 192 GLY A 193 ASP A 194
SITE 2 AC1 12 SER A 195 SER A 214 TRP A 215 GLY A 216
SITE 3 AC1 12 SER A 217 SER A 218 HOH A 466 HOH A 510
SITE 1 AC2 22 HIS B 57 ILE B 99 LYS B 175 SER B 190
SITE 2 AC2 22 CYS B 191 GLY B 193 SER B 195 SER B 214
SITE 3 AC2 22 TRP B 215 GLY B 216 SER B 217 SER B 218
SITE 4 AC2 22 HOH B 431 HOH B 447 HOH B 536 HOH B 540
SITE 5 AC2 22 ASN C 18 ALA C 185 GLY C 187 THR C 222
SITE 6 AC2 22 SER C 223 HOH C 466
SITE 1 AC3 15 HIS C 57 ASP C 102 LYS C 175 SER C 190
SITE 2 AC3 15 CYS C 191 MET C 192 GLY C 193 ASP C 194
SITE 3 AC3 15 SER C 195 SER C 214 TRP C 215 GLY C 216
SITE 4 AC3 15 SER C 217 SER C 218 HOH C 408
SITE 1 AC4 22 ASN A 18 ALA A 185 SER A 186 THR A 222
SITE 2 AC4 22 SER A 223 HIS D 57 LYS D 175 SER D 190
SITE 3 AC4 22 CYS D 191 MET D 192 GLY D 193 ASP D 194
SITE 4 AC4 22 SER D 195 SER D 214 TRP D 215 GLY D 216
SITE 5 AC4 22 SER D 217 CYS D 220 HOH D 410 HOH D 411
SITE 6 AC4 22 HOH D 415 HOH D 445
CRYST1 45.610 109.340 89.070 90.00 93.47 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021925 0.000000 0.001329 0.00000
SCALE2 0.000000 0.009146 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011248 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
